ABSTRACT Title of dissertation: CAPILLARY ISOELECTRIC FOCUSING-BASED MULTIDIMENSIONAL PEPTIDE/PROTEIN SEPARATIONS FOR PROTEOMICS ANALYSIS Yueju Wang, Doctor of Philosophy, 2005 Dissertation directed by: Professor Cheng S. Lee Department of Chemistry and Biochemistry With the completion of the human genome project, the proteomics has become the focus of research interest for better understanding the complex biological processes. The mass spectrometry (MS) detection of vast number and broad dynamic range of the proteins requires that sample fractionation and separation be performed prior to MS analysis. Realizing the limitations of gel-based proteomic techniques, capillary- based and gel free separation technologies are presented as attractive alternatives holding the promises of high separation efficiency and resolution, broad dynamic range, easy system automation as well as high throughput. Coupled with laser free microdissection technology, the combination of CIEF with nano-RPLC in an automated and integrated platform was employed for comprehensive and sensitive proteome studies of limited protein quantities obtained from tissue samples. The peptides were first separated and concentrated by CIEF and were sequentially fractionated. All the CIEF fractions were further resolved by nano-RPLC, followed by tandem MS analysis. A total of 6,866 fully tryptic peptides were detected, leading to the identification of 1,820 distinct proteins. Due to limited peptide sequence coverage of identified proteins, the bottom-up approaches provide very limited molecular information about the intact proteins, particularly towards the detection of post-translational modifications. In contrast, top-down methods are advantageous for the detection of protein modifications. To improve separation efficiency and resolution of nano-RPLC separations for intact proteins, various chromatography conditions, including the chain length of the stationary phase, the column temperature, and the ion-pairing agent utilized in the mobile phase, were optimized using model proteins. Building upon the experience in the development of automated and integrated multidimensional peptide separation platform and the optimization of protein chromatography separation, a top-down proteome characterization of yeast cell lysates was further evaluated. An overall system capacity of 4,320-7,200 was achieved and a total of 534 distinct yeast protein masses were measured, yet required a protein loading of only 9.6 ?g. This protein loading is two to three orders of magnitude less than those used in current top-down proteome techniques, illustrating the potential usage of this proteome technology for the analysis of protein profiles within small cell populations or limited tissue samples. CAPILLARY ISOELECTRIC FOCUSING-BASED MULTIDIMENSIONAL PEPTIDE/PROTEIN SEPARATIONS FOR PROTEOMICS ANALYSIS By Yueju Wang Dissertation submitted to the Faculty of the Graduate School of the University of Maryland, College Park in partial fulfillment of the requirements for the degree of Doctor of Philosophy 2005 Advisory Committee: Professor Cheng S. Lee, Chair Professor Daniel E. Falvey Professor Catherine C. Fenselau Professor Sang Bok Lee Professor William E. Bentley ii TABLE OF CONTENTS LIST OF FIGURES .........................................................................................................iii LIST OF TABLES........................................................................................................... iv CHAPTER 1 RECENT ADVANCES IN CAPILLARY SEPARATIONS FOR PROTEOMICS ................................................................................... 1 1.1 INTRODUCTION TO PROTEOMICS............................................................... 1 1.2 CAPILLARY SEPARATIONS IN PROTEOMICS ........................................... 4 1.3 PROJECT DESCRIPTION................................................................................ 16 1.4 ACKNOWLEDGEMENT ................................................................................. 20 CHAPTER 2 PROTEOME ANALYSIS OF MICRODISSECTED TUMOR TISSUE USING A CAPILLARY ISOELECTRIC FOCUSING- BASED MULTIDIMENSIONAL SEPARATION PLATFORM COUPLED WITH ESI-TANDEM MS ........................................... 21 2.1 INTRODUCTION ............................................................................................. 21 2.2 EXPERIMENTAL SECTION........................................................................... 25 2.3 RESULTS AND DISCUSSION........................................................................ 30 2.4 CONCLUSION.................................................................................................. 42 2.5 ACKNOWLEDGEMENT ................................................................................. 44 CHAPTER 3 EFFECTS OF CHROMATOGRAPHY CONDITIONS ON INTACT PROTEIN SEPARATIONS FOR TOP-DOWN PROTEOMICS 45 3.1 INTRODUCTION ............................................................................................. 45 3.2 EXPERIMENTAL SECTION.......................................................................... 48 3.3 RESULTS AND DISCUSSION........................................................................ 51 3.4 CONCLUSION.................................................................................................. 62 3.5 ACKNOWLEDGEMENT ................................................................................. 63 CHAPTER 4 INTEGRATED CAPILLARY ISOELECTRIC FOCUSING/NANO- REVERSED PHASE LIQUID CHROMATOGRAPHY COUPLED WITH ESI-MS FOR CHARACTERIZATION OF INTACT YEAST PROTEINS ......................................................... 64 4.1 INTRODUCTION ............................................................................................. 64 4.2 EXPERIMENTAL SECTION........................................................................... 68 4.3 RESULTS AND DISCUSSION........................................................................ 72 4.4 CONCLUSION.................................................................................................. 82 4.5 ACKNOWLEDGEMENT ................................................................................. 84 CHAPTER 5 CONCLUSION........................................................................................ 85 APPENDIX??.............................................................................................................. 91 REFERENCES?.......................................................................................................... 127 iii LIST OF FIGURES Figure 2-1.......................................................................................................................... 30 Figure 2-2.......................................................................................................................... 32 Figure 2-3.......................................................................................................................... 33 Figure 2-4.......................................................................................................................... 35 Figure 2-5.......................................................................................................................... 37 Figure 2-6.......................................................................................................................... 40 Figure 3-1.......................................................................................................................... 52 Figure 3-2.......................................................................................................................... 54 Figure 3-3.......................................................................................................................... 56 Figure 3-4.......................................................................................................................... 57 Figure 3-5.......................................................................................................................... 59 Figure 4-1.......................................................................................................................... 74 Figure 4-2.......................................................................................................................... 75 Figure 4-3.......................................................................................................................... 76 Figure 4-4.......................................................................................................................... 80 Figure 4-5.......................................................................................................................... 81 iv LIST OF TABLES Table 1 .............................................................................................................................. 41 1 CHAPTER 1 RECENT ADVANCES IN CAPILLARY SEPARATIONS FOR PROTEOMICS Jonathan W. Cooper, Yueju Wang, and Cheng S. Lee Electrophoresis 25, 3913-3926 (2004) 1.1 INTRODUCTION TO PROTEOMICS As the sequence of the human genome continuously achieves further confidence, the door has already opened toward an effort at the fundamental understanding of complex biological processes, including development, differentiation, and signal transduction. These processes generally involve the coordinated expression and interaction of multiple genes and proteins in a synergistic effort. The identification and quantification of the multiple proteins that constitute and control a particular process is fundamental toward understanding the regulation of that biological system. Additionally, the ability to monitor the presence or absence of particular proteins, an increase or decrease in protein expression, a change in protein microheterogeneity, or a combination of these modifications may be useful toward the early detection and diagnosis of a wide spectrum of known diseases [1,2]. The information gained through proteomics, the large-scale analysis of gene products and their covalent modifications contained within a specific cell type at a particular cell state, will contribute greatly to our understanding not only of gene 2 function, but also of the role that individual proteins, and protein-protein complexes play in biological systems. For example, the transformation of a normal cell into a cancer cell requires multiple genetic modifications or changes, such as alterations in cell cycles specific for protein modifications or mechanisms of DNA repair. The identification of gene products either distinctive to cancers, or those playing a role related to their development, will help define the sequence of molecular events that eventually lead to cancer. It is clear that a profound impact will be made directly on disease related research ranging from the ability to enhance early detection and diagnosis of disease to the identification of biologically relevant targets for drug development and screening. Mass spectrometry (MS) employing matrix-assisted laser desorption/ionization (MALDI) [3,4] and electrospray ionization (ESI) [5] has evolved to become an essential tool in the bioanalytical laboratory for the identification and sequencing of protein [6]. The vast number and broad dynamic range of the proteins present in the expressed proteome of a typical organism requires that several fractionation and/or separation steps be performed on the sample prior to MS analysis. Two- dimensional polyacrylamide gel electrophoresis (2-D PAGE) has seemingly remained the method of choice for separating thousands of proteins in a single run [7-10] while simultaneously offering a ?differential display? analysis of protein expression. The two dimensions of a 2-D PAGE separation are isoelectric focusing in a pH gradient and sodium dodecyl sulfate (SDS)-PAGE. Each protein spot provides a rough measure of isoelectric point (pI) and molecular weight of the protein within 5-10%. However, 2-D PAGE is a relatively slow, labor intensive, and cumbersome technology. 2-D PAGE results from different laboratories can be difficult to compare, and sensitivity is limited 3 by the amount of a protein needed to visualize a spot, typically in the low-nanogram range for silver staining. Gel protein identification and the study of protein modifications generally involve gel spot excision, proteolytic digestion, peptide extraction/concentration, MS analysis of each protein spot. Unfortunately, many of the most important regulatory proteins, expressed at extremely low levels, are excluded in the combined 2-D PAGE-MS technique unless extensive fractionation of large quantities of protein together with the processing of a large number of narrow-range gels [11]. The disadvantage of these strategies, however, is that they all require much larger amounts of proteins, and therefore may be impractical for studies of small cell populations or tissue samples. Furthermore, the 2-D PAGE-MS approach still struggles in the degree of demonstrated coverage for a given proteome (i.e. for proteins with isoelectric points (pIs), molecular masses, or hydrophobicity at the extremes), sensitivity, and throughput [11,12]. 4 1.2 CAPILLARY SEPARATIONS IN PROTEOMICS Recognizing the severe constrains of gel-based separation techniques, a considerable effort has been focused on the development of liquid phase-based or non-gel proteome technologies enabling the rapid, broad, and sensitive analysis of complex proteomic samples through the combination of various chromatography methods with MS or tandem MS analysis [13-18]. Not surprisingly, much of this work has centered on the evaluation of capillary chromatography separations for the analysis of peptide mixtures obtained from proteolytic digestion of cell lysates. While direct analysis of peptide mixtures obtained from the digestion of complex cell lysates offers a greater potential for the identification of lower abundance proteins than 2-D PAGE [13,16], this bottom-up (shotgun) approach [13-18] provides very limited molecular information about the intact proteins, particularly for the detection of post-translational modifications (PTMs) [19]. PTMs include co- or post-translation covalent modifications to the protein structure and proteolytic processing of the translated protein. Such modifications may be overlooked in analyses using peptide-based proteome technique, where only a fraction of the total theoretical peptide population of a given protein may be identified [13,14,18]. The top-down method [17,20-23], in which intact proteins rather than peptides are measured, may be advantageous for the detection of PTMs. Furthermore, the top-down approach to protein sequence analysis using tandem MS may allow complete protein characterization far more efficiently than shotgun proteome technology using tryptic peptides. Realization of the potentials of the top-down technique, however, requires the processing and the separation of intact proteins to be brought to the similar level as those routinely achieved in shotgun proteomics for peptides [13-18]. 5 Single Dimension Capillary Separations The utilization of high-efficiency capillary reversed-phase liquid chromatography (CRPLC) has become increasingly attractive for the analysis of complex peptide mixtures [24]. Smith and co-workers have developed a series of high-efficiency separations based on the combination of various capillary chromatography columns with inner diameters ranging from 15 to 150 ?m [24,25]. Employing commercially available switching valves containing 150 ?m channels, narrow bore separation columns operating at 10,000 psi were coupled with larger solid phase extraction columns. The integrated system offers an increase in sample processing capacity roughly 400 fold as to sample solution volume and roughly 10 fold for sample mass loading for both soluble and membrane protein tryptic digests. The ability to identify 1,100-1,500 unique peptides in a 5-hr period while covering a hydrophobicity range approaching 98% of all possible tryptic peptides in the sample was demonstrated using an 11.4 Tesla Fourier transform ion cyclotron (FTICR)-MS [25]. The high resolution and sensitivity, and, of particular utility, high mass accuracy of FTICR together with reproducible CRPLC separation made possible a new concept of ?accurate mass-time tags? that could largely eliminate the need for time-consuming tandem MS measurements [26]. Horvath and co-workers [27,28] have employed displacement chromatography to achieve selective enrichment of trace analytes during reversed-phase separations. Based on the retention behavior of peptide components in the elution mode, selective analyte enrichment and high-resolution separation were achieved in a single step by the combination of an organic eluant such as acetonitrile with the displacer in elution-modified displacement chromatography. Accordingly, the sensitive ESI-MS 6 detection of a protein kinase A peptide substrate at low fmol levels, which was added as a trace marker component to a tryptic digest of bovine serum proteins or to a human growth hormone peptide digest, was achieved at a concentration ratio of 1:10 5 or 1:10 6 . In addition to the separation of complex peptide mixtures, single dimension separation techniques, including isoelectric focusing gel [29], capillary isoelectric focusing (CIEF) [30,31], capillary zone electrophoresis (CZE) [20], and RPLC [32,33], have been employed for processing protein mixtures prior to MS analysis. One characteristic inherent to capillary electrophoresis is the small sample volume that can be successfully applied to obtain a high-resolution analysis. As a good portion of the important proteins contained in a proteomic sample may be present at low levels, it becomes important to combine sample preparation/concentration in-line with the subsequent electrophoretic separations while avoiding analyte loss or dilution due to manual handling and transfer procedures. For protein samples in high conductivity media, an on-capillary sample stacking method has been developed by Wei and Yeung [34] without the need for sample desalting. By employing an etched porous joint not only as a molecular sieve, but also as an electrical junction, proteins and peptides may be concentrated in the discreet plug determined by the size of the etched region. After stacking, the narrow sample zone was introduced into the separation portion of the capillary by either hydrodynamic or electrokinetic forces, and CZE was then completed for resolution of the concentrated analytes. Additionally, Janini and co-workers [35] have demonstrated an on column sample enrichment technique utilizing a C 18 impregnated solid phase extraction disk within the capillary flow path to collect and enrich the sample to be studied. 7 While CIEF involves the application of a mixture containing protein/peptide analytes and carrier ampholytes in the entire capillary, the column volume still limits sample loading. To increase sample loading and, in turn, the final concentrations of focused analytes, an approach based on the dynamic electrokinetic injection of proteins/peptides from a solution reservoir was demonstrated by Chen et al. [36]. The charged proteins and peptides continuously migrated into the column whereupon they encountered the pH gradient established by preexisting carrier ampholytes for focusing and separation. The dynamic introduction and focusing was directly controlled by various electrokinetic conditions, including applied electric field strength and the injection time. An increase in the loading capacity of yeast peptide was determined to range from 8 to 45-fold of that obtained in conventional CIEF, and an overall concentration factor of 1400-7700 was achieved in comparison with the concentrations of dilute yeast peptides originally present in the sample. Still, the use of only a single separation dimension may not provide sufficient peak capacity for the resolution of complex protein and peptide mixtures, putting significant constraints on the detection sensitivity and dynamic range of the MS. It should be emphasized that the peak capacity of 2-D separation is the product of the peak capacities of the individual one-dimensional methods [37]. Thus, various non-gel-based 2-D separation schemes have been developed recently in an effort to alleviate the shortcomings in 2-D PAGE while reserving the ability to resolve complex peptide/protein mixtures prior to MS analysis. 8 Multidimensional Capillary Separations Capillary liquid chromatography-capillary liquid chromatography. Yates and co-workers have demonstrated a shotgun proteomics approach named multidimensional protein identification technology [14,15], which combines multidimensional liquid chromatography with ESI-tandem MS. The combination of strong cation exchange chromatography with high-efficiency nano-RPLC was employed by Shen and co-workers to obtain ultra-high-resolution of peptide mixtures in conjunction with tandem MS for characterization of the human plasma proteome [38]. The use of multidimensional chromatography separations has resulted in better utilization of the MS dynamic range and reduced discrimination among peptides during ionization, thus achieving a dynamic range of greater than 8 orders of magnitude in relative protein abundance. By using a total of 365 ?g of human plasma, 800-1682 human proteins were identified, dependent on criteria used for the identification. The selective detection of phosphopeptides from proteolytic digests is a challenging and highly relevant task in many proteomics applications. Phosphopeptides are generally present in small amounts with the need for selective isolation or enrichment before identification. Selective enrichment of phosphopeptides can be achieved using immobilized metal affinity chromatography (IMAC), followed by base elution [39]. Unfortunately, this method often results in the isolation of many nonphosphorylated peptides via nonspecific interactions. The selectivity of the IMAC toward phosphopeptides was significantly enhanced by converting all peptides to their corresponding methyl esters, drastically eliminating confounding binding via carboxylate groups [40]. Furthermore, Pinkse and co-workers [41] reported an automated method for 9 the enrichment of phosphopeptides from protein digests employing a 2-D column setup, with titanium oxide-based solid-phase as the first dimension and reversed-phase as the second dimension. Proteolytic digests of three different autophosphorylation forms of the 153 kDa homodimeric cGMP-dependent protein kinase were analyzed, and eight phosphorylation sites were identified, including two previously uncharacterized sites, namely, Ser-26 and Ser-44. In addition to performing protein isoelectric focusing in a preparative- scale Rotofor [42-44], Yan et al. [45] have employed an anion exchange column to achieve protein fractionation in a chromatofocusing mode using a pH-gradient in the mobile phase. The collected fractions eluted from a pH gradient of 4-7 were injected into a nonporous reversed-phase column as the second separation dimension for further analysis. The proteins eluted from the reversed-phase column were identified using both on-line ESI-MS and off-line faction collection followed by proteolytic digestion prior to MALDI-MS. Recently, Meng et al. have demonstrated combination of preparative-scale acid-labile surfactant-PAGE with RPLC for protein fractionation [22,23]. Proteins eluted from RPLC were subjected to protein sequence analysis using tandem MS to facilitate the detection of incorrectly predicted translational start sites and proteolytic processing of proteins such as removal of signal peptides or activation of pro-proteins to create functional proteins. These approaches currently require the use of FTICR-MS/MS for obtaining protein-sequencing measurements [20-23] and are also limited by the relative scarcity of bioinformatic tools to efficiently analyze this type of data, although these are under development [21]. 10 Capillary liquid chromatography-capillary electrophoresis. On-line coupling of size-exclusion chromatography with CZE was achieved by Stroink et al. via a reversed-phase trap column [46,47]. The size-resolved fraction retained in the trap column was then eluted into CZE for further analysis. A 2-D RPLC-CZE technique was developed by Issaq and co-workers [48,49] and employed towards the rapid and broad mapping of complex samples, including tryptic digests of cell extracts. Fractions from a micro-RPLC separation were collected every 30 s by an automated fraction collector into a 96-well microtiter plate. After concentration by drying under vacuum, the fractions were reconstituted with deionized water, and each was analyzed simultaneously in the second dimension by a 96-array CZE system based on charge-to-size ratio, and detected by UV absorption or laser-induced fluorescence. Instead of using UV or fluorescence detection, Janini et al. [50] have combined RPLC-CZE separations with ESI-tandem MS towards the identification of peptides in complex mixtures. A serum sample was depleted of high-abundance proteins, digested with trypsin, and then separated by RPLC and collected into 96 fractions. These fractions, collected off-line from the RPLC separation, were subjected to sequential CZE separations through a sheathless ESI interface that was integrated on the separation capillary. A key feature of this work is the employment of RPLC in lieu of ion exchange fractionation, where there is a large degree of overlap. The CZE-MS results demonstrated less than 15% overlap between neighboring RPLC fractions, leading to a more sensitive proteome analysis. Capillary electrophoresis-liquid chromatography. On-line combination of CIEF with CRPLC has been developed by Chen et al. [51,52]. In addition to analyte 11 focusing and concentration, CIEF as the first separation dimension resolves peptides on the basis of their differences in pI and offers greater resolving power than that achieved in strong cation exchange of a multidimensional liquid chromatography system [14,15]. The grouping of two highly resolving and completely orthogonal separation techniques of CIEF and CRPLC, together with analyte focusing and concentration, significantly enhances the dynamic range and sensitivity of MS toward the identification of lower abundance proteins. Capillary electrophoresis-capillary electrophoresis. By using a dialysis interface, Yang et al. [53,54] have constructed a 2-D capillary electrophoresis system consisting of CIEF coupled with either CZE or capillary gel electrophoresis (CGE) for the analysis of model proteins. Mohan and co-workers [55,56] have developed an integrated multidimensional electrokinetic-based separation/concentration platform employing a microdialysis junction as the interface for on-line combination of CIEF with transient capillary isotachophoresis (CITP)/CZE coupled with ESI-FTICR-MS for achieving the high resolution and sensitive analysis of complex proteome mixtures. In addition to the high-resolving power afforded by both the CIEF and CZE separations, the electrokinetic focusing/stacking effects of CIEF and CITP greatly enhance the dynamic range and detection sensitivity of MS for protein identification. This multidimensional electrokinetic-based platform offers overall peak capacity comparable to those obtained using multidimensional liquid chromatography system, but with a much shorter run time and no need for column regeneration. Most importantly, a total of 1,174 unique proteins, corresponding to 26.5% proteome coverage, were identified from the cytosolic fraction of S. oneidensis, while requiring <500 ng of proteolytic digest loaded in the CIEF capillary. 12 The sensitive capabilities of the multidimensional electrokinetic-based approach are attributed to the concentration effect in CIEF, the electrokinetic stacking of CITP, the nanoscale peak volume in CZE, the ?accurate mass tag? strategy for protein/peptide identification, and the high-sensitivity, high-resolution, and high-mass measurement accuracy of FTICR-MS. Sheng and Pawliszyn [57] demonstrated a 2-D electrokinetic separation system by coupling micellar electrokinetic chromatography (MEKC) in the first dimension with CIEF in the second dimension. To afford the combination of these orthogonal separation mechanisms, a 10-port valve with two conditioning loops was employed to collect the fractions eluting from the first dimension, provide the dialysis desalting of each surfactant rich fraction, and also act as the direct interface between MEKC and CIEF. Within the dialysis loop, salt and other unwanted first dimension effluent components were eliminated and carrier ampholytes were added prior to the second dimension separation. Peak broadening during the dialysis did not have significant impact on the second dimension separation due to the inherent concentrating effect in CIEF. Michaels and co-workers [58] detailed a 2-D electrokinetic separation system by combining submicellar capillary electrophoresis in the first dimension with CZE in the second dimension for high sensitivity protein analysis. Protein fractions from the first dimension separation were transferred to a second dimension capillary through an injection interface, where CZE was performed and followed by laser-induced fluorescence detection. Hu et al. [59] further combined capillary sieving electrophoresis on the basis of a SDS-pullulan buffer system with MEKC for the study of protein 13 expression in single mammalian cells. After a 6-min-long size-based separation, over 100 transfers of fractions from the first capillary were introduced into a second capillary for further separation by MEKC over an approximately 3.5-hr-long period. The ability to achieve sensitive protein profiling was demonstrated through the generation of protein fingerprints from single native MC3T3-E1 osteoprogenitor cells and MC3T3-E1 cells transfected with the human transcription regulator TWIST. Multidimensional proteome separations using microfluidics. Thermal time constants in microfluidics tend to be extremely small due to the large surface area to volume ratio, reducing the onset of significant Joule heating during electrokinetic separations and thus allowing higher separation voltages for shorter analysis times and equivalent or better separation resolution than capillary-based techniques toward complex mixtures. In addition to reduced size and power requirements leading to improved portability, microfluidic systems also hold great promise for realizing multidimensional separations in a single integrated system. To this end, several research groups have explored the application of microfluidics to perform multidimensional peptide and protein separations. Ramsey and co-workers have demonstrated 2-D separation of peptide mixtures in a microfluidic device using MEKC and CZE as the first and second dimensions, respectively [60,61]. Gottschlich et al. have also fabricated a spiral shaped glass channel coated with a C 18 stationary phase for performing RPLC separation of trypsin-digested peptides [62]. By employing a cross interface, the eluted peptides from MEKC [60,61] or RPLC [62] were sampled by a rapid CZE separation in a short glass microchannel. Additionally, Herr and co-workers have coupled CIEF with CZE for 2-D 14 separations of model proteins using plastic microfluidics [63]. Instead of using a cross interface [60-63], Wang et al. have combined CIEF with CZE or CGE using microfluidic valves [64]. In each of these examples, the multiple separation dimensions are performed serially, without the ability to simultaneously sample all proteins or peptides separated in the first dimension for parallel analysis in the second dimension. As an early step toward this goal, a microfabricated quartz device has been proposed by Becker and co-workers with a single channel for the first dimension and an array of 500 parallel channels with submicron dimensions as the second dimension positioned orthogonally to the first dimension channel [65]. In a further step, Chen et al. described a 2-D capillary electrophoresis system based on a 6-layer poly (dimethylsiloxane) (PDMS) microfluidic system [66]. The system consisted of a 25 mm-long microchannel for performing CIEF, with an intersecting array of parallel 60 mm-long microchannels for achieving CGE. This 6-layer PDMS microfluidic device, however, required the alignment, bonding, removal, re-alignment, and re-bonding of various combinations of the six layers to perform a full 2-D protein separation. An integrated protein concentration/separation system, combining CIEF with CGE on a single-layer 2-D microfluidic network, has been reported by Li and co- workers [67]. The ability to introduce and isolate multiple separation media in plastic microfluidic network was one of two key requirements for achieving multidimensional protein separations. The second requirement resided in the quantitative transfer of focused proteins from the first to second separation dimensions without significant loss in the resolution acquired from the first dimension. Rather than sequentially sampling 15 protein analytes eluted from CIEF, focused proteins were electrokinetically transferred into an array of orthogonal microchannels and further resolved by CGE in a parallel and high throughput format. Resolved proteins were monitored using non-covalent, environment-sensitive, fluorescent probes such as SYPRO Red. A 2-D protein separation was completed in less than 10 min with an overall peak capacity of around 1,700 using a chip with planar dimensions of as small as 2 cm x 3 cm. 16 1.3 PROJECT DESCRIPTION The sequencing of several organisms? genomes, including the human?s one, has opened the way for the so-called postgenomic era, which is now routinely coined as ?proteomics?. The most basic task in proteomics remains the detection and identification of proteins from a biological sample, and the most traditional way to achieve this goal consists of protein separations performed by 2-D PAGE. Still, the 2-D PAGE-MS approach remains lacking in proteome coverage (for proteins having extreme pIs or molecular masses as well as for membrane proteins), dynamic range, sensitivity, and throughput. Consequently, considerable efforts have been devoted to the development of non-gel-based proteome separation technologies in an effort to alleviate the shortcomings in 2-D PAGE while reserving the ability to resolve complex protein and peptide mixtures prior to MS analysis. It should be emphasized that the extremely high resolution of 2-D PAGE for protein separation is mostly contributed by isoelectric focusing in the first separation dimension. By transferring isoelectric focusing separation from gel to capillary format, it has been demonstrated that the focusing effect of CIEF not only contributes to high resolution protein/peptide separation [68,69], but also provides significant enhancement in analyte concentration. It should be noted that the entire CIEF capillary is initially filled with a solution containing proteins/peptides and carrier ampholytes for the creation of a pH gradient inside the capillary. Upon completion of analyte focusing, the self- sharpening effect greatly restricts analyte diffusion and contributes to analyte stacking in narrow focused bands. 17 This project therefore aims to further develop and optimize on-line combination of CIEF with nano-RPLC in an integrated platform for performing multidimensional separations of complex peptide and protein mixtures toward comprehensive and sensitive proteome studies. Chapter 2 demonstrates the ability to perform sensitive proteome analysis on the limited protein quantities available through tissue microdissection. CIEF combined with nano-RPLC in an automated and integrated platform not only provides systematic resolution of complex peptide mixtures based on their differences in pI and hydrophobicity, but also eliminates peptide loss and analyte dilution. In comparison with strong cation exchange chromatography [13-18], the significant advantages of electrokinetic focusing-based separations include high resolving power, high concentration and narrow analyte bands, and effective usage of ESI-tandem MS toward peptide identifications. Through the use of CIEF-based multidimensional peptide separations, a total of 6,866 fully tryptic peptides were detected, leading to the identification of 1,820 distinct proteins. These high mass accuracy and high confidence identifications were generated from 3 proteome runs of a single glioblastoma multiforme tissue sample, each run consuming only 10 ?g of total protein, an amount corresponding to 20,000 selectively isolated cells. Instead of performing multiple runs of multidimensional separations, the overall peak capacity can be greatly enhanced for mining deeper into tissue proteomics by increasing the number of CIEF fractions without an accompanying increase in sample consumption. Building upon the experience in the development of CIEF-based multidimensional peptide separation platform, research efforts are later directed toward 18 the application of combined CIEF with nano-RPLC for concentrating and resolving intact proteins from complex cell lysates. To improve the peak capacity of nano-RPLC for the resolution of protein mixtures within individual CIEF fractions, effects of various chromatography conditions, including alkyl chain length in the stationary phase, capillary column temperature, and ion-pairing agent, on the resolution of intact proteins are studied and reported in Chapter 3. Optimal chromatography conditions include the use of C 18 column heated at 60 0 C and the addition of trifluoroacetic acid instead of heptafluorobutyric acid as the ion-paring agent in the mobile phase. Under optimized chromatography conditions, there are no significant differences in the separation performance of yeast cell lysates present in the native versus denatured states. An integrated protein concentration/separation platform, combining CIEF with nano-RPLC, is developed and presented in Chapter 4 to provide significant protein concentration and high resolving power for the analysis of complex protein mixtures. Upon completion of protein focusing, the proteins are sequentially and hydrodynamically loaded into individual trap columns using a group of microinjection and microselection valves. Repeated protein loadings and injections into trap columns are carried out automatically until the entire CIEF capillary content is sampled and fractionated. Each CIEF fraction ?parked? in separate trap columns is further resolved using nano-RPLC, and the eluants are analyzed using ESI- MS. By taking only 9 CIEF fractions, an overall system capacity of 4,320- 7,200 is achieved in this study for the analysis of intact proteins obtained from the soluble fraction of yeast cell lysates. Further enhancement to the overall system capacity can be realized by increasing the number of CIEF fractions and slowing the solvent gradient in 19 nano-RPLC at the expense of analysis time. The CIEF-based multidimensional concentration/separation platform enables the measurement of 534 distinct yeast protein masses over a mass range of 5-70 kDa, yet requires a protein loading of only 9.6 ?g. This protein loading is two to three orders of magnitude less than those used in current 2-D PAGE and top-down proteome techniques [22,23,42-45], illustrating the potential usage of this proteome technology for the analysis of protein profiles within small cell populations or limited tissue samples. 20 1.4 ACKNOWLEDGEMENT We thank the National Cancer Institute (CA107988 and CA103086) for supporting portions of our research reviewed in this article. 21 CHAPTER 2 PROTEOME ANALYSIS OF MICRODISSECTED TUMOR TISSUE USING A CAPILLARY ISOELECTRIC FOCUSING-BASED MULTIDIMENSIONAL SEPARATION PLATFORM COUPLED WITH ESI-TANDEM MS Yueju Wang, Paul A. Rudnick, Erin L. Evans, Jie Li, Zhengping Zhuang, Don L. DeVoe, Cheng S. Lee, and Brian M. Balgley Submitted to Analytical Chemistry for Consideration of Publication 2.1 INTRODUCTION Biological systems are typically multi-tiered and exhibit complex interdependent interactions. Thus, it is widely accepted that instead of the classic single gene or single marker approach, molecular profiling has supplanted the single gene approach enabling the simultaneous expression monitoring of many genes or proteins. Tissue specific genomics or proteomics data can only be generated if the samples investigated consist of homogenous cell populations, in which no unwanted cells of different types and/or developmental stages obscure the results. One of the main problems with the analysis of tissue samples, either at the level of genes or proteins, is the heterogeneous nature of the sample; many different cell types are typically present in tissue biopsies, and in the case of diseased tissue, small numbers of abnormal cells may lie within or adjacent to unaffected areas. 22 Infrared laser capture microdissection (LCM) technology [70,71] provides a straightforward method for procuring homogeneous subpopulations of cells or tumor structures for biochemical and molecular biological analyses [72]. LCM is the technique of choice for selectively isolating diseased cells from normal cells within a tissue specimen, followed by microgenomic analysis using oligonucleotide and cDNA arrays [73-75]. Through subsequent application of recently developed approaches of mRNA amplification in a pool of isolated total RNA, it is now possible to perform complex high- throughput mRNA expression profiling by microdissecting and processing even single- cell samples [76-78]. All of these molecular profiling tools may be applied to generate specific genetic fingerprints for defined and individual lesions and for certain stages of a disease, as well as for characterizing transitional and developmental changes. Proteomics studies offer a powerful complementary approach to nucleic acid-based investigation. In the absence of protein amplification techniques, proteomic analysis of tissue specimens procured by LCM and other microdissection techniques [79- 82] is severely constrained by limiting sample amounts ranging from 10 3 -10 5 cells, corresponding to a total protein content of 0.1-10 ?g [71]. Cells isolated and captured by LCM have been directly analyzed using MALDI-MS [83-85]. The m/z signals or peaks obtained from MALDI-MS are correlated with protein distribution within a specific region of the tissue sample and can be used to construct ion density maps or specific molecular images for virtually every signal detected in the analysis. Additionally, Surface-enhanced laser desorption/ionization-mass spectrometry (SELDI-MS) has been reported as a relatively simple and rapid protein biomarker analysis tool with potential clinical utility [86-89]. Although SELDI-MS spectral peaks do not provide protein 23 identifications, the resulting fingerprint patterns have been explored for diagnostic applications including the early detection of several types of cancers. However, reproducibility of sample preparation and mass spectra among different laboratories has been problematic for both methodological and biological reasons, and little physical meaning can be attributed to the spectral peaks in the absence of identification [89]. Current proteome separation platforms, including 2-D PAGE and shotgun- based multidimensional liquid chromatography separations [13-18], however, require large cellular samples which are generally incompatible with the protein quantities obtained from LCM samples. While limited 2-D PAGE analyses of LCM-derived tissue samples have been attempted [90-93], these studies involve significant manual effort and time (from 3 hr to 4 days, depending on tissue type) to extract sufficient amounts of protein for obtaining good visual quality of gel patterns, while providing little proteome information beyond a relatively small number of high abundance protein identifications. In addition, the 2-D PAGE-MS approach suffers from low throughput and poor reproducibility, and remains lacking in proteome coverage, dynamic range, and sensitivity [11]. Peak capacity improvements in multidimensional liquid chromatography separations [13-18] have increased the number of detected peptides and proteins identified as a result of better use of the MS dynamic range and reduced discrimination during ionization. However, the minimal quantity of available sample from LCM captured cells has restricted analysis to the use of only a single chromatography separation prior to tandem MS analysis in recent studies [94,95] and limited the ability for mining deeper into the tissue proteome. Since the sizes of human tissue biopsies are 24 becoming significantly smaller due to early detection and diagnosis, a more effective discovery-based proteome technology is critically needed to enable sensitive studies of protein profiles within tissue specimens procured by LCM and other microdissection techniques [79-82]. As demonstrated in our previous studies [52,56], the key to establishing sensitive proteome analysis is attributed to high analyte concentrations in small peak volumes as the result of electrokinetic focusing/stacking and high resolving, multidimensional separation techniques in an integrated platform, thereby enhancing the dynamic range and detection sensitivity of MS. Our research efforts in this work further characterize and optimize the on-line combination of CIEF with nano-RPLC. Comparisons of peptide separations using CIEF versus strong cation exchange chromatography as the first separation dimension in multidimensional protein identification technology [13-18] are studied for their impacts on subsequent ESI-MS- based peptide identification. The capabilities of CIEF-based multidimensional separations for the analysis of protein profiles within small cell populations are demonstrated using a microdissected glioblastoma multiforme tissue sample. 25 2.2 EXPERIMENTAL SECTION Materials and Reagents Fused-silica capillaries (100 ?m i.d./365 ?m o.d. and 50 ?m i.d./365 ?m o.d.) were acquired from Polymicro Technologies (Phoenix, AZ). Acetic acid, ammonium hydroxide, high resolution ampholyte 3-10, dithiothreitol (DTT), and iodoacetamide (IAM) were obtained from Sigma (St. Louis, MO). Acetonitrile, hydroxypropyl cellulose (average MW 100,000), tris(hydroxymethyl)aminomethane (Tris), and urea were purchased from Fisher Scientific (Pittsburgh, PA). Heptafluorobutyric acid (HFBA) was acquired from Pierce (Rockford, IL). All solutions were prepared using water purified by a Nanopure II system (Dubuque, IA) and further filtered with a 0.22 ?m membrane (Costar, Cambridge, MA). Tissue Microdissection and Protein Digestion Tumor tissues of glioblastoma multiforme were collected at the time of surgery. The tissue was completely covered with optimal cutting temperature medium, immediately frozen in liquid nitrogen, and stored at -80 0 C until analyzed. Selective tissue microdissection was performed as previously described [82]. Briefly, a single 10- ?m-thick section was taken and stained with hematoxylin and eosin for histological evaluation. A semi-quantitative cell count was performed on tumor-rich (> 90% tumor cells) areas that were not compromised by inflammation, necrosis, or stromal or endothelial proliferation. Subsequently, these areas were subjected to selective tumor dissection from serial sections. A fine needle rigidly attached to a 3-axis micromanipulator was used 26 to mechanically mill tissue around the periphery of the selected regions. The depth of cut was progressively increased by changing the z-axis on the manipulator while navigating along the desired path, until the region was fully separated from the bulk tissue. The needle could then be used to remove the small section from the cover slip for placement in a sample vial. This simple approach is analogous to traditional manual tissue dissection, but with a miniature cutting tool replacing the dissection scalpel, and a micropositioner suitable for automation used for cutting depth and path control. The primary goal was to selectively enrich 100,000 tumor cells from each tissue sample in less than 30 min, using 5-10 consecutive sections. These serial sections were not stained and tissue microdissection was performed under strict morphologic control. Procurement of normal brain or areas of inflammation, necrosis, hemorrhage, or stromal or vascular proliferation was strictly avoided. The microdissected cells were placed directly into a microcentrifuge tube containing 20 mM Tris at pH 8.0. The cellular proteins were collected in the supernatant by centrifugation at 20,000g for 20 min. Proteins in the supernatant were denatured and reduced in solution containing 8 M urea and 10 mg/mL DTT. IAM was added to 20 mg/mL and the solution was incubated at 37 0 C for 1 hr in the dark. The solution was then diluted 4-fold with 100 mM ammonium acetate at pH 8.0. Trypsin was added at a 1:50 enzyme to substrate ratio and the solution was incubated at 37 0 C overnight. Tryptic digests were desalted using a Peptide MacroTrap column (Michrom Bioresources, Auburn, CA), lyophilized to dryness using a SpeedVac (Thermo, San Jose, CA), and then stored at -37 0 C. 27 Integrated CIEF/Nano-RPLC Multidimensional Peptide Concentration/Separation An on-line combination of CIEF with nano-RPLC has been developed and described in detail in previous work [52] and was employed for systematically resolving peptide digests based on their differences in pI and hydrophobicity. To perform multidimensional peptide separations, a 80-cm CIEF capillary (100 ?m i.d./365 ?m o.d.) was coated with hydroxypropyl cellulose for the elimination of electroosmotic flow and protein adsorption onto the capillary wall [96]. The capillary was initially filled with a solution containing 2% ampholyte 3-10 and 1.67 mg/mL tryptic peptides. Solutions of 0.5% ammonium hydroxide at pH 10.5 and 0.1 M acetic acid at pH 2.5 were employed as the catholyte and the anolyte, respectively. Focusing was performed at an electric field strength of 300 V/cm over the entire CIEF capillary. The current decreased continuously as the result of peptide focusing. Once the current reduced to ~10% of the original value, usually within 30 min, the focusing was considered to be complete. The focused peptides were sequentially and hydrodynamically fractionated into either 14 or 28 unique fractions. Nano-RPLC of each CIEF fraction was performed using an Ultimate pump (Dionex, Sunnyvale, CA) connected to a 15-cm pulled-tip fused silica capillary (50 ?m i.d./365 ?m o.d.) packed with 5-?m porous C 18 reversed-phase particles. Peptides were eluted using a 60-min linear gradient from 5 to 45% acetonitrile containing 0.02% HFBA and 0.02% formic acid at a flow rate of 200 nL/min. The eluants were monitored using a qTOF micro (Waters, Milford, MA) mass spectrometer and mass spectra were acquired from 500-1900 m/z for 1 sec, followed by 3 data dependent MS/MS scans from 50-1900 m/z for 3 sec each. 28 Peptide Data Analysis The resulting MS data files were analyzed by ProteinLynx Global Server 2.0 (Waters) to de-isotope and lock-mass- correct the raw data into peak list file suitable for database searching. Peptide and protein identifications were made using MASCOT 2.0 (Matrix Science, London, UK). Protein identifications are based on peptide identifications in the human International Protein Index (2.28) distributed and maintained by the European Bioinformatics Institute (http://www.ebi.ac.uk/IPI/IPIhuman.html). MASCOT searches were carried out at a precursor mass tolerance of 60 ppm, a 0.2 Da fragment mass tolerance; enzyme was trypsin (full); allowing 1 missed cleavage; carbamidomethyl as a fixed modification; and oxidized methionine, Y, S and T phosphorylations, and N-term and K acetylations as a variable modifications. Because MASCOT does not consider mass accuracy when assigning significance scores, an empirical threshold in place of the MASCOT Identity Threshold was calculated using a reversed database search [97]. This threshold was calculated by searching the same data files with the same search parameters against a reversed human International Protein Index database. Hits to the reversed database, with the exception of those peptides occurring in the forward search or to peptides containing residues with mass differences beyond the resolution limits of the instrument (Q->K, I->L), were considered false positive. A threshold score corresponding to a user defined false positive rate can then be extrapolated from a simple linear regression of and exponential plot of MASCOT ions score versus the false positive rate. Runs containing >1,000 spectra typically produce a linear regression with an R 2 value of >0.98. In this study, the false positive rate was kept to less than 5%. Mass accuracy based thresholds (MATH) have 29 been shown to accurately reduce false negative identifications, while controllably limiting false positive identifications, and improve the predictive power of a typical MASCOT search using qTOF data sets [97]. MASCOT results were parsed using MP.pm (Calibrant Biosystems, Rockville, MD) and stored for reporting and data visualization in proteome BiNDR databases accessible by web-interface (Calibrant Biosystems). 30 2.3 RESULTS AND DISCUSSION Gliomas are the most common primary tumors of the brain, with an incidence in the United States of nearly 20,000-25,000 new cases per year. Half of all gliomas, including the anaplastic astrocytomas and glioblastoma multiforme, exhibit aggressive behavior. In this study, a single 10-?m-thick tissue section was taken from a glioblastoma multiforme sample and stained with hematoxylin and eosin for histological evaluation (Fig. 2-1). A semiquantitative cell count was performed on tumor-rich areas (> 90% tumor cells) that were not compromised by inflammation, necrosis, or stromal or endothelial proliferation. Subsequently, these areas were subjected to careful tumor microdissection [82]. Selective enrichment of approximately 100,000 tumor cells was obtained from the microdisection of 5 -10 consecutive sections in each tissue sample. Figure 2-1 Optical microscope photograph of stained glioblastoma multiforme tissue section 31 These microdissected cells contained roughly 50 ?g protein for analysis. A 80-cm long capillary with a 100 ?m i.d. employed in this study offered a peptide loading of 10 ?g for each proteome analysis using a 1.67 mg/mL peptide digest solution prepared from the microdissection-procured tissue sample. As shown in Fig. 2-2, the CIEF separation performance of tryptic peptides obtained from the protein extract of glioblastoma multiforme was evaluated by hydrodynamically mobilizing focused proteins passing a UV detector placed near the cathodic end of the capillary. Initially, the entire content of the CIEF capillary was split into 14 individual fractions. All CIEF fractions were further resolved by nano-RPLC and the eluants were measured using ESI-tandem MS. Displayed in Fig. 2-3 are the base peak chromatograms of a representative CIEF/nano-RPLC analysis of tryptic peptides obtained from the microdissection of a glioblastoma multiforme sample. The percentage of identified peptides present in more than one CIEF fraction was only around 10-15%, significantly less than 40-80% obtained from the multidimensional LC system using strong cation exchange coupled with reversed-phase separations [14]. A high degree of peptide overlapping in the first dimension unnecessarily burdens the subsequent separation and greatly reduces the overall peak capacity in a multidimensional separation system. The presence of high abundance peptides in multiple fractions negatively impacts the selection of low abundance peptides for tandem MS identification. Additionally, the poor resolution of low abundance peptides adversely affects their final concentrations in the eluting peaks prior to the ESI- MS analysis. 32 0 0.4 0.8 1.2 1.6 2 0510 15 20 25 30 35 40 45 Time (min) U V A b s o r b a n c e ( m A U ) Figure 2-2 CIEF-UV analysis of tryptic peptides obtained from microdissection- procured glioblastoma multiforme tissue sample. Capillary: hydroxypropyl cellulose coating, 80 cm x 100 ?m i.d. x 365 ?m o.d.; anolyte: 0.1 M acetic acid at pH 2.5; catholyte: 0.5% w/w ammonium hydroxide at pH 10.5; electric field strength: 300 V/cm; hydrodynamic mobilization; detection: UV absorbance at 280 nm, 7 cm from cathodic end. 33 Figure 2-3 Base peak chromatograms of a representative CIEF/nano-RPLC multidimensional separation of 10 ?g peptide digest prepared from microdissection-procured glioblastoma multiforme tissue sample. Each number represents the sequence of CIEF fractions further analyzed by nano-RPLC from basic to acid pHs. 34 The high resolution nature of pI-based separations, including CIEF [52,69], was further supported by Stephenson and co-workers [98,99] who employed immobilized pH gradient gels in the first dimension, followed by RPLC and subsequent tandem MS analysis. The pI values of peptides identified in each CIEF fraction were calculated using the ?iep? program developed by the European Molecular Biology Open Source Software Suite (EMBOSS) group. As shown in Fig. 2-4, the CIEF separation was able to cover a wide pH range of 3.1-10.8 using a 2% ampholyte 3-10 solution. In comparison with immobilized pH gradient gels [98,99], the significant advantages of CIEF include the ability to use higher electric fields resulting in rapid and ultrahigh resolution separations, improved reproducibility in pI fractions resulting from the use of gel free separation medium, and the amenability to automation and seamless coupling with nano-RPLC in an integrated platform while avoiding potential sample loss, analyte dilution, and any post-gel peptide extraction/concentration procedures. 35 Figure 2-4 Distribution of peptide?s pI and solution charge state in each CIEF fraction. In addition to the significant peptide fraction overlap resulting from strong cation exchange chromatography, peptides are separated in a mixed-mode based on their ionic charge and hydrophobicity [18]. The majority of doubly charged peptides are eluted over approximately 25% of the entire salt gradient [18]. Typically 70-90% of peptide identifications in shotgun proteomics are made through tandem MS fragmentation of doubly charged ions [14,18]. Therefore, fractions containing the majority of peptide identifications tend to be clustered at the early part of the salt elution gradient, corresponding to the presence of doubly charged peptides [18,99]. In contrast, CIEF provides an even distribution of doubly charged peptides over the entire pH gradient (Fig. 2-4), thereby maximizing the informative potential of MS measurements. 36 Due to the limited protein quantities extracted from microdissection- procured tissue specimens, a single RPLC separation was performed in recent studies [94,95] for the analysis of selected cell populations. However, the use of only a single separation dimension may not provide sufficient peak capacity for the resolution of complex peptide mixtures, putting significant burdens on the detection sensitivity and dynamic range of the MS. By employing CIEF-based multidimensional separations, a total of 6,866 fully tryptic peptides were detected, leading to the identification of 1,820 distinct proteins (see APPENDIX). These identifications were generated from 3 runs of a single glioblastoma multiforme tissue sample, with each run consuming only 10 ?g of total protein and were based on high mass accuracy (60 ppm) and high confidence (5% false positive) hits to fully tryptic peptides. This ultrasensitive capability of CIEF-based multidimensional separations may enable the use of proteome analysis for the assessment of specimen quality and reproducibility procured from the same tissue, and in turn, allow the evaluation and optimization of microdissection technologies [70,71,79-82] and tissue sample preparation. In addition to tracking the cumulative totals of protein identifications, the percentage of overlapping proteins was approximately 70% across any two runs (Fig. 2- 5). A total of 700 proteins, corresponding to 38.5% of collective data set, were found in all three runs. For each additional run, the percentage increase in cumulative protein identifications was approximately 25-35% and decreased with increasing numbers of analysis runs. This percentage increase in cumulative protein identifications was higher than 10-15% obtained from the analysis of yeast cell lysates using multidimensional 37 liquid chromatography separations [100], likely as a result of the complexity of the human tissue proteome. Figure 2-5 The overlap in the proteins identified from three CIEF-nano-RPLC-ESI- MS/MS runs using a single glioblastoma multiforme tissue sample. The intrinsic high resolution of CIEF allows the number of fractions sampled in the first separation dimension to be further increased. The excellent reproducibility together with straightforward fractionation enables user discretion as to which fractions are to be analyzed in the off-line approach, and interesting fractions may be revisited (reanalyzed) or repeatedly accumulated for identification of extremely low abundance peptides. By comparing the results obtained from runs containing 14 and 28 CIEF fractions, the number of distinct proteins identified from a single proteome experiment of 28 CIEF fractions was comparable or slightly higher than the cumulative data set achieved using two runs of 14 CIEF fractions. For the proteome analysis of limited tissue samples, further enhancement in the overall peak capacity for mining 38 deeper into the proteome can therefore be realized by simply increasing the number of CIEF fractions without an accompanying increase in sample consumption. In contrast, Peng and co-workers [18] have significantly increased the number of strong cation exchange chromatography fractions, but obtained comparable numbers of peptide and protein identifications as those reported by Washburn and colleagues [13]. A variety of protein classes, including structural proteins, metabolic enzymes, receptors, and proteins involved in transcription, translation, and post- translational modification of gene products, were identified from microdissection- procured glioblastoma multiforme tissue samples. A number of biologically relevant proteins, such as annexin I and nestin, were unambiguously identified. A total of 18 unique peptides (peptides matching on single database entry) (Table 2-1), corresponding to greater than 50% protein sequence coverage, led to the identification of annexin I which is related to tumor aggressiveness and angiogenesis, and found exclusively in tumor vessels [101,102]. On the other hand, nestin, which is linked to neural stem cell differentiation [103,104], was identified by 16 unique peptides (sequence in ?italic? in Table 2-1) out of a total of 19 distinct peptide identifications. Examples of tandem MS spectra leading to peptide identifications are shown in Fig. 2-6. For the identification of peptides eluted from multidimensional separations, tandem MS instruments such as a qTOF mass spectrometer employed in this study acquire peptide MS/MS spectra which encode the peptide sequences. Traditionally, this acquisition has been done in a data-dependent way, whereby the instrument relies on a preliminary scan, performed as the peptides enter the instrument, to select peptides for fragmentation and generation of tandem MS spectra. However, data-dependent scanning 39 cannot acquire spectra fast enough to identify all the peptides as they enter the MS instrument, so many peptide and subsequent protein identifications are missed. Newly introduced rapid-scanning linear ion-trap instruments can acquire MS/MS spectra up to five times faster than earlier generations of MS instruments. Furthermore, parallel, rather than serial, collision-induced dissociation (CID) of peptides has been demonstrated by several research groups [105-109] for increasing the mass spectrometric duty cycle. Thus, the use of rapid-scanning MS instruments or parallel (or data-independent) CID coupled with CIEF-based multidimensional separations should greatly increase the sequence coverage of identified proteins and total proteome coverage within limited tissue samples or small cell populations. 40 Figure 2-6 MS/MS spectra of (A) WGPGSSVGSLQALSSSQR and (B) KGTDVNVFNTILTTR leading to the identification of nestin and annexin I , respectively. 41 Table 1 List of Peptides Identified for Nestin and Annexin I Peptide Sequence Exp. Mass Error (Da) Error (ppm) Score Nestin EESEAEAPR 1016.45 0.0060 5.9 43.00 SLEEDLETLK 1175.61 0.0151 12.9 47.54 AHADDELAALR 1180.59 0.0048 4.1 56.57 SAGQENLETLK 1188.62 0.0189 15.9 39.53 VGLNAQAACAPR 1226.64 0.0183 14.9 47.46 SLETEILESLK 1260.69 0.0114 9.0 62.59 EIQDSQVPLEK 1284.68 0.0208 16.2 51.25 DNLAEELEGVAGR 1371.67 0.0119 8.7 75.51 GEGEGQIWGLVEK 1400.70 0.0088 6.2 90.97 TLENQSHETLER 1455.70 0.0005 0.3 84.51 QGLQSQIAQVLEGR 1525.83 0.0087 5.7 58.40 VAIPASVLPGPEEPGGQR 1772.93 0.0166 9.3 66.26 VAIPASVLPGPEEPGGQR 1772.94 0.0016 0.9 52.76 WGPGSSVGSLQALSSSQR 1802.89 0.0018 1.0 106.42 DLEEAGGLGTEFSELPGK 1847.88 0.0003 0.2 64.77 SLEEEGQELPQSADVQR 1913.87 0.0219 11.5 59.02 SLDQEIARPLENENQEFLK 2272.14 0.0051 2.3 44.52 LGSLLPVLSPTSLPSPLPATLETPVPAFLK 3054.74 0.0233 7.6 27.71 SLEGNLETFLFPGTENQELVSSLQENLESLTALEK 3878.87 0.0655 16.9 57.72 Annexin I CLTAIVK 803.46 0.0006 0.7 31.89 VLDLELK 828.49 0.0092 11.1 34.98 NALLSLAK 828.50 0.0099 12.0 44.68 AMVSEFLK 965.48 0.0092 9.6 52.36 DITSDTSGDFR 1212.53 0.0078 6.4 57.74 TPAQFDADELR 1261.61 0.0190 15.1 76.96 CATSKPAFFAEK 1355.67 0.0157 11.6 46.84 GVDEATIIDILTK 1386.77 0.0123 8.9 72.57 GVDEATIIDILTKR 1542.86 0.0008 0.5 67.23 ALTGHLEEVVLALLK 1604.96 0.0112 7.0 90.92 KGTDVNVFNTILTTR 1677.88 0.0297 17.7 129.34 GLGTDEDTLIEILASR 1701.87 0.0088 5.2 129.79 KALTGHLEEVVLALLK 1733.09 0.0452 26.1 79.72 SEDFGVNEDLADSDAR 1738.73 0.0041 2.4 83.35 AAYLQETGKPLDETLK 1775.92 0.0060 3.4 62.79 AAYLQETGKPLDETLKK 1904.04 0.0117 6.1 76.35 MYGISLCQAILDETKGDYEK 2333.08 0.0122 5.2 31.02 GGPGSAVSPYPTFNPSSDVAALHK 2355.16 0.0090 3.8 103.65 42 2.4 CONCLUSION To address the issue of cell heterogeneity in the tissue section, LCM [70,71] and other microdissection techniques [79-82] have been developed to provide a rapid and straightforward method for isolating selected subpopulations of cells for downstream molecular analysis, effectively enabling purification of the molecules of interest by eliminating DNA, RNA, or protein interference from the surrounding tissue. However, a more significant problem of microdissection-based tissue sample preparation is the lack of sample availability for mining deeper into the proteome using current 2-D PAGE [90-93] and shotgun technologies [13-18,94,95], greatly impacting the efforts toward the assessment of sample quality and the discovery of tumor biomarkers. Coupled with the laser-free microdissection technology [82], CIEF-based multidimensional peptide separations were employed to enable the analysis of protein profiles within small cell populations procured from glioblastoma multiforme tissue samples. Compared with strong cation exchange chromatography utilized as the first dimension in multidimensional protein identification technology [13-18], CIEF not only contributed to high resolution peptide separation based on their differences in pI, but also allowed effective usage of MS-based peptide identifications by even distribution of doubly charged peptides over the entire pH gradient. Instead of performing multiple runs of multidimensional separations, comparable or even better proteome results can be achieved by simply increasing the number of CIEF fractions due to the intrinsic high resolution nature of electrokinetic focusing. This unique feature is particularly important for the proteome analysis of limited tissue samples. 43 The analysis of a single glioblastoma multiforme tissue sample led to the identification of a total of 6,866 fully tryptic peptides, corresponding to 1,820 distinct protein identifications. To greatly enhance the sequence coverage of identified proteins and total proteome coverage within limited tissue samples or small cell populations, our future work will focus on the application of rapid-scanning linear ion-trap instrumentation and/or data-independent CID [105-109] for increasing the mass spectrometric duty cycle. In addition to biomarker discovery, the ability to perform comprehensive and sensitive tissue proteome analysis will also allow the evaluation of sample quality and reproducibility for the validation and optimization of microdissection technologies. 44 2.5 ACKNOWLEDGEMENT We thank the National Cancer Institute (CA103086 and CA107988) and the National Center for Research Resources (RR21239) for supporting portions of this research. 45 CHAPTER 3 EFFECTS OF CHROMATOGRAPHY CONDITIONS ON INTACT PROTEIN SEPARATIONS FOR TOP-DOWN PROTEOMICS Yueju Wang, Brian M. Balgley, Paul A. Rudnick, and Cheng S. Lee Journal of Chromatography A, 1073, 35-41 (2005) 3.1 INTRODUCTION The vast number of proteins present in the proteome of a typical organism requires that separations be performed on the mixture prior to introduction into the mass spectrometer. 2-D PAGE is still the method of choice for separating thousands of proteins in a single run [7-10] while offering a ?differential display? of protein expression. However, the identification of gel resolved proteins and the study of protein modifications typically involve the separate excision, proteolytic digestion, peptide extraction/concentration, and MS analysis of each protein spot [110,111]. All of these procedures, even when semi-automated using the commercially available robotic sample and liquid handling systems, are time-consuming tasks prone to significant sample loss and analyte dilution. Thus, the 2-D PAGE-MS approach remains lacking in proteome coverage, dynamic range, sensitivity, and throughput [11,12]. Consequently, considerable efforts have been devoted to the development of non-gel-based and bottom-up (or shotgun) proteome technologies through the combination of various chromatography methods with MS or tandem MS analysis [13- 18]. These peptide separation techniques fully exploit the sensitivity achievable with conventional mass spectrometers (roughly 10 -16 mol as opposed to 10 -14 mol in 46 conjunction with 2-D PAGE), allowing many additional proteins to be identified. However, the bottom-up approaches provide very limited molecular information about the intact proteins where only a fraction of the total theoretical peptide population of a given protein may be identified. By comparing with shotgun methodologies, the top-down proteome techniques [20-23], in which intact proteins rather than peptides are measured, are advantageous for the detection of PTMs [19]. PTMs include co- or post-translation covalent modifications to the protein structure and proteolytic processing of the translated protein. Furthermore, the top-down approaches to protein sequence analysis using tandem MS may allow complete protein characterization far more efficiently than shotgun proteome technologies using protein digests. In order to achieve the full potential of top- down approaches, the processing and separation of intact proteins still have to be brought to a similar level as those routinely achieved in shotgun proteomics. A variety of separation technologies, including gel-based isoelectric focusing [29], CIEF [30,31], CZE [20], and RPLC [32,33], have been utilized for resolving intact proteins prior to MS analysis. The application of only a single separation dimension, however, provides insufficient peak capacity for the resolution of complex protein mixtures. Thus, several recent attempts have involved off-line combinations of preparative scale isoelectric focusing [42-44] or acid-labile surfactant-based polyacrylamide gel electrophoresis [22,23] with RPLC in the development of multidimensional protein separation platforms. The collected protein fractions from either isoelectric focusing or gel electrophoresis were further resolved using RPLC as the second separation dimension prior to MS analysis. 47 It is clear that RPLC plays a major role in both single and multidimensional protein separation platforms in an effort to increase the overall peak capacity for the resolution of complex intact protein mixtures such as cell lysates. Total peak capacity improvements in protein separations contribute to increased number of proteins identified in top-down proteomics due to better use of the MS dynamic range and reduced discrimination during ionization. Thus, the main objective of the present study is to carefully examine the effects of various chromatography conditions, including alkyl chain length in the stationary phase, capillary column temperature, and ion-pairing agent, on the resolution of intact proteins. By using nano-RPLC-ESI- MS, we further investigate potential differences in chromatography separation and ESI measurement of yeast intact proteins as the result of the protein denaturation process. Denatured proteins collected in RPLC fractions can be directly subjected to proteolytic digestion for obtaining their corresponding peptides and peptide sequences, particularly toward the MS identification of high molecular mass proteins [42-45]. 48 3.2 EXPERIMENTAL SECTION Materials and Chemicals Fused-silica capillaries (50 ?m i.d./365 ?m o.d.) were acquired from Polymicro Technologies (Phoenix, AZ). Model proteins, including bovine serum albumin (bovine, pI 5.60, 66,433.0 Daltons), cytochrome c (equine, pI 9.59, 12,362.0 Daltons), myoglobin (equine, pI 7.36, 16,951.5 Daltons), and ribonuclease A (bovine, pI 8.64, 13,688.1 Daltons), DTT, and IAM were obtained from Sigma (St. Louis, MO). Acetonitrile, DNase, formic acid, glycerol, magnesium chloride, TFA, Tris, and urea were purchased from Fisher Scientific (Pittsburgh, PA). HFBA was acquired from Pierce (Rockford, IL). All solutions were prepared using water purified by a Nanopure II system (Dubuque, IA) and further filtered with a 0.22 ?m membrane (Costar, Cambridge, MA). Soluble Fraction of Intact Proteins from S. cerevisiae The yeast cells (Sigma) were suspended in a buffer which consisted of 10 mM Tris (pH 7.0), 5 mM magnesium chloride, 0.1 mM DTT, and 10% glycerol. The cells were disrupted by sonication for the release of cellular proteins. After sonication, DNase was added with a final concentration of 50 ?g/mL for the cleavage and removal of nucleic acids. The cellular proteins were collected in the supernatant by centrifugation at 20,000g for 10 min. The protein solution was then desalted using a regenerated cellulose membrane (Millipore, Bedford, MA) with a 5,000 molecular weight cutoff. Yeast cytosol proteins were denatured and reduced in a 20 mM Tris buffer containing 8 M urea and 0.1 M DTT for 2 hr at 37 0 C under a nitrogen atmosphere. Proteins were alkylated by adding excess IAM with a final concentration of 50 mM and 49 the reaction was allowed to proceed for 30 min at room temperature in the dark. A PD-10 size exclusion column (Amersham Pharmacia Biotech, Uppsala, Sweden) was employed for buffer exchange and proteins were eluted in a solution containing 2 M urea and 10 mM Tris at pH 8.0. The total protein concentration was determined using the Bradford method (Bio-Rad, Richmond, CA) and was around 2 mg/mL. Nano-RPLC-ESI-MS Analysis of Model Proteins and Soluble Fraction of Intact Proteins from S. cerevisiae The tip at the end of a 16-cm-long fused silica capillary (50 ?m i.d. x 365 ?m o.d.) was flame-pulled and packed with 13 cm of 5-?m C 4 - or C 18 -bonded particles (Phenomenex, Torrance, CA). The C 18 -bonded particles in methanol were introduced into the capillary by gradually increasing the pressure from 100 to 2,000 psi using an Agilent 1100 capillary LC pump (Avondale, PA). The packed capillary was left under pressure for 10 hr and then depressurized overnight. A microcross (Upchurch Scientific, Oak Harbor, WA) containing a platinum electrode was employed to apply an ESI voltage of 1.8 kV and reduce the flow of Agilent 1100 capillary LC pump from 2 ?L/min to an effective flow rate of 200 nL/min. A 30-min linear gradient from 10% to 65% acetonitrile (containing 0.1% TFA or 0.02% HFBA) was utilized to perform intact model protein separations. The linear gradient was further extended from 30- to 60-min for the analysis of complex yeast cell lysates. The eluants from nano-RPLC were monitored using a Micromass qTOF micro mass spectrometer (Manchester, United Kingdom). Mass spectra were collected from 600 to 1900 m/z using a scan time of 2.0 s. Automated analysis of the nano-RPLC- 50 ESI-MS data files were performed using Protein Trawler software (Bioanalyte, Portland, ME) [112,113]. The program summed all data within a specified time interval, utilized Micromass MaxEnt 1 to deconvolute multiply charged ions, centered the results, carried out a threshold selection, and reported the mass, intensity, and retention time of each protein in a text file. The program repeated this process across sequential portions of the chromatogram. 51 3.3 RESULTS AND DISCUSSION The reduction of column i.d. from few hundred ?m [13] to as small as 15 ?m [24] in capillary liquid chromatography has resulted in higher peptide concentrations within smaller peak volumes, thus enabling more sensitive MS detection. Nano-RPLC equipped with a 50 ?m i.d. capillary column was therefore employed in this study to evaluate the effects of various chromatography conditions on intact protein separations and allow ultrasensitive characterization of model proteins and yeast cell lysates using ESI-MS. Due to the use of ESI-MS detection, the differences in chromatography separation and protein intensity were further revealed among the samples containing the soluble fraction of yeast cell lysates in the native versus denatured/reduced/alkylated states. Effect of Alkyl Chain Length in the Stationary Phase on Intact Protein Separations Four model proteins, including bovine serum albumin, cytochrome c, myoglobin, and ribonuclease A, were prepared in 10 mM Tris at pH 7.0 with a final concentration of 0.1 ?M for each model protein. The effect of alkyl chain length in the stationary phase on chromatography separation of model proteins was studied and shown in Figs. 3-1A and 3-1B as the base peak chromatograms acquired from capillary columns packed with 5-?m C 4 - and C 18 -bonded particles, respectively. All protein peaks were directly identified on the basis of mass spectra of protein analytes taken from the average of scans under the peaks. 52 Figure 3-1 Comparison of model protein separations using (A) C 4 and (B) C 18 columns. Column temperature: 25 0 C; elution order: 1-ribonuclease A, 2-cytochrome c, 3-bovine serum albumin, and 4-myoglobin; mobile phase: a 30-min linear gradient from 10% to 65% acetonitrile (containing 0.1% TFA) at a flow rate of 200 nL/min; sample loading: 100 femtomole for each model protein (1 ?L injection of 0.1 ?M protein solution). 53 As anticipated [114], the elution time of model proteins increased with increasing alkyl chain length. Furthermore, the reconstructed ion chromatograms were obtained using the most intense m/z ions from each protein envelope and displayed in Figs. 3-2A and 3-2B for the separations carried out by the C 4 and C 18 columns, respectively. Both the separation efficiency and resolution of model proteins achieved in the C 18 column were considerably better than those obtained from the C 4 column, particularly for early eluted proteins such as ribonuclease A and cytochrome c. Still, potential sample loss due to irreversible protein adsorption onto the C 18 stationary phase may outweigh the benefits of better separation performance and may adversely impact the ability to perform comprehensive proteome analysis, particularly toward the identification of low abundance proteins. Thus, both C 4 and C 18 reversed phase columns have been utilized by several research groups for the analysis complex protein mixtures such as cell lysates in top-down proteomics [22,23,42-45,112,113]. Effect of Ion-Pairing Agent on Intact Protein Separations To improve chromatography separations, ion-pairing agents are commonly used to sharpen peak shapes [115]. In contrast to ion pairing agents of alkanesulfonic acids, perfluorinated carboxylic acids up to four carbon atoms are known to be volatile and therefore well suited for ESI-MS detection. The downside to the use of perfluorinated carboxylic acids is their ionization suppression effect. Some of the decrease in MS sensitivity, however, can be regained through increased analyte concentrations in sharpened peaks due to the ?concentration sensitive? behavior of nano-ESI-MS [116]. 54 Figure 3-2 Reconstructed ion chromatograms of model protein separations using (A) C 4 and (B) C 18 columns. Each model protein is represented using its most intense m/z ion from the ESI protein envelope: m/z 893.7 for myoglobin, m/z 1332.9 for bovine serum albumin, m/z 825.4 for cytochrome c, and m/z 1245.7 for ribonuclease A. 55 In shotgun proteomics, Yates and co-workers [13,14] have substituted acetic acid with 0.02% HFBA for the analysis of a trypsin-digested sample of soluble proteins from S. cerevisiae using strong cation exchange chromatography coupled with RPLC. By comparing with an acetic acid buffer system, more than three times as many peptides were identified using HFBA in their work. Adding HFBA improved the dynamic range of the analysis and allowed for the acquisition of more low-abundance peptides. By using a C 18 column, the effect of ion-paring agent on intact protein separations was investigated by adding either 0.1% TFA (Fig. 1B) or 0.02% HFBA (Fig. 3-3) into the mobile phase. In contrast to the conclusion obtained from shotgun proteome studies [13,14], the use of 0.02% HFBA as ion-pairing agent resulted in significant deterioration of separation resolution among model proteins, particularly between bovine serum albumin and myoglobin. Further increase in HFBA concentration contributed to dramatic reduction in protein ion intensities measured by ESI-MS (data not shown). Effect of Column Temperature on Intact Protein Separations At high column temperatures, the mobile phase viscosity is reduced, and concomitantly, the diffusivity of the analyte is enhanced. More importantly, the sorption kinetics of the analyte is also accelerated with increasing temperature. Consequently, the column efficiency is expected to be higher at elevated column temperatures [117,118]. Thus, the effect of column temperature on intact protein separation performance was evaluated by raising the column temperature from 25 to 60 0 C using a column heater. By comparing with the results shown in Fig. 3-1B, the base peak chromatogram displayed in Fig. 3-4 not only demonstrated improved separation resolution and efficiency among 56 various protein conformers at high column temperature, but also presented strong protein ion intensities as the result of enhanced ESI prior to MS detection. Due to the limitation on MS scan speed, no attempts were pursued in increasing the mobile phase flow rate for further enhancing the column efficiency and achieving high speed chromatography separations. Figure 3-3 Base peak chromatogram for illustrating the effect of ion-paring agent on nano-RPLC-ESI-MS separation of model proteins. C 18 column temperature: 25 0 C.; elution order: 1-ribonuclease A, 2-cytochrome c, 3- bovine serum albumin, and 4-myoglobin; mobile phase: a 30-min linear gradient from 10% to 65% acetonitrile (containing 0.02% HFBA) at a flow rate of 200 nL/min; sample loading: 100 femtomole for each model protein (1 ?L injection of 0.1 ?M protein solution). 57 Figure 3-4 Base peak chromatogram for illustrating the effect of column temperature on nano-RPLC-ESI-MS separation of model proteins. C 18 column temperature: 60 0 C.; elution order: 1-ribonuclease A, 2-cytochrome c, 3- bovine serum albumin, and 4-myoglobin; mobile phase: a 30-min linear gradient from 10% to 65% acetonitrile (containing 0.1% TFA) at a flow rate of 200 nL/min; sample loading: 100 femtomole for each model protein (1 ?L injection of 0.1 ?M protein solution). 58 Nano-RPLC-ESI-MS Analysis of Native and Denatured/Reduced/Alkylated Yeast Cell Lysates In addition to the characterization of model proteins, the soluble fraction of intact proteins from S. cerevisiae in the native state was analyzed using nano-RPLC- ESI-MS in this study. As shown in Fig. 3-5A, the peak width (4) for a protein eluting from the column is as small as 10 s which corresponds to a peak capacity of 360 over a gradient run time of 60 min. Further enhancement in the peak capacity can be realized by slowing the solvent gradient in nano-RPLC and increasing the column length at the expense of analysis time [24]. Still, the peak capacity of any single dimension separations is insufficient for processing the number of proteins that expected from even a eukaryotic organism such as S. cerevisiae proteome (> 6,000 proteins). It has been estimated that up to 10,000 proteins may be commonly present in human serum, most of which would be present at very low relative abundance [119]. The large variation of protein relative abundances having potential biological significance in mammalian systems (> 6-9 orders of magnitude) also presents a major analytical challenge for proteomics. Thus, the use of multidimensional protein separations, including combinations of isoelectric focusing [42-44,120] or polyacrylamide gel electrophoresis [22,23] with RPLC, not only contributes to reduction in protein complexity prior to MS analysis, but also increases the number of proteins identified due to better use of the MS dynamic range and reduced discrimination during ionization. 59 Figure 3-5 Base peak chromatograms for the soluble fraction of yeast cell lysates in the (A) native and (B) denatured states using nano-RPLC-ESI- MS. C 18 column temperature: 60 0 C.; mobile phase: a 60-min linear gradient from 10% to 65% acetonitrile (containing 0.1% TFA) at a flow rate of 200 nL/min; sample loading: 2 ?g of total yeast protein (1 ?L injection of 2 mg/mL yeast protein solution) spiked with ribonuclease A. Eluted ribonuclease A peaks are marked with * and the mass spectra taken from the average of scans under the peaks are shown as insets. 60 Top-down proteome approaches offer excellent molecular level information for the intact proteins, but currently require the use of FTICR-MS/MS for obtaining protein-sequencing measurements [20-23]. Furthermore, top-down technologies are also limited by the relative scarcity of bioinformatic tools to efficiently analyze this type of data, although these are under development [21]. Thus, on-line proteolytic digestion of eluted proteins or off-line fraction collection of resolved proteins followed by subsequent digestion [42-45] can greatly facilitate protein identification through peptide mass mapping or peptide sequences obtained from tandem MS using conventional mass spectrometers. Instead of spreading proteolytic peptides over the entire multidimensional separation in the bottom-up approach, the peptides and their sequences can be directly linked with the corresponding proteins in this combined top- down/bottom-up methodology, possibly resulting in increased peptide sequence coverage of identified proteins. In order to implement the combined top-down/bottom-up proteome analysis in our future work, we therefore investigated potential differences in chromatography separation and ESI-MS measurement of yeast intact proteins present in the native versus denatured states. This is because these denatured, reduced, and alkylated proteins eluted from nano-RPLC can be directed toward to a miniaturized trypsin membrane reactor [121] for performing on-line and real time proteolytic digestion prior to MS analysis. The chromatography separation results obtained from the same yeast protein sample which was further denatured, reduced, and alkylated (Fig. 3-5B) were compared with the analysis using yeast proteins in the native state (Fig. 3-5A). In general, there were no significant differences in the separation efficiency and resolution 61 of native versus denatured proteins using nano-RPLC. The elution time of denatured, reduced, and alkylated proteins was slightly earlier than that of corresponding native proteins. This is evidenced by comparing the elution times of ribonuclease A (labeled by * in Figs. 3-5A and 3-5B) which was spiked into the yeast protein samples. By comparing with the ESI protein envelope of native ribonuclease A (inset in Fig. 3- 5A), the mass spectrum of denatured and alkylated ribonuclease A (inset in Fig. 3-5B) not only confirmed complete alkylation, but also displayed an increase in its average charge state as the result of denaturation process. The deconvoluted masses of native and alkylated ribonuclease A were measured as 13,690.7 and 14,147.5 daltons, respectively. The alkylation of each cysteine residue results in addition mass of 57.0 daltons. Thus, the difference in protein mass between native and alkylated ribonuclease A corresponds to the alkylation of all eight cysteines present in ribonuclease A. Furthermore, the protein denaturation process often results in improved MS intensity as the denatured state of a protein exhibits an open conformation and accepts more protons than the native state. 62 3.4 CONCLUSION For top-down proteomics, total peak capacity improvements in protein separations will clearly contribute to increased number of proteins identified due to better use of the MS dynamic range and reduced discrimination during ionization. Thus, the effects of various chromatography conditions, including alkyl chain length in the stationary phase, capillary column temperature, and ion-pairing agent, on the resolution of intact proteins are examined in this study using nano-RPLC-ESI-MS. Optimal chromatography conditions include the use of C 18 column heated at 60 0 C and the addition of trifluoroacetic acid instead of heptafluorobutyric acid as the ion-paring agent in the mobile phase. We further investigate potential differences in chromatography separation and ESI measurement of yeast intact proteins as the result of the protein denaturation process. Under optimized chromatography conditions, there are no significant differences in the separation performance of yeast cell lysates present in the native versus denatured states. Denatured yeast proteins resolved and eluted from nano-RPLC can be subjected to proteolytic digestion in an on- or off-line approach to provide improved protein sequence coverage toward protein identification in a combined top-down/bottom-up proteome platform. Due to the complexity of typical cell lysates, protein digests related to individual protein peaks resolved and eluted from nano-RPLC may require further separations prior to MS analysis. In this regard, the capillary format of the nanoscale trypsin membrane reactor recently developed in our laboratory [121] lends itself to further peptide concentration and separation using high speed capillary isotachophoresis/capillary zone electrophoresis prior to ESI-MS. 63 3.5 ACKNOWLEDGEMENT Support for this work by the National Cancer Institute (CA107988) is gratefully acknowledged. 64 CHAPTER 4 INTEGRATED CAPILLARY ISOELECTRIC FOCUSING/NANO- REVERSED PHASE LIQUID CHROMATOGRAPHY COUPLED WITH ESI-MS FOR CHARACTERIZATION OF INTACT YEAST PROTEINS Yueju Wang, Brian M. Balgley, Paul A. Rudnick, Don L. DeVoe, Cheng S. Lee Journal of Proteome Research 4, 36-42 (2005) 4.1 INTRODUCTION The vast number of proteins present in the proteome of a typical organism requires that separations be performed on the mixture prior to introduction into a mass spectrometer for protein identification and quantification. While direct analysis of peptide mixtures obtained from the digestion of complex cell lysates in current shotgun (bottom- up) proteome technologies [13-18,122,123] offers greater potential for the analysis of low abundance proteins than 2-D PAGE, bottom-up approaches provide very limited molecular information about the intact proteins, particularly towards the detection of PTMs [19]. Such modifications may be overlooked in analyses using peptide-based approaches, where only a fraction of the total theoretical peptide population of a given protein may be identified. For example, the average number of unique peptides leading to each protein identification has been reported to be around 3.73-5.01 for the yeast proteome analysis together with 33.9%-42.1% of yeast proteins identified by only a single peptide 65 [13,14,18]. To enhance the ability of shotgun proteome approaches toward the identification of PTMs, Yates and co-workers have combined the proteolytic cleavage activities of different enzymes to generate overlapping peptides [124]. In such experiments, a protein mixture is digested using three different enzymes: trypsin that cleaves in a site-specific manner and two others (subtilisin and elastase) that cleave nonspecifically. The use of multiple enzymes for increased sequence coverage of proteins was further demonstrated by Choudhary et al. [125] for the analysis of human plasma. In contrast, the top-down proteome techniques [20-23,126,127], in which intact proteins rather than peptides are measured, are advantageous for the detection of PTMs. Furthermore, top-down approaches to protein sequence analysis using tandem mass spectrometry (MS n ) may allow complete protein characterization far more efficiently than shotgun proteome technologies using protein digests. Realizing the potential of top-down approaches, however, requires that the processing and separation of intact proteins be brought to a similar level as those routinely achieved in shotgun proteomics. Single dimension protein separations, including isoelectric focusing gel [29], CIEF [30,31], CZE [20], and RPLC [32,33], have been employed for processing protein mixtures prior to MS analysis. However, the use of only a single separation dimension may not provide sufficient peak capacity for the resolution of complex mixtures, putting significant constraints on the detection sensitivity and dynamic range of the MS. Recent developments in multidimensional protein separations have been based on off-line combinations of preparative scale isoelectric focusing [42-44] or gel 66 electrophoresis [22,23,126] with RPLC for processing complex protein mixtures. Lubman and co-workers have performed isoelectric focusing in a Rotofor using approximately 10 mg of protein from whole cell lysates over a 5 hr period [42-44]. They have also employed an anion exchange column to achieve protein fractionation in a chromatofocusing mode [45] over a pH range of 4-7 due to the difficulty in obtaining reproducible, wide range pH-gradients. Additionally, acid-labile surfactant-based preparative polyacrylamide gel electrophoresis was utilized by Kelleher and co-workers for processing 1-300 [22,23,126] mg of total yeast proteins. The collected protein fractions from either isoelectric focusing or gel electrophoresis were further resolved using RPLC as the second separation dimension prior to MS analysis. As demonstrated in our previous studies [52,56], the key to establishing ultrasensitive proteome analysis is attributed to high analyte concentrations in small peak volumes as the result of electrokinetic focusing/stacking and high-resolving multidimensional separation techniques, thereby effectively exploiting the dynamic range and detection sensitivity of MS. Building upon the experience in the development of CIEF-based shotgun proteome techniques [52-56], our research efforts in this work present the application of combined CIEF with nano-RPLC for concentrating and resolving intact proteins. The grouping of two highly resolving and completely orthogonal separation techniques greatly enhances the system peak capacity for analyzing complex protein mixtures while eliminating protein loss and dilution in an integrated and automated platform. Beyond the characterization of model proteins achieved by Zhou and Johnston [128], our results clearly illustrate the ability of CIEF/nano-RPLC coupled with ESI-MS to provide the detection of a large number of yeast protein envelopes and 67 deconvoluted molecular masses. Most significantly, all these measurements are carried out with a protein loading which is two to three orders of magnitude lower than those employed by the current top-down proteome separation techniques [22,23,42-45,126]. 68 4.2 EXPERIMENTAL SECTION Materials and Reagents Fused-silica capillaries (100 ?m i.d./365 ?m o.d. and 50 ?m i.d./365 ?m o.d.) were acquired from Polymicro Technologies (Phoenix, AZ). Acetic acid, ammonium hydroxide, DTT, and IAM were obtained from Sigma (St. Louis, MO). Acetonitrile, DNase, formic acid, glycerol, hydroxypropyl cellulose (average MW 100,000), magnesium chloride, thiourea, TFA, Tris, and urea were purchased from Fisher Scientific (Pittsburgh, PA). Pharmalyte 3-10 was acquired from Amersham Pharmacia Biotech (Uppsala, Sweden). All solutions were prepared using water purified by a Nanopure II system (Dubuque, IA) and further filtered with a 0.22 ?m membrane (Costar, Cambridge, MA). Soluble Fraction of Intact Proteins from S. cerevisiae The yeast cells (Sigma) were suspended in a buffer which consisted of 10 mM Tris (pH 8.0), 5 mM magnesium chloride, 0.1 mM DTT, and 10% glycerol. The cells were disrupted by sonication for the release of cellular proteins. After sonication, DNase was added to a final concentration of 50 ?g/mL for the cleavage and removal of nucleic acids. The soluble proteins were collected in the supernatant by centrifugation at 20,000g for 10 min. The protein solution was then desalted using a regenerated cellulose membrane (Millipore, Bedford, MA) with a 5,000 Da molecular weight cutoff. Yeast cytosolic proteins were denatured and reduced in a 10 mM Tris buffer containing 8 M urea and 100 mM DTT for 2 hr at 37 0 C under a nitrogen atmosphere. Proteins were alkylated by adding excess IAM to a final concentration of 69 250 mM and the reaction was allowed to proceed for 30 min at room temperature in the dark. A PD-10 size exclusion column (Amersham Pharmacia Biotech) was employed for buffer exchange and proteins were eluted in a solution containing 10 mM Tris. The total protein concentration was determined using the Bradford method (Bio-Rad, Richmond, CA) and was around 2 mg/mL. Integrated CIEF/Nano-RPLC Multidimensional Protein Concentration/Separation Platform An on-line combination of CIEF with nano-RPLC has been developed and described in detail in previous work [52] and was employed for systematically resolving complex peptide mixtures based on their differences in pI and hydrophobicity. To perform multidimensional protein separations, a 60-cm CIEF capillary (100 ?m i.d./365 ?m o.d.) was coated with hydroxypropyl cellulose for the elimination of electroosmotic flow and protein adsorption onto the capillary wall [96]. The capillary was initially filled with a solution containing 1% pharmalyte 3-10, 4 M urea, 2 M thiourea, and 2 mg/mL intact proteins obtained from the soluble fraction of yeast cell lysates. There were no column performance changes for more than 20 runs of CIEF separations using the coated capillary. The stability of hydroxypropyl coated capillaries has been further supported by the work of Shen and Smith [96]. Solutions of 0.5% ammonium hydroxide at pH 10.5 and 0.1 M acetic acid at pH 2.5 were employed as the catholyte and the anolyte, respectively. Focusing was performed at an electric field strength of 300 V/cm over the entire CIEF capillary. The current decreased continuously as the result of protein focusing. Once the current reduced 70 to ~10% of the original value, usually within 30 min, the focusing was considered to be complete. The focused proteins were sequentially and hydrodynamically loaded into an injection loop in a 6-port microinjection valve (Upchurch Scientific, Oak Harbor, WA). The loaded proteins were then injected into a C 18 reversed-phase trap column using a Harvard Apparatus 22 syringe pump (Holliston, MA) through a 6-port microselection valve (Upchurch Scientific). Repeated protein loadings and injections into various trap columns were automated and controlled using LabView (National Instruments, Austin, TX) until the entire CIEF capillary content was sampled into 9 unique fractions. No significant band broadening in the CIEF capillary was anticipated over the entire protein loading and injection process for a period of approximately 10 min based on limited protein diffusion. Trap columns were prepared ?in-house?. The effluent end of a 8-cm-long fused-silica capillary (100 ?m i.d./365 ?m o.d.) was connected to an inline microfilter assembly (Upchurch Scientific). The C 18 -bonded particles (5-?m diameter, 300-? pores, Phenomenex, Torrance, CA) in methanol were introduced into the capillary by gradually increasing the pressure from 100 to 2,000 psi using an Agilent 1100 capillary LC pump (Avondale, PA). The capillary packed with 3 cm of C 18 -bonded particles was left under pressure for 10 hr and then depressurized overnight. Due to the highly charged and hydrophilic nature of carrier ampholytes (Pharmalyte 3-10) employed for the generation of a pH gradient during the CIEF step, ampholytes were eluted from the trap columns into a waste reservoir prior to the nano- RPLC separations using a 0.1% TFA solution. An Agilent 1100 capillary LC pump was then employed to generate a 40-min linear gradient from 10% to 65% acetonitrile 71 (containing 0.1% TFA and 0.3% formic acid) at a flow rate of 200 nL/min. Through the use of a second 6-port microselection valve (Upchurch Scientific), the mobile phase was delivered into the individual trap column, followed by a 13-cm-long capillary column (50 ?m i.d. x 365 ?m o.d.) packed with 5-?m porous C 18 reversed-phase particles. All 9 isoelectric focusing fractions collected in the trap columns were analyzed in sequence from acidic to basic pI and the eluants from nano-RPLC were monitored using a Micromass qTOF mass spectrometer (Manchester, United Kingdom). A microcross (Upchurch Scientific) containing a platinum electrode was employed to apply an ESI voltage of 1.8 kV and was placed in-line with and upstream of the chromatography column. Mass spectra were collected from 600 to 1900 m/z using a scan time of 1.0 s. Automated analysis of the nano-RPLC-ESI- MS data files were performed using Protein Trawler software (Bioanalyte, Portland, ME) [112,113]. Approximately 40-min of each nano-RPLC run was divided into 80 30-s slices. The mass spectra of these 30-s slices were summed and averaged, and Micromass MaxEnt1 was employed as the deconvolution algorithm over a mass range of 5-100 kDa. No baseline subtraction or smoothing was used, as these manipulations were empirically determined to interfere with protein mass deconvolution. Post-processing of the deconvoluted protein peaks was performed using routines provided with Protein Trawler. Briefly, peaks within 30 Da and occurring within 90-s were only included once and were considered to be the result of bleeding or band broadening of the same protein. Post- processing also included the elimination of 1/2 and 2X mass peaks which are common artifacts of the deconvolution algorithm 72 4.3 RESULTS AND DISCUSSION CIEF Separations of Intact Proteins from Soluble Fraction of Yeast Cell Lysates Preparative scale isoelectric focusing separations have been performed using a Rotofor cell containing a solution pH gradient [42-44] , micro anion exchange chromatography combined with pH gradient elution [45], and gel membranes containing the desired pHs [98,99,129,130] for processing mgs of protein samples obtained from cell lysates. By taking advantage of the large surface area to volume ratio in fused-silica capillaries for effectively dissipating joule heating at high electric fields, CIEF not only establishes a rapid and high resolution protein/peptide separation, but also affords a typical concentration factor of at least 100 times as the result of the focusing effect. Furthermore, CIEF provides a direct capillary interface for on-line combination with nano-RPLC in an integrated and multidimensional separation platform for resolving complex peptide and protein mixtures as demonstrated in our previous studies [52] and this work, respectively. As shown in Fig. 4-1, the CIEF separation performance of intact proteins from the soluble fraction of yeast cell lysates was initially evaluated by hydrodynamically mobilizing focused proteins passing a UV detector placed near the cathodic end of the capillary. Protein bandwidth after focusing was as small as 2.0 mm inside a 60-cm long CIEF capillary by applying electric field strength of 300 V/cm over a pH gradient from 3 to 10. This yielded to a sample concentration factor of ~300 and a baseline resolution (resolution, R s , of 1.5) of ~ 200 peaks. Furthermore, a 60-cm long capillary with a 100 ?m i.d. employed in this study offered a sample loading volume of ~4.8 ?L and a total protein loading of ~9.6 ?g using a 2 mg/mL yeast protein solution. Further enhancement 73 in sample loading can be achieved using the dynamic introduction and focusing approach demonstrated in our previous work [131]. Integrated CIEF/Nano-RPLC Separations of Intact Proteins from Yeast Cell Lysates Instead of using the ?stop and go? mode for on-line coupling of CIEF with capillary RPLC in the characterization of model proteins [128], a combination of computer controlled microinjection and microselection valves was utilized for automatically and reproducibly loading focused protein fractions into individual trap columns for the subsequent second dimension nano-RPLC analyses. As shown in Fig. 4- 2, the yeast proteins were systematically resolved based on their differences in pI and hydrophobicity using the combined CIEF/nano-RPLC separations in an integrated platform. The peak width for a protein eluting from the chromatography column (Fig. 4-2) was as small as 10 s which corresponds to a peak capacity of 160 over a gradient run time of 40 min. Further improvement in the peak capacity can be realized by slowing the solvent gradient in nano-RPLC and increasing the column length [24]. Because the separation mechanisms in CIEF and nano-RPLC are completely orthogonal, the overall peak capacity of multidimensional CIEF/nano-RPLC separations was estimated to be around 1,440 (9 fractions from CIEF x 160 from CRPLC) over a run time of approximately 6 hr. By acquiring and confidently deconvoluting 3-5 ESI protein envelopes (Fig. 4-3) over the elution of any single peak from nano-RPLC using qTOF- 74 MS, an overall system capacity of 4,320-7,200 was achieved in this study for the analysis of complex protein mixtures such as yeast cell lysates. 0.25 0.75 1.25 1.75 2.25 2.75 0 10 20 30 40 50 60 70 80 90 100 A b s or ba nc e ( m A u) Time (min) A b s or ba nc e ( m A u) Figure 4-1 CIEF-UV Analysis of intact proteins in the soluble fraction obtained from S. cerevisiae cell lysates. Capillary: hydroxypropyl cellulose coating, 60 cm x 100 ?m i.d. x 365 ?m o.d.; anolyte: 0.1 M acetic acid at pH 2.5; catholyte: 0.5% w/w ammonium hydroxide at pH 10.5; electric field strength: 300 V/cm; hydrodynamic mobilization; detection: UV absorbance at 280 nm, 7 cm from cathodic end. 75 Figure 4-2 Base peak chromatograms of a representative CIEF/nano-RPLC multidimensional separation of 9.6 ?g of yeast intact proteins obtained from the soluble fraction of cell lysates. Each number represents the sequence of CIEF fractions further analyzed by nano-RPLC from acidic to basic pHs. 76 Figure 4-3 The mass spectrum of a chromatography peak eluted at 35.7 min for the nano-RPLC separation of the second CIEF fraction. The inset presents deconvoluted protein masses which are labeled together with the corresponding protein envelopes using *, +, and #, respectively. 77 Reproducibility of protein separation and identification using the combined CIEF/nano-RPLC-ESI- MS approach was examined by performing multiple runs of identical yeast protein samples. For two analyses performed on consecutive days, the elution times of the same proteins in CRPLC differed by less than 0.3 min (data not shown). The elution times were slightly different, the shifts, however, were consistent across the analysis. The slight variation in elution times was mainly contributed by the difficulty in generating the same nanoflow rate using the current capillary LC pump equipped with an external flow splitter. The intrinsic high resolution of CIEF allows the number of protein fractions sampled in the first separation dimension to be further increased. The excellent reproducibility of CIEF separation, together with the use of trap columns for ?parking? the CIEF fractions in an automated platform, enables user discretion as to which fractions are to be analyzed in the off-line approach, and interesting fractions may be revisited (reanalyzed) or repeatedly accumulated for identification of extremely low abundance proteins. Further enhancement in the overall system capacity can be realized by increasing the number of CIEF fractions and slowing the solvent gradient in nano-RPLC at the expense of analysis time. To significantly reduce the overall run time, the ability to deposit eluted peptides/proteins onto MALDI target for subsequent MS analysis offers a promising platform for high-throughput proteome studies using a multiplexed LC system [132]. Recently, Ericson and co-workers have developed an automated non-contact deposition interface by employing a pulsed electric field for transferring the eluants from multiple parallel columns directly onto MALDI targets [133]. 78 ESI-MS Analysis of Intact Proteins Eluted from CIEF/Nano-RPLC Multidimensional Protein Separations The Protein Trawler program was utilized to automatically sum all data within a specified time interval, deconvolute multiply charged ions, carry out a threshold selection, eliminate deconvolution artifacts, and report protein mass, intensity, and retention time in a text file. The program repeated this process across sequential portions of the chromatogram of each nano-RPLC-ESI- MS run. As a result, a total of 534 distinct protein masses between 5 and 70 kDa were identified from the CIEF/nano-RPLC-ESI- MS analysis of intact proteins obtained from the soluble fraction of yeast cell lysates. A 2-D map of identified protein masses is displayed in Fig. 4-4 with the estimated pI ranges for each CIEF fraction. By using 1% Pharmalyte 3-10, the CIEF separation was able to cover a wide pH range of 3.3-9.6. The pI range analyzed in this study was comparable to those reported using a Rotofor cell containing a solution pH gradient [42-44] and gel membranes containing immobilized pHs [98,99,129,130], but significantly wider than that obtained from micro anion exchange chromatography combined with pH gradient elution [45]. However, very basic proteins with pIs equal to or greater than 10 may not be resolved or could be lost to the catholyte using the currently available carrier ampholytes. The competitive advantages of CIEF/nano-RPLC protein separations are mostly attributed to the high resolving power and analyte concentration effect in CIEF together with the elimination of analyte loss and dilution in an automated and integrated platform. The amount of intact proteins employed for performing yeast proteome analysis was around 9.6 ?g (2 mg/mL x 4.8 ?L of capillary volume in CIEF) which is two to three 79 orders of magnitude less than those utilized in current 2-D PAGE and top-down proteome techniques [22,23,42-45,126]. Instead of using significantly higher amounts of sample materials and additional sample fractionation procedures, the combination of analyte focusing/concentration with two highly resolving and orthogonal separation mechanisms in an integrated platform significantly enhances both the dynamic range and the sensitivity of MS toward the proteome analysis. A database dump file ?protein_properties.tab? containing computed molecular masses and pIs of translated yeast open reading frames (ORFs) was downloaded from the Saccharomyces Genome Database at Stanford University. By excluding ORFs with a ?dubious? classification, a total of 5,792 ?characterized? and ?uncharacterized? gene products were used as the constituents of the predicted yeast proteome. The ratio of the number of deconvoluted protein masses to the number of predicted proteins in each molecular mass region was summarized in Fig. 4-5 from 5 to 70 kDa. Approximately 74% of predicted yeast proteins exhibit molecular masses within the range of 5-70 kDa. Due to the discrimination of the ESI process against MS detection of medium to high molecular weight proteins, the percentage of yeast proteome coverage was around 14%-58% in the molecular mass range of 5-30 kDa and decreased significantly with increasing molecular mass from 30 to 70 kDa. Such bias against high molecular mass proteins is in agreement with those reported using top-down protein identification and sequence measurements [22,23,42-45,126]. 80 Figure 4-4 2-D map of deconvoluted protein masses versus pI within each CIEF fraction for the analysis of yeast cell lysates using CIEF/nano-RPLC-ESI- MS. The logarithm of protein intensity is represented in gray scale on the map. 81 Improvements in protein detection can be achieved by enhancements in the deconvolution process for the ESI-multiply charged envelopes and employment of ultrahigh resolution and sensitivity of Fourier transform ion cyclotron resonance (FTICR)-MS. In comparison with shotgun proteomics [13-18,122,123], the lack of effective ESI of intact proteins may still adversely impact the ability to perform comprehensive proteome analysis using top-down techniques [20-23,126,127], particularly in the identification of low abundance proteins. As reported by Meng and co- workers [23], most of the 117 yeast gene products identified and characterized today are highly abundant proteins in the 5-39 kDa range. Figure 4-5 The ratio of the number of deconvoluted protein masses to the number of predicted yeast proteins in individual molecular mass regions from 5 to 70 kDa. 82 4.4 CONCLUSION As an automated and integrated approach, the on-line combination of CIEF with nano-RPLC offers analyte focusing for concentrating dilute protein samples of biological origin while providing excellent resolving power for the characterization of complex protein mixtures based on differences in pI and hydrophobicity. By obtaining a peak capacity of 1,440 from combined CIEF/nano-RPLC separations and acquiring 3-5 ESI protein envelopes over the elution of any chromatography peak using qTOF-MS, an overall system capacity of 4,320-7,200 is achieved in this study for the analysis of intact proteins obtained from the soluble fraction of S. cerevisiae. The intrinsic high resolution of CIEF allows the number of fractions sampled in the first separation dimension to be further increased. More CIEF fractions can be obtained by increasing the number of microselection valves and trap columns, or by employing microselection valves with a higher number of ports. By using only the soluble fraction of yeast cell lysates, a total of 534 distinct protein masses were identified over a wide protein mass range of 5-70 kDa, requiring a protein loading of less than 10 ?g. This protein loading is two to three orders of magnitude less than those utilized in current 2-D PAGE and top-down proteome techniques [22,23,42-45,126]. Future work includes directly coupling of CIEF/nano- RPLC separations with a newly developed nanoscale trypsin membrane reactor [121] for enabling real-time and effective digestion of resolved proteins in a combined top- down/bottom-up proteome analysis. Instead of spreading proteolytic peptides over the entire multidimensional separation as in shotgun proteomics, the proposed top- down/bottom-up proteome technology will allow direct correlation of the peptides and 83 their sequences with the corresponding proteins and measured protein masses, and will greatly facilitate the characterization of proteins containing PTMs. 84 4.5 ACKNOWLEDGEMENT Support for this work by the National Cancer Institute (CA107988 and CA103086) is gratefully acknowledged. 85 CHAPTER 5 CONCLUSION The sequencing of several organisms? genomes, including the human?s one, has opened the way for the so-called postgenomic era, which is now routinely coined as ?proteomics?. The most basic task in proteomics remains the detection and identification of proteins from a biological sample, and the most traditional way to achieve this goal consists of protein separations performed by 2-D PAGE. Still, the 2-D PAGE-MS approach remains lacking in proteome coverage (for proteins having extreme isoelectric points or molecular masses as well as for membrane proteins), dynamic range, sensitivity, and throughput. Consequently, considerable efforts have been devoted to the development of non-gel-based proteome separation technologies in an effort to alleviate the shortcomings in 2-D PAGE while reserving the ability to resolve complex protein and peptide mixtures prior to mass spectrometry analysis. Thus, this dissertation first reviewed recent advances in capillary-based separation techniques, including capillary liquid chromatography and capillary electrophoresis, and combinations of multiples of these separation mechanisms. In comparison with 2D-PAGE, the capillary-based separation technologies offer the capabilities of system automation, high throughput analysis, and increased detection dynamic range, and are becoming effective front-end tools for MS-based proteome analysis. By transferring isoelectric focusing separation from gel to capillary format, it has been demonstrated that the focusing effect of CIEF not only contributes to high resolution protein/peptide separation, but also provides significant enhancement in 86 analyte concentration. Besides the analysis of tryptic peptides obtained from yeast cell lysates in our previous studies, CIEF-based multidimensional peptide separation platform was further developed and optimized in this work for enabling comprehensive and ultrasensitive characterization of protein profiles within limited tissue samples. In addition to establishing a micro-sample introduction technique, a combination of computer controlled microinjection and microselection valves was utilized for automatically and reproducibly fractionating pI-resolved peptides for the subsequent second dimension analyses. By using the combination of various carrier ampholytes, the separation range of CIEF has been extended to at least pI 12. The reduction of chromatography column inner diameter to as small as 50 ?m together with the increase in the number of CIEF fractions significantly enhance both the overall separation peak capacity and the dynamic range and detection sensitivity of MS critically needed for performing comprehensive proteome studies. In this study, protein profiles within small cell populations procured from glioblastoma multiforme tissues were analyzed using combined CIEF-nano-RPLC separations equipped with ESI-qTOF-MS. In comparison with strong cation exchange as the first separation dimension in current multidimensional chromatography system, CIEF not only exhibited higher separation resolution and less degree of peptide overlapping among fractions, but also allowed more effective usage of MS-based peptide identifications by providing an even distribution of doubly charged peptides over the entire pH gradient. Moreover, because of the high resolving power of CIEF, the number of peptide and protein identifications can be greatly increased by simply increasing the number of pI fractions instead of performing multiple proteome runs. The ability to mine 87 deep into the proteome of limited samples can therefore be realized without an accompanying increase in sample consumption. Realizing the shortcomings of limited protein sequence coverage and thus limited intact molecular information obtained from bottom-up (shotgun) approaches, research efforts have also been made toward the development of top-down proteome techniques. Top-down methods, in which intact proteins rather than peptides are measured, are advantageous for the analysis of protein modifications. Building upon the experience in the development of CIEF-based shotgun proteome technologies, this project further aimed to expand the applications of combined CIEF-nano-RPLC separations for the analysis of complex protein mixtures such as yeast cell lysates. As a first step toward the optimization of multidimensional protein separations, effects of various chromatography conditions, including alkyl chain length in the stationary phase, capillary column temperature, and ion-pairing agent, on the resolution of intact proteins have been studied using nano-RPLC-ESI- MS. Optimal chromatography conditions included the use of C 18 column heated at 60 0 C and the addition of trifluoroacetic acid instead of heptafluorobutyric acid as the ion-paring agent in the mobile phase. Under optimized chromatography conditions, there were no significant differences in the separation performance of yeast cell lysates present in the native versus denatured states. As one of research directions in future proteome studies, denatured proteins resolved and eluted from nano-RPLC can be subjected to proteolytic digestion in an on- or off-line approach to provide improved protein sequence coverage toward protein identification in a combined top-down/bottom-up proteome platform. 88 As an automated and integrated approach, the on-line combination of CIEF with nano-RPLC offers analyte focusing for concentrating dilute protein samples of biological origin while providing excellent resolving power for the characterization of complex protein mixtures based on differences in pI and hydrophobicity. A key feature of combined CIEF-nano-RPLC separations in an integrated platform includes the elimination of analyte loss and dilution as the result of many manually operated sample handling, protein separation, and transfer steps in the current top-down processes. Sample loss and dilution may adversely impact the ability to perform comprehensive proteome analysis, particularly toward the identification of low abundance proteins. By obtaining a peak capacity of 1,440 from combined CIEF/nano-RPLC separations and acquiring 3-5 ESI protein envelopes over the elution of any chromatography peak using qTOF-MS, an overall system capacity of 4,320-7,200 has been achieved in this study for the analysis of intact proteins obtained from the soluble fraction of yeast cell lysates. The CIEF-based multidimensional concentration/separation platform enabled the measurement of 534 distinct yeast protein masses over a mass range of 5-70 kDa, yet required a protein loading of only 9.6 ?g. This protein loading is two to three orders of magnitude less than those used in current 2-D PAGE and top-down proteome techniques, illustrating the potential usage of this proteome technology for the analysis of protein profiles within small cell populations or limited tissue samples. In conclusion, my research goal is to develop the novel bioanalytical technologies and tools that support comprehensive survey of proteins in cells and tissues, particular for the analysis of low abundance proteins. Instead of using significantly higher amounts of protein materials and additional sample fractionation procedures, the key to 89 establishing ultrasensitive proteome analysis is attributed to attain high analyte concentrations in small peak volumes as the result of electrokinetic focusing and high resolving multidimensional separation techniques in an integrated platform, thus enhancing the dynamic range and detection sensitivity of MS measurements. Future work includes the investigation of combined top-down and bottom-up approaches in order to leverage the unique capabilities provided by both approaches in an integrated platform. The integrated top-down/bottom-up proteome technology is expected to significantly increase the peptide sequence coverage of identified proteins and greatly facilitate the analysis of protein modifications. Realizing the potential of integrated top-down/bottom- up proteome technology, however, requires the development of novel bioinformatics tools to allow direct correlation of the peptides and their sequences with the corresponding proteins and measured protein masses in a single proteome analysis. 90 91 APPENDIX Protein Number ID Description Mass pI Peptide Hits Distinct Peptides % Coverage 1 IPI00025363.1 GLIAL FIBRILLARY ACIDIC PROTEIN, ASTROCYTE. 49880 5.2 217 41 77.55 2 IPI00007752.1 TUBULIN BETA-2 CHAIN. 49831 4.52 179 22 72.13 3 IPI00022434.1 SERUM ALBUMIN PRECURSOR. 69367 6.21 175 39 65.35 4 IPI00031370.1 TUBULIN, BETA POLYPEPTIDE. 49953 4.52 174 21 68.31 5 IPI00160897.1 HYPOTHETICAL PROTEIN. 49586 4.51 173 21 71.4 6 IPI00220286.1 POLYUBIQUITIN UBC. 77039 7.94 172 6 65.11 7 IPI00021439.1 ACTIN, CYTOPLASMIC 1. 41737 5.15 171 20 63.47 8 IPI00021440.1 ACTIN, CYTOPLASMIC 2. 41793 5.16 170 20 63.47 9 IPI00013475.1 BETA TUBULIN (TUBULIN, BETA POLYPEPTIDE) (DJ40E16.7.1) (NOVEL PROTEIN SIMILAR TO TUBULIN BETA POLYPEPTIDE. 49907 4.52 167 21 68.31 10 IPI00142634.1 TUBULIN BETA-5 CHAIN. 49671 4.52 166 19 62.16 11 IPI00011654.1 TUBULIN BETA-1 CHAIN. 49759 4.49 160 17 53.15 12 IPI00180675.3 TUBULIN, ALPHA 3. 52312 4.82 155 25 59.02 13 IPI00328696.7 HEMOGLOBIN ALPHA CHAIN. 15126 9.09 149 12 95.74 14 IPI00387144.2 TUBULIN ALPHA-1 CHAIN. 50152 4.7 148 25 61.64 15 IPI00396304.1 TUBULIN, ALPHA, UBIQUITOUS. 50152 4.7 148 25 61.64 16 IPI00023598.1 TUBULIN BETA-5 CHAIN. 49631 4.54 146 19 64.86 17 IPI00218816.1 BETA GLOBIN. 15998 7.32 146 12 93.88 18 IPI00218343.3 TUBULIN ALPHA-6 CHAIN. 52631 5.13 145 23 50.74 19 IPI00179709.4 SPLICE ISOFORM 1 OF Q13748 TUBULIN ALPHA-2 CHAIN. 49960 4.74 134 19 48 20 IPI00375289.1 SIMILAR TO TUBULIN ALPHA-3/ALPHA-7 CHAIN (ALPHA-TUBULIN 3/7). 50839 4.74 134 19 47.06 21 IPI00334432.1 --none found in database-- 15396 7.9 128 8 73.76 22 IPI00257508.4 DIHYDROPYRIMIDINASE RELATED PROTEIN-2. 62294 6.33 126 24 66.96 23 IPI00013683.2 TUBULIN BETA-4 CHAIN. 50433 4.57 122 15 47.11 24 IPI00152453.1 HYPOTHETICAL PROTEIN. 88382 5.69 120 14 23.21 25 IPI00384697.1 SIMILAR TO ALPHA-FETOPROTEIN. 47360 6.29 120 24 58.99 26 IPI00216976.1 ALDOLASE C, FRUCTOSE-BISPHOSPHATE. 39456 6.86 119 23 75 27 IPI00015786.2 SPECTRIN ALPHA CHAIN, BRAIN. 284897 5.05 116 61 34.32 28 IPI00021428.1 ACTIN, ALPHA SKELETAL MUSCLE. 42051 5.05 116 12 31.3 29 IPI00023006.1 ACTIN, ALPHA CARDIAC. 42019 5.05 116 12 31.3 30 IPI00218345.1 SPLICE ISOFORM 2 OF Q13748 TUBULIN ALPHA-2 CHAIN. 46112 4.78 115 16 44.26 31 IPI00007750.1 TUBULIN ALPHA-4 CHAIN. 49924 4.69 113 22 55.13 32 IPI00003865.1 SPLICE ISOFORM 1 OF P11142 HEAT SHOCK COGNATE 71 KDA PROTEIN. 70898 5.16 112 26 43.96 33 IPI00328163.1 SIMILAR TO TUBULIN ALPHA 2. 37218 4.62 110 19 71.64 34 IPI00216773.3 SIMILAR TO SERUM ALBUMIN PRECURSOR. 45297 6.15 109 22 59.05 35 IPI00177441.4 SIMILAR TO TUBULIN ALPHA-3/ALPHA-7 CHAIN (ALPHA-TUBULIN 3/7). 49859 4.77 106 13 38.89 36 IPI00385560.1 ACTIN ALPHA 1 SKELETAL MUSCLE PROTEIN. 28151 5.96 104 10 37.01 37 IPI00008603.1 ACTIN, AORTIC SMOOTH MUSCLE. 42009 5.05 103 10 28.38 38 IPI00025416.1 ACTIN, GAMMA-ENTERIC SMOOTH MUSCLE. 41877 5.16 103 10 28.46 39 IPI00000816.1 14-3-3 PROTEIN EPSILON. 29174 4.36 100 18 70.2 40 IPI00154491.1 --none found in database-- 44980 6.71 100 6 62.41 41 IPI00215736.2 ALPHA ENOLASE. 47038 7.46 100 24 65.36 42 IPI00328602.3 HEAT SHOCK 90KDA PROTEIN 1, ALPHA. 84674 4.66 99 29 41.8 43 IPI00382950.1 BETA-GLOBIN GENE FROM A THALASSEMIA PATIENT. 18931 6.78 99 10 65.14 44 IPI00383815.1 HYPOTHETICAL PROTEIN. 36299 5.52 96 21 56.78 45 IPI00037070.1 SPLICE ISOFORM 2 OF P11142 HEAT SHOCK COGNATE 71 KDA PROTEIN. 53921 5.8 95 21 46.68 46 IPI00328347.1 PYRUVATE KINASE, M2 ISOZYME. 57783 7.93 95 29 69.81 47 IPI00022977.1 CREATINE KINASE, B CHAIN. 42644 5.3 94 22 71.65 92 48 IPI00383237.1 PYRUVATE KINASE, M1 ISOZYME. 58168 7.93 93 28 66.23 49 IPI00387164.1 HYPOTHETICAL PROTEIN FLJ32377. 43649 6.22 93 6 61.86 50 IPI00180818.2 FRUCTOSE-BISPHOSPHATE ALDOLASE A. 39289 8.2 89 17 61.98 51 IPI00395757.1 ALDOLASE A. 39420 8.2 89 17 61.81 52 IPI00219018.1 GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE. 36053 8.73 88 16 58.21 53 IPI00021263.1 14-3-3 PROTEIN ZETA/DELTA. 27745 4.43 86 16 71.02 54 IPI00220644.5 PYRUVATE KINASE 3 ISOFORM 2. 58293 7.78 86 27 62.66 55 IPI00010728.3 MICROTUBULE-ASSOCIATED PROTEIN 2 ISOFORM 3. 202759 4.59 85 41 33.21 56 IPI00003842.1 SPLICE ISOFORM MAP2B OF P11137 MICROTUBULE-ASSOCIATED PROTEIN 2. 199611 4.55 83 40 33.17 57 IPI00334775.1 HYPOTHETICAL PROTEIN. 84843 5.01 82 24 35.41 58 IPI00034283.1 SIMILAR TO TUBULIN, BETA, 4. 49857 4.51 81 11 33.18 59 IPI00166768.1 HYPOTHETICAL PROTEIN. 36649 8.02 81 14 41.54 60 IPI00029111.1 DIHYDROPYRIMIDINASE RELATED PROTEIN-3. 61963 6.45 77 20 51.05 61 IPI00216005.3 TUBULIN ALPHA-8 CHAIN. 52591 4.91 75 13 32.63 62 IPI00180776.1 --none found in database-- 27742 4.36 74 13 54.29 63 IPI00216318.1 TYROSINE 3-MONOOXYGENASE/TRYPTOPHAN 5-MONOOXYGENASE ACTIVATION PROTEIN, BETA POLYPEPTIDE. 28082 4.47 74 14 66.26 64 IPI00024067.1 CLATHRIN HEAVY CHAIN 1. 191615 5.42 73 28 22.93 65 IPI00383331.1 --none found in database-- 15921 8.27 70 4 34.25 66 IPI00216171.1 ENOLASE 2. 47269 4.65 67 16 58.99 67 IPI00021369.1 ALPHA CRYSTALLIN B CHAIN. 20159 7.38 65 14 80.57 68 IPI00169383.1 PHOSPHOGLYCERETE KINASE 1. 44615 8.27 65 18 54.68 69 IPI00295540.1 PHOSPHOGLYCERATE KINASE 1. 44597 8.27 65 18 54.68 70 IPI00220642.1 TYROSINE 3-MONOOXYGENASE/TRYPTOPHAN 5-MONOOXYGENASE ACTIVATION PROTEIN, GAMMA POLYPEPTIDE. 28303 4.52 64 15 63.97 71 IPI00006664.4 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A. 17881 7.97 62 14 82.32 72 IPI00010154.1 RAB GDP DISSOCIATION INHIBITOR ALPHA. 50583 4.75 62 20 57.49 73 IPI00012011.1 COFILIN, NON-MUSCLE ISOFORM. 18502 8.29 60 12 72.89 74 IPI00245171.3 HEMOGLOBIN DELTA CHAIN. 19496 8.24 60 9 57.06 75 IPI00021716.1 TRANSKETOLASE. 67878 7.73 59 17 40.45 76 IPI00328807.3 TRIOSEPHOSPHATE ISOMERASE. 26538 6.91 59 16 77.42 77 IPI00306589.1 UBIQUITIN B. 25762 7.6 58 6 66.38 78 IPI00333602.1 --none found in database-- 49640 4.45 58 8 21.27 79 IPI00384875.1 MUTANT BETA-GLOBIN. 9689 8.52 58 5 66.29 80 IPI00016801.1 GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL PRECURSOR. 61398 7.91 56 20 44.62 81 IPI00018146.1 14-3-3 PROTEIN TAU. 27764 4.41 56 14 48.98 82 IPI00335160.1 --none found in database-- 49595 4.63 56 7 15.16 83 IPI00219217.1 LACTATE DEHYDROGENASE B. 36638 5.93 55 14 41.02 84 IPI00292496.1 BETA-TUBULIN 4Q. 49776 4.52 55 7 15.09 85 IPI00382845.1 --none found in database-- 18197 7.97 55 13 70.06 86 IPI00382470.1 HSP89-ALPHA-DELTA-N. 63252 4.75 54 20 40.63 87 IPI00182840.2 SIMILAR TO BETA-TUBULIN 4Q. 71234 5.13 53 6 9.09 88 IPI00258879.2 SIMILAR TO BETA ACTIN. 41661 5.56 52 6 13.1 89 IPI00027350.1 PEROXIREDOXIN 2. 21892 5.76 51 8 33.33 90 IPI00174849.2 --none found in database-- 48278 4.73 51 6 12.01 91 IPI00374080.1 SIMILAR TO PEPTIDYLPROLYL ISOMERASE A (CYCLOPHILIN A). 20754 6.36 51 11 55.56 92 IPI00375400.1 PEROXIREDOXIN 2 ISOFORM B. 15989 6.53 51 8 44.9 93 IPI00017855.1 ACONITATE HYDRATASE, MITOCHONDRIAL PRECURSOR. 85425 7.65 50 19 34.23 94 IPI00385209.1 --none found in database-- 90518 8.19 50 19 32.25 95 IPI00374165.1 SIMILAR TO POTE PROTEIN. 116971 6.69 46 9 8.96 96 IPI00385600.1 --none found in database-- 69976 7.22 46 17 36.16 97 IPI00219446.1 PROSTATIC BINDING PROTEIN. 21057 7.65 44 12 83.42 98 IPI00384084.1 --none found in database-- 15980 8.72 44 4 31.51 99 IPI00385497.1 --none found in database-- 18522 9.04 44 11 65.12 93 100 IPI00005614.2 SPLICE ISOFORM LONG OF Q01082 SPECTRIN BETA CHAIN, BRAIN 1. 275518 5.28 43 30 17.5 101 IPI00248359.2 SIMILAR TO POTE PROTEIN. 108369 6.84 42 7 7.08 102 IPI00385244.1 PHOSPHOGLYCERATE MUTASE 1 (BRAIN). 28804 7.22 42 13 70.87 103 IPI00291006.1 MALATE DEHYDROGENASE, MITOCHONDRIAL PRECURSOR. 35531 8.9 41 13 52.07 104 IPI00010182.1 SPLICE ISOFORM A 1 OF P07108 ACYL-COA-BINDING PROTEIN. 9913 6.54 40 6 73.26 105 IPI00216319.1 TYROSINE 3/TRYPTOPHAN 5 -MONOOXYGENASE ACTIVATION PROTEIN, ETA POLYPEPTIDE. 28219 4.47 40 8 32.52 106 IPI00027146.1 GLUTAMATE DEHYDROGENASE 2, MITOCHONDRIAL PRECURSOR. 61434 8.67 38 14 25.27 107 IPI00031461.1 RAB GDP DISSOCIATION INHIBITOR BETA. 50663 6.39 38 10 25.84 108 IPI00218836.1 SPLICE ISOFORM 2 OF P07108 ACYL-COA-BINDING PROTEIN. 11793 5.24 38 5 53.85 109 IPI00383071.1 --none found in database-- 26943 8.21 38 9 33.33 110 IPI00384026.1 HUMAN FULL-LENGTH CDNA 5-PRIME END OF CLONE CS0DN005YI08 OF ADULT BRAIN OF HOMO SAPIENS. 29031 4.84 38 7 24.43 111 IPI00182680.3 SIMILAR TO ALPHA-TUBULIN. 37407 4.53 37 9 22.94 112 IPI00003269.1 SIMILAR TO CYTOPLASMIC BETA-ACTIN. 42003 5.29 36 4 11.17 113 IPI00007702.1 HEAT SHOCK-RELATED 70 KDA PROTEIN 2. 70021 5.42 36 10 15.02 114 IPI00018511.1 TUBULIN BETA-4Q CHAIN. 48435 4.91 36 5 10.14 115 IPI00027388.3 --none found in database-- 17989 7.51 36 9 44.17 116 IPI00160552.1 TENASCIN-R. 149548 4.44 36 15 15.39 117 IPI00303476.1 ATP SYNTHASE BETA CHAIN, MITOCHONDRIAL PRECURSOR. 56560 5.07 36 14 44.23 118 IPI00328230.1 SPLICE ISOFORM SHORT OF Q01082 SPECTRIN BETA CHAIN, BRAIN 1. 253113 5.16 36 27 17.02 119 IPI00374162.1 SIMILAR TO POTE PROTEIN. 116972 6.99 36 6 5.01 120 IPI00376456.1 SIMILAR TO FKSG30. 60497 5.62 36 6 9.74 121 IPI00013890.1 14-3-3 PROTEIN SIGMA. 27774 4.39 35 4 12.5 122 IPI00025447.1 ELONGATION FACTOR 1-ALPHA 1. 50141 9.5 35 8 21.21 123 IPI00219524.2 SIMILAR TO PHOSPHOGLYCERATE MUTASE 1 (PHOSPHOGLYCERATE MUTASE ISOZYME B) (PGAM-B) (BPG-DEPENDENT PGAM 1). 22850 6.04 35 11 75.25 124 IPI00333015.1 BETA-SPECTRIN 2 ISOFORM 2. 251419 5.25 35 26 16.47 125 IPI00386513.1 SIMILAR TO STRATIFIN. 24336 4.47 35 4 14.35 126 IPI00216312.1 VIMENTIN. 53686 4.77 34 17 40.99 127 IPI00307063.1 TRUNCATED BETA-GLOBIN. 6542 9.37 34 3 45.76 128 IPI00184899.4 DIHYDROPYRIMIDINASE RELATED PROTEIN-1. 62184 7.03 33 9 23.95 129 IPI00329351.3 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL PRECURSOR. 61213 5.55 33 14 35.48 130 IPI00006510.1 TUBB1 HUMAN BETA TUBULIN 1, CLASS VI (DJ543J19.4) (BETA TUBULIN 1, CLASS VI. 50327 4.82 32 4 6.43 131 IPI00299399.3 S100 CALCIUM-BINDING PROTEIN, BETA. 10713 4.25 32 3 40.22 132 IPI00018352.1 UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L1. 24824 5.18 31 8 55.61 133 IPI00387176.1 HYPOTHETICAL PROTEIN FLJ32204. 47488 4.72 31 15 39.02 134 IPI00026119.2 UBIQUITIN-ACTIVATING ENZYME E1. 117849 5.5 30 17 25.61 135 IPI00219301.3 MYRISTOYLATED ALANINE-RICH PROTEIN KINASE C SUBSTRATE. 31545 4.13 30 9 35.24 136 IPI00298547.1 RNA-BINDING PROTEIN REGULATORY SUBUNIT. 19891 6.78 30 11 66.67 137 IPI00335118.1 --none found in database-- 40424 5.23 30 8 21.53 138 IPI00004358.2 GLYCOGEN PHOSPHORYLASE, BRAIN FORM. 96696 6.85 28 15 22.06 139 IPI00008868.3 MICROTUBULE-ASSOCIATED PROTEIN 1B (MAP 1B) [Contains: MAP1 LIGHT CHAIN LC1]. 270620 4.44 28 20 12.56 140 IPI00163249.3 SIMILAR TO HEAT SHOCK COGNATE 71 KDA PROTEIN. 63392 5.78 28 8 13.24 141 IPI00220483.1 SPLICE ISOFORM B1 OF P22626 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS A2/B1. 43349 9.72 28 11 34.31 142 IPI00291099.2 SPLICE ISOFORM LONG OF P23471 RECEPTOR-TYPE PROTEIN-TYROSINE PHOSPHATASE ZETA PRECURSOR. 260427 4.63 28 9 4.61 143 IPI00374770.1 MICROTUBULE-ASSOCIATED PROTEIN 1B ISOFORM 2. 256710 4.43 28 20 13.24 144 IPI00396378.1 SPLICE ISOFORM A2 OF P22626 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS A2/B1. 41925 9.58 28 11 35.34 145 IPI00014850.2 ASTROCYTIC PHOSPHOPROTEIN PEA-15. 15040 4.66 27 8 70.77 146 IPI00067590.1 --none found in database-- 9644 9.29 27 4 56.18 147 IPI00220327.1 KERATIN 1. 66067 8.33 27 8 13.66 148 IPI00384970.1 HEAT SHOCK PROTEIN BETA. 14066 4.4 27 5 32.31 149 IPI00386715.1 C-MYC PROMOTER-BINDING PROTEIN. 37087 7.19 27 7 21.19 150 IPI00014424.1 ELONGATION FACTOR 1-ALPHA 2. 50470 9.5 26 5 11.66 151 IPI00022774.1 TRANSITIONAL ENDOPLASMIC RETICULUM ATPASE (TER ATPASE) (15S MG(2+)- ATPASE P97 SUBUNIT) (VALOSIN CONTAINING PROTEIN) (VCP) [Contains: VALOSIN]. 89322 4.89 26 16 25.43 94 152 IPI00033946.1 HEAT SHOCK 70KDA PROTEIN 1B. 70025 5.31 26 13 29.64 153 IPI00216283.1 SPLICE ISOFORM SHORT OF P23471 RECEPTOR-TYPE PROTEIN-TYROSINE PHOSPHATASE ZETA PRECURSOR. 163444 4.85 26 8 6.53 154 IPI00216691.1 PROFILIN 1. 15054 8.46 26 9 87.86 155 IPI00304925.1 HEAT SHOCK 70 KDA PROTEIN 1. 70052 5.31 26 13 29.64 156 IPI00024323.3 SIMILAR TO FKSG30. 77208 7.25 25 4 5.99 157 IPI00031523.1 HEAT SHOCK PROTEIN 86. 35674 4.27 25 5 15.71 158 IPI00219757.6 GLUTATHIONE S-TRANSFERASE P. 24677 5.81 25 7 47.75 159 IPI00234002.2 SIMILAR TO HEAT SHOCK COGNATE 71 KDA PROTEIN. 65588 5.44 25 8 12.03 160 IPI00015671.1 HYPOTHETICAL PROTEIN FLJ21665. 49909 5.96 24 6 11.66 161 IPI00233214.2 CALMODULIN. 16706 3.84 24 8 94.59 162 IPI00293683.1 MICROTUBULE-ASSOCIATED PROTEIN TAU ISOFORM 4. 36760 10.06 24 9 40.34 163 IPI00333562.1 --none found in database-- 36748 6.98 24 2 5.15 164 IPI00007682.2 VACUOLAR ATP SYNTHASE CATALYTIC SUBUNIT A, UBIQUITOUS ISOFORM. 68304 5.16 23 9 17.18 165 IPI00027175.1 SORCIN. 21676 5.2 23 7 61.11 166 IPI00075248.1 CALMODULIN 2. 17557 3.89 23 7 66.45 167 IPI00081025.1 CALMODULIN. 17163 3.82 23 7 67.76 168 IPI00163984.2 --none found in database-- 33366 5.2 23 8 30.74 169 IPI00181828.3 COFILIN, MUSCLE ISOFORM. 23759 8.2 23 5 27.98 170 IPI00220171.1 SPLICE ISOFORM FETAL-TAU OF P10636 MICROTUBULE-ASSOCIATED PROTEIN TAU. 32813 10.77 23 8 37.46 171 IPI00220173.1 SPLICE ISOFORM TAU-B OF P10636 MICROTUBULE-ASSOCIATED PROTEIN TAU. 39589 9.17 23 8 31.05 172 IPI00220174.1 SPLICE ISOFORM TAU-C OF P10636 MICROTUBULE-ASSOCIATED PROTEIN TAU. 42472 7.43 23 8 28.85 173 IPI00220362.2 10 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL. 15224 10.05 23 5 39.01 174 IPI00334215.1 --none found in database-- 45330 6.29 23 5 6.86 175 IPI00386854.1 HYPOTHETICAL PROTEIN. 28412 4.51 23 8 36.55 176 IPI00013769.1 ALPHA ENOLASE, LUNG SPECIFIC. 49477 5.97 22 5 13.54 177 IPI00157721.4 --none found in database-- 42109 5.59 22 3 7.18 178 IPI00258965.2 SIMILAR TO ELONGATION FACTOR 1 ALPHA. 45401 7.1 22 3 8.35 179 IPI00291005.2 CYTOSOLIC MALATE DEHYDROGENASE. 36426 7.45 22 6 26.05 180 IPI00293276.3 MACROPHAGE MIGRATION INHIBITORY FACTOR (GLYCOSYLATION-INHIBITING FACTOR). 12476 8.05 22 2 17.39 181 IPI00383758.1 GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE, MUSCLE. 35876 7.07 22 7 19.46 182 IPI00386621.1 SIMILAR TO CALMODULIN 2. 16507 4.08 22 6 66.67 183 IPI00396248.1 SORCIN ISOFORM B. 20345 4.92 22 6 36.07 184 IPI00019683.3 --none found in database-- 48356 4.9 21 2 6.7 185 IPI00022881.1 SPLICE ISOFORM 1 OF P53675 CLATHRIN HEAVY CHAIN 2. 187030 5.67 21 7 5.37 186 IPI00024102.1 TRANSALDOLASE. 37540 6.8 21 8 25.52 187 IPI00027497.2 GLUCOSE-6-PHOSPHATE ISOMERASE. 63147 8.55 21 7 21.51 188 IPI00100470.1 ALPHA-TUBULIN ISOTYPE H2-ALPHA. 10899 3.91 21 4 48.98 189 IPI00217506.1 NUCLEOLIN. 76344 4.31 21 8 16.12 190 IPI00300446.1 SPLICE ISOFORM 2 OF P53675 CLATHRIN HEAVY CHAIN 2. 180296 5.58 21 7 5.56 191 IPI00385804.1 HYPOTHETICAL PROTEIN FLJ34423. 74325 4.26 21 8 16.59 192 IPI00017454.1 HYPOTHETICAL PROTEIN FLJ13940. 27546 8.59 20 2 11.62 193 IPI00024915.2 PEROXIREDOXIN 5, MITOCHONDRIAL PRECURSOR. 22026 8.77 20 8 51.87 194 IPI00026836.1 MICROTUBULE-ASSOCIATED PROTEIN TAU ISOFORM 3. 40007 10.13 20 8 33.94 195 IPI00027429.1 HYPOTHETICAL PROTEIN. 18829 5.68 20 6 33.13 196 IPI00179330.2 UBIQUITIN AND RIBOSOMAL PROTEIN S27A PRECURSOR. 17965 10.25 20 6 34.62 197 IPI00215747.1 FATTY ACID BINDING PROTEIN 7, BRAIN. 14889 5.25 20 6 41.67 198 IPI00219010.1 FERRITIN, HEAVY POLYPEPTIDE 1. 22178 6.34 20 5 31.05 199 IPI00219568.2 PHOSPHOGLYCERATE KINASE 2. 44796 8.82 20 4 11.27 200 IPI00220828.1 THYMOSIN, BETA 4. 5053 4.72 20 4 59.09 201 IPI00296120.1 SIMILAR TO SIMILARITY TO MONOUBIQUITIN/CARBOXY-EXTENSION PROTEIN FUSION. 11722 11.17 20 6 52.94 202 IPI00337838.1 UBIQUITIN-52 AMINO ACID FUSION PROTEIN. 14728 10.51 20 6 42.19 203 IPI00376164.1 THYMOSIN-LIKE 2. 5040 6.82 20 4 59.09 95 204 IPI00395917.1 --none found in database-- 22077 6.34 20 5 31.22 205 IPI00006663.1 ALDEHYDE DEHYDROGENASE, MITOCHONDRIAL PRECURSOR. 56381 7.05 19 8 24.95 206 IPI00015964.3 NEUROMODULIN. 28398 4.67 19 9 54.48 207 IPI00021841.1 APOLIPOPROTEIN A-I PRECURSOR. 30778 5.5 19 9 34.83 208 IPI00025499.1 MICROTUBULE-ASSOCIATED PROTEIN TAU ISOFORM 2. 45850 8.62 19 7 24.04 209 IPI00215965.1 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 ISOFORM B. 38747 9.46 19 8 26.61 210 IPI00216049.1 SPLICE ISOFORM 1 OF Q07244 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K. 50976 5.18 19 9 26.13 211 IPI00216746.1 SPLICE ISOFORM 2 OF Q07244 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K. 51028 4.94 19 9 26.08 212 IPI00217976.3 MICROTUBULE-ASSOCIATED PROTEIN TAU ISOFORM 1. 78878 6.69 19 7 13.98 213 IPI00220175.1 SPLICE ISOFORM TAU-E OF P10636 MICROTUBULE-ASSOCIATED PROTEIN TAU. 42836 9.53 19 7 25.79 214 IPI00220301.1 PEROXIREDOXIN 6. 25035 6.29 19 8 50.45 215 IPI00220342.1 DIMETHYLARGININE DIMETHYLAMINOHYDROLASE 1. 31122 5.61 19 7 27.72 216 IPI00258419.2 SIMILAR TO HEAT SHOCK COGNATE 71 KDA PROTEIN. 68249 4.91 19 7 11.27 217 IPI00301277.1 HEAT SHOCK 70 KDA PROTEIN 1-HOM. 70375 5.82 19 7 15.6 218 IPI00328348.2 UBIQUITIN A-52 RESIDUE RIBOSOMAL PROTEIN FUSION PRODUCT 1. 16175 10.6 19 5 34.75 219 IPI00333785.1 --none found in database-- 20074 6.33 19 1 5.59 220 IPI00375818.1 SIMILAR TO GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL PRECURSOR (GDH). 18997 6.67 19 6 40.94 221 IPI00376990.2 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 ISOFORM A. 34196 9.63 19 8 30.94 222 IPI00396395.1 NG,NG-DIMETHYLARGININE DIMETHYLAMINOHYDROLASE 1. 30991 5.61 19 7 27.82 223 IPI00396492.1 --none found in database-- 27478 4.8 19 4 13.58 224 IPI00025252.1 PROTEIN DISULFIDE ISOMERASE A3 PRECURSOR. 56782 6.28 18 10 28.91 225 IPI00105585.5 --none found in database-- 21666 4.14 18 6 46.63 226 IPI00173781.3 SIMILAR TO HEAT SHOCK PROTEIN HSP 90-ALPHA (HSP 86). 64432 8.19 18 5 7.94 227 IPI00247601.2 SIMILAR TO GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE, LIVER (GAPDH). 72249 8 18 3 4.15 228 IPI00333470.1 --none found in database-- 40503 6.04 18 2 4.63 229 IPI00334610.1 --none found in database-- 41064 5.92 18 2 4.61 230 IPI00375306.1 PEROXIREDOXIN 5 PRECURSOR ISOFORM B. 17394 9.01 18 7 57.06 231 IPI00018939.1 BA92K2.2. 17967 10.03 17 5 24.36 232 IPI00027230.1 ENDOPLASMIN PRECURSOR. 92469 4.48 17 9 16.19 233 IPI00142798.2 SIMILAR TO PEPTIDYLPROLYL ISOMERASE A (CYCLOPHILIN A). 15631 9.78 17 6 43.97 234 IPI00176590.2 SIMILAR TO HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 (HELIX- DESTABILIZING PROTEIN) (SINGLE-STRAND BINDING PROTEIN) (HNRNP CORE PROTEIN A1) (HDP). 32353 7.32 17 7 26.73 235 IPI00218570.1 PHOSPHOGLYCERATE MUTASE 2 (MUSCLE). 28850 9.33 17 4 14.23 236 IPI00329801.5 ANNEXIN A5. 35806 4.66 17 8 31.66 237 IPI00376165.1 THYMOSIN-LIKE 4. 5113 4.72 17 3 45.45 238 IPI00000874.1 PEROXIREDOXIN 1. 22110 8.31 16 4 19.6 239 IPI00010130.1 GLUTAMINE SYNTHETASE. 42064 6.88 16 7 21.72 240 IPI00027499.1 SPLICE ISOFORM 1 OF P06748 NUCLEOPHOSMIN. 32575 4.39 16 7 30.95 241 IPI00030809.1 GAMMA-G GLOBIN. 16969 6.34 16 1 6.45 242 IPI00031012.2 SIMILAR TO HEMOGLOBIN, GAMMA G. 16126 7.23 16 1 6.8 243 IPI00217471.1 EPSILON GLOBIN. 16203 9.1 16 1 6.8 244 IPI00220706.1 SIMILAR TO HEMOGLOBIN, GAMMA A. 16128 7.23 16 1 6.8 245 IPI00220740.1 SPLICE ISOFORM 2 OF P06748 NUCLEOPHOSMIN. 29465 4.22 16 7 34.34 246 IPI00332720.1 HEMOGLOBIN GAMMA-A AND GAMMA-G CHAINS. 16009 7.23 16 1 6.85 247 IPI00339269.1 HEAT SHOCK 70 KDA PROTEIN 6. 71028 6.01 16 6 11.04 248 IPI00375307.1 PEROXIREDOXIN 5 PRECURSOR ISOFORM C. 12837 9.49 16 5 50.4 249 IPI00382844.1 ACONITASE. 65347 7.92 16 5 12.33 250 IPI00003362.1 78 KDA GLUCOSE-REGULATED PROTEIN PRECURSOR. 72333 4.79 15 8 18.2 251 IPI00009532.1 4-AMINOBUTYRATE AMINOTRANSFERASE, MITOCHONDRIAL PRECURSOR. 56557 7.68 15 7 17 252 IPI00016638.1 ATP SYNTHASE ALPHA CHAIN, MITOCHONDRIAL PRECURSOR. 59751 9.56 15 5 15.19 253 IPI00021766.3 SPLICE ISOFORM 1 OF Q9NQC3 RETICULON 4. 129931 4.14 15 9 13.84 254 IPI00086909.3 SIMILAR TO EPSILON ISOFORM OF 14-3-3 PROTEIN. 42284 4.58 15 4 12.83 255 IPI00101135.1 HYPOTHETICAL PROTEIN. 65309 4.75 15 11 26.83 96 256 IPI00177728.2 CYTOSOLIC NONSPECIFIC DIPEPTIDASE. 52954 5.81 15 9 26.47 257 IPI00240029.5 STATHMIN. 17171 5.8 15 6 35.14 258 IPI00299024.4 BRAIN ACID SOLUBLE PROTEIN 1. 22562 4.3 15 8 53.54 259 IPI00333941.1 --none found in database-- 22028 8.48 15 6 33.33 260 IPI00386492.1 SIMILAR TO TRANSALDOLASE 1. 35329 9.41 15 5 17.92 261 IPI00395947.1 4-AMINOBUTYRATE AMINOTRANSFERASE PRECURSOR. 62284 8.87 15 7 15.29 262 IPI00012507.1 GTP-BINDING NUCLEAR PROTEIN RAN. 24423 7.59 14 6 34.72 263 IPI00032826.1 HSC70-INTERACTING PROTEIN. 41332 4.92 14 6 21.14 264 IPI00042578.2 SIMILAR TO HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 (HELIX- DESTABILIZING PROTEIN) (SINGLE-STRAND BINDING PROTEIN) (HNRNP CORE PROTEIN A1) (HDP). 30383 8.2 14 5 19.08 265 IPI00046057.1 HUNC18B. 68736 6.76 14 10 20.4 266 IPI00063228.3 SIMILAR TO EUKARYOTIC TRANSLATION ELONGATION FACTOR 1 ALPHA 2. 41980 7.8 14 2 5.19 267 IPI00077402.2 SIMILAR TO UBIQUITIN AND RIBOSOMAL PROTEIN S27A PRECURSOR. 22190 9.9 14 3 12.18 268 IPI00084828.1 SPLICE ISOFORM 1 OF Q64320 SYNTAXIN BINDING PROTEIN 1. 67569 6.96 14 10 20.71 269 IPI00156444.4 SIMILAR TO HEAT SHOCK PROTEIN HSP 90-BETA (HSP 84) (HSP 90). 53868 4.79 14 8 18.03 270 IPI00164463.3 --none found in database-- 18122 6.66 14 6 43.11 271 IPI00183526.1 SIMILAR TO NUCLEOLIN. 51357 4.43 14 5 14.26 272 IPI00218733.1 SUPEROXIDE DISMUTASE 1, SOLUBLE. 15936 6.07 14 8 55.84 273 IPI00289396.1 HYPOTHETICAL PROTEIN FLJ30394. 42500 6.39 14 8 26.06 274 IPI00332208.2 --none found in database-- 23852 6.79 14 7 36.28 275 IPI00382804.1 EEF1A PROTEIN. 24196 10.24 14 2 8.81 276 IPI00383405.1 --none found in database-- 21680 8.32 14 7 41.27 277 IPI00385358.1 --none found in database-- 23812 7.11 14 7 37.14 278 IPI00395637.1 --none found in database-- 34937 8.92 14 7 23.56 279 IPI00396452.1 --none found in database-- 24387 4.41 14 4 19.25 280 IPI00003406.1 DREBRIN. 71425 4.1 13 7 14.48 281 IPI00009802.1 SPLICE ISOFORM V0 OF P13611 VERSICAN CORE PROTEIN PRECURSOR. 372820 4.15 13 7 2.59 282 IPI00012048.1 NUCLEOSIDE DIPHOSPHATE KINASE A. 17149 6.11 13 5 41.45 283 IPI00014398.1 SKELETAL MUSCLE LIM-PROTEIN 1. 31895 8.37 13 5 22.86 284 IPI00018206.1 ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL PRECURSOR. 47476 9.38 13 6 16.74 285 IPI00047642.3 --none found in database-- 43066 9.43 13 3 6.3 286 IPI00176692.2 SIMILAR TO HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 (HELIX- DESTABILIZING PROTEIN) (SINGLE-STRAND BINDING PROTEIN) (HNRNP CORE PROTEIN A1) (HDP-1) (TOPOISOMERASE-INHIBITOR SUPPRESSED). 28788 9.73 13 4 17.31 287 IPI00215629.1 SPLICE ISOFORM V2 OF P13611 VERSICAN CORE PROTEIN PRECURSOR. 182062 4.52 13 7 5.36 288 IPI00215631.1 SPLICE ISOFORM VINT OF P13611 VERSICAN CORE PROTEIN PRECURSOR. 369688 4.13 13 7 2.61 289 IPI00219029.1 ASPARTATE AMINOTRANSFERASE 1. 46247 7.01 13 8 26.63 290 IPI00337778.2 SIMILAR TO PHYTANOYL-COA HYDROXYLASE INTERACTING PROTEIN. 39066 7.15 13 7 25 291 IPI00374732.1 SIMILAR TO PEPTIDYLPROLYL ISOMERASE A (CYCLOPHILIN A). 19330 8.77 13 5 35.75 292 IPI00374975.2 PUTATIVE PHOSPHOGLYCERATE MUTASE 3. 28777 6.63 13 4 24.8 293 IPI00375531.1 NM23-H1. 19654 5.29 13 5 35.59 294 IPI00375839.1 SIMILAR TO PHOSPHOGLYCERATE MUTASE 1 (PHOSPHOGLYCERATE MUTASE ISOZYME B) (PGAM-B) (BPG-DEPENDENT PGAM 1). 21007 6.16 13 3 11.58 295 IPI00396476.1 --none found in database-- 58771 4.94 13 2 3.92 296 IPI00001453.2 ALPHA-INTERNEXIN. 55391 5.09 12 7 14.83 297 IPI00001734.2 SPLICE ISOFORM 1 OF Q9Y617 PHOSPHOSERINE AMINOTRANSFERASE. 40423 7.77 12 6 18.11 298 IPI00007765.2 STRESS-70 PROTEIN, MITOCHONDRIAL PRECURSOR. 73680 6.01 12 11 20.47 299 IPI00011107.2 ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL PRECURSOR. 50909 8.95 12 7 18.58 300 IPI00026260.1 NUCLEOSIDE DIPHOSPHATE KINASE B. 17298 8.69 12 5 42.11 301 IPI00107634.2 CHONDROITIN SULFATE PROTEOGLYCAN BEHAB/BREVICAN. 99148 4.28 12 8 10.98 302 IPI00163187.6 HYPOTHETICAL PROTEIN. 55136 7.26 12 7 15.6 303 IPI00172579.1 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE. 53802 5.61 12 6 15.18 304 IPI00180730.1 --none found in database-- 50154 9.41 12 3 8.01 305 IPI00186036.2 --none found in database-- 19050 8.35 12 5 17.42 306 IPI00215628.1 SPLICE ISOFORM V1 OF P13611 VERSICAN CORE PROTEIN PRECURSOR. 265050 4.17 12 6 3.28 97 307 IPI00215630.1 SPLICE ISOFORM V3 OF P13611 VERSICAN CORE PROTEIN PRECURSOR. 74293 7.38 12 6 12.06 308 IPI00216900.1 SIMILAR TO MICROTUBULE-ASSOCIATED PROTEIN 2. 58954 10.4 12 5 16.99 309 IPI00218319.1 SPLICE ISOFORM 2 OF P06753 TROPOMYOSIN ALPHA 3 CHAIN. 29033 4.44 12 6 27.02 310 IPI00218320.1 SPLICE ISOFORM 3 OF P06753 TROPOMYOSIN ALPHA 3 CHAIN. 28955 4.46 12 6 27.13 311 IPI00218474.2 BETA ENOLASE. 47003 7.84 12 4 11.95 312 IPI00219478.1 SPLICE ISOFORM 2 OF Q9Y617 PHOSPHOSERINE AMINOTRANSFERASE. 35189 6.66 12 6 20.68 313 IPI00261068.2 --none found in database-- 16467 8.76 12 4 18.67 314 IPI00332474.1 --none found in database-- 18152 9.09 12 4 19.39 315 IPI00374327.1 MICROTUBULE-ASSOCIATED PROTEIN 2 ISOFORM 4. 52874 10.3 12 5 18.92 316 IPI00374399.1 SIMILAR TO HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 (HELIX- DESTABILIZING PROTEIN) (SINGLE-STRAND BINDING PROTEIN) (HNRNP CORE PROTEIN A1) (HDP). 24239 9.6 12 5 26.84 317 IPI00374686.1 SIMILAR TO HYPOTHETICAL PROTEIN MGC37309. 18838 8.9 12 5 28.66 318 IPI00382894.1 TPMSK3. 28809 4.41 12 6 27.13 319 IPI00386739.2 CHONDROITIN SULFATE PROTEOGLYCAN BEHAB/BREVICAN. 99118 4.28 12 8 10.98 320 IPI00013808.1 ALPHA-ACTININ 4. 104854 5.12 11 7 11.75 321 IPI00020599.1 CALRETICULIN PRECURSOR. 48142 4.04 11 6 23.02 322 IPI00021383.1 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A3. 39686 8.77 11 5 14.78 323 IPI00021828.1 CYSTATIN B. 11140 7.73 11 3 45.92 324 IPI00025366.1 CITRATE SYNTHASE, MITOCHONDRIAL PRECURSOR. 51706 8.21 11 5 12.23 325 IPI00030144.1 CYCLOPHILIN-LC. 18182 9.76 11 4 20.73 326 IPI00031045.1 DESTRIN. 18506 7.97 11 4 23.64 327 IPI00062209.1 HYPOTHETICAL PROTEIN. 17098 6.38 11 2 5.1 328 IPI00174760.2 SIMILAR TO HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 (HELIX- DESTABILIZING PROTEIN) (SINGLE-STRAND BINDING PROTEIN) (HNRNP CORE PROTEIN A1) (HDP). 27551 5.21 11 5 20.88 329 IPI00335314.1 --none found in database-- 34736 5.34 11 2 2.53 330 IPI00374137.1 SIMILAR TO PHOSPHATIDYLETHANOLAMINE-BINDING PROTEIN (PEBP) (PROSTATIC BINDING PROTEIN) (HCNPPP) (NEUROPOLYPEPTIDE H3) (RAF KINASE INHIBITOR PROTEIN) (RKIP). 10844 5.7 11 2 22.92 331 IPI00383539.1 CITRATE SYNTHASE PRECURSOR ISOFORM B. 44703 7.2 11 5 14.25 332 IPI00386685.2 CITRATE SYNTHASE PRECURSOR ISOFORM A. 55633 8.96 11 5 11.24 333 IPI00006482.1 SPLICE ISOFORM LONG OF P05023 SODIUM/POTASSIUM-TRANSPORTING ATPASE ALPHA-1 CHAIN PRECURSOR. 112896 5.15 10 6 7.82 334 IPI00012007.2 ADENOSYLHOMOCYSTEINASE. 47716 6.29 10 5 16.2 335 IPI00013944.2 SPLICE ISOFORM C2 OF P07910 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS C1/C2. 33688 4.69 10 5 19.28 336 IPI00019359.2 KERATIN, TYPE I CYTOSKELETAL 9. 62064 4.89 10 7 13.96 337 IPI00025318.1 SH3 DOMAIN-BINDING GLUTAMIC ACID-RICH-LIKE PROTEIN. 12774 4.91 10 3 28.95 338 IPI00027107.3 TU TRANSLATION ELONGATION FACTOR, MITOCHONDRIAL. 49875 7.68 10 8 25.27 339 IPI00029028.1 FOUR AND A HALF LIM DOMAINS 1 PROTEIN ISOFORM C. 22017 8.53 10 3 18.56 340 IPI00055606.2 LIM PROTEIN SLIMMER. 36263 9.15 10 3 11.15 341 IPI00072377.1 TEMPLATE ACYIVATING FACTOR-I ALPHA. 33489 3.95 10 4 17.93 342 IPI00092176.2 SIMILAR TO TYROSINE 3/TRYPTOPHAN 5 -MONOOXYGENASE ACTIVATION PROTEIN, EPSILON POLYPEPTIDE. 27744 6.79 10 2 7.11 343 IPI00107555.1 PROFILIN 2 ISOFORM B. 15088 5.88 10 3 29.29 344 IPI00165579.3 PP856. 43908 6.44 10 6 22.19 345 IPI00168184.1 HYPOTHETICAL PROTEIN FLJ34068. 56803 5.4 10 8 21.22 346 IPI00168839.1 FAM10A5. 41378 4.68 10 4 12.74 347 IPI00176715.2 SIMILAR TO FERRITIN HEAVY CHAIN (FERRITIN H SUBUNIT). 27186 6.5 10 3 16.1 348 IPI00216592.1 SPLICE ISOFORM C1 OF P07910 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS C1/C2. 32356 4.68 10 5 20.14 349 IPI00219468.1 PROFILIN 2 ISOFORM A. 15046 7.04 10 3 29.29 350 IPI00236240.2 SIMILAR TO FERRITIN HEAVY CHAIN (FERRITIN H SUBUNIT). 47023 8.97 10 3 8.92 351 IPI00289862.3 PROTEIN KIAA0193. 46382 4.39 10 4 11.84 352 IPI00293579.1 SPLICE ISOFORM MAP2C OF P11137 MICROTUBULE-ASSOCIATED PROTEIN 2. 49768 10.19 10 4 17.83 353 IPI00301311.1 SET PROTEIN. 32103 3.85 10 4 18.77 354 IPI00302840.1 SODIUM/POTASSIUM-TRANSPORTING ATPASE ALPHA-3 CHAIN. 111735 5.02 10 6 8.79 355 IPI00328587.4 SIMILAR TO ENOLASE 1,. 42342 5.71 10 5 8.51 356 IPI00385025.1 ISOCITRATE DEHYDROGENASE. 46815 7.21 10 6 17.42 357 IPI00385372.1 --none found in database-- 34547 4.97 10 5 21.29 98 358 IPI00003021.1 SODIUM/POTASSIUM-TRANSPORTING ATPASE ALPHA-2 CHAIN PRECURSOR. 112265 5.33 9 5 6.47 359 IPI00003479.1 MITOGEN-ACTIVATED PROTEIN KINASE 1. 41390 6.99 9 5 15.83 360 IPI00013881.4 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H. 49229 6.25 9 4 13.36 361 IPI00021304.1 KERATIN, TYPE II CYTOSKELETAL 2 EPIDERMAL. 65865 8.17 9 3 5.58 362 IPI00022463.1 SEROTRANSFERRIN PRECURSOR. 77050 7.13 9 6 11.03 363 IPI00024919.1 THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE, MITOCHONDRIAL PRECURSOR. 27693 7.88 9 6 26.95 364 IPI00025054.1 SPLICE ISOFORM LONG OF Q00839 HETEROGENOUS NUCLEAR RIBONUCLEOPROTEIN U. 90479 5.8 9 6 10.44 365 IPI00164792.1 PROTHYMOSIN ALPHA. 11828 3.38 9 5 36.11 366 IPI00180240.1 THYMOSIN-LIKE 3. 5235 4.72 9 2 26.09 367 IPI00218038.1 ST13-LIKE TUMOR SUPPRESSOR. 27407 4.72 9 4 22.5 368 IPI00219209.1 SPLICE ISOFORM 4 OF Q9NQC3 RETICULON 4. 106360 4.13 9 7 11.98 369 IPI00220503.4 DYNACTIN 2. 44820 4.81 9 7 23.89 370 IPI00295624.1 HYPOTHETICAL PROTEIN. 71595 4.17 9 5 9.52 371 IPI00299633.1 DJ1071L10.1. 5043 4.72 9 2 27.27 372 IPI00302898.1 PROTHYMOSIN ALPHA. 12072 3.41 9 5 35.45 373 IPI00332603.1 --none found in database-- 34063 8.19 9 4 19.11 374 IPI00374151.1 PEROXIREDOXIN 3 ISOFORM B. 25839 7.54 9 6 28.99 375 IPI00376163.1 THYMOSIN-LIKE 1. 5071 4.72 9 2 27.27 376 IPI00376295.1 MITOGEN-ACTIVATED PROTEIN KINASE 1. 41404 7.16 9 5 15.83 377 IPI00384369.1 SIMILAR TO TROPOMYOSIN 1, ALPHA. 32621 4.69 9 5 17.77 378 IPI00386491.2 SPLICE ISOFORM SHORT OF Q00839 HETEROGENOUS NUCLEAR RIBONUCLEOPROTEIN U. 89724 5.6 9 6 10.58 379 IPI00396479.1 --none found in database-- 24078 4.39 9 4 22.9 380 IPI00003815.1 RHO GDP-DISSOCIATION INHIBITOR 1. 23207 4.74 8 3 30.88 381 IPI00003881.1 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN F. 45672 5.31 8 4 13.73 382 IPI00004574.1 IG KAPPA CHAIN C REGION. 11609 5.68 8 3 51.89 383 IPI00010779.1 SPLICE ISOFORM 1 OF P07226 TROPOMYOSIN ALPHA 4 CHAIN. 28522 4.36 8 4 15.73 384 IPI00013508.2 ALPHA-ACTININ 1. 102974 5.04 8 4 5.49 385 IPI00018140.2 GRY-RBP. 69633 8.88 8 5 9.79 386 IPI00022314.1 SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL PRECURSOR. 24722 8.45 8 4 20.27 387 IPI00027165.1 SPLICE ISOFORM R-TYPE OF P30613 PYRUVATE KINASE, ISOZYMES R/L. 61830 7.83 8 2 2.96 388 IPI00027223.2 ISOCITRATE DEHYDROGENASE [NADP] CYTOPLASMIC. 46659 7 8 4 15.22 389 IPI00027442.1 ALANYL-TRNA SYNTHETASE. 106801 5.13 8 6 10.23 390 IPI00028888.1 SPLICE ISOFORM 1 OF Q14103 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN D0. 38434 8.01 8 5 18.31 391 IPI00048940.3 --none found in database-- 29068 8.13 8 3 14.18 392 IPI00074333.1 HYPOTHETICAL PROTEIN. 25826 5.61 8 5 24.35 393 IPI00107117.1 PEPTIDYLPROLYL ISOMERASE B. 23743 10.07 8 4 16.2 394 IPI00152471.1 GUANINE NUCLEOTIDE-BINDING PROTEIN G(O), ALPHA SUBUNIT 2. 40087 5.69 8 4 14.69 395 IPI00164416.3 --none found in database-- 17889 7.88 8 3 16.46 396 IPI00174920.2 SIMILAR TO CITRATE SYNTHASE PRECURSOR. 51440 7.23 8 4 9.87 397 IPI00179589.1 MYOTROPHIN. 12895 5.18 8 5 63.56 398 IPI00181260.1 PHOSPHOFRUCTOKINASE, MUSCLE. 85183 8.07 8 5 7.56 399 IPI00217465.1 H1 HISTONE FAMILY, MEMBER 2. 21365 11.71 8 3 18.31 400 IPI00218115.3 SPLICE ISOFORM 1 OF P06753 TROPOMYOSIN ALPHA 3 CHAIN. 32950 4.38 8 4 13.33 401 IPI00218407.4 ALDOLASE B. 39473 7.96 8 1 1.92 402 IPI00219585.1 SPLICE ISOFORM 2 OF P08237 6-PHOSPHOFRUCTOKINASE, MUSCLE TYPE. 81644 7.68 8 5 7.89 403 IPI00220281.1 GUANINE NUCLEOTIDE BINDING PROTEIN (G PROTEIN), ALPHA ACTIVATING ACTIVITY POLYPEPTIDE O. 40051 5.19 8 4 14.69 404 IPI00220684.1 SPLICE ISOFORM 3 OF Q14103 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN D0. 32835 8.43 8 5 21.24 405 IPI00220827.1 THYMOSIN, BETA 10. 5026 5.02 8 3 63.64 406 IPI00243603.2 SIMILAR TO PYRUVATE KINASE, M1 ISOZYME (PYRUVATE KINASE MUSCLE ISOZYME) (CYTOSOLIC THYROID HORMONE-BINDING PROTEIN) (CTHBP) (THBP1). 55507 6.45 8 5 10.16 407 IPI00291928.1 RAS-RELATED PROTEIN RAB-14. 23927 6.13 8 4 22.79 408 IPI00304824.3 HYPOTHETICAL PROTEIN. 24750 8.45 8 4 20.27 409 IPI00332370.3 PYRUVATE KINASE L. 65043 7.75 8 2 2.81 99 410 IPI00334441.1 --none found in database-- 10362 9.08 8 3 30.53 411 IPI00334779.1 SPLICE ISOFORM L-TYPE OF P30613 PYRUVATE KINASE, ISOZYMES R/L. 58494 7.05 8 2 3.13 412 IPI00374228.1 SIMILAR TO MGC37309 PROTEIN. 29623 8.26 8 3 12.46 413 IPI00375401.1 PEROXIREDOXIN 2 ISOFORM C. 15819 9.49 8 2 13.38 414 IPI00375676.1 HYPOTHETICAL PROTEIN DKFZP686L19147. 26825 5.61 8 5 23.24 415 IPI00385058.1 HYPOTHETICAL PROTEIN. 25702 7.7 8 3 23.31 416 IPI00385732.1 --none found in database-- 18987 8.78 8 5 26.49 417 IPI00386745.1 ACTININ, ALPHA 1. 103058 5.07 8 4 5.49 418 IPI00395553.1 MYOTROPHIN. 12764 5.18 8 5 64.1 419 IPI00395915.1 SIMILAR TO NS1-ASSOCIATED PROTEIN 1. 58736 7.65 8 5 11.57 420 IPI00396072.1 HYPOTHETICAL PROTEIN. 25674 8.45 8 3 23.5 421 IPI00010810.1 ELECTRON TRANSFER FLAVOPROTEIN ALPHA-SUBUNIT, MITOCHONDRIAL PRECURSOR. 35080 8.57 7 5 24.62 422 IPI00014177.1 SEPTIN 2. 41487 6.58 7 3 10.8 423 IPI00015139.2 SIMILAR TO HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 (HELIX- DESTABILIZING PROTEIN) (SINGLE-STRAND BINDING PROTEIN) (HNRNP CORE PROTEIN A1) (HDP). 25124 6.42 7 3 11.45 424 IPI00015550.3 PROTHYMOSIN ALPHA. 11954 3.42 7 4 22.94 425 IPI00015842.1 RETICULOCALBIN 1 PRECURSOR. 38890 4.61 7 5 20.24 426 IPI00020956.1 HEPATOMA-DERIVED GROWTH FACTOR. 26788 4.39 7 6 37.92 427 IPI00020984.1 CALNEXIN PRECURSOR. 67568 4.21 7 6 12.5 428 IPI00023504.1 RAS-RELATED PROTEIN RAB-3A. 24984 4.62 7 3 17.73 429 IPI00024990.6 METHYLMALONATE-SEMIALDEHYDE DEHYDROGENASE [ACYLATING], MITOCHONDRIAL PRECURSOR. 57840 8.69 7 5 11.59 430 IPI00026230.1 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H'. 49264 6.25 7 3 9.58 431 IPI00029997.1 6-PHOSPHOGLUCONOLACTONASE. 27547 5.95 7 3 27.13 432 IPI00046595.2 SIMILAR TO PYRUVATE KINASE, M1 ISOZYME (PYRUVATE KINASE MUSCLE ISOZYME) (CYTOSOLIC THYROID HORMONE-BINDING PROTEIN) (CTHBP) (THBP1). 38068 6.51 7 2 4.31 433 IPI00056467.6 SIMILAR TO TEMPLATE ACYIVATING FACTOR-I ALPHA. 25908 4.73 7 3 18.3 434 IPI00076042.2 SHORT HEAT SHOCK PROTEIN 60 HSP60S2. 27096 4.34 7 3 14.34 435 IPI00100160.1 HYPOTHETICAL PROTEIN. 136376 5.54 7 5 4.55 436 IPI00101645.1 PUTATIVE ADENOSYLHOMOCYSTEINASE 3. 66721 7.39 7 4 6.55 437 IPI00159175.1 HYPOTHETICAL PROTEIN. 66668 7.44 7 4 6.7 438 IPI00176697.3 --none found in database-- 29153 8.31 7 3 15.15 439 IPI00179155.1 --none found in database-- 24613 4.99 7 4 24.35 440 IPI00179377.2 SIMILAR TO 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL PRECURSOR (HSP60) (60 KDA CHAPERONIN) (CPN60) (HEAT SHOCK PROTEIN 60) (HSP-60) (MITOCHONDRIAL MATRIX PROTEIN P1) (P60 LYMPHOCYTE PROTEIN) (HUCHA60). 56672 5.38 7 4 11.93 441 IPI00179721.3 SIMILAR TO HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 (HELIX- DESTABILIZING PROTEIN) (SINGLE-STRAND BINDING PROTEIN) (HNRNP CORE PROTEIN A1) (HDP-1) (TOPOISOMERASE-INHIBITOR SUPPRESSED). 30103 6.4 7 3 10.39 442 IPI00182938.3 PUTATIVE ADENOSYLHOMOCYSTEINASE 2. 71654 8.11 7 4 6.12 443 IPI00186290.3 ELONGATION FACTOR 2. 97752 6.82 7 4 6.35 444 IPI00215761.3 ATP-DEPENDENT DNA HELICASE II, 70 KDA SUBUNIT. 69712 6.61 7 6 12.99 445 IPI00216134.1 SPLICE ISOFORM 2 OF P09493 TROPOMYOSIN 1 ALPHA CHAIN. 26549 4.47 7 3 13.66 446 IPI00216757.1 SPLICE ISOFORM SHORT OF P05023 SODIUM/POTASSIUM-TRANSPORTING ATPASE ALPHA-1 CHAIN PRECURSOR. 74140 5.87 7 3 5.73 447 IPI00216947.2 SIMILAR TO HEAT SHOCK 70KD PROTEIN BINDING PROTEIN. 34791 4.62 7 3 13.18 448 IPI00217466.1 H1 HISTONE FAMILY, MEMBER 3. 22350 11.79 7 2 10.41 449 IPI00217467.1 H1 HISTONE FAMILY, MEMBER 4. 21865 11.8 7 2 10.5 450 IPI00217473.1 ZETA GLOBIN. 15637 8.51 7 1 4.93 451 IPI00220683.1 SPLICE ISOFORM 2 OF Q14103 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN D0. 36272 8.34 7 4 15.48 452 IPI00220685.1 SPLICE ISOFORM 4 OF Q14103 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN D0. 30672 8.73 7 4 18.12 453 IPI00220766.1 GLYOXALASE I. 20720 5.08 7 3 25.54 454 IPI00243289.4 HYPOTHETICAL PROTEIN XP_292029. 30355 5.04 7 1 2.6 455 IPI00253411.2 --none found in database-- 38301 5.79 7 1 3.54 456 IPI00290982.5 DYNEIN HEAVY CHAIN, CYTOSOLIC. 532367 6.36 7 5 1.74 457 IPI00298289.1 SPLICE ISOFORM 2 OF Q9NQC3 RETICULON 4. 40318 4.41 7 3 13.67 458 IPI00300020.3 EXCITATORY AMINO ACID TRANSPORTER 2. 62104 6.51 7 4 6.79 459 IPI00328108.5 DESMIN. 53530 4.94 7 3 5.76 460 IPI00328188.1 FATTY ACID SYNTHASE. 273427 6.41 7 5 3.03 100 461 IPI00335276.3 HYPOTHETICAL PROTEIN. 43255 4.41 7 3 12.75 462 IPI00337654.1 PROTHYMOSIN ALPHA. 8030 3.44 7 3 34.72 463 IPI00374113.1 SIMILAR TO PEPTIDYL-PRO CIS TRANS ISOMERASE. 50546 8.56 7 2 2.79 464 IPI00374247.1 SIMILAR TO HEAT SHOCK PROTEIN HSP 90-BETA (HSP 84). 11111 4.02 7 2 14.58 465 IPI00376110.1 SIMILAR TO RHO GDP-DISSOCIATION INHIBITOR 1 (RHO GDI 1) (RHO-GDI ALPHA). 25377 6.3 7 2 13.9 466 IPI00376262.1 SIMILAR TO PEPTIDYL-PRO CIS TRANS ISOMERASE. 27042 8.22 7 2 5.31 467 IPI00376272.1 SIMILAR TO CYCLOPHILIN-LC. 23765 9.24 7 3 9.22 468 IPI00376415.1 SIMILAR TO PEPTIDYL-PRO CIS TRANS ISOMERASE. 19047 10.51 7 2 7.56 469 IPI00376771.1 SIMILAR TO PEPTIDYL-PRO CIS TRANS ISOMERASE. 19737 9.31 7 2 7.1 470 IPI00382617.1 P37 AUF1. 31481 7.45 7 4 18.18 471 IPI00382931.1 PLACENTA IMMUNOREGULATORY FACTOR PLIF. 19490 8.79 7 2 13.94 472 IPI00386068.1 HYPOTHETICAL PROTEIN. 85409 5.16 7 5 7.27 473 IPI00395343.1 THYROID AUTOANTIGEN 70KDA (KU ANTIGEN). 69843 6.61 7 6 12.97 474 IPI00000230.1 HYPOTHETICAL PROTEIN. 34944 4.5 6 3 8.77 475 IPI00003370.1 SPLICE ISOFORM 1 OF Q16623 SYNTAXIN 1A. 33023 4.88 6 5 28.13 476 IPI00005719.1 SPLICE ISOFORM 1 OF P11476 RAS-RELATED PROTEIN RAB-1A. 22678 6 6 3 17.07 477 IPI00006612.1 CLATHRIN COAT ASSEMBLY PROTEIN AP180. 92502 4.45 6 3 5.4 478 IPI00008529.1 60S ACIDIC RIBOSOMAL PROTEIN P2. 11665 4.14 6 4 69.57 479 IPI00008964.1 RAS-RELATED PROTEIN RAB-1B. 22171 5.38 6 3 17.41 480 IPI00009865.1 KERATIN, TYPE I CYTOSKELETAL 10. 59519 4.87 6 4 10.46 481 IPI00010796.1 PROTEIN DISULFIDE ISOMERASE PRECURSOR. 57116 4.49 6 5 18.31 482 IPI00011229.1 CATHEPSIN D PRECURSOR. 44552 6.5 6 4 11.65 483 IPI00013991.1 SPLICE ISOFORM 1 OF P07951 TROPOMYOSIN BETA CHAIN. 32851 4.36 6 2 6.69 484 IPI00014230.1 COMPLEMENT COMPONENT 1, Q SUBCOMPONENT BINDING PROTEIN, MITOCHONDRIAL PRECURSOR. 31362 4.47 6 3 9.57 485 IPI00014581.1 SPLICE ISOFORM 1 OF P09493 TROPOMYOSIN 1 ALPHA CHAIN. 32709 4.39 6 3 9.51 486 IPI00016513.1 RAS-RELATED PROTEIN RAB-10. 22541 8.61 6 2 11 487 IPI00019888.1 SUCCINATE SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL PRECURSOR. 57215 8.37 6 4 10.09 488 IPI00021751.2 NEUROFILAMENT TRIPLET H PROTEIN. 112479 6 6 2 1.36 489 IPI00024107.1 SPLICE ISOFORM 1 OF P37840 ALPHA-SYNUCLEIN. 14460 4.37 6 2 13.57 490 IPI00028196.2 SIMILAR TO KIAA1765 PROTEIN. 104424 9.71 6 2 3.01 491 IPI00029091.1 PUTATIVE NUCLEOSIDE DIPHOSPHATE KINASE. 15529 8.83 6 3 27.01 492 IPI00032904.1 BETA-SYNUCLEIN. 14288 4.09 6 2 14.18 493 IPI00045410.2 SIMILAR TO NUCLEOPHOSMIN 1. 32995 4.34 6 2 6.73 494 IPI00073958.1 HYPOTHETICAL PROTEIN. 18648 8.18 6 2 23.78 495 IPI00140827.2 SIMILAR TO SMT3 SUPPRESSOR OF MIF TWO 3 HOMOLOG 2. 17755 6.25 6 2 13.75 496 IPI00165028.1 PROTHYMOSIN ALPHA. 11349 3.41 6 3 24.76 497 IPI00175108.2 SIMILAR TO HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K ISOFORM A. 50289 4.89 6 3 6.54 498 IPI00175156.2 SIMILAR TO HEAT SHOCK 70KD PROTEIN BINDING PROTEIN. 42873 5.05 6 3 10.68 499 IPI00176998.2 SIMILAR TO TROPOMYOSIN 3. 28884 4.38 6 4 18.15 500 IPI00178083.1 HYPOTHETICAL PROTEIN FLJ35393. 21697 4.51 6 4 24.46 501 IPI00180954.2 COLD-INDUCIBLE RNA-BINDING PROTEIN. 18648 9.82 6 3 26.74 502 IPI00185362.1 SIMILAR TO NEURAL CELL ADHESION MOLECULE 1. 66271 4.52 6 4 7.62 503 IPI00215902.1 ALDO-KETO REDUCTASE FAMILY 1, MEMBER B1. 35853 6.99 6 4 11.71 504 IPI00215916.1 CYTOCHROME C. 11749 10.16 6 2 27.62 505 IPI00216975.1 SPLICE ISOFORM 2 OF P07226 TROPOMYOSIN ALPHA 4 CHAIN. 32723 4.38 6 2 6.69 506 IPI00218467.1 SPLICE ISOFORM 2-4 OF P37840 ALPHA-SYNUCLEIN. 11372 8.88 6 2 16.96 507 IPI00218667.1 STATHMIN 2. 24926 9.02 6 2 8.68 508 IPI00218793.2 PARATHYMOSIN. 11530 3.83 6 3 22.55 509 IPI00218820.1 SPLICE ISOFORM 3 OF P07951 TROPOMYOSIN BETA CHAIN. 28684 4.29 6 2 7.66 510 IPI00220271.1 ALDO-KETO REDUCTASE FAMILY 1, MEMBER A1. 36573 6.79 6 4 18.46 511 IPI00220709.3 SPLICE ISOFORM 2 OF P07951 TROPOMYOSIN BETA CHAIN. 32990 4.32 6 2 6.69 512 IPI00220737.1 SPLICE ISOFORM N-CAM 120 OF P13592 NEURAL CELL ADHESION MOLECULE 1, 120 KDA ISOFORM PRECURSOR. 83770 4.5 6 4 6.04 101 513 IPI00221222.1 ACTIVATED RNA POLYMERASE II TRANSCRIPTION COFACTOR 4. 14365 10.32 6 4 37.01 514 IPI00258810.2 --none found in database-- 29189 9.77 6 3 12.02 515 IPI00259825.2 SIMILAR TO NUCLEOPHOSMIN 1. 43866 4.97 6 2 4.95 516 IPI00295684.1 KERATIN 10. 58827 4.82 6 4 10.62 517 IPI00299149.1 UBIQUITIN-LIKE PROTEIN SMT3B. 10871 5.16 6 2 23.16 518 IPI00302448.1 NEURAL CELL ADHESION MOLECULE 1, 140 KDA ISOFORM PRECURSOR. 93361 4.5 6 4 5.42 519 IPI00332161.1 IG GAMMA-1 CHAIN C REGION. 36106 8.31 6 3 13.33 520 IPI00333730.2 --none found in database-- 27500 5.01 6 3 19.84 521 IPI00334144.1 --none found in database-- 22353 6.37 6 3 24.14 522 IPI00334545.2 --none found in database-- 46431 4.7 6 1 1.68 523 IPI00336008.1 ALDEHYDE DEHYDROGENASE 5A1 PRECURSOR ISOFORM 1. 58653 8.16 6 4 9.85 524 IPI00374397.1 SIMILAR TO TROPOMYOSIN 4. 24982 4.87 6 2 8.84 525 IPI00374519.1 SIMILAR TO RAB1B, MEMBER RAS ONCOGENE FAMILY. 22017 5.05 6 3 17.41 526 IPI00374689.1 SIMILAR TO ATP-DEPENDENT DNA HELICASE II, 70 KDA SUBUNIT (LUPUS KU AUTOANTIGEN PROTEIN P70) (KU70) (70 KDA SUBUNIT OF KU ANTIGEN) (THYROID- LUPUS AUTOANTIGEN) (TLAA) (CTC BOX BINDING FACTOR 75 KDA SUBUNIT) (CTCBF) (CTC75). 54430 8.87 6 5 13.68 527 IPI00375315.1 SIMILAR TO HEAT SHOCK PROTEIN HSP 90-ALPHA (HSP 86). 19507 4.44 6 2 12.2 528 IPI00376005.1 EUKARYOTIC INITIATION FACTOR 5A ISOFORM I VARIANT A. 20170 7.02 6 3 25.54 529 IPI00376012.1 SIMILAR TO HYPOTHETICAL PROTEIN MGC37309. 23413 9.19 6 3 11.66 530 IPI00376379.1 KERATIN 1B. 61801 5.78 6 1 2.08 531 IPI00376794.1 SIMILAR TO THYMOSIN-LIKE 4. 13915 4.7 6 1 4.8 532 IPI00383445.1 SIMILAR TO APOBEC-1 COMPLEMENTATION FACTOR. 46268 9.19 6 3 8.29 533 IPI00384938.1 HYPOTHETICAL PROTEIN DKFZP686N02209. 52852 8.61 6 3 9.13 534 IPI00385332.1 HYPOTHETICAL PROTEIN. 51204 8.28 6 3 9.36 535 IPI00385621.1 PROTHYMOSIN ALPHA. 11679 3.46 6 3 24.3 536 IPI00386314.1 FLJ00064 PROTEIN. 30383 5.38 6 3 22.1 537 IPI00395322.1 EUKARYOTIC TRANSLATION INITIATION FACTOR 5A. 16701 4.86 6 3 30.72 538 IPI00395738.1 --none found in database-- 18721 9.95 6 3 26.59 539 IPI00395871.1 HUMAN FULL-LENGTH CDNA CLONE CS0DA009YK08 OF NEUROBLASTOMA OF HOMO SAPIENS. 25230 4.35 6 4 21.24 540 IPI00001593.1 LYSOSOMAL PRO-X CARBOXYPEPTIDASE PRECURSOR. 55800 7.23 5 3 9.88 541 IPI00002966.1 HEAT SHOCK 70 KDA PROTEIN 4. 94300 4.9 5 3 5.6 542 IPI00003925.3 PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT, MITOCHONDRIAL PRECURSOR. 39219 6.63 5 4 14.21 543 IPI00005089.1 NEURONAL TROPOMODULIN. 39595 4.93 5 2 7.41 544 IPI00007102.1 CGI-150 PROTEIN. 55012 8.86 5 4 11.9 545 IPI00008994.2 SPLICE ISOFORM 1 OF Q9UN36 NDRG2 PROTEIN. 40798 4.87 5 5 21.56 546 IPI00009476.2 SPLICE ISOFORM C OF P13592 NEURAL CELL ADHESION MOLECULE 1, 120 KDA ISOFORM PRECURSOR. 83985 4.6 5 3 4.34 547 IPI00011134.1 HEAT SHOCK 70 KDA PROTEIN 7. 26907 7.62 5 2 11.74 548 IPI00011515.1 PROTEIN KINASE C AND CASEIN KINASE SUBSTRATE IN NEURONS PROTEIN 1. 50966 4.89 5 3 8.56 549 IPI00012074.1 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN R. 70943 8.32 5 4 7.9 550 IPI00012503.1 SPLICE ISOFORM SAP-MU-0 OF P07602 PROACTIVATOR POLYPEPTIDE PRECURSOR [Contains: SAPOSIN A (PROTEIN A); SAPOSIN B (SPHINGOLIPID ACTIVATOR PROTEIN 1) (SAP-1) (CEREBROSIDE SULFATE ACTIVATOR) (CSACT) (DISPERSIN) (SULFATIDE/GM1 ACTIVATOR); SAPOSIN C (CO-BETA-G 58113 4.82 5 3 6.68 551 IPI00013004.1 SPLICE ISOFORM 1 OF O00764 PYRIDOXAL KINASE. 35102 6.05 5 2 10.26 552 IPI00013894.1 STRESS-INDUCED-PHOSPHOPROTEIN 1. 62639 6.78 5 3 7.73 553 IPI00018853.1 TROPOMYOSIN ISOFORM. 28420 4.59 5 2 7.82 554 IPI00022799.1 SPLICE ISOFORM 2 OF P55087 AQUAPORIN 4. 34830 7.75 5 3 11.15 555 IPI00026781.1 FATTY ACID SYNTHASE (EC 2.3.1.85) [Includes: EC 2.3.1.38; EC 2.3.1.39; EC 2.3.1.41; EC 1.1.1.100; EC 4.2.1.61; EC 1.3.1.10; EC 3.1.2.14]. 273102 6.64 5 3 1.68 556 IPI00027117.1 SIMILAR TO RAN-SPECIFIC GTPASE-ACTIVATING PROTEIN (RAN BINDING PROTEIN 1) (RANBP1). 23351 4.87 5 2 10.95 557 IPI00027569.1 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN C-LIKE DJ845O24.4. 32142 4.67 5 3 11.6 558 IPI00027834.1 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN L. 60187 7.13 5 4 8.24 559 IPI00028946.1 RETICULON PROTEIN 3. 25609 8.76 5 1 4.66 560 IPI00032458.4 SIMILAR TO SODIUM/POTASSIUM-TRANSPORTING ATPASE ALPHA-4 CHAIN (SODIUM PUMP 4) (NA+/K+ ATPASE 4). 110885 5.62 5 2 2.4 561 IPI00032575.1 HYPOTHETICAL PROTEIN. 34793 5.28 5 4 19.17 562 IPI00033600.1 YEAST SDS22 HOMOLOG. 41564 4.55 5 2 8.06 102 563 IPI00064001.2 --none found in database-- 26127 8.44 5 1 5.53 564 IPI00073603.2 SIMILAR TO PEPTIDYL-PRO CIS TRANS ISOMERASE. 23310 7.93 5 3 8.65 565 IPI00076129.3 --none found in database-- 38230 5.25 5 2 6.48 566 IPI00106604.3 SIMILAR TO PEPTIDYL-PRO CIS TRANS ISOMERASE. 19225 8.5 5 2 6.11 567 IPI00161971.1 HYPOTHETICAL PROTEIN. 10870 5.73 5 1 12.63 568 IPI00165677.1 DJ681N20.2 (NOVEL PROTEIN SIMILAR TO FERRITIN, LIGHT POLYPEPTIDE. 20075 5.56 5 3 22.86 569 IPI00168728.1 FLJ00385 PROTEIN. 56111 7.64 5 2 5.89 570 IPI00177423.2 SIMILAR TO RETICULON PROTEIN 3 (NEUROENDOCRINE-SPECIFIC PROTEIN-LIKE 2) (NSP-LIKE PROTEIN II) (NSPLII). 25523 8.76 5 1 4.66 571 IPI00186711.2 SIMILAR TO PLECTIN 1, INTERMEDIATE FILAMENT BINDING PROTEIN, 500KD. 531990 5.76 5 5 1.3 572 IPI00215884.1 SPLICING FACTOR, ARGININE/SERINE-RICH 1 (SPLICING FACTOR 2, ALTERNATE SPLICING FACTOR). 27745 10.77 5 4 16.53 573 IPI00215914.1 ADP-RIBOSYLATION FACTOR 1. 20697 6.8 5 2 19.89 574 IPI00215917.1 ADP-RIBOSYLATION FACTOR 3. 20601 7.6 5 2 19.89 575 IPI00216135.1 SPLICE ISOFORM 3 OF P09493 TROPOMYOSIN 1 ALPHA CHAIN. 32876 4.42 5 2 6.69 576 IPI00216320.1 SPLICE ISOFORM 2 OF O00764 PYRIDOXAL KINASE. 31808 5.82 5 2 11.27 577 IPI00216393.1 SPLICE ISOFORM NON-BRAIN OF P09496 CLATHRIN LIGHT CHAIN A. 23662 4.17 5 4 20.64 578 IPI00217903.2 SIMILAR TO TUBULIN BETA. 21641 4.54 5 2 12.77 579 IPI00218108.1 SPLICE ISOFORM 2 OF Q9UN36 NDRG2 PROTEIN. 39289 5.05 5 5 22.41 580 IPI00218109.1 SPLICE ISOFORM 3 OF Q9UN36 NDRG2 PROTEIN. 39679 5.06 5 5 22.22 581 IPI00218591.1 SPLICE ISOFORM ASF-2 OF Q07955 SPLICING FACTOR, ARGININE/SERINE-RICH 1. 31868 5.7 5 4 14.09 582 IPI00218592.1 SPLICE ISOFORM ASF-3 OF Q07955 SPLICING FACTOR, ARGININE/SERINE-RICH 1. 22329 8.16 5 4 20.5 583 IPI00218919.1 ATPASE, H+/K+ EXCHANGING, ALPHA POLYPEPTIDE. 114091 5.54 5 2 2.71 584 IPI00219824.1 SPLICE ISOFORM SAP-MU-6 OF P07602 PROACTIVATOR POLYPEPTIDE PRECURSOR [Contains: SAPOSIN A (PROTEIN A); SAPOSIN B (SPHINGOLIPID ACTIVATOR PROTEIN 1) (SAP-1) (CEREBROSIDE SULFATE ACTIVATOR) (CSACT) (DISPERSIN) (SULFATIDE/GM1 ACTIVATOR); SAPOSIN C (CO-BETA-G 58356 4.77 5 3 6.65 585 IPI00219825.1 SPLICE ISOFORM SAP-MU-9 OF P07602 PROACTIVATOR POLYPEPTIDE PRECURSOR [Contains: SAPOSIN A (PROTEIN A); SAPOSIN B (SPHINGOLIPID ACTIVATOR PROTEIN 1) (SAP-1) (CEREBROSIDE SULFATE ACTIVATOR) (CSACT) (DISPERSIN) (SULFATIDE/GM1 ACTIVATOR); SAPOSIN C (CO-BETA-G 58484 4.77 5 3 6.64 586 IPI00221098.1 SPLICE ISOFORM 2 OF Q16623 SYNTAXIN 1A. 29632 4.54 5 4 25.77 587 IPI00221099.1 SPLICE ISOFORM 3 OF Q16623 SYNTAXIN 1A. 28995 5.2 5 4 26.69 588 IPI00221189.1 SPLICE ISOFORM 1 OF P55087 AQUAPORIN 4. 32300 6.86 5 3 11.96 589 IPI00239077.1 HISTIDINE TRIAD NUCLEOTIDE BINDING PROTEIN 1. 13802 6.96 5 2 34.92 590 IPI00239540.2 --none found in database-- 36517 4.73 5 1 2.14 591 IPI00243604.2 SIMILAR TO HEAT SHOCK 70KD PROTEIN BINDING PROTEIN. 34413 4.9 5 2 7.47 592 IPI00247185.2 --none found in database-- 30007 9.92 5 3 12.69 593 IPI00247776.2 SIMILAR TO GLUTAMINE SYNTHETASE (GLUTAMATE--AMMONIA LIGASE). 36070 6.44 5 2 6.01 594 IPI00256777.2 --none found in database-- 12235 8.23 5 2 10.81 595 IPI00259350.2 SIMILAR TO ACONITASE 2. 84975 6.98 5 2 3.9 596 IPI00259901.2 SIMILAR TO PEPTIDYLPROLYL ISOMERASE A (CYCLOPHILIN A). 49928 9.15 5 2 7.62 597 IPI00296039.5 SPLICE ISOFORM 4 OF P09493 TROPOMYOSIN 1 ALPHA CHAIN. 32848 4.4 5 2 6.69 598 IPI00299147.4 UBIQUITIN-LIKE PROTEIN SMT3A. 14817 7.62 5 1 8.96 599 IPI00301563.3 RAN-SPECIFIC GTPASE-ACTIVATING PROTEIN. 28792 8.49 5 2 8.73 600 IPI00305457.3 ALPHA-1-ANTITRYPSIN PRECURSOR. 46737 5.31 5 4 15.31 601 IPI00333204.1 --none found in database-- 45209 5 5 2 5.54 602 IPI00333592.1 --none found in database-- 84896 6.47 5 3 5.61 603 IPI00333982.2 HUMAN FULL-LENGTH CDNA CLONE CS0DI019YF20 OF PLACENTA OF HOMO SAPIENS. 57486 8.05 5 2 5.75 604 IPI00375339.2 SPLICE ISOFORM 1 OF Q13733 SODIUM/POTASSIUM-TRANSPORTING ATPASE ALPHA-4 CHAIN. 114166 6.61 5 2 2.33 605 IPI00375381.1 --none found in database-- 20961 4.8 5 1 6.01 606 IPI00376170.1 SIMILAR TO PEPTIDYL-PRO CIS TRANS ISOMERASE. 19942 6.85 5 2 10.33 607 IPI00376651.1 SIMILAR TO SMT3 SUPPRESSOR OF MIF TWO 3 HOMOLOG 2. 10814 7.52 5 1 12.63 608 IPI00377005.1 --none found in database-- 28823 4.45 5 3 13.77 609 IPI00382606.1 FACTOR VII ACTIVE SITE MUTANT IMMUNOCONJUGATE. 75553 7.01 5 2 4.42 610 IPI00383556.1 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN UP2. 24198 7.93 5 3 20.44 611 IPI00383795.1 MUTANT BETA-GLOBIN. 1952 7.36 5 1 44.44 612 IPI00383842.1 HYPOTHETICAL PROTEIN. 18605 9.11 5 1 9.09 103 613 IPI00384653.1 PROTHYMOSIN A14. 11058 3.41 5 2 10.89 614 IPI00395700.1 --none found in database-- 78434 9.06 5 3 6.13 615 IPI00395771.1 PROTEIN PHOSPHATASE-1 REGULATORY SUBUNIT 7 ALPHA2. 36837 4.85 5 2 9.15 616 IPI00395912.1 HYPOTHETICAL PROTEIN. 57156 7.76 5 2 5.76 617 IPI00396462.1 --none found in database-- 20500 5.39 5 2 6.88 618 IPI00003971.1 SPLICE ISOFORM RTN1-A OF Q16799 RETICULON 1. 83618 4.33 4 2 2.32 619 IPI00004618.1 IG GAMMA-4 CHAIN C REGION. 35941 7.41 4 1 4.89 620 IPI00005981.1 NEURONAL PROTEIN. 31454 8 4 3 14.89 621 IPI00007346.1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H. 19208 8.22 4 1 3.39 622 IPI00007812.1 VACUOLAR ATP SYNTHASE SUBUNIT B, BRAIN ISOFORM. 56501 5.55 4 4 13.11 623 IPI00009790.1 6-PHOSPHOFRUCTOKINASE, TYPE C. 85596 7.6 4 3 4.46 624 IPI00011454.1 GLUCOSIDASE II ALPHA SUBUNIT. 109438 6.18 4 4 7.04 625 IPI00013164.1 PERIPHERIN. 53878 5.22 4 2 4.03 626 IPI00014263.1 SPLICE ISOFORM LONG OF Q15056 EUKARYOTIC TRANSLATION INITIATION FACTOR 4H. 27385 7.36 4 2 16.94 627 IPI00014587.1 SPLICE ISOFORM BRAIN OF P09496 CLATHRIN LIGHT CHAIN A. 27077 4.15 4 3 9.68 628 IPI00014898.1 SPLICE ISOFORM 1 OF Q15149 PLECTIN 1. 531737 5.74 4 4 0.98 629 IPI00016666.1 METALLOTHIONEIN-III. 6927 4.5 4 2 47.06 630 IPI00016832.1 SPLICE ISOFORM SHORT OF P25786 PROTEASOME SUBUNIT ALPHA TYPE 1. 29556 6.6 4 3 15.21 631 IPI00017763.3 NUCLEOSOME ASSEMBLY PROTEIN 1-LIKE 4. 42823 4.32 4 2 7.47 632 IPI00018067.1 SYNTAXIN 1B. 33431 5.74 4 3 13.54 633 IPI00019376.1 HYPOTHETICAL PROTEIN FLJ10849. 49398 6.8 4 4 9.32 634 IPI00019755.1 GLUTATHIONE TRANSFERASE OMEGA 1. 27566 6.54 4 2 9.13 635 IPI00019952.1 NEURONAL MEMBRANE GLYCOPROTEIN M6-A. 31210 4.95 4 1 5.04 636 IPI00021840.1 40S RIBOSOMAL PROTEIN S6. 28681 11.52 4 3 9.24 637 IPI00022640.1 NEUROGRANIN. 7618 8.06 4 2 19.23 638 IPI00023860.1 NUCLEOSOME ASSEMBLY PROTEIN 1-LIKE 1. 45374 4.09 4 2 6.91 639 IPI00024129.1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE C. 22763 8.69 4 1 2.83 640 IPI00024993.1 ENOYL-COA HYDRATASE, MITOCHONDRIAL PRECURSOR. 31371 8.19 4 3 18.28 641 IPI00025491.1 EUKARYOTIC INITIATION FACTOR 4A-I. 46154 5.12 4 4 11.08 642 IPI00026154.1 PROTEIN KINASE C SUBSTRATE, 80 KDA PROTEIN, HEAVY CHAIN. 59296 4.05 4 3 5.88 643 IPI00026268.1 GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) BETA SUBUNIT 1. 37377 5.85 4 3 11.47 644 IPI00029623.1 PROTEASOME SUBUNIT ALPHA TYPE 6. 27399 6.74 4 3 14.23 645 IPI00029631.1 ENHANCER OF RUDIMENTARY HOMOLOG. 12259 5.72 4 1 10.58 646 IPI00031141.1 40S RIBOSOMAL PROTEIN SA. 32854 4.51 4 3 16.95 647 IPI00031169.1 RAS-RELATED PROTEIN RAB-2A. 23546 6.51 4 3 19.81 648 IPI00031820.1 PHENYLALANYL-TRNA SYNTHETASE ALPHA CHAIN. 57564 7.96 4 2 4.92 649 IPI00032230.2 SPLICE ISOFORM A OF Q9Y2J2 BAND 4.1-LIKE PROTEIN 3. 120678 4.84 4 3 3.5 650 IPI00032256.1 ALPHA-2-MACROGLOBULIN PRECURSOR. 163278 6.39 4 4 3.19 651 IPI00032808.1 RAS-RELATED PROTEIN RAB-3D. 24267 4.53 4 2 11.87 652 IPI00061114.1 RAS-RELATED PROTEIN RAB-3C. 25952 4.85 4 2 11.45 653 IPI00062037.1 SIMILAR TO RIKEN CDNA 6720463E02 GENE. 10350 7.5 4 3 42.7 654 IPI00107552.1 SIMILAR TO HEAT SHOCK 70KD PROTEIN BINDING PROTEIN. 41305 4.98 4 2 7.05 655 IPI00147581.1 SIMILAR TO PEPTIDYLPROLYL ISOMERASE A (CYCLOPHILIN A). 19853 9.05 4 2 6.67 656 IPI00157890.1 SIMILAR TO PEPTIDYLPROLYL ISOMERASE A. 17712 6.14 4 2 7.55 657 IPI00159927.1 NEUROCAN CORE PROTEIN PRECURSOR. 142973 5.03 4 1 1.59 658 IPI00164538.1 --none found in database-- 15558 6.02 4 1 7.35 659 IPI00167953.3 BTB AND KELCH DOMAIN CONTAINING 3. 69839 5 4 1 1.14 660 IPI00173720.2 --none found in database-- 18469 7.97 4 1 3.59 661 IPI00182986.3 SIMILAR TO HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN C (C1/C2). 32215 4.53 4 2 7.51 662 IPI00183968.1 HYPOTHETICAL PROTEIN FLJ35371. 28223 4.41 4 3 11.52 663 IPI00184471.2 SIMILAR TO DESTRIN - PIG. 11561 4.95 4 2 20.39 664 IPI00215716.1 SPLICE ISOFORM B OF Q9Y2J2 BAND 4.1-LIKE PROTEIN 3. 96514 5.1 4 3 4.62 104 665 IPI00215780.1 40S RIBOSOMAL PROTEIN S19. 21585 11.6 4 3 16.24 666 IPI00215942.1 SPLICE ISOFORM 2 OF Q15149 PLECTIN 1. 518447 5.46 4 4 1.01 667 IPI00215943.1 SPLICE ISOFORM 3 OF Q15149 PLECTIN 1. 518006 5.45 4 4 1.01 668 IPI00217296.1 SPLICE ISOFORM 3 OF Q15257 PROTEIN PHOSPHATASE 2A, REGULATORY SUBUNIT B'. 33481 6.24 4 2 7.14 669 IPI00217872.1 SPLICE ISOFORM 2 OF P36871 PHOSPHOGLUCOMUTASE. 61928 5.72 4 3 7.79 670 IPI00217966.1 LACTATE DEHYDROGENASE A. 36689 8.45 4 3 9.94 671 IPI00218491.1 SPLICE ISOFORM LONG OF P25786 PROTEASOME SUBUNIT ALPHA TYPE 1. 30239 7 4 3 14.87 672 IPI00218493.1 HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE 1. 24579 6.67 4 2 10.55 673 IPI00218728.1 PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE, ISOFORM IB, ALPHA SUBUNIT (45KD). 46638 7.4 4 3 8.54 674 IPI00219328.1 SPLICE ISOFORM 3 OF Q12906 INTERLEUKIN ENHANCER-BINDING FACTOR 3. 82848 8.26 4 3 4.58 675 IPI00219329.1 SPLICE ISOFORM 4 OF Q12906 INTERLEUKIN ENHANCER-BINDING FACTOR 3. 75554 8.58 4 3 5.01 676 IPI00219330.1 SPLICE ISOFORM 5 OF Q12906 INTERLEUKIN ENHANCER-BINDING FACTOR 3. 74653 8.37 4 3 5.07 677 IPI00219525.3 PHOSPHOGLUCONATE DEHYDROGENASE. 53140 7.25 4 3 8.49 678 IPI00219526.2 SPLICE ISOFORM 1 OF P36871 PHOSPHOGLUCOMUTASE. 61318 6.73 4 3 7.84 679 IPI00220894.1 SPLICE ISOFORM SHORT OF Q15056 EUKARYOTIC TRANSLATION INITIATION FACTOR 4H. 25200 8.41 4 2 18.42 680 IPI00221136.3 GLIA MATURATION FACTOR BETA. 16992 6 4 2 18.62 681 IPI00243423.1 SIMILAR TO PEPTIDYL-PRO CIS TRANS ISOMERASE. 17570 8.61 4 2 7.5 682 IPI00248321.4 SIMILAR TO PEPTIDYLPROLYL ISOMERASE A (CYCLOPHILIN A). 23482 7.96 4 3 17.76 683 IPI00258866.2 SIMILAR TO GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE, LIVER (GAPDH). 76394 4.74 4 1 2.01 684 IPI00293102.3 SPLICE ISOFORM 2 OF Q15257 PROTEIN PHOSPHATASE 2A, REGULATORY SUBUNIT B'. 40682 5.8 4 2 5.87 685 IPI00298788.3 SPLICE ISOFORM 1 OF Q12906 INTERLEUKIN ENHANCER-BINDING FACTOR 3. 95384 9.02 4 3 3.91 686 IPI00298789.1 SPLICE ISOFORM 2 OF Q12906 INTERLEUKIN ENHANCER-BINDING FACTOR 3. 76079 7.81 4 3 4.99 687 IPI00300562.2 RAS-RELATED PROTEIN RAB-3B. 24758 4.61 4 2 11.87 688 IPI00301364.2 S-PHASE KINASE-ASSOCIATED PROTEIN 1A ISOFORM B. 18658 4.15 4 2 15.95 689 IPI00301975.1 PLACENTAL RIBONUCLEASE INHIBITOR. 49842 4.44 4 2 8.04 690 IPI00328127.4 VESICLE-ASSOCIATED MEMBRANE PROTEIN 2. 12518 8.48 4 2 28.7 691 IPI00328328.2 EUKARYOTIC INITIATION FACTOR 4A-II. 46394 5.13 4 4 11.06 692 IPI00333105.1 --none found in database-- 33270 8.54 4 3 8.9 693 IPI00333411.5 SPLICE ISOFORM 1 OF Q15257 PROTEIN PHOSPHATASE 2A, REGULATORY SUBUNIT B'. 36789 6.25 4 2 6.5 694 IPI00334738.1 --none found in database-- 21933 6.1 4 2 13.33 695 IPI00374056.1 SIMILAR TO FERRITIN HEAVY CHAIN (FERRITIN H SUBUNIT). 23034 7.28 4 1 4.93 696 IPI00376109.1 SIMILAR TO PROLYL 4-HYDROXYLASE, BETA SUBUNIT. 69727 4.74 4 3 7.96 697 IPI00376531.1 SIMILAR TO PEPTIDYL-PRO CIS TRANS ISOMERASE. 16359 9.41 4 2 8.05 698 IPI00376539.1 SIMILAR TO PEPTIDYL-PRO CIS TRANS ISOMERASE. 12140 8.76 4 1 5.31 699 IPI00376592.1 SIMILAR TO TUC-4B. 16598 9.15 4 1 7.74 700 IPI00382995.1 CYTOPLASMIC PROTEIN NDR1. 39531 7.02 4 4 15.73 701 IPI00383020.1 SIMILAR TO 6-PHOSPHOGLUCONOLACTONASE. 20237 10.32 4 2 22 702 IPI00383111.1 KERATIN 10. 57247 4.72 4 2 5.53 703 IPI00383182.1 PP3895. 14799 8.61 4 2 23.7 704 IPI00383581.1 ALPHA GLUCOSIDASE II ALPHA SUBUNIT. 106874 6.06 4 4 7.2 705 IPI00383751.1 CALRETICULIN=CALCIUM BINDING PROTEIN. 24455 4.17 4 2 19.16 706 IPI00386819.1 VACUOLAR ATP SYNTHASE CATALYTIC SUBUNIT A, OSTEOCLAST ISOFORM. 68178 4.91 4 1 2.44 707 IPI00395027.1 CHONDROITIN SULFATE PROTEOGLYCAN BEHAB/BREVICAN. 71671 4.11 4 2 3.13 708 IPI00395742.1 --none found in database-- 40316 7.22 4 4 15.47 709 IPI00395884.1 --none found in database-- 22145 9.15 4 2 10.61 710 IPI00000861.1 LIM AND SH3 DOMAIN PROTEIN 1. 29717 7.07 3 3 13.79 711 IPI00003348.1 GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) BETA SUBUNIT 2. 37331 5.85 3 2 6.18 712 IPI00003420.1 T-CELL ACTIVATION PROTEIN. 37031 5.28 3 1 3.06 713 IPI00003856.1 VACUOLAR ATP SYNTHASE SUBUNIT E. 26145 8.37 3 1 6.19 714 IPI00004902.1 ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT. 27844 8.31 3 3 12.55 715 IPI00005705.1 SPLICE ISOFORM GAMMA-1 OF P36873 SERINE/THREONINE PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT. 36984 6.5 3 2 10.84 716 IPI00005978.1 SPLICING FACTOR, ARGININE/SERINE-RICH 2. 25575 12.38 3 2 14.93 105 717 IPI00006935.1 EUKARYOTIC TRANSLATION INITIATION FACTOR 5AII. 16793 5.28 3 1 7.84 718 IPI00006980.1 PROTEIN C14ORF166. 28068 6.64 3 2 11.48 719 IPI00008161.2 POTASSIUM-TRANSPORTING ATPASE ALPHA CHAIN 2. 115899 6.52 3 1 1.25 720 IPI00008274.1 ADENYLYL CYCLASE-ASSOCIATED PROTEIN. 51673 8.2 3 3 6.95 721 IPI00008453.1 CORONIN 1C. 53249 7.09 3 2 8.86 722 IPI00008586.1 NEUROGLYCAN C. 57025 4.01 3 1 2.41 723 IPI00009032.1 LUPUS LA PROTEIN. 46837 7.14 3 2 7.6 724 IPI00010204.1 SPLICE ISOFORM LONG OF P23152 SPLICING FACTOR, ARGININE/SERINE-RICH 3. 19330 12.14 3 2 15.85 725 IPI00010470.1 SPLICE ISOFORM SNAP-25B OF P13795 SYNAPTOSOMAL-ASSOCIATED PROTEIN 25. 23315 4.39 3 2 10.68 726 IPI00010740.1 SPLICE ISOFORM LONG OF P23246 SPLICING FACTOR, PROLINE-AND GLUTAMINE- RICH. 76149 9.95 3 2 4.53 727 IPI00011200.2 D-3-PHOSPHOGLYCERATE DEHYDROGENASE. 56650 6.7 3 3 7.88 728 IPI00011253.1 40S RIBOSOMAL PROTEIN S3. 26688 10.26 3 2 10.7 729 IPI00012493.1 40S RIBOSOMAL PROTEIN S20. 13373 10.71 3 2 19.33 730 IPI00013043.1 25 KDA BRAIN-SPECIFIC PROTEIN. 23694 10.12 3 1 7.31 731 IPI00015473.3 EXCITATORY AMINO ACID TRANSPORTER 1. 59572 8.69 3 1 2.21 732 IPI00016342.1 RAS-RELATED PROTEIN RAB-7. 23490 6.59 3 3 18.36 733 IPI00016786.1 SPLICE ISOFORM 2 OF P21181 CELL DIVISION CONTROL PROTEIN 42 HOMOLOG. 21259 6.51 3 3 20.42 734 IPI00017597.1 MICROTUBULE-ASSOCIATED PROTEIN RP/EB FAMILY MEMBER 3. 31982 5.23 3 1 3.56 735 IPI00019329.1 DYNEIN LIGHT CHAIN 1, CYTOPLASMIC. 10366 7.5 3 2 17.98 736 IPI00019599.1 DNA-BINDING PROTEIN (EC 6.3.2.19) (DJ1185N5.1.4) (UBIQUITIN- CONJUGATING ENZYME E2 VARIANT 1. 25797 8.47 3 3 13.12 737 IPI00019901.1 SPLICE ISOFORM 1 OF P35611 ALPHA ADDUCIN. 80955 5.61 3 1 1.36 738 IPI00019982.5 VESICLE-ASSOCIATED MEMBRANE PROTEIN 3. 11178 9.26 3 1 17.17 739 IPI00020356.2 MICROTUBULE-ASSOCIATED PROTEIN 1A (MAP 1A) (PROLIFERATION-RELATED PROTEIN P80) [Contains: MAP1 LIGHT CHAIN LC2]. 306642 4.57 3 3 1.64 740 IPI00021347.1 UBIQUITIN-CONJUGATING ENZYME E2-18 KDA UBCH7. 17862 8.79 3 1 14.29 741 IPI00021842.1 APOLIPOPROTEIN E PRECURSOR. 36154 5.42 3 1 4.73 742 IPI00022007.1 WISKOTT-ALDRICH SYNDROME PROTEIN FAMILY MEMBER 1. 61652 6.43 3 1 1.61 743 IPI00022134.1 PUTATIVE SMALL GTP-BINDING PROTEIN. 18659 10.24 3 1 6.75 744 IPI00022970.1 NUCLEOPROTEIN TPR. 265601 4.72 3 2 0.64 745 IPI00024282.1 RAS-RELATED PROTEIN RAB-8B. 23584 9.54 3 1 5.31 746 IPI00024638.1 CREATINE KINASE, UBIQUITOUS MITOCHONDRIAL PRECURSOR. 47037 8.47 3 2 4.32 747 IPI00024911.1 ENDOPLASMIC RETICULUM PROTEIN ERP29 PRECURSOR. 28993 7.49 3 2 7.66 748 IPI00024989.4 SPLICE ISOFORM 1 OF P22061 PROTEIN-L-ISOASPARTATE(D-ASPARTATE) O- METHYLTRANSFERASE. 27373 8.32 3 2 9.88 749 IPI00025849.1 ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32 FAMILY MEMBER A. 28585 3.72 3 3 16.06 750 IPI00026133.1 PARATHYROID HORMONE RECEPTOR PRECURSOR. 62236 7.09 3 1 1.27 751 IPI00026182.1 CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 2. 32949 5.65 3 3 16.43 752 IPI00026271.1 40S RIBOSOMAL PROTEIN S14. 16273 10.79 3 3 29.14 753 IPI00026546.1 PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB BETA SUBUNIT. 25569 5.8 3 3 28.38 754 IPI00027423.1 SERINE/THREONINE PROTEIN PHOSPHATASE PP1-ALPHA 1 CATALYTIC SUBUNIT. 37512 6.25 3 2 10.61 755 IPI00028481.1 RAS-RELATED PROTEIN RAB-8. 23668 9.54 3 1 5.31 756 IPI00028627.3 P PROTEIN. 92894 7.18 3 1 0.72 757 IPI00029744.1 SINGLE-STRANDED DNA-BINDING PROTEIN, MITOCHONDRIAL PRECURSOR. 17260 10.04 3 2 20.27 758 IPI00029992.2 SIMILAR TO 67 KDA LAMININ RECEPTOR. 30715 4.2 3 2 14.44 759 IPI00030296.1 BM-010. 36153 7.55 3 3 9.94 760 IPI00030363.1 ACETYL-COA ACETYLTRANSFERASE, MITOCHONDRIAL PRECURSOR. 45200 9.21 3 2 7.03 761 IPI00030962.6 DNA-BINDING PROTEIN. 19228 8.45 3 3 17.06 762 IPI00031022.1 SIMILAR TO HEAT SHOCK PROTEIN, 110 KDA. 15689 4.38 3 2 21.62 763 IPI00035033.8 SIMILAR TO RAB12 PROTEIN. 36315 8.57 3 1 3.24 764 IPI00038378.2 E-1 ENZYME. 28933 4.4 3 2 13.03 765 IPI00060801.1 RAS-RELATED PROTEIN RAB-39B. 24622 7.97 3 1 5.16 766 IPI00061178.1 SIMILAR TO RNA BINDING MOTIF PROTEIN, X CHROMOSOME. 42142 10.21 3 3 8.21 767 IPI00069363.1 SIMILAR TO EUKARYOTIC INITIATION FACTOR 5A. 16789 4.61 3 1 7.79 768 IPI00070778.1 --none found in database-- 21273 7.21 3 3 20.42 106 769 IPI00073180.5 RAS-RELATED PROTEIN RAB-37. 24684 6.28 3 1 4.95 770 IPI00098624.1 HYPOTHETICAL PROTEIN KIAA0968. 59022 7.47 3 2 5.88 771 IPI00107625.1 SPLICE ISOFORM SNAP-25A OF P13795 SYNAPTOSOMAL-ASSOCIATED PROTEIN 25. 23336 4.47 3 2 10.68 772 IPI00140696.3 --none found in database-- 30066 8.06 3 3 8.99 773 IPI00144127.2 SIMILAR TO HEAT SHOCK 70KD PROTEIN BINDING PROTEIN. 41649 5.11 3 2 8.13 774 IPI00150205.1 SIMILAR TO OCULOCUTANEOUS ALBINISM II (PINK-EYE DILUTION. 90520 7.26 3 1 0.74 775 IPI00150520.4 --none found in database-- 36881 4.32 3 1 3.15 776 IPI00151594.4 SIMILAR TO KERATIN 8. 58664 7.24 3 2 3.88 777 IPI00163974.2 --none found in database-- 18957 4.14 3 1 7.19 778 IPI00165284.2 HYPOTHETICAL PROTEIN. 44123 4.17 3 1 2.31 779 IPI00169392.2 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE II GAMMA. 66963 8.52 3 2 5.13 780 IPI00172450.1 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE II GAMMA ISOFORM 3. 58365 7.19 3 2 5.98 781 IPI00172452.1 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE II GAMMA ISOFORM 6. 56944 7.31 3 2 6.15 782 IPI00172636.1 HYPOTHETICAL PROTEIN. 54128 7.27 3 2 6.49 783 IPI00176663.2 SIMILAR TO ELONGATION FACTOR 1-ALPHA 1 (EF-1-ALPHA-1) (ELONGATION FACTOR 1 A-1) (EEF1A-1) (ELONGATION FACTOR TU) (EF-TU). 19883 9.66 3 1 4.81 784 IPI00176873.1 --none found in database-- 17875 8.04 3 1 14.29 785 IPI00179415.3 SERINE/THREONINE PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT, ALPHA ISOFORM. 63068 5.82 3 3 5.66 786 IPI00182944.2 SPLICE ISOFORM 3 OF Q13554 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II BETA CHAIN. 54074 7.16 3 2 6.47 787 IPI00183066.2 SPLICE ISOFORM 7 OF Q13554 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II BETA CHAIN. 50955 7.43 3 2 6.9 788 IPI00183356.1 RAS-RELATED PROTEIN RAB-4A. 31568 9.61 3 1 3.81 789 IPI00184363.1 GLYCOLIPID TRANSFER PROTEIN. 23850 7.49 3 1 7.18 790 IPI00185565.6 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN. 56297 7.42 3 2 6.21 791 IPI00187143.1 HYPOTHETICAL PROTEIN. 27506 6.28 3 1 4.44 792 IPI00215638.2 ATP-DEPENDENT RNA HELICASE A. 140877 6.76 3 2 2.28 793 IPI00215715.1 SPLICE ISOFORM B OF Q9UQM7 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II ALPHA CHAIN. 55262 7.65 3 2 6.34 794 IPI00215802.1 SPLICE ISOFORM SHORT OF P23152 SPLICING FACTOR, ARGININE/SERINE-RICH 3. 14203 10.5 3 2 20.97 795 IPI00215983.1 CARBONIC ANHYDRASE I. 28870 7.14 3 2 15.71 796 IPI00216131.1 SPLICE ISOFORM 2 OF P22061 PROTEIN-L-ISOASPARTATE(D-ASPARTATE) O- METHYLTRANSFERASE. 24562 6.51 3 2 11.01 797 IPI00216184.1 SPLICE ISOFORM II OF Q13492 PHOSPHATIDYLINOSITOL-BINDING CLATHRIN ASSEMBLY PROTEIN. 68899 7.72 3 1 1.89 798 IPI00216298.1 THIOREDOXIN. 11693 4.42 3 1 12.38 799 IPI00216311.4 VILLIN 2. 69413 6.17 3 3 6.48 800 IPI00216378.1 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE II GAMMA ISOFORM 1. 62165 7.44 3 2 5.58 801 IPI00216613.1 SPLICE ISOFORM SHORT OF P23246 SPLICING FACTOR, PROLINE-AND GLUTAMINE- RICH. 72263 9.74 3 2 4.78 802 IPI00217236.2 BETA-TUBULIN COFACTOR A. 12855 4.94 3 2 18.52 803 IPI00217297.1 SPLICE ISOFORM 4 OF Q15257 PROTEIN PHOSPHATASE 2A, REGULATORY SUBUNIT B'. 31859 6.42 3 1 2.85 804 IPI00217507.3 NEUROFILAMENT 3 (150KDA MEDIUM). 102448 4.58 3 1 0.98 805 IPI00218084.2 SIMILAR TO EUKARYOTIC INITIATION FACTOR 5A. 16773 4.61 3 1 7.79 806 IPI00218130.1 GLYCOGEN PHOSPHORYLASE. 97092 7.03 3 2 3.33 807 IPI00218187.1 SPLICE ISOFORM GAMMA-2 OF P36873 SERINE/THREONINE PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT. 38518 5.99 3 2 10.39 808 IPI00218236.3 SERINE/THREONINE PROTEIN PHOSPHATASE PP1-BETA CATALYTIC SUBUNIT. 40321 7.23 3 2 9.83 809 IPI00218414.1 CARBONIC ANHYDRASE II. 29246 7.47 3 3 15 810 IPI00219067.1 GLUTATHIONE S-TRANSFERASE M2. 25745 6.29 3 2 14.22 811 IPI00219165.1 SPLICE ISOFORM 2 OF Q13554 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II BETA CHAIN. 56379 7.43 3 2 6.16 812 IPI00219166.1 SPLICE ISOFORM 5 OF Q13554 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II BETA CHAIN. 58009 7.31 3 2 5.98 813 IPI00219205.1 KERATIN 8. 53704 5.26 3 2 4.14 814 IPI00219622.1 PROTEASOME ALPHA 2 SUBUNIT. 25899 7.55 3 1 8.12 815 IPI00219684.1 FATTY ACID BINDING PROTEIN 3. 14858 6.8 3 2 17.29 816 IPI00219812.1 SPLICE ISOFORM RTN1-B OF Q16799 RETICULON 1. 38950 4.9 3 1 3.65 817 IPI00219813.1 SPLICE ISOFORM RTN1-C OF Q16799 RETICULON 1. 23576 9.25 3 1 6.25 818 IPI00220158.1 SPLICE ISOFORM 3 OF P35611 ALPHA ADDUCIN. 84303 5.79 3 1 1.3 819 IPI00220991.1 SIMILAR TO ADAPTOR-RELATED PROTEIN COMPLEX 2, BETA 1 SUBUNIT. 105692 4.98 3 3 4.94 820 IPI00221234.1 ANTIQUITIN. 55366 6.85 3 3 7.44 107 821 IPI00221305.2 SPLICE ISOFORM 4 OF Q13554 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II BETA CHAIN. 72727 7.93 3 2 4.67 822 IPI00233929.2 SIMILAR TO ALDOSE REDUCTASE (AR) (ALDEHYDE REDUCTASE). 35858 8.02 3 2 6.01 823 IPI00237671.1 SIMILAR TO NEUROFILAMENT, LIGHT POLYPEPTIDE 68KDA. 61517 4.32 3 1 1.66 824 IPI00246022.2 --none found in database-- 49438 6.26 3 1 2.64 825 IPI00251507.1 SPLICE ISOFORM SYNAPSIN IB OF P17600 SYNAPSIN I. 69876 10.44 3 3 7.17 826 IPI00253279.1 SPLICE ISOFORM 2 OF P35611 ALPHA ADDUCIN. 69985 6.41 3 1 1.58 827 IPI00259367.2 SIMILAR TO ATPASE, H+ TRANSPORTING, LYSOSOMAL 31KD, V1 SUBUNIT E ISOFORM 1. 26093 8.4 3 1 6.19 828 IPI00259889.2 SIMILAR TO AHCY PROTEIN. 54363 7.48 3 1 2.62 829 IPI00260188.2 SIMILAR TO HEAT SHOCK 70KD PROTEIN BINDING PROTEIN. 38191 5.73 3 1 4.08 830 IPI00290738.1 SPLICE ISOFORM I OF Q13492 PHOSPHATIDYLINOSITOL-BINDING CLATHRIN ASSEMBLY PROTEIN. 70695 7.71 3 1 1.84 831 IPI00290928.2 GUANINE NUCLEOTIDE-BINDING PROTEIN, ALPHA-13 SUBUNIT. 44050 8.13 3 1 2.92 832 IPI00293126.1 TUBULIN-SPECIFIC CHAPERONE B. 27326 4.78 3 3 15.16 833 IPI00294304.4 HISTONE H1.0. 20732 11.6 3 2 11.92 834 IPI00296053.2 FUMARATE HYDRATASE, MITOCHONDRIAL PRECURSOR. 54694 9.17 3 2 6.85 835 IPI00296678.1 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE (CAM KINASE) II GAMMA. 59048 7.77 3 2 5.88 836 IPI00298090.1 SPLICE ISOFORM 6 OF Q13554 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II BETA CHAIN. 55223 7.44 3 2 6.3 837 IPI00299571.2 PROTEIN DISULFIDE ISOMERASE A6 PRECURSOR. 48212 4.7 3 3 9.52 838 IPI00299977.1 14 KDA PHOSPHOHISTIDINE PHOSPHATASE. 13833 5.98 3 2 24.8 839 IPI00300096.2 RAS-RELATED PROTEIN RAB-35. 26927 9.24 3 1 4.64 840 IPI00300568.3 SPLICE ISOFORM SYNAPSIN IA OF P17600 SYNAPSIN I. 73954 10.41 3 3 6.81 841 IPI00302030.2 RAS-RELATED PROTEIN RAB-30. 23058 4.61 3 1 5.42 842 IPI00304802.3 DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL PRECURSOR. 48640 9.19 3 1 3.09 843 IPI00306351.2 ESTERASE D. 31463 7.02 3 1 7.8 844 IPI00306959.5 KERATIN 7. 51419 5.14 3 2 4.26 845 IPI00328744.2 GUANINE NUCLEOTIDE BINDING PROTEIN (G PROTEIN) ALPHA 12. 44251 10.42 3 1 2.89 846 IPI00329441.1 RAB11B. 23339 5.35 3 1 5.19 847 IPI00332724.1 --none found in database-- 38675 8 3 1 2.47 848 IPI00332970.1 SIMILAR TO RAB37, MEMBER OF RAS ONCOGENE FAMILY. 24169 6.36 3 1 5.09 849 IPI00333383.1 ADAPTER-RELATED PROTEIN COMPLEX 2 BETA 1 SUBUNIT. 104553 5.02 3 3 5.02 850 IPI00333769.1 --none found in database-- 29617 8.75 3 3 9.06 851 IPI00333776.1 SPLICE ISOFORM 1 OF Q92823 NEURONAL CELL ADHESION MOLECULE PRECURSOR. 143894 5.37 3 2 1.99 852 IPI00333777.1 SPLICE ISOFORM 2 OF Q92823 NEURONAL CELL ADHESION MOLECULE PRECURSOR. 136618 5.82 3 2 2.1 853 IPI00333778.1 SPLICE ISOFORM 3 OF Q92823 NEURONAL CELL ADHESION MOLECULE PRECURSOR. 130668 5.9 3 2 2.2 854 IPI00333779.1 SPLICE ISOFORM 4 OF Q92823 NEURONAL CELL ADHESION MOLECULE PRECURSOR. 131046 5.6 3 2 2.2 855 IPI00333781.1 SPLICE ISOFORM 5 OF Q92823 NEURONAL CELL ADHESION MOLECULE PRECURSOR. 144379 5.37 3 2 1.99 856 IPI00334174.1 SPLICE ISOFORM 2 OF P11476 RAS-RELATED PROTEIN RAB-1A. 15331 8.3 3 2 17.02 857 IPI00334271.1 SPLICE ISOFORM 1 OF Q13554 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II BETA CHAIN. 60387 7.31 3 2 5.72 858 IPI00334344.1 SPLICE ISOFORM 1 OF Q13555 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II GAMMA CHAIN. 53011 7.38 3 2 6.57 859 IPI00334587.1 SPLICE ISOFORM 2 OF Q99729 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A/B. 35968 6.95 3 1 4.22 860 IPI00334713.1 SPLICE ISOFORM 3 OF Q99729 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A/B. 30588 8.18 3 1 4.91 861 IPI00335789.1 --none found in database-- 73268 7.41 3 2 4.63 862 IPI00336118.1 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE II GAMMA ISOFORM 4. 55961 7.19 3 2 6.26 863 IPI00374126.1 SIMILAR TO 40S RIBOSOMAL PROTEIN SA (P40) (34/67 KDA LAMININ RECEPTOR) (COLON CARCINOMA LAMININ-BINDING PROTEIN) (NEM/1CHD4) (MULTIDRUG RESISTANCE-ASSOCIATED PROTEIN MGR1-AG). 27902 4.62 3 2 9.24 864 IPI00375127.1 SIMILAR TO KIAA0038. 32604 9.23 3 1 4.42 865 IPI00375900.1 SIMILAR TO PROTEIN 40KD. 17887 4.4 3 2 14.02 866 IPI00376220.1 ADDUCIN 1 (ALPHA) ISOFORM D. 73333 6.52 3 1 1.51 867 IPI00376561.1 SIMILAR TO TEMPLATE ACYIVATING FACTOR-I ALPHA. 34608 4.24 3 1 3.28 868 IPI00377060.1 REGULATORY SUBUNIT PR 53 OF PROTEIN PHOSPHATASE 2A ISOFORM C. 15387 7.14 3 1 6.06 869 IPI00377174.1 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE IIB ISOFORM 4. 57938 7.31 3 2 6 870 IPI00377175.1 SIMILAR TO ESTERASE D. 32424 7.49 3 1 7.59 871 IPI00377185.1 CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE II DELTA ISOFORM 2. 54114 7.13 3 2 6.49 872 IPI00382475.1 PNAS-20. 9025 12.05 3 2 21.52 108 873 IPI00382793.1 --none found in database-- 25223 9.28 3 1 6.48 874 IPI00384016.1 HUMAN FULL-LENGTH CDNA 5-PRIME END OF CLONE CS0DJ009YL13 OF T CELLS (JURKAT CELL LINE) OF HOMO SAPIENS. 29625 8.5 3 1 5.02 875 IPI00384121.1 HUMAN FULL-LENGTH CDNA CLONE CS0DC015YM23 OF NEUROBLASTOMA OF HOMO SAPIENS. 36455 5.02 3 3 14.16 876 IPI00384514.1 UEV1BS. 17084 8.01 3 3 19.21 877 IPI00385112.1 SIMILAR TO RAB41. 24162 9.2 3 1 5.12 878 IPI00385140.1 MASA. 23759 4.65 3 2 16.19 879 IPI00385786.1 HYPOTHETICAL PROTEIN FLJ35170. 23195 12.33 3 2 16.42 880 IPI00385962.1 --none found in database-- 37493 6.68 3 3 9.51 881 IPI00386604.1 HYPOTHETICAL PROTEIN. 51774 4.76 3 3 6.55 882 IPI00386803.1 LIM AND SH3 PROTEIN 1. 36014 8.73 3 3 11.15 883 IPI00394706.1 PHAPI PROTEIN. 15325 4.2 3 3 29.85 884 IPI00394880.1 ALPHA GLUCOSIDASE II ALPHA SUBUNIT. 85834 6.22 3 3 6.23 885 IPI00396440.1 SIMILAR TO HYPOTHETICAL PROTEIN. 58871 9.36 3 1 1.1 886 IPI00396468.1 --none found in database-- 42695 6.38 3 2 3.27 887 IPI00396539.1 RAS-RELATED PROTEIN RAB-4B. 23587 5.86 3 1 5.16 888 IPI00000335.1 HIT-17KDA. 17162 9.61 2 1 12.27 889 IPI00000581.1 HSPC263. 31686 4.64 2 2 9.09 890 IPI00000875.1 ELONGATION FACTOR 1-GAMMA. 50119 6.64 2 2 5.26 891 IPI00000949.1 MU-CRYSTALLIN HOMOLOG. 33776 4.79 2 1 6.69 892 IPI00001683.1 SPLICE ISOFORM LONG OF Q9Y5P2 TAXOL RESISTANT ASSOCIATED PROTEIN 3. 14409 10.58 2 1 4.72 893 IPI00001813.3 HYPOTHETICAL PROTEIN KIAA1542. 179055 9.23 2 1 0.42 894 IPI00001816.1 HYPOTHETICAL PROTEIN KIAA1541. 55545 7.47 2 1 2.94 895 IPI00002375.1 TROPOMODULIN 1. 40569 4.74 2 1 3.06 896 IPI00003377.1 SPLICE ISOFORM 1 OF Q16629 SPLICING FACTOR, ARGININE/SERINE-RICH 7. 27367 12.33 2 1 5.88 897 IPI00003391.2 ODZ, ODD OZ/TEN-M HOMOLOG 1. 305245 6.43 2 1 0.18 898 IPI00003935.1 HISTONE H2B.Q. 13789 11 2 2 20.8 899 IPI00004534.3 PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE. 144664 5.55 2 1 1.64 900 IPI00004839.1 CRK-LIKE PROTEIN. 33777 6.73 2 1 3.96 901 IPI00005159.1 ACTIN- LIKE PROTEIN 2. 44761 6.72 2 2 4.57 902 IPI00005250.1 REGULATOR OF G-PROTEIN SIGNALING 17. 24359 5.43 2 1 2.38 903 IPI00005859.1 CYTOKERATIN TYPE II. 59504 7.87 2 1 2.18 904 IPI00006443.1 LAMBDA-CRYSTALLIN HOMOLOG. 34301 6.34 2 1 3.55 905 IPI00007189.1 SPLICE ISOFORM 1 OF P21181 CELL DIVISION CONTROL PROTEIN 42 HOMOLOG. 21311 5.83 2 2 11.52 906 IPI00007423.1 ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32 FAMILY MEMBER B. 28788 3.67 2 2 11.55 907 IPI00007906.1 MYOSIN-REACTIVE IMMUNOGLOBULIN HEAVY CHAIN VARIABLE REGION. 13695 7.24 2 1 4.13 908 IPI00008040.1 PROTEIN-ARGININE DEIMINASE TYPE I. 74607 6.46 2 1 1.36 909 IPI00008433.2 40S RIBOSOMAL PROTEIN S5. 22876 10.31 2 2 15.69 910 IPI00008527.1 60S ACIDIC RIBOSOMAL PROTEIN P1. 11514 3.95 2 1 14.04 911 IPI00009439.1 SYNAPTOTAGMIN I. 47573 8.33 2 2 4.98 912 IPI00009867.1 KERATIN, TYPE II CYTOSKELETAL 5. 62461 8.25 2 1 2.03 913 IPI00010271.1 SPLICE ISOFORM A OF P15154 RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1. 21450 8.65 2 2 12.5 914 IPI00010320.1 CHROMOBOX PROTEIN HOMOLOG 1. 21418 4.57 2 1 5.95 915 IPI00010405.3 SPLICE ISOFORM LONG OF Q01973 TYROSINE-PROTEIN KINASE TRANSMEMBRANE RECEPTOR ROR1 PRECURSOR. 104313 7.17 2 1 0.75 916 IPI00010720.1 T-COMPLEX PROTEIN 1, EPSILON SUBUNIT. 59671 5.34 2 2 6.1 917 IPI00011604.1 GLYCINE CLEAVAGE SYSTEM H PROTEIN, MITOCHONDRIAL PRECURSOR. 18911 4.56 2 1 11.56 918 IPI00011666.2 SIMILAR TO HYPOTHETICAL PROTEIN KIAA0415. 164677 8.46 2 1 0.66 919 IPI00011932.3 SIMILAR TO HEAT SHOCK 70 KDA PROTEIN 12A. 79538 7.41 2 2 3.61 920 IPI00011937.1 PEROXIREDOXIN 4. 30540 6.24 2 1 2.95 921 IPI00012136.1 SPLICE ISOFORM BI-1-GGCAG OF O00555 VOLTAGE-DEPENDENT P/Q-TYPE CALCIUM CHANNEL ALPHA-1A SUBUNIT. 282365 9.1 2 2 0.68 922 IPI00012388.1 TRANSCRIPTION INTERMEDIARY FACTOR 1-BETA. 88550 5.55 2 1 3.59 923 IPI00013075.1 P60 KATANIN. 55965 6.88 2 1 1.02 924 IPI00013157.1 C367G8.3 (NOVEL PROTEIN SIMILAR TO RPL23A. 17508 10.92 2 1 8.33 109 925 IPI00013179.1 PROSTAGLANDIN-H2 D-ISOMERASE PRECURSOR. 21029 7.94 2 2 17.37 926 IPI00013193.1 SPLICE ISOFORM 1 OF Q13402 MYOSIN VIIA. 254406 8.74 2 1 0.23 927 IPI00013698.1 ACID CERAMIDASE PRECURSOR. 44650 7.71 2 2 8.61 928 IPI00013838.1 51C PROTEIN. 126809 9.16 2 1 0.44 929 IPI00013877.2 SPLICE ISOFORM 1 OF P31942 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H3. 36926 6.87 2 2 7.8 930 IPI00013896.1 GUANINE NUCLEOTIDE -BINDING PROTEIN BETA SUBUNIT-LIKE PROTEIN 12.3. 35077 7.77 2 2 7.26 931 IPI00013917.1 40S RIBOSOMAL PROTEIN S12. 14395 6.75 2 1 7.63 932 IPI00014312.1 SPLICE ISOFORM 1 OF Q13618 CULLIN HOMOLOG 3. 88930 8.7 2 1 0.65 933 IPI00014589.1 SPLICE ISOFORM BRAIN OF P09497 CLATHRIN LIGHT CHAIN B. 25190 4.28 2 2 13.97 934 IPI00015029.1 TELOMERASE-BINDING PROTEIN P23. 18697 4.11 2 1 7.5 935 IPI00015141.1 CREATINE KINASE, SARCOMERIC MITOCHONDRIAL PRECURSOR. 47520 8.31 2 1 1.43 936 IPI00015911.1 DIHYDROLIPOAMIDE DEHYDROGENASE, MITOCHONDRIAL PRECURSOR. 54150 7.76 2 1 2.75 937 IPI00016621.2 ADAPTER-RELATED PROTEIN COMPLEX 2 ALPHA 2 SUBUNIT. 105162 6.82 2 2 4.84 938 IPI00016932.1 INOSITOL POLYPHOSPHATE 5-PHOSPHATASE. 138585 6.49 2 1 0.4 939 IPI00017340.5 PLACENTAL THROMBIN INHIBITOR. 42590 4.93 2 2 7.98 940 IPI00017448.1 40S RIBOSOMAL PROTEIN S21. 9111 8.75 2 1 12.05 941 IPI00017596.1 MICROTUBULE-ASSOCIATED PROTEIN RP/EB FAMILY MEMBER 1. 29999 4.76 2 2 10.45 942 IPI00017726.1 SPLICE ISOFORM 1 OF Q99714 3-HYDROXYACYL-COA DEHYDROGENASE TYPE II. 26923 7.94 2 2 14.18 943 IPI00018259.3 GROUP IID SECRETORY PHOSPHOLIPASE A2 PRECURSOR. 16546 8.27 2 1 3.45 944 IPI00018524.1 HISTONE H2A.E. 13805 11.53 2 1 14.96 945 IPI00018534.1 HISTONE H2B.C. 13821 11 2 2 20.8 946 IPI00018952.1 U2 SMALL NUCLEAR RIBONUCLEOPROTEIN AUXILIARY FACTOR 35 KDA SUBUNIT RELATED-PROTEIN 1. 57643 9.9 2 1 1.04 947 IPI00019512.2 SIMILAR TO MYOSIN HEAVY CHAIN, NONMUSCLE TYPE B (CELLULAR MYOSIN HEAVY CHAIN, TYPE B) (NONMUSCLE MYOSIN HEAVY CHAIN-B) (NMMHC-B). 229928 5.25 2 2 0.66 948 IPI00019600.1 MMS2. 16363 8.43 2 2 13.79 949 IPI00019642.1 HYPOTHETICAL PROTEIN KIAA0291. 115837 6.7 2 2 3.06 950 IPI00019927.2 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 7. 37025 6.75 2 1 5.25 951 IPI00020101.1 HISTONE H2B.A/G/K. 13775 11 2 2 20.8 952 IPI00020436.2 RAS-RELATED PROTEIN RAB-11B. 24488 5.73 2 2 9.17 953 IPI00020850.1 SERINE/THREONINE PROTEIN PHOSPHATASE 2A, 55 KDA REGULATORY SUBUNIT B, BETA ISOFORM. 51710 6.4 2 1 3.16 954 IPI00020906.1 INOSITOL-1(OR 4)-MONOPHOSPHATASE. 30189 4.91 2 2 13 955 IPI00020955.1 3-OXO-5-BETA-STEROID 4-DEHYDROGENASE. 37377 7.58 2 1 1.84 956 IPI00021266.1 60S RIBOSOMAL PROTEIN L23A. 17695 11.16 2 1 8.33 957 IPI00021794.2 LYSOSOMAL PROTECTIVE PROTEIN PRECURSOR. 54466 6.59 2 1 1.25 958 IPI00022004.1 SPLICE ISOFORM 2 OF Q92556 ENGULFMENT AND CELL MOTILITY PROTEIN 1. 28742 6.37 2 1 2.43 959 IPI00022082.2 SIMILAR TO SEPTIN KIAA0202B. 84898 9.51 2 1 1.44 960 IPI00022334.1 ORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL PRECURSOR. 48535 7.05 2 1 2.51 961 IPI00022892.2 THY- 1 MEMBRANE GLYCOPROTEIN PRECURSOR. 17935 8.93 2 1 9.32 962 IPI00023591.1 TRANSCRIPTIONAL ACTIVATOR PROTEIN PUR-ALPHA. 34911 6.39 2 1 9.01 963 IPI00023785.2 DEAD BOX POLYPEPTIDE 17 ISOFORM P82. 80272 8.37 2 2 2.74 964 IPI00024157.1 FK506-BINDING PROTEIN 3. 25177 9.96 2 1 4.91 965 IPI00024913.1 SPLICE ISOFORM LONG OF P30042 ES1 PROTEIN HOMOLOG, MITOCHONDRIAL PRECURSOR. 28142 8.4 2 2 13.06 966 IPI00026216.3 PUROMYCIN-SENSITIVE AMINOPEPTIDASE. 103302 5.44 2 2 2.5 967 IPI00026272.1 HISTONE H2A.M. 14041 11.66 2 1 14.73 968 IPI00026516.1 SUCCINYL-COA:3-KETOACID-COENZYME A TRANSFERASE, MITOCHONDRIAL PRECURSOR. 56158 7.52 2 2 4.42 969 IPI00026958.1 SPLICE ISOFORM SHORT OF P22570 NADPH:ADRENODOXIN OXIDOREDUCTASE, MITOCHONDRIAL PRECURSOR. 53809 8.4 2 1 1.02 970 IPI00027139.1 INOSITOL POLYPHOSPHATE 1-PHOSPHATASE. 43998 4.91 2 1 3.01 971 IPI00027464.1 SPLICE ISOFORM 1 OF P06705 CALCINEURIN B SUBUNIT ISOFORM 1. 19169 4.4 2 1 5.92 972 IPI00027487.1 CREATINE KINASE, M CHAIN. 43101 7.28 2 1 1.57 973 IPI00027770.1 SYNAPTOPHYSIN. 33845 4.41 2 2 7.03 974 IPI00027809.1 SPLICE ISOFORM 1 OF P16299 SERINE/THREONINE PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT, BETA ISOFORM. 59024 5.75 2 2 3.44 975 IPI00028006.1 PROTEASOME SUBUNIT BETA TYPE 2. 22836 7.04 2 1 5.47 976 IPI00028508.1 RAS-RELATED PROTEIN RAB-11A. 24394 6.53 2 2 9.26 110 977 IPI00029751.1 SPLICE ISOFORM 1 OF Q12860 CONTACTIN PRECURSOR. 113320 5.69 2 1 0.88 978 IPI00031128.1 SIMILAR TO RIKEN CDNA 2610024G14 GENE. 78458 8.86 2 1 0.72 979 IPI00031562.1 H2A HISTONE FAMILY, MEMBER L. 14121 11.66 2 1 14.62 980 IPI00032234.1 HISTONE H2B. 13890 11 2 2 20.63 981 IPI00033025.1 SEPTIN 7. 48787 9.14 2 2 8.37 982 IPI00033153.1 NUCLEAR RNA EXPORT FACTOR 1. 70182 8.7 2 1 0.81 983 IPI00043499.1 PROBABLE UROCANATE HYDRATASE. 74831 6.78 2 1 0.74 984 IPI00044779.1 TC4 PROTEIN. 12233 9.8 2 2 26.61 985 IPI00045512.1 HEMICENTIN. 613704 6.44 2 1 0.09 986 IPI00048961.2 SIMILAR TO 60S RIBOSOMAL PROTEIN L7A (SURFEIT LOCUS PROTEIN 3) (PLA-X POLYPEPTIDE). 23850 10.75 2 1 5.16 987 IPI00056357.1 HYPOTHETICAL PROTEIN. 18795 6.68 2 1 6.36 988 IPI00059685.1 HYPOTHETICAL PROTEIN. 44004 7.7 2 2 8.74 989 IPI00062003.1 SIMILAR TO ACETYL-COENZYME A ACETYLTRANSFERASE 1. 17201 10.57 2 1 10.49 990 IPI00063234.1 SIMILAR TO PROTEIN KINASE, CAMP-DEPENDENT, REGULATORY, TYPE II, ALPHA. 43067 4.71 2 2 8.9 991 IPI00063472.2 SIMILAR TO PROTEASOME SUBUNIT ALPHA TYPE 6 (PROTEASOME IOTA CHAIN) (MACROPAIN IOTA CHAIN) (MULTICATALYTIC ENDOPEPTIDASE COMPLEX IOTA CHAIN) (27 KDA PROSOMAL PROTEIN) (PROS-27) (P27K). 35186 10.07 2 1 4.19 992 IPI00065073.1 HYPOTHETICAL PROTEIN FLJ25413. 16636 9.01 2 1 4.11 993 IPI00073442.4 SIMILAR TO RIKEN CDNA 1600013K19. 24867 10.82 2 1 2.25 994 IPI00075558.4 SIMILAR TO 60S RIBOSOMAL PROTEIN L7A (SURFEIT LOCUS PROTEIN 3) (PLA-X POLYPEPTIDE). 21549 10.99 2 1 5.85 995 IPI00081836.1 DJ86C11.1. 13906 11.53 2 1 14.84 996 IPI00082404.2 SIMILAR TO 60S RIBOSOMAL PROTEIN L7A (SURFEIT LOCUS PROTEIN 3) (PLA-X POLYPEPTIDE). 21953 11.22 2 1 5.7 997 IPI00088730.3 --none found in database-- 30919 9.18 2 1 2.42 998 IPI00101405.1 FARNESYL DIPHOSPHATE SYNTHASE. 48275 6.02 2 2 7.16 999 IPI00102165.1 H2A HISTONE FAMILY, MEMBER J ISOFORM 1. 16610 10.88 2 1 12.26 1000 IPI00104450.2 SIMILAR TO PHOSPHOSERINE AMINOTRANSFERASE ISOFORM 1. 40331 5.98 2 2 6.78 1001 IPI00145399.2 SIMILAR TO 67 KDA LAMININ RECEPTOR. 27169 4.54 2 1 5.33 1002 IPI00145540.3 SIMILAR TO TROPOMYOSIN 3. 24801 4.17 2 1 6.67 1003 IPI00148061.2 SIMILAR TO LACTATE DEHYDROGENASE 1, A CHAIN. 25626 8.01 2 1 5.13 1004 IPI00151138.1 SIMILAR TO 60S ACIDIC RIBOSOMAL PROTEIN P1. 10091 4.26 2 1 16.67 1005 IPI00152635.1 ADAMTS-17 PRECURSOR. 121100 8.09 2 1 0.46 1006 IPI00152785.1 DJ193B12.2. 13906 11 2 2 20.63 1007 IPI00152906.1 HISTONE H2B.B. 13805 11 2 2 20.8 1008 IPI00154852.1 FLJ00246 PROTEIN. 157811 4.72 2 1 0.4 1009 IPI00156689.1 HYPOTHETICAL PROTEIN. 41920 6.25 2 2 7.89 1010 IPI00163147.4 --none found in database-- 44915 5.01 2 2 4.6 1011 IPI00163328.3 GLYCOGEN PHOSPHORYLASE, LIVER FORM. 97208 7.17 2 1 1.42 1012 IPI00163743.2 HYPOTHETICAL PROTEIN KIAA0169. 195699 6.71 2 2 0.86 1013 IPI00164623.2 COMPLEMENT C3 PRECURSOR [Contains: C3A ANAPHYLATOXIN]. 187235 6.34 2 2 1.56 1014 IPI00165049.1 SIMILAR TO HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 (HELIX- DESTABILIZING PROTEIN) (SINGLE-STRAND BINDING PROTEIN) (HNRNP CORE PROTEIN A1) (HDP-1) (TOPOISOMERASE-INHIBITOR SUPPRESSED). 34495 9.51 2 1 2.18 1015 IPI00166293.1 HYPOTHETICAL PROTEIN FLJ33901. 13908 11 2 2 20.63 1016 IPI00166342.1 HYPOTHETICAL PROTEIN FLJ33648. 27035 5.06 2 1 2.07 1017 IPI00167313.1 HYPOTHETICAL PROTEIN FLJ40089. 65287 9.17 2 1 0.89 1018 IPI00168895.1 FORKHEAD TRANSCRIPTION FACTOR. 18064 7.7 2 1 3.36 1019 IPI00170645.1 HISTONE H2A. 13988 11.55 2 1 14.73 1020 IPI00171874.1 RAS GUANYL RELEASING PROTEIN 3. 78332 6.79 2 1 0.87 1021 IPI00175039.2 SIMILAR TO NEUROFIBROMIN. 78168 7.39 2 1 0.71 1022 IPI00175190.2 SIMILAR TO DJ702J19.1 (GLYCINE CLEAVAGE SYSTEM PROTEIN H (AMINOMETHYL CARRIER)). 18883 4.4 2 1 11.56 1023 IPI00176593.1 SIMILAR TO ACTIN-RELATED PROTEIN 2. 44705 6.33 2 2 4.57 1024 IPI00176610.1 SIMILAR TO UNACTIVE PROGESTERONE RECEPTOR, 23 KD. 18694 4.16 2 1 7.5 1025 IPI00176755.2 SIMILAR TO 60S RIBOSOMAL PROTEIN L23A. 17707 11.16 2 1 8.33 1026 IPI00176799.1 SIMILAR TO HYPOTHETICAL PROTEIN. 85105 4.55 2 2 4.15 1027 IPI00178188.3 DYNEIN LIGHT CHAIN 2B, CYTOPLASMIC. 10855 7.68 2 2 21.88 111 1028 IPI00178416.1 RAS GUANYL RELEASING PROTEIN 3 (CALCIUM AND DAG-REGULATED). 78203 6.79 2 1 0.87 1029 IPI00179437.3 RHO-SPECIFIC GUANINE NUCLEOTIDE EXCHANGE FACTOR P114. 118022 6.74 2 1 0.48 1030 IPI00180277.3 SIMILAR TO KERATIN 8, TYPE II CYTOSKELETAL - HUMAN. 42608 4.46 2 1 2.9 1031 IPI00180671.2 DKFZP564O123 PROTEIN. 30196 10.17 2 1 1.82 1032 IPI00181738.1 PROTEIN PHOSPHATASE 3 CATALYTIC SUBUNIT BETA3. 58081 6.01 2 2 3.5 1033 IPI00182180.1 CGI-77 PROTEIN. 33813 5.93 2 1 1.71 1034 IPI00184845.1 UNCHARACTERIZED HEMATOPOIETIC STEM/PROGENITOR CELLS PROTEIN MDS026. 14995 7.99 2 1 10.22 1035 IPI00185361.3 SIMILAR TO RIKEN CDNA 2810021H22 GENE. 68501 9.89 2 2 1.33 1036 IPI00215717.1 SPLICE ISOFORM C OF Q9Y2J2 BAND 4.1-LIKE PROTEIN 3. 69521 6.16 2 2 4.41 1037 IPI00215753.1 SPLICE ISOFORM 2 OF Q13402 MYOSIN VIIA. 250489 8.87 2 1 0.23 1038 IPI00215756.1 SPLICE ISOFORM 5 OF Q13402 MYOSIN VIIA. 240657 9 2 1 0.24 1039 IPI00215758.1 SPLICE ISOFORM 6 OF Q13402 MYOSIN VIIA. 250982 8.58 2 1 0.23 1040 IPI00215759.1 SPLICE ISOFORM 7 OF Q13402 MYOSIN VIIA. 249977 8.58 2 1 0.23 1041 IPI00215907.1 SPLICE ISOFORM 2 OF Q16629 SPLICING FACTOR, ARGININE/SERINE-RICH 7. 15573 10.08 2 1 10.37 1042 IPI00216106.1 SPLICE ISOFORM 3 OF Q9NTK5 PUTATIVE GTP-BINDING PROTEIN PTD004. 31440 8.01 2 1 5.4 1043 IPI00216313.1 VISININ-LIKE 1. 22142 4.76 2 2 12.04 1044 IPI00216347.1 SPLICE ISOFORM 2B OF Q13409 DYNEIN INTERMEDIATE CHAIN 2, CYTOSOLIC. 70645 4.88 2 2 4.91 1045 IPI00216348.1 SPLICE ISOFORM 2C OF Q13409 DYNEIN INTERMEDIATE CHAIN 2, CYTOSOLIC. 68426 4.95 2 2 5.07 1046 IPI00216349.1 SPLICE ISOFORM 2D OF Q13409 DYNEIN INTERMEDIATE CHAIN 2, CYTOSOLIC. 67552 4.77 2 2 5.12 1047 IPI00216403.1 H4 HISTONE FAMILY, MEMBER C. 11367 11.91 2 1 11.65 1048 IPI00216456.2 HISTONE H2A.L. 13974 11.66 2 1 14.73 1049 IPI00216457.3 H2A HISTONE FAMILY, MEMBER O. 14095 11.55 2 1 14.62 1050 IPI00216459.1 H2B HISTONE FAMILY, MEMBER E. 13989 11 2 2 20.63 1051 IPI00216492.1 SPLICE ISOFORM 2 OF P31942 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H3. 35239 6.87 2 2 8.16 1052 IPI00216493.1 SPLICE ISOFORM 3 OF P31942 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H3. 31525 7.36 2 2 9.09 1053 IPI00216494.1 SPLICE ISOFORM 4 OF P31942 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H3. 22322 5.51 2 2 12.56 1054 IPI00216495.1 SPLICE ISOFORM 5 OF P31942 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H3. 16084 6.39 2 2 18.62 1055 IPI00216496.1 SPLICE ISOFORM 6 OF P31942 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H3. 15413 6.39 2 2 19.42 1056 IPI00216641.1 SPLICE ISOFORM 2 OF Q12860 CONTACTIN PRECURSOR. 111867 5.52 2 1 0.89 1057 IPI00216731.1 H1 HISTONE FAMILY, MEMBER T, TESTIS-SPECIFIC. 22019 12.28 2 1 5.31 1058 IPI00217423.3 HYALURONAN BINDING PROTEIN. 56575 4.13 2 1 1.72 1059 IPI00217442.1 MULTIPLE ANKYRIN REPEATS SINGLE KH DOMAIN PROTEIN ISOFORM 2. 277175 5.69 2 1 0.23 1060 IPI00217469.1 H1 HISTONE FAMILY, MEMBER 1. 21842 11.76 2 1 5.12 1061 IPI00217497.1 SPLICE ISOFORM BI-1(V1) OF O00555 VOLTAGE-DEPENDENT P/Q-TYPE CALCIUM CHANNEL ALPHA-1A SUBUNIT. 256777 8.56 2 2 0.75 1062 IPI00217498.1 SPLICE ISOFORM BI-1(V1)-GGCAG OF O00555 VOLTAGE-DEPENDENT P/Q-TYPE CALCIUM CHANNEL ALPHA-1A SUBUNIT. 282209 9.08 2 2 0.68 1063 IPI00217499.1 SPLICE ISOFORM BI-1(V2) OF O00555 VOLTAGE-DEPENDENT P/Q-TYPE CALCIUM CHANNEL ALPHA-1A SUBUNIT. 280944 8.92 2 2 0.68 1064 IPI00217906.1 SIMILAR TO GUANINE NUCLEOTIDE BINDING PROTEIN (G PROTEIN), ALPHA INHIBITING ACTIVITY POLYPEPTIDE 2. 38473 5.14 2 1 3.54 1065 IPI00218445.1 SPLICE ISOFORM SHORT OF Q9Y5P2 TAXOL RESISTANT ASSOCIATED PROTEIN 3. 12654 10.3 2 1 5.45 1066 IPI00218468.1 SPLICE ISOFORM 2-5 OF P37840 ALPHA-SYNUCLEIN. 13109 4.18 2 1 4.76 1067 IPI00218482.1 SPLICE ISOFORM SHORT OF P30042 ES1 PROTEIN HOMOLOG, MITOCHONDRIAL PRECURSOR. 24729 8.25 2 2 14.77 1068 IPI00218767.1 SPLICE ISOFORM 2 OF P35557 HEXOKINASE D. 52136 4.78 2 1 1.07 1069 IPI00218768.1 SPLICE ISOFORM 3 OF P35557 HEXOKINASE D. 52035 4.88 2 1 1.08 1070 IPI00218862.1 SPLICE ISOFORM 2 OF P16299 SERINE/THREONINE PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT, BETA ISOFORM. 58013 5.34 2 2 3.5 1071 IPI00219005.1 FK506-BINDING PROTEIN 4. 51805 5.11 2 2 7.63 1072 IPI00219153.1 RIBOSOMAL PROTEIN L22 PROPROTEIN. 14787 9.75 2 1 8.59 1073 IPI00219218.2 LACTATE DEHYDROGENASE C. 36253 7.86 2 1 3.61 1074 IPI00219219.1 BETA-GALACTOSIDASE BINDING LECTIN PRECURSOR. 14716 5.15 2 2 22.96 1075 IPI00219304.1 SPLICE ISOFORM 2 OF P06705 CALCINEURIN B SUBUNIT ISOFORM 1. 24979 4.81 2 1 4.63 1076 IPI00219448.1 SPLICE ISOFORM 2 OF O00154 CYTOSOLIC ACYL COENZYME A THIOESTER HYDROLASE. 27041 7 2 2 10.98 1077 IPI00219532.1 SPLICE ISOFORM 1 OF Q92556 ENGULFMENT AND CELL MOTILITY PROTEIN 1. 83829 6.22 2 1 0.83 1078 IPI00219563.1 SPLICE ISOFORM A OF Q9NQ66 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA 1. 138567 6.12 2 1 0.41 1079 IPI00219593.1 PROTEIN KINASE, CAMP-DEPENDENT, REGULATORY, TYPE II, BETA. 46346 4.55 2 1 3.83 112 1080 IPI00219675.1 SPLICE ISOFORM B OF P15154 RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1. 23467 8.82 2 2 11.37 1081 IPI00219774.1 PROTEIN KINASE, CAMP-DEPENDENT, REGULATORY, TYPE II, ALPHA. 45518 4.7 2 2 8.42 1082 IPI00219953.1 UMP-CMP KINASE. 25855 8.1 2 1 6.58 1083 IPI00220067.6 LEUCINE AMINOPEPTIDASE. 56049 7.8 2 2 6.36 1084 IPI00220403.1 H2B HISTONE FAMILY, MEMBER F. 13950 11 2 2 20.63 1085 IPI00220578.1 GUANINE NUCLEOTIDE BINDING PROTEIN (G PROTEIN), ALPHA INHIBITING ACTIVITY POLYPEPTIDE 3. 40532 5.37 2 1 3.39 1086 IPI00220803.1 MARCKS-LIKE PROTEIN. 19529 4.34 2 2 14.36 1087 IPI00220834.4 ATP-DEPENDANT DNA HELICASE II. 82705 5.58 2 2 4.1 1088 IPI00220855.1 SIMILAR TO H2A HISTONE FAMILY, MEMBER O. 14019 11.55 2 1 14.73 1089 IPI00221118.1 SPLICE ISOFORM LONG OF P22570 NADPH:ADRENODOXIN OXIDOREDUCTASE, MITOCHONDRIAL PRECURSOR. 54451 8.33 2 1 1.01 1090 IPI00232721.2 SIMILAR TO NUCLEAR RNA EXPORT FACTOR 2. 102429 8.02 2 1 0.65 1091 IPI00232796.2 SIMILAR TO STRESS-INDUCED-PHOSPHOPROTEIN 1 (STI1) (HSP70/HSP90- ORGANIZING PROTEIN) (TRANSFORMATION-SENSITIVE PROTEIN IEF SSP 3521). 60808 6.66 2 1 2.43 1092 IPI00235690.2 SIMILAR TO TEMPLATE ACYIVATING FACTOR-I ALPHA. 34369 4 2 1 4.38 1093 IPI00239692.1 SIMILAR TO 40S RIBOSOMAL PROTEIN SA (P40) (34/67 KD LAMININ RECEPTOR). 9847 10.06 2 1 14.29 1094 IPI00240020.5 KERATIN, TYPE II CYTOSKELETAL 6A. 59914 8.16 2 1 2.13 1095 IPI00241841.4 KERATIN 6L. 57836 7.22 2 1 2.24 1096 IPI00244083.3 SPLICE ISOFORM 1 OF P35557 HEXOKINASE D. 55643 5.16 2 1 1.01 1097 IPI00246053.1 SIMILAR TO PEPTIDYLPROLYL ISOMERASE A (CYCLOPHILIN A). 24298 8.68 2 2 4.91 1098 IPI00246188.1 SIMILAR TO PEPTIDYL-PRO CIS TRANS ISOMERASE. 18294 8.75 2 2 6.55 1099 IPI00246616.1 HYPOTHETICAL PROTEIN KIAA0291. 112981 6.76 2 2 3.13 1100 IPI00246673.2 SIMILAR TO CYTOKERATIN 8. 59070 5.63 2 1 2.1 1101 IPI00247629.2 SIMILAR TO RPL7A PROTEIN. 51100 10.78 2 1 2.38 1102 IPI00251211.2 SIMILAR TO HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 (HELIX- DESTABILIZING PROTEIN) (SINGLE-STRAND BINDING PROTEIN) (HNRNP CORE PROTEIN A1). 62657 8.01 2 1 1.23 1103 IPI00251464.2 HYPOTHETICAL PROTEIN XP_294997. 33925 6.93 2 1 1.63 1104 IPI00255316.1 HISTONE 1, H2AD. 14107 11.55 2 1 14.62 1105 IPI00257462.2 HISTONE H2B.H. 13805 11 2 2 20.8 1106 IPI00258043.1 --none found in database-- 11621 10.09 2 2 23.81 1107 IPI00259806.2 --none found in database-- 29109 7.13 2 2 8.55 1108 IPI00260178.2 SIMILAR TO KERATIN 8, TYPE II CYTOSKELETAL - HUMAN. 53411 4.87 2 1 2.28 1109 IPI00260388.3 PHD FINGER PROTEIN 2. 121232 9.72 2 1 0.54 1110 IPI00290078.1 KERATIN, TYPE II CYTOSKELETAL 4. 57295 6.55 2 1 2.06 1111 IPI00290416.1 SPLICE ISOFORM 1 OF Q9NTK5 PUTATIVE GTP-BINDING PROTEIN PTD004. 44744 7.99 2 1 3.79 1112 IPI00290566.1 T-COMPLEX PROTEIN 1, ALPHA SUBUNIT. 60344 5.96 2 2 4.5 1113 IPI00291262.2 CLUSTERIN PRECURSOR. 55192 6.57 2 2 4.83 1114 IPI00291347.1 SPLICE ISOFORM BI-1(V2,V3) OF O00555 VOLTAGE-DEPENDENT P/Q-TYPE CALCIUM CHANNEL ALPHA-1A SUBUNIT. 282651 9.1 2 2 0.68 1115 IPI00291373.1 ADRENOLEUKODYSTROPHY PROTEIN. 82909 9.2 2 1 0.67 1116 IPI00291383.1 HEMICENTIN. 613518 6.48 2 1 0.09 1117 IPI00291419.2 CYTOSOLIC ACETOACETYL-COENZYME A THIOLASE. 41296 6.7 2 1 2.77 1118 IPI00291764.1 H2A HISTONE FAMILY, MEMBER C. 14091 11.55 2 1 14.62 1119 IPI00293655.2 ATP-DEPENDENT HELICASE DDX1. 86436 7.04 2 2 3.85 1120 IPI00293665.4 KERATIN, TYPE II CYTOSKELETAL 6B. 59868 8.16 2 1 2.13 1121 IPI00293867.3 D-DOPACHROME TAUTOMERASE. 12712 7.42 2 1 11.02 1122 IPI00294178.1 SERINE/THREONINE PROTEIN PHOSPHATASE 2A, 65 KDA REGULATORY SUBUNIT A, BETA ISOFORM. 66201 4.57 2 1 3 1123 IPI00295542.1 NUCLEOBINDIN 1 PRECURSOR. 53821 4.92 2 2 7.81 1124 IPI00296350.3 KERATIN, TYPE II CYTOSKELETAL 6F. 59936 8.16 2 1 2.13 1125 IPI00297714.1 GAMMA-SYNUCLEIN. 13301 4.62 2 2 22.83 1126 IPI00298306.3 SERINE-PROTEIN KINASE ATM. 350644 6.75 2 1 0.16 1127 IPI00298363.2 FAR UPSTREAM ELEMENT BINDING PROTEIN 2. 72709 8.05 2 2 3.25 1128 IPI00299076.1 RECEPTOR-BINDING CANCER ANTIGEN EXPRESSED ON SISO CELLS. 24377 6.08 2 1 2.35 1129 IPI00299145.4 TYPE II KERATIN K6H. 60025 8.16 2 1 2.13 1130 IPI00299573.4 RIBOSOMAL PROTEIN L7A. 29996 11.32 2 1 4.14 1131 IPI00300725.2 KERATIN, TYPE II CYTOSKELETAL 6C. 60069 8.16 2 1 2.13 113 1132 IPI00301909.3 HYPOTHETICAL PROTEIN. 36629 9.67 2 1 1.57 1133 IPI00302712.1 SPLICE ISOFORM 2A OF Q13409 DYNEIN INTERMEDIATE CHAIN 2, CYTOSOLIC. 71755 4.92 2 2 4.84 1134 IPI00302925.1 T-COMPLEX PROTEIN 1, THETA SUBUNIT. 59621 5.3 2 2 4.01 1135 IPI00303133.3 HISTONE H2B.J. 13761 11 2 2 20.8 1136 IPI00303315.1 H2A HISTONE FAMILY, MEMBER A. 14135 11.66 2 1 14.62 1137 IPI00304490.3 HYPOTHETICAL PROTEIN KIAA1764. 119885 6.17 2 1 0.78 1138 IPI00304692.1 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN G. 42332 10.39 2 2 6.14 1139 IPI00305692.2 THIOREDOXIN-LIKE PROTEIN. 35546 4.88 2 2 11.95 1140 IPI00306301.1 PYRUVATE DEHYDROGENASE E1 COMPONENT ALPHA SUBUNIT, SOMATIC FORM, MITOCHONDRIAL PRECURSOR. 43296 8.14 2 1 3.33 1141 IPI00328202.2 GUANINE NUCLEOTIDE-BINDING PROTEIN G(I), ALPHA-2 SUBUNIT. 40320 5.2 2 1 3.39 1142 IPI00328343.6 PROBABLE ATP-DEPENDENT RNA HELICASE P47. 53243 5.51 2 2 6.44 1143 IPI00329665.2 HISTONE H2B.S. 13813 11.05 2 2 20.8 1144 IPI00329717.3 HISTONE H2B.R. 13773 11 2 2 20.8 1145 IPI00332418.2 RIBOSOMAL PROTEIN L7A. 27358 11.16 2 1 4.56 1146 IPI00332452.3 HYPOTHETICAL PROTEIN FLJ20288. 73616 8.19 2 1 0.87 1147 IPI00332511.4 SERINE/THREONINE PROTEIN PHOSPHATASE 2A, 55 KDA REGULATORY SUBUNIT B, ALPHA ISOFORM. 58255 7.23 2 1 2.76 1148 IPI00333841.3 SEPTIN KIAA0202D. 52498 6.66 2 1 2.43 1149 IPI00334168.1 --none found in database-- 49350 4.85 2 1 2.49 1150 IPI00335053.1 --none found in database-- 37874 9.99 2 1 1.98 1151 IPI00335449.1 PROTEIN PHOSPHATASE 2 (FORMERLY 2A), REGULATORY SUBUNIT A (PR 65), BETA ISOFORM. 73585 4.69 2 1 2.7 1152 IPI00336094.1 SPLICE ISOFORM 2 OF Q99714 3-HYDROXYACYL-COA DEHYDROGENASE TYPE II. 25984 7.29 2 2 14.68 1153 IPI00337415.1 GUANINE NUCLEOTIDE-BINDING PROTEIN G(I), ALPHA-1 SUBUNIT. 41147 6.27 2 1 3.32 1154 IPI00339230.1 SPLICE ISOFORM 3 OF Q16629 SPLICING FACTOR, ARGININE/SERINE-RICH 7. 15257 9.88 2 1 10.61 1155 IPI00339285.1 HISTONE H2B.N. 13776 10.89 2 2 20.8 1156 IPI00373922.1 SIMILAR TO 60S RIBOSOMAL PROTEIN L7A (SURFEIT LOCUS PROTEIN 3) (PLA-X POLYPEPTIDE). 27765 11.35 2 1 4.49 1157 IPI00373935.1 SIMILAR TO 40S RIBOSOMAL PROTEIN SA (P40) (34/67 KDA LAMININ RECEPTOR) (COLON CARCINOMA LAMININ-BINDING PROTEIN) (NEM/1CHD4) (MULTIDRUG RESISTANCE-ASSOCIATED PROTEIN MGR1-AG). 30638 4.43 2 2 13.5 1158 IPI00374199.1 SIMILAR TO TROPOMYOSIN 3. 19174 4.45 2 1 8.24 1159 IPI00374249.1 SIMILAR TO ENSANGP00000025329. 26487 10.87 2 1 4.7 1160 IPI00374259.1 ATAXIA TELANGIECTASIA MUTATED PROTEIN ISOFORM 2. 195978 6.75 2 1 0.29 1161 IPI00374876.1 HYPOTHETICAL PROTEIN XP_353305. 21818 10.24 2 1 2.65 1162 IPI00375843.1 HYPOTHETICAL PROTEIN DKFZP686J1375. 54176 5.05 2 1 2.26 1163 IPI00376041.1 HYPOTHETICAL PROTEIN. 63446 4.69 2 1 0.89 1164 IPI00376493.1 PHD FINGER PROTEIN 2 ISOFORM B. 120992 10.07 2 1 0.54 1165 IPI00376647.1 SIMILAR TO PEPTIDYLPROLYL ISOMERASE A. 17978 6.27 2 2 6.96 1166 IPI00376664.1 SIMILAR TO PEPTIDYLPROLYL ISOMERASE A. 14624 6.08 2 2 8.15 1167 IPI00376688.1 N-ACYLSPHINGOSINE AMIDOHYDROLASE (ACID CERAMIDASE) 1 ISOFORM B. 46494 7.97 2 2 8.27 1168 IPI00376972.1 BETA ISOFORM OF REGULATORY SUBUNIT B55, PROTEIN PHOSPHATASE 2 ISOFORM B. 52017 7.02 2 1 3.14 1169 IPI00376973.1 BETA ISOFORM OF REGULATORY SUBUNIT B55, PROTEIN PHOSPHATASE 2 ISOFORM C. 49333 6.7 2 1 3.31 1170 IPI00376974.1 BETA ISOFORM OF REGULATORY SUBUNIT B55, PROTEIN PHOSPHATASE 2 ISOFORM D. 50371 6.58 2 1 3.24 1171 IPI00376997.1 HISTONE H2B.L. 13805 11 2 2 20.8 1172 IPI00377199.1 HISTONE H2B.D. 17842 11.46 2 2 16.46 1173 IPI00382458.1 SPLICE ISOFORM 2 OF Q13618 CULLIN HOMOLOG 3. 86234 8.1 2 1 0.67 1174 IPI00382459.1 SPLICE ISOFORM 3 OF Q13618 CULLIN HOMOLOG 3. 81093 8.72 2 1 0.71 1175 IPI00382480.1 IG HEAVY CHAIN V-III REGION BRO. 13227 6.49 2 1 4.17 1176 IPI00382536.1 IG HEAVY CHAIN V-II REGION MCE. 13792 8.76 2 1 4 1177 IPI00382725.1 CEI-A PROTEIN PRECURSOR. 19292 11.9 2 1 2.81 1178 IPI00383317.1 PRO2275. 13097 9.66 2 1 15 1179 IPI00383853.1 HYPOTHETICAL PROTEIN. 40660 7.4 2 2 5.48 1180 IPI00384339.2 KATNA1 PROTEIN. 41120 10.09 2 1 1.38 1181 IPI00384365.1 SIMILAR TO CHROMOSOME 8 OPEN READING FRAME 2. 25355 8.57 2 1 3.93 1182 IPI00384536.1 HYPOTHETICAL PROTEIN KIAA1764. 108166 5.6 2 1 0.86 1183 IPI00385149.1 HYPOTHETICAL PROTEIN. 14577 3.63 2 2 10.29 114 1184 IPI00385216.1 LAMBDA-CRYSTALLIN. 35419 6.1 2 1 3.45 1185 IPI00385314.1 TRIM28 PROTEIN. 79474 5.85 2 1 3.98 1186 IPI00385447.1 DJ224A6.1.2 (CELL DIVISION CYCLE 42. 26643 6.51 2 2 9.44 1187 IPI00385928.1 HYPOTHETICAL PROTEIN FLJ90472. 78431 8.86 2 1 0.72 1188 IPI00386438.2 KERATIN, TYPE II CYTOSKELETAL 6D. 42468 5.05 2 1 3.13 1189 IPI00394837.1 RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 ISOFORM RAC1C. 16797 9.23 2 2 16.22 1190 IPI00395319.1 HYPOTHETICAL PROTEIN KIAA1595. 54113 10 2 2 1.7 1191 IPI00395561.1 SPLICE ISOFORM B OF Q9NQ66 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA 1. 133703 6.35 2 1 0.43 1192 IPI00000051.2 PREFOLDIN SUBUNIT 1. 14210 6.81 1 1 9.02 1193 IPI00000494.1 MSTP030. 34363 10.21 1 1 4.71 1194 IPI00000534.2 SIMILAR TO KIAA1671 PROTEIN. 193711 8.64 1 1 0.28 1195 IPI00000760.1 NG,NG-DIMETHYLARGININE DIMETHYLAMINOHYDROLASE 2. 29644 5.9 1 1 5.61 1196 IPI00001348.4 HYPOTHETICAL PROTEIN KIAA0542. 144083 11.42 1 1 0.41 1197 IPI00002135.1 TRANSFORMING ACIDIC COILED-COIL-CONTAINING PROTEIN 3. 90360 4.69 1 1 0.6 1198 IPI00002647.2 WISKOTT-ALDRICH SYNDROME PROTEIN FAMILY MEMBER 4. 68189 6.68 1 1 1.12 1199 IPI00002949.5 --none found in database-- 52314 4.93 1 1 2.77 1200 IPI00003327.1 ADP-RIBOSYLATION FACTOR-LIKE PROTEIN 3. 20456 7.35 1 1 12.09 1201 IPI00003399.1 TYPE II MEMBRANE PROTEIN. 20652 4.55 1 1 8.79 1202 IPI00004203.5 HYPOTHETICAL PROTEIN FLJ22059. 98900 8.11 1 1 0.78 1203 IPI00004290.1 HYPOTHETICAL PROTEIN DJ434O14.5. 87055 5.72 1 1 0.66 1204 IPI00004408.1 SPLICE ISOFORM 2 OF Q9UEY8 GAMMA ADDUCIN. 79155 6.26 1 1 1.7 1205 IPI00004450.1 TESTES SPECIFIC HETEROGENOUS NUCLEAR RIBONUCLEOPROTEIN G-T. 42784 10.72 1 1 3.57 1206 IPI00004488.1 VACUOLAR ATP SYNTHASE SUBUNIT F. 13358 5.19 1 1 10.08 1207 IPI00004501.1 SPLICE ISOFORM 1 OF P11277 SPECTRIN BETA CHAIN, ERYTHROCYTE. 246322 4.9 1 1 0.47 1208 IPI00004557.3 SIMILAR TO KIAA0367. 315796 4.05 1 1 0.17 1209 IPI00004656.1 BETA-2-MICROGLOBULIN PRECURSOR. 13715 6.51 1 1 8.4 1210 IPI00004838.1 SPLICE ISOFORM CRK-II OF P46108 PROTO-ONCOGENE C-CRK. 33872 5.44 1 1 5.59 1211 IPI00004924.1 DEF-6 PROTEIN. 73910 5.89 1 1 1.58 1212 IPI00005198.1 NF45 PROTEIN. 44697 8.32 1 1 2.71 1213 IPI00005474.3 PHOSPHOLYSINE PHOSPHOHISTIDINE INORGANIC PYROPHOSPHATE PHOSPHATASE. 29193 6.36 1 1 7.78 1214 IPI00005589.1 WUGSC:H_DJ0844F09.1 PROTEIN. 15751 11.6 1 1 9.63 1215 IPI00005646.1 HYPOTHETICAL PROTEIN KIAA0635. 99213 5.64 1 1 1.06 1216 IPI00005824.1 VELI 1. 25997 9.1 1 1 6.87 1217 IPI00005969.1 F-ACTIN CAPPING PROTEIN ALPHA-1 SUBUNIT. 32923 5.42 1 1 5.94 1218 IPI00006079.1 HYPOTHETICAL PROTEIN KIAA0164. 106122 10.61 1 1 1.96 1219 IPI00006158.1 LYMPHOID-RESTRICTED MEMBRANE PROTEIN. 62093 5.74 1 1 1.44 1220 IPI00006254.1 PERIPHERAL BENZODIAZEPINE RECEPTOR INTERACTING PROTEIN. 200150 4.78 1 1 0.27 1221 IPI00006328.1 ATPASE INHIBITOR, MITOCHONDRIAL PRECURSOR. 12249 10.05 1 1 9.43 1222 IPI00006504.1 SPLICE ISOFORM 1 OF Q9NR50 TRANSLATION INITIATION FACTOR EIF-2B GAMMA SUBUNIT. 50240 6.41 1 1 1.11 1223 IPI00007087.1 F-BOX ONLY PROTEIN 2. 33257 4.01 1 1 4.07 1224 IPI00007834.1 SPLICE ISOFORM 1 OF Q01484 ANKYRIN 2. 430344 4.77 1 1 0.2 1225 IPI00007847.1 UEV1AS. 11842 9.46 1 1 8.74 1226 IPI00007926.1 RCL. 19108 4.69 1 1 9.77 1227 IPI00008055.1 HYPOTHETICAL PROTEIN KIAA1285. 87733 6 1 1 0.51 1228 IPI00008200.1 HYPOTHETICAL PROTEIN KIAA1197. 157165 9.54 1 1 0.54 1229 IPI00008332.1 MYELIN TRANSCRIPTION FACTOR 1. 122329 4.53 1 1 0.89 1230 IPI00008418.1 SPLICE ISOFORM 1 OF Q9NR28 SMAC PROTEIN, MITOCHONDRIAL PRECURSOR. 27131 5.72 1 1 5.02 1231 IPI00008511.1 NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5. 67027 9.32 1 1 1.16 1232 IPI00008524.1 POLYADENYLATE-BINDING PROTEIN 1. 70671 10 1 1 1.73 1233 IPI00008998.1 HSPC121. 44423 9.47 1 1 5.63 1234 IPI00009159.2 SIMILAR TO 40S RIBOSOMAL PROTEIN S6 (PHOSPHOPROTEIN NP33). 28425 10.82 1 1 2.38 1235 IPI00009227.2 BCL-2-ASSOCIATED TRANSCRIPTION FACTOR SHORT FORM. 100216 10.57 1 1 2.07 115 1236 IPI00009328.2 PROBABLE ATP-DEPENDENT HELICASE DDX48. 46871 6.69 1 1 1.95 1237 IPI00009468.3 SIMILAR TO VACUOLAR PROTEIN SORTING 35. 140263 7.25 1 1 0.8 1238 IPI00009887.1 SPLICE ISOFORM 2 OF Q9HBY8 SERINE/THREONINE-PROTEIN KINASE SGK2. 47604 7.5 1 1 1.17 1239 IPI00009922.1 DC50. 12349 11 1 1 5.5 1240 IPI00009995.2 ETS TRANSCRIPTION FACTOR. 62711 6.68 1 1 0.86 1241 IPI00010270.1 RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 2. 21429 7.7 1 1 5.21 1242 IPI00010402.1 SH3 DOMAIN-BINDING GLUTAMIC ACID-RICH-LIKE PROTEIN 3. 10438 4.56 1 1 10.75 1243 IPI00010415.2 SPLICE ISOFORM 1 OF O00154 CYTOSOLIC ACYL COENZYME A THIOESTER HYDROLASE. 41796 8.66 1 1 3.16 1244 IPI00010420.1 HYPOTHETICAL PROTEIN. 35022 10.46 1 1 3.49 1245 IPI00010496.1 HYPOTHETICAL PROTEIN KIAA1045. 48030 5.88 1 1 3.98 1246 IPI00010970.2 HYPOTHETICAL PROTEIN KIAA1617. 101667 6.68 1 1 0.55 1247 IPI00011274.1 JKTBP2. 46438 9.98 1 1 3.81 1248 IPI00011603.2 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 3. 60978 8.75 1 1 0.94 1249 IPI00011702.2 PROTEIN KIAA0406. 122069 5.85 1 1 0.92 1250 IPI00011730.2 SIMILAR TO ELASTIN MICROFIBRIL INTERFACE LOCATED PROTEIN 5. 82647 7.76 1 1 0.78 1251 IPI00011964.1 ADDUCIN 2 ISOFORM F. 56350 5.3 1 1 2.38 1252 IPI00011982.1 ADDUCIN 2 ISOFORM G. 46168 5.26 1 1 2.91 1253 IPI00012341.1 SPLICE ISOFORM SRP40-1 OF Q13243 SPLICING FACTOR, ARGININE/SERINE-RICH 5. 31264 12.1 1 1 1.84 1254 IPI00012345.2 SPLICE ISOFORM SRP55-1 OF Q13247 SPLICING FACTOR, ARGININE/SERINE-RICH 6. 39587 11.94 1 1 2.62 1255 IPI00012441.1 SPLICE ISOFORM 1 OF O43426 SYNAPTOJANIN 1. 173346 7.44 1 1 0.83 1256 IPI00012451.1 GUANINE NUCLEOTIDE-BINDING PROTEIN BETA SUBUNIT 4. 37567 5.85 1 1 2.94 1257 IPI00012682.1 SIMILAR TO DEATH-ASSOCIATED PROTEIN. 11880 10.72 1 1 7.48 1258 IPI00012751.1 40S RIBOSOMAL PROTEIN S28. 7841 11.33 1 1 13.04 1259 IPI00012893.2 SPLICE ISOFORM 1 OF O43566 REGULATOR OF G-PROTEIN SIGNALING 14. 64601 9.25 1 1 0.67 1260 IPI00013290.1 SIMILAR TO HEPATOMA-DERIVED GROWTH FACTOR, RELATED PROTEIN 2. 74230 7.62 1 1 2.24 1261 IPI00013296.1 40S RIBOSOMAL PROTEIN S18. 17719 11.6 1 1 7.24 1262 IPI00013396.1 U1 SMALL NUCLEAR RIBONUCLEOPROTEIN C. 17394 10.14 1 1 7.55 1263 IPI00013415.1 40S RIBOSOMAL PROTEIN S7. 22127 10.86 1 1 11.34 1264 IPI00013485.1 40S RIBOSOMAL PROTEIN S2. 31324 10.9 1 1 4.44 1265 IPI00013860.1 3-HYDROXYISOBUTYRATE DEHYDROGENASE, MITOCHONDRIAL PRECURSOR. 35329 8.26 1 1 5.65 1266 IPI00013888.1 INTEGRAL MEMBRANE PROTEIN 2A. 29741 5.49 1 1 1.52 1267 IPI00013949.1 SMALL GLUTAMINE-RICH TETRATRICOPEPTIDE REPEAT-CONTAINING PROTEIN. 34063 4.51 1 1 2.88 1268 IPI00014151.1 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 6. 45531 5.29 1 1 3.86 1269 IPI00014439.1 DIHYDROPTERIDINE REDUCTASE. 25804 7.45 1 1 7.38 1270 IPI00014455.3 R31167_1, PARTIAL PROTEIN. 53887 5.07 1 1 1 1271 IPI00014537.1 SPLICE ISOFORM 1 OF O43852 CALUMENIN PRECURSOR. 37107 4.23 1 1 3.49 1272 IPI00014754.3 SIMILAR TO 40S RIBOSOMAL PROTEIN SA (P40) (34/67 KDA LAMININ RECEPTOR) (COLON CARCINOMA LAMININ-BINDING PROTEIN) (NEM/1CHD4) (MULTIDRUG RESISTANCE-ASSOCIATED PROTEIN MGR1-AG). 23486 4.21 1 1 2.83 1273 IPI00014925.1 ATP-DEPENDENT DNA HELICASE Q4. 133077 8.12 1 1 0.83 1274 IPI00015018.1 INORGANIC PYROPHOSPHATASE. 32660 5.64 1 1 3.46 1275 IPI00015115.1 SIMILAR TO AC45. 25310 9.99 1 1 4.46 1276 IPI00015148.3 RAS-RELATED PROTEIN RAP-1B. 20825 5.39 1 1 6.52 1277 IPI00015157.1 HYPOTHETICAL PROTEIN. 16313 10.38 1 1 9.03 1278 IPI00015180.1 APICAL-LIKE PROTEIN. 176410 7.09 1 1 0.37 1279 IPI00015351.1 AD039. 24178 5.56 1 1 4.27 1280 IPI00015526.2 SPLICE ISOFORM 1 OF Q9H9B1 HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-9 SPECIFIC 5. 138182 5.83 1 1 0.39 1281 IPI00015730.1 PROSTAGLANDIN F2-ALPHA RECEPTOR. 40055 9.11 1 1 1.67 1282 IPI00015826.1 ATP-BINDING CASSETTE, SUB-FAMILY B, MEMBER 10, MITOCHONDRIAL PRECURSOR. 79099 10.41 1 1 0.81 1283 IPI00015891.1 PREFOLDIN SUBUNIT 4. 15314 4.15 1 1 8.96 1284 IPI00015973.1 BAND 4.1-LIKE PROTEIN 2. 112588 5.13 1 1 1 1285 IPI00016456.1 ADENOVIRUS 5 E1A-BINDING PROTEIN. 66203 8.3 1 1 1.6 1286 IPI00016664.1 FORKHEAD BOX PROTEIN E2. 52389 11.25 1 1 1 1287 IPI00016734.1 HOMEOBOX PROTEIN ENGRAILED-1. 40101 10.09 1 1 1.28 116 1288 IPI00016768.1 L-LACTATE DEHYDROGENASE A-LIKE. 41943 8.89 1 1 1.57 1289 IPI00016783.1 NUCLEAR TRANSITION PROTEIN 2. 15641 12.14 1 1 4.35 1290 IPI00017025.2 SIMILAR TO PEPTIDYL-PRO CIS TRANS ISOMERASE. 21072 7.74 1 1 2.55 1291 IPI00017297.1 MATRIN 3. 94623 6.19 1 1 2.48 1292 IPI00017367.1 RADIXIN. 68564 6.3 1 1 1.54 1293 IPI00017704.1 COACTOSIN-LIKE PROTEIN. 15945 5.31 1 1 11.27 1294 IPI00017870.1 BA13B9.3. 55152 4.55 1 1 1.8 1295 IPI00018195.1 MITOGEN-ACTIVATED PROTEIN KINASE 3. 43136 6.74 1 1 3.96 1296 IPI00018214.1 SPLICE ISOFORM 1 OF P25912 MAX PROTEIN. 18275 6.25 1 1 6.25 1297 IPI00018262.1 ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32 FAMILY MEMBER C. 26762 3.86 1 1 4.7 1298 IPI00018272.1 PYRIDOXINE-5'-PHOSPHATE OXIDASE. 29988 7.09 1 1 3.45 1299 IPI00018342.2 ADENYLATE KINASE ISOENZYME 1. 21635 8.99 1 1 7.22 1300 IPI00018398.2 26S PROTEASE REGULATORY SUBUNIT 6A. 49204 4.87 1 1 3.19 1301 IPI00018465.1 T-COMPLEX PROTEIN 1, ETA SUBUNIT. 59367 7.73 1 1 2.58 1302 IPI00018590.1 SIMILARITY BY BLASTN TO AF063018. 40925 9.71 1 1 1.63 1303 IPI00018693.1 OLFACTORY RECEPTOR 1Q1. 35616 8.96 1 1 1.59 1304 IPI00018768.1 TRANSLIN. 26183 6.41 1 1 5.26 1305 IPI00018871.1 HYPOTHETICAL PROTEIN FLJ10702. 21539 8.62 1 1 12.37 1306 IPI00018931.2 VACUOLAR PROTEIN SORTING 35. 91707 5.17 1 1 1.26 1307 IPI00018963.1 SPLICE ISOFORM 1 OF Q9NVD7 ALPHA-PARVIN. 42244 5.74 1 1 1.34 1308 IPI00019171.1 SH3-CONTAINING GRB2-LIKE PROTEIN 2. 39962 5.14 1 1 4.55 1309 IPI00019345.1 RAS-RELATED PROTEIN RAP-1A. 20987 6.55 1 1 6.52 1310 IPI00019355.1 REGULATORY PROTEIN TSC-22. 15680 4.87 1 1 8.33 1311 IPI00019884.1 ALPHA-ACTININ 2. 103854 5.13 1 1 1.68 1312 IPI00019904.1 SPLICE ISOFORM 1 OF P35612 BETA ADDUCIN. 80854 5.73 1 1 1.65 1313 IPI00019997.1 HYPOTHETICAL PROTEIN FLJ11215. 21834 8.7 1 1 8.12 1314 IPI00020008.1 UBIQUITIN-LIKE PROTEIN NEDD8. 9072 9 1 1 17.28 1315 IPI00020075.1 HYPOTHETICAL PROTEIN FLJ11342. 33933 8.77 1 1 6.21 1316 IPI00020273.1 ATP-SENSITIVE INWARD RECTIFIER POTASSIUM CHANNEL 10. 42508 8.2 1 1 1.32 1317 IPI00020546.1 ASH1. 332768 9.95 1 1 0.2 1318 IPI00021034.1 COLLAGEN ALPHA 1(IV) CHAIN PRECURSOR. 160611 8.42 1 1 0.3 1319 IPI00021122.1 OLFACTORY RECEPTOR 17-1. 32021 10.42 1 1 2.02 1320 IPI00021338.1 DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL PRECURSOR. 65781 5.95 1 1 2.44 1321 IPI00021396.1 VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2 PRECURSOR. 151527 5.64 1 1 0.37 1322 IPI00021435.1 PROTEASOME 26S ATPASE SUBUNIT 2. 48634 5.65 1 1 2.54 1323 IPI00021808.1 HISTIDYL-TRNA SYNTHETASE. 57410 5.56 1 1 0.98 1324 IPI00021819.1 CYTOCHROME P450 2D6. 55802 7.26 1 1 1.21 1325 IPI00021885.1 SPLICE ISOFORM ALPHA-E OF P02671 FIBRINOGEN ALPHA/ALPHA-E CHAIN PRECURSOR [Contains: FIBRINOPEPTIDE A]. 94973 5.87 1 1 1.73 1326 IPI00021954.1 GOLGI-SPECIFIC BREFELDIN A-RESISTANCE GUANINE NUCLEOTIDE EXCHANGE FACTOR 1. 206446 5.5 1 1 0.32 1327 IPI00022326.1 OLFACTORY RECEPTOR 10A5. 35519 8.94 1 1 1.58 1328 IPI00022432.1 TRANSTHYRETIN PRECURSOR. 15887 5.58 1 1 8.84 1329 IPI00023004.2 EUKARYOTIC TRANSLATION INITIATION FACTOR 1A, Y-CHROMOSOMAL. 16311 4.84 1 1 7.69 1330 IPI00023048.2 ELONGATION FACTOR 1-DELTA. 31122 4.63 1 1 3.2 1331 IPI00023138.1 RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 3. 21379 8.27 1 1 5.21 1332 IPI00023258.2 SIMILAR TO TRANSCRIPTION INITIATION FACTOR TFIID 105 KDA SUBUNIT (TAFII- 105) (TAFII105). 101928 9.88 1 1 0.73 1333 IPI00023601.1 PROTEOGLYCAN LINK PROTEIN PRECURSOR. 40166 7.45 1 1 3.39 1334 IPI00024664.1 SPLICE ISOFORM LONG OF P45974 UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 5. 95786 4.65 1 1 1.86 1335 IPI00024670.2 POLYPOSIS LOCUS PROTEIN 1. 21133 8.29 1 1 5.95 1336 IPI00024920.1 ATP SYNTHASE DELTA CHAIN, MITOCHONDRIAL PRECURSOR. 17490 5.19 1 1 8.33 1337 IPI00025084.1 CALCIUM-DEPENDENT PROTEASE, SMALL SUBUNIT. 28316 4.82 1 1 8.58 1338 IPI00025329.1 60S RIBOSOMAL PROTEIN L19. 23466 12.03 1 1 8.67 1339 IPI00025340.1 HYPOTHETICAL PROTEIN. 31698 6.51 1 1 4.73 117 1340 IPI00025477.2 SPLICE ISOFORM ALPHA-1B-1 OF Q00975 VOLTAGE-DEPENDENT N-TYPE CALCIUM CHANNEL ALPHA-1B SUBUNIT. 264305 8.75 1 1 0.47 1341 IPI00025710.1 PROTEIN C21ORF59. 33224 7.55 1 1 1.72 1342 IPI00025961.1 HYPOTHETICAL PROTEIN KIAA1411. 170604 5.1 1 1 0.39 1343 IPI00026138.2 SIMILAR TO RIBOSOMAL PROTEIN S3A. 29847 10.3 1 1 3.79 1344 IPI00026167.1 NHP2-LIKE PROTEIN 1. 14174 8.64 1 1 8.59 1345 IPI00026314.1 GELSOLIN PRECURSOR, PLASMA. 85698 6.19 1 1 1.66 1346 IPI00026519.1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE, MITOCHONDRIAL PRECURSOR. 22040 9.95 1 1 2.42 1347 IPI00026533.4 HYPOTHETICAL PROTEIN FLJ20032. 130277 7.85 1 1 0.43 1348 IPI00027500.1 TRANSFORMING PROTEIN RHOA. 21768 5.89 1 1 5.18 1349 IPI00027626.1 T-COMPLEX PROTEIN 1, ZETA SUBUNIT. 58024 6.65 1 1 3.95 1350 IPI00027717.1 COMPONENT OF GEMS 4. 119990 6 1 1 0.66 1351 IPI00027860.1 PROBABLE SERINE PROTEASE HTRA4 PRECURSOR. 50979 8.07 1 1 1.05 1352 IPI00027862.2 PROBABLE SERINE PROTEASE HTRA3 PRECURSOR. 48608 7.1 1 1 3.97 1353 IPI00027996.1 70 KDA WD-REPEAT TUMOR REJECTION ANTIGEN HOMOLOG. 100575 5.55 1 1 1.19 1354 IPI00028004.2 PROTEASOME SUBUNIT BETA TYPE 3. 22949 6.51 1 1 7.8 1355 IPI00028277.2 SIMILAR TO KIAA1752 PROTEIN. 61383 4.83 1 1 2.6 1356 IPI00028448.1 BRAIN-SPECIFIC ANGIOGENESIS INHIBITOR 3 PRECURSOR. 171491 7.06 1 1 0.33 1357 IPI00028454.1 HYPOTHETICAL PROTEIN KIAA1692. 97050 6.65 1 1 0.7 1358 IPI00028951.2 POTENTIAL PHOSPHOLIPID-TRANSPORTING ATPASE VA. 167688 8.43 1 1 0.33 1359 IPI00028975.2 SPLICE ISOFORM II OF Q14141 SEPTIN 6. 49717 6.65 1 1 2.3 1360 IPI00029208.1 MYOSIN LIGHT CHAIN ALKALI, SMOOTH-MUSCLE ISOFORM. 16830 4.19 1 1 8.67 1361 IPI00029413.1 OLFACTORY RECEPTOR 10A1. 25309 8.94 1 1 2.2 1362 IPI00029485.2 SPLICE ISOFORM P150 OF Q14203 DYNACTIN 1. 141695 5.58 1 1 1.72 1363 IPI00029534.1 AMIDOPHOSPHORIBOSYLTRANSFERASE PRECURSOR. 57399 6.74 1 1 1.16 1364 IPI00029626.1 ELF-1 RELATED PROTEIN. 70984 6.08 1 1 0.75 1365 IPI00029717.1 SPLICE ISOFORM ALPHA OF P02671 FIBRINOGEN ALPHA/ALPHA-E CHAIN PRECURSOR [Contains: FIBRINOPEPTIDE A]. 69757 8.17 1 1 2.33 1366 IPI00030023.1 HISTAMINE N-METHYLTRANSFERASE. 33295 4.98 1 1 3.42 1367 IPI00030126.1 PROBABLE G PROTEIN-COUPLED RECEPTOR GPR18. 38062 9.65 1 1 1.21 1368 IPI00030154.1 PROTEASOME ACTIVATOR COMPLEX SUBUNIT 1. 28723 5.83 1 1 4.82 1369 IPI00030267.1 HYPOTHETICAL PROTEIN. 180827 6.72 1 1 0.3 1370 IPI00030536.2 SPLICE ISOFORM 1 OF Q9HCH5 SYNAPTOTAGMIN-LIKE PROTEIN 2. 102666 8.15 1 1 0.66 1371 IPI00030907.1 ALPHA-2 CATENIN. 105282 5.53 1 1 0.52 1372 IPI00031422.3 CARDIAC SODIUM CHANNEL ALPHA SUBUNIT NAV1.5. 226812 5.15 1 1 0.45 1373 IPI00031519.1 SPLICE ISOFORM 1 OF P26358 DNA (CYTOSINE-5)-METHYLTRANSFERASE 1. 183165 7.81 1 1 0.37 1374 IPI00031522.2 TRIFUNCTIONAL ENZYME ALPHA SUBUNIT, MITOCHONDRIAL PRECURSOR (TP- ALPHA) (78 KDA GASTRIN-BINDING PROTEIN) [Includes: LONG-CHAIN ENOYL-COA HYDRATASE (EC 4.2.1.17); LONG CHAIN 3-HYDROXYACYL-COA DEHYDROGENASE (EC 1.1.1.35)]. 83000 9.52 1 1 1.83 1375 IPI00031812.1 NUCLEASE SENSITIVE ELEMENT BINDING PROTEIN 1. 35924 10.31 1 1 5.86 1376 IPI00032050.2 WW DOMAIN BINDING PROTEIN 2. 28087 5.72 1 1 3.83 1377 IPI00032461.1 GUANINE DEAMINASE. 51003 5.45 1 1 2.64 1378 IPI00033904.2 SIMILAR TO RIBOSOMAL PROTEIN S3A. 29971 10.47 1 1 3.79 1379 IPI00034319.1 DIVALENT CATION TOLERANT PROTEIN CUTA. 16833 4.87 1 1 17.31 1380 IPI00035766.2 SIMILAR TO PEPTIDYL-PRO CIS TRANS ISOMERASE. 17525 7.89 1 1 3.14 1381 IPI00037283.1 DYNAMIN-LIKE PROTEIN DYMPLE ISOFORM. 78061 6.68 1 1 1 1382 IPI00037448.1 GLYOXYLATE REDUCTASE. 35668 7.44 1 1 5.49 1383 IPI00043606.1 HYPOTHETICAL PROTEIN FLJ31030. 66043 9 1 1 0.7 1384 IPI00045051.1 PUR-BETA. 33241 5.06 1 1 4.17 1385 IPI00045396.1 SPLICE ISOFORM 2 OF O43852 CALUMENIN PRECURSOR. 37135 4.18 1 1 3.49 1386 IPI00045438.1 SOLUTE CARRIER FAMILY 26, MEMBER 9 ISOFORM A. 86988 8.33 1 1 0.63 1387 IPI00045498.1 JKTBP1DELTA6. 27191 8.99 1 1 6.56 1388 IPI00045527.1 PROTEOGLYCAN LINK PROTEIN. 40894 6.5 1 1 3.33 1389 IPI00045729.1 HYPOTHETICAL PROTEIN FLJ14981. 48585 5.33 1 1 1.11 1390 IPI00045864.1 HYPOTHETICAL PROTEIN FLJ14710. 65622 9.1 1 1 1.04 118 1391 IPI00047526.3 SIMILAR TO 40S RIBOSOMAL PROTEIN S3A (V-FOS TRANSFORMATION EFFECTOR PROTEIN). 22075 10.46 1 1 5.18 1392 IPI00050096.4 SIMILAR TO MITOCHONDRIAL ACONITASE. 41937 10.03 1 1 2.71 1393 IPI00050933.5 SIMILAR TO PHOSPHOSERINE AMINOTRANSFERASE ISOFORM 1. 41929 8.04 1 1 2.88 1394 IPI00052316.2 SIMILAR TO PEPTIDYLPROLYL ISOMERASE A. 16975 6.59 1 1 3.31 1395 IPI00056312.1 HYPOTHETICAL PROTEIN FLJ25628. 22502 4.56 1 1 4.5 1396 IPI00056521.1 SPLICE ISOFORM 1 OF Q969W9 TRANSMEMBRANE PROSTATE ANDROGEN- INDUCED PROTEIN. 31609 6.89 1 1 1.74 1397 IPI00058448.3 SIMILAR TO PROTEIN TYROSINE PHOSPHATASE. 70608 8.12 1 1 1.3 1398 IPI00059975.1 SPLICE ISOFORM 2 OF Q9HCH5 SYNAPTOTAGMIN-LIKE PROTEIN 2. 42736 9.42 1 1 1.6 1399 IPI00060031.1 SIMILAR TO HYPOTHETICAL PROTEIN FLJ10702. 21416 7.93 1 1 12.37 1400 IPI00060762.2 SIMILAR TO RIBOSOMAL PROTEIN L7. 33826 10.99 1 1 3.09 1401 IPI00063849.1 SPLICE ISOFORM 2 OF Q9NP97 DYNEIN LIGHT CHAIN 2A, CYTOPLASMIC. 5060 5.71 1 1 19.15 1402 IPI00064239.1 HYPOTHETICAL PROTEIN KIAA1784. 127547 5.18 1 1 0.43 1403 IPI00064351.1 HYPOTHETICAL PROTEIN FLJ14825. 43273 5.12 1 1 1.32 1404 IPI00064352.1 HYPOTHETICAL PROTEIN FLJ14824. 17023 7.68 1 1 8.11 1405 IPI00064579.3 BTB/POZ DOMAIN CONTAINING PROTEIN 6. 45925 5.33 1 1 1.46 1406 IPI00066374.1 SMOOTH MUSCLE AND NON-MUSCLE MYOSIN ALKALI LIGHT CHAIN ISOFORM 4. 12939 4.53 1 1 11.21 1407 IPI00068174.2 SIMILAR TO PEPTIDYLPROLYL ISOMERASE A (CYCLOPHILIN A). 38117 9.04 1 1 1.44 1408 IPI00070907.4 HYPOTHETICAL PROTEIN XP_351183. 32585 5.97 1 1 2.01 1409 IPI00074224.8 --none found in database-- 17143 4.84 1 1 7.33 1410 IPI00074962.1 ANKYRIN 2 ISOFORM 1. 433745 4.79 1 1 0.2 1411 IPI00075272.1 HYPOTHETICAL PROTEIN FLJ32194. 44434 6.79 1 1 3.72 1412 IPI00076579.3 SIMILAR TO T-COMPLEX PROTEIN 1, ALPHA SUBUNIT (TCP-1-ALPHA) (CCT- ALPHA). 54758 6.73 1 1 1.98 1413 IPI00083938.1 SIMILAR TO 40S RIBOSOMAL PROTEIN S16. 16412 10.6 1 1 7.53 1414 IPI00084423.4 SIMILAR TO 60S RIBOSOMAL PROTEIN L17 (L23) (AMINO ACID STARVATION- INDUCED PROTEIN) (ASI). 13053 10.85 1 1 12.28 1415 IPI00091258.4 SIMILAR TO 3-5 RNA EXONUCLEASE. 81440 5.07 1 1 0.94 1416 IPI00097447.4 SIMILAR TO ADENYLYL CYCLASE-ASSOCIATED PROTEIN 1 (CAP 1). 49300 8.01 1 1 2.44 1417 IPI00097790.1 WAS PROTEIN FAMILY, MEMBER 2. 54284 5.16 1 1 1.41 1418 IPI00098756.2 SIMILAR TO ADAPTOR-RELATED PROTEIN COMPLEX 2, BETA 1 SUBUNIT. 100424 5.95 1 1 1.22 1419 IPI00101968.1 HYPOTHETICAL PROTEIN FLJ14461. 49042 4.72 1 1 2.51 1420 IPI00102498.2 SOLUTE CARRIER FAMILY 26, MEMBER 9 ISOFORM B. 101680 8.63 1 1 0.54 1421 IPI00102896.1 RAS-RELATED PROTEIN RAB-2B. 24214 7.97 1 1 5.56 1422 IPI00103616.1 DYSLEXIA SUSCEPTIBILITY 1 CANDIDATE GENE 1 PROTEIN. 48455 9.27 1 1 1.43 1423 IPI00103647.1 CILIARY DYNEIN HEAVY CHAIN 7. 461143 5.82 1 1 0.17 1424 IPI00104136.2 SIMILAR TO NUCLEAR RNA HELICASE, DECD VARIANT OF DEAD BOX FAMILY. 49130 5.39 1 1 2.34 1425 IPI00104899.2 SIMILAR TO 60S RIBOSOMAL PROTEIN L17 (L23). 12755 10.8 1 1 9.01 1426 IPI00105119.1 HYPOTHETICAL PROTEIN FLJ25373. 46520 6.62 1 1 1.21 1427 IPI00106663.1 HYPOTHETICAL PROTEIN KIAA0849. 107911 5.22 1 1 0.52 1428 IPI00140345.3 SIMILAR TO 40S RIBOSOMAL PROTEIN SA (P40) (34/67 KDA LAMININ RECEPTOR). 36157 4.69 1 1 2.99 1429 IPI00141564.1 HYPOTHETICAL PROTEIN. 78194 6.6 1 1 0.84 1430 IPI00141809.2 SIMILAR TO HIGH MOBILITY GROUP PROTEIN HOMOLOG HMG4. 23922 10.34 1 1 2.84 1431 IPI00141925.1 ZINC FINGER PROTEIN 342. 50810 8.98 1 1 1.05 1432 IPI00144153.1 SIMILAR TO PROTEIN 40KD. 14077 7.68 1 1 7.75 1433 IPI00145331.2 BA317E16.3. 14167 11 1 1 8.66 1434 IPI00146260.1 SIMILAR TO ACTIVATED RNA POLYMERASE II TRANSCRIPTIONAL COACTIVATOR P15 (PC4) (P14). 14229 10.39 1 1 11.02 1435 IPI00146935.1 DYNAMIN-LIKE PROTEIN. 81891 6.8 1 1 0.95 1436 IPI00148255.1 SECOND MITOCHONDRIA-DERIVED ACTIVATOR OF CASPASE ISOFORM SMAC- DELTA, PRECURSOR. 22284 5.73 1 1 6.15 1437 IPI00152108.1 F-BOX ONLY PROTEIN 2. 33328 4.01 1 1 4.05 1438 IPI00152242.1 HYPOTHETICAL PROTEIN. 19735 10.27 1 1 7.56 1439 IPI00154890.1 PROTEIN SERINE/THREONINE PHOSPHATASE 4 SUBUNIT PP4RMEG. 107004 4.38 1 1 0.53 1440 IPI00156774.2 SIMILAR TO RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 ISOFORM RAC1. 21543 9.14 1 1 7.29 1441 IPI00157556.5 --none found in database-- 64711 8.57 1 1 0.85 1442 IPI00157813.1 MAX PROTEIN. 15395 7.24 1 1 7.46 119 1443 IPI00158128.1 SPLICE ISOFORM 3 OF P25912 MAX PROTEIN. 12099 5.93 1 1 9.71 1444 IPI00160587.2 SIMILAR TO 40S RIBOSOMAL PROTEIN S6 (PHOSPHOPROTEIN NP33). 26351 11.05 1 1 2.59 1445 IPI00160836.3 --none found in database-- 42157 4.58 1 1 2.67 1446 IPI00161313.2 SIMILAR TO FOLATE HYDROLASE. 88682 6.06 1 1 0.5 1447 IPI00161846.2 SIMILAR TO PROTEIN 40KD. 19072 7.51 1 1 5.71 1448 IPI00164007.1 SMALL GTP-BINDING PROTEIN. 6306 5.56 1 1 15.09 1449 IPI00165222.2 --none found in database-- 11625 6.51 1 1 6.67 1450 IPI00165486.5 SIMILAR TO RIBOSOMAL PROTEIN S2. 45408 10.48 1 1 3.06 1451 IPI00166058.1 SIMILAR TO HYPOTHETICAL GENE LOC136555. 12255 9.65 1 1 3.6 1452 IPI00166250.1 HYPOTHETICAL PROTEIN FLJ37882. 44031 9.96 1 1 1.6 1453 IPI00166271.1 HYPOTHETICAL PROTEIN FLJ34952. 13616 11.47 1 1 4.72 1454 IPI00166825.1 SIMILAR TO HYPOTHETICAL PROTEIN FLJ14981. 50662 5.48 1 1 1.06 1455 IPI00167002.2 ETS-RELATED TRANSCRIPTION FACTOR ELF-1. 67456 4.84 1 1 0.81 1456 IPI00167400.4 HYPOTHETICAL PROTEIN FLJ40200. 58798 6.55 1 1 1.93 1457 IPI00167491.2 SIMILAR TO ZINC FINGER PROTEIN 432. 71162 10.05 1 1 0.8 1458 IPI00167784.1 HYPOTHETICAL PROTEIN FLJ36749. 27957 8.61 1 1 2.4 1459 IPI00167879.1 HYPOTHETICAL PROTEIN FLJ36000. 15015 8.14 1 1 3.52 1460 IPI00167967.1 HYPOTHETICAL PROTEIN FLJ35542. 24855 8.1 1 1 2.64 1461 IPI00168368.1 HYPOTHETICAL PROTEIN FLJ90378. 34237 7.84 1 1 2.17 1462 IPI00168438.1 HYPOTHETICAL PROTEIN. 16885 9.68 1 1 3.9 1463 IPI00168509.2 HYPOTHETICAL PROTEIN FLJ13725. 131873 6.24 1 1 0.49 1464 IPI00170744.1 MYELOID ELF-1 LIKE FACTOR. 70730 5.3 1 1 0.75 1465 IPI00170796.1 SPLICE ISOFORM 1 OF Q9UBQ0 VACUOLAR PROTEIN SORTING 29. 20506 6.79 1 1 7.14 1466 IPI00171160.1 SIMILAR TO 37 KDA LEUCINE-RICH REPEAT (LRR) PROTEIN. 51800 8.34 1 1 1.36 1467 IPI00171230.1 HYPOTHETICAL PROTEIN KIAA1081. 115109 6.24 1 1 0.9 1468 IPI00171480.1 HYPOTHETICAL PROTEIN FLJ90246. 69856 7.12 1 1 0.77 1469 IPI00171741.2 PIGGYBAC TRANSPOSABLE ELEMENT DERIVED 4. 67004 9.62 1 1 1.2 1470 IPI00171903.1 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN M. 77516 9.1 1 1 2.19 1471 IPI00172421.3 S-PHASE KINASE-ASSOCIATED PROTEIN 1A ISOFORM A. 18063 4.08 1 1 8.75 1472 IPI00172585.1 SERINE/THREONINE-PROTEIN KINASE SGK3. 57108 6.92 1 1 1.01 1473 IPI00173565.3 --none found in database-- 28163 5.27 1 1 2.77 1474 IPI00175146.2 HYPOTHETICAL PROTEIN KIAA0546. 218331 8.12 1 1 0.26 1475 IPI00175151.2 SIMILAR TO HYPOTHETICAL PROTEIN. 223811 8.03 1 1 0.25 1476 IPI00176219.1 SIMILAR TO NEPHRONECTIN SHORT ISOFORM. 61907 8.38 1 1 0.88 1477 IPI00176375.1 HYPOTHETICAL PROTEIN. 185782 6.9 1 1 0.36 1478 IPI00176686.2 SIMILAR TO RIBOSOMAL PROTEIN L6. 32336 10.93 1 1 2.79 1479 IPI00176721.1 SIMILAR TO RIBOSOMAL PROTEIN S2. 31392 11.08 1 1 4.47 1480 IPI00176823.1 SIMILAR TO 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL PRECURSOR (HSP60) (60 KDA CHAPERONIN) (CPN60) (HEAT SHOCK PROTEIN 60) (HSP-60) (MITOCHONDRIAL MATRIX PROTEIN P1) (P60 LYMPHOCYTE PROTEIN) (HUCHA60). 12103 8.44 1 1 11.82 1481 IPI00176841.1 SIMILAR TO S-PHASE KINASE-ASSOCIATED PROTEIN 1A ISOFORM A. 16920 4.53 1 1 9.4 1482 IPI00176996.2 --none found in database-- 26168 7.97 1 1 2.94 1483 IPI00177010.2 SIMILAR TO TRANSLATION INITIATION FACTOR EIF-4A II - MOUSE. 46056 4.64 1 1 3.42 1484 IPI00178607.5 BH3 INTERACTING DOMAIN DEATH AGONIST ISOFORM 1. 31798 6.91 1 1 5.28 1485 IPI00179076.1 DJ1172N10.1 (UBIQUITIN SPECIFIC PROTEASE 9, X CHROMOSOME. 172064 5.47 1 1 0.4 1486 IPI00179357.1 TITIN. 3.82E+06 6.25 1 1 0.01 1487 IPI00180139.3 --none found in database-- 55267 8.39 1 1 1.22 1488 IPI00180384.1 HYPOTHETICAL PROTEIN KIAA0944. 461773 5.82 1 1 0.17 1489 IPI00181391.4 SIMILAR TO MENINGIOMA EXPRESSED ANTIGEN 5. 110453 6.21 1 1 0.61 1490 IPI00181684.1 ELKS. 108793 6.57 1 1 0.95 1491 IPI00181771.1 --none found in database-- 10322 8.32 1 1 5.62 1492 IPI00181921.1 ADDUCIN 2 ISOFORM C. 46551 4.98 1 1 2.85 1493 IPI00183349.6 R31155_1. 84252 10.02 1 1 1.22 1494 IPI00183643.1 GOLIATH PROTEIN. 46405 9.05 1 1 2.63 120 1495 IPI00183664.2 --none found in database-- 42485 9.5 1 1 2.48 1496 IPI00183679.2 SPLICE ISOFORM 2 OF Q969W9 TRANSMEMBRANE PROSTATE ANDROGEN- INDUCED PROTEIN. 27900 6.51 1 1 1.98 1497 IPI00184119.2 --none found in database-- 106202 8.98 1 1 0.62 1498 IPI00184284.2 SPLICE ISOFORM 2 OF Q9UBQ0 VACUOLAR PROTEIN SORTING 29. 20927 7.07 1 1 6.99 1499 IPI00184799.2 --none found in database-- 24156 8.94 1 1 3.88 1500 IPI00185197.3 SIMILAR TO CGI-55 PROTEIN. 40188 6.87 1 1 1.36 1501 IPI00185238.3 --none found in database-- 62594 8.38 1 1 0.88 1502 IPI00185256.2 SEX COMB ON MIDLEG HOMOLOG 1 ISOFORM 2. 72072 9.68 1 1 0.77 1503 IPI00185798.2 --none found in database-- 34164 6.97 1 1 5.97 1504 IPI00186101.2 --none found in database-- 32528 8.22 1 1 2.99 1505 IPI00186586.4 SIMILAR TO HYPOTHETICAL PROTEIN FLJ10101. 54698 8.17 1 1 1.21 1506 IPI00186815.2 SPLICE ISOFORM 2 OF O43566 REGULATOR OF G-PROTEIN SIGNALING 14. 38536 8.46 1 1 1.13 1507 IPI00187110.2 SIMILAR TO SEX COMB ON MIDLEG-LIKE 1. 73354 9.71 1 1 0.76 1508 IPI00215719.1 60S RIBOSOMAL PROTEIN L18. 22659 12.28 1 1 5.5 1509 IPI00215879.1 SPLICE ISOFORM SRP55-3 OF Q13247 SPLICING FACTOR, ARGININE/SERINE-RICH 6. 38419 11.56 1 1 2.69 1510 IPI00215911.1 APEX NUCLEASE. 35554 8.26 1 1 5.35 1511 IPI00215918.1 ADP-RIBOSYLATION FACTOR 4. 20511 7.26 1 1 11.67 1512 IPI00215919.1 ADP-RIBOSYLATION FACTOR 5. 20530 6.79 1 1 11.67 1513 IPI00215948.1 ALPHA2(E)-CATENIN. 102776 6.25 1 1 0.54 1514 IPI00216139.1 SPLICE ISOFORM I OF Q14141 SEPTIN 6. 48873 6.8 1 1 2.34 1515 IPI00216141.1 SPLICE ISOFORM V OF Q14141 SEPTIN 6. 49167 6.8 1 1 2.33 1516 IPI00216163.3 SPLICE ISOFORM 1 OF Q9NP97 DYNEIN LIGHT CHAIN 2A, CYTOPLASMIC. 13364 9.89 1 1 10.26 1517 IPI00216256.1 SPLICE ISOFORM SHORT OF O75083 WD-REPEAT PROTEIN 1. 58002 6.89 1 1 3 1518 IPI00216443.1 SPLICE ISOFORM 3 OF Q9H9B1 HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-9 SPECIFIC 5. 125404 5.74 1 1 0.43 1519 IPI00216470.1 PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE TYPE II BETA. 47378 7.37 1 1 3.37 1520 IPI00216472.1 SPLICE ISOFORM NON-BRAIN OF P09497 CLATHRIN LIGHT CHAIN B. 23181 4.34 1 1 4.74 1521 IPI00216704.1 SPLICE ISOFORM 2 OF P11277 SPECTRIN BETA CHAIN, ERYTHROCYTE. 267680 5.03 1 1 0.43 1522 IPI00216719.1 ELKS EPSILON. 128086 5.8 1 1 0.81 1523 IPI00216720.1 ELKS GAMMA. 81967 6.6 1 1 1.25 1524 IPI00217009.1 FK506-BINDING PROTEIN 1A. 15727 10.14 1 1 9.72 1525 IPI00217154.1 SPLICE ISOFORM 1 OF Q9HBY8 SERINE/THREONINE-PROTEIN KINASE SGK2. 41175 6.73 1 1 1.36 1526 IPI00217683.1 SPLICE ISOFORM 2 OF Q02952 A-KINASE ANCHOR PROTEIN 12. 181647 4.1 1 1 1.19 1527 IPI00217691.1 SIMILAR TO NUCLEAR FACTOR. 110097 6.52 1 1 0.51 1528 IPI00218013.3 TRIPIN. 144718 8.2 1 1 0.4 1529 IPI00218075.1 PROTEIN FAM9B. 22438 5.08 1 1 2.69 1530 IPI00218242.1 SPLICE ISOFORM ALPHA-2 OF O15165 PROTEIN C18ORF1. 32072 6.59 1 1 1.74 1531 IPI00218243.1 SPLICE ISOFORM BETA-1 OF O15165 PROTEIN C18ORF1. 27600 7.57 1 1 2.02 1532 IPI00218244.1 SPLICE ISOFORM BETA-2 OF O15165 PROTEIN C18ORF1. 25772 8.34 1 1 2.17 1533 IPI00218310.1 EXOSOME COMPLEX EXONUCLEASE RRP41. 27637 6.6 1 1 1.95 1534 IPI00218371.1 PHOSPHORIBOSYL PYROPHOSPHATE SYNTHETASE 1-LIKE 1. 34839 6.31 1 1 4.09 1535 IPI00218782.1 F-ACTIN CAPPING PROTEIN BETA SUBUNIT. 30629 5.78 1 1 4.78 1536 IPI00218847.1 ACID PHOSPHATASE 1 ISOFORM B. 17977 6.88 1 1 6.96 1537 IPI00219077.1 LEUKOTRIENE A4 HYDROLASE. 69285 6.1 1 1 2.13 1538 IPI00219114.1 SPLICE ISOFORM P135 OF Q14203 DYNACTIN 1. 127404 5.09 1 1 1.92 1539 IPI00219126.2 SPLICE ISOFORM 3 OF O43566 REGULATOR OF G-PROTEIN SIGNALING 14. 64745 8.82 1 1 0.67 1540 IPI00219127.1 SPLICE ISOFORM 4 OF O43566 REGULATOR OF G-PROTEIN SIGNALING 14. 21781 10.15 1 1 1.99 1541 IPI00219157.1 RIBOSOMAL PROTEIN L27A. 16561 11.64 1 1 7.43 1542 IPI00219207.1 SPLICE ISOFORM 3 OF Q9NQC3 RETICULON 4. 22395 9.78 1 1 7.04 1543 IPI00219274.1 SYNAPTOTAGMIN II. 46830 8.12 1 1 2.39 1544 IPI00219365.1 MOESIN. 67820 6.32 1 1 1.56 1545 IPI00219451.1 SPLICE ISOFORM 5 OF O00154 CYTOSOLIC ACYL COENZYME A THIOESTER HYDROLASE. 38991 8.47 1 1 3.43 1546 IPI00219452.1 SPLICE ISOFORM 6 OF O00154 CYTOSOLIC ACYL COENZYME A THIOESTER HYDROLASE. 36568 7.88 1 1 3.65 121 1547 IPI00219616.1 PHOSPHORIBOSYL PYROPHOSPHATE SYNTHETASE 1. 34834 6.98 1 1 4.09 1548 IPI00219861.1 ACID PHOSPHATASE 1 ISOFORM C. 18042 6.73 1 1 6.96 1549 IPI00219865.1 SPLICE ISOFORM 2 OF Q9NR28 SMAC PROTEIN, MITOCHONDRIAL PRECURSOR. 21233 4.48 1 1 6.45 1550 IPI00219929.1 SPLICE ISOFORM 2 OF P25912 MAX PROTEIN. 17202 6.52 1 1 6.62 1551 IPI00220002.1 SPLICE ISOFORM 2 OF O75781 PARALEMMIN. 37157 4.62 1 1 4.08 1552 IPI00220026.1 SPLICE ISOFORM 2 OF P22303 ACETYLCHOLINESTERASE PRECURSOR. 69909 6.91 1 1 0.93 1553 IPI00220323.5 SPLICE ISOFORM ALPHA-1 OF O15165 PROTEIN C18ORF1. 36484 6.82 1 1 1.52 1554 IPI00220365.2 EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA, 1 ISOFORM 4. 154805 4.82 1 1 0.71 1555 IPI00220373.1 INSULYSIN. 118022 6.74 1 1 0.59 1556 IPI00220412.1 S100 CALCIUM BINDING PROTEIN A1. 10546 4.13 1 1 22.34 1557 IPI00220431.1 SPLICE ISOFORM ALPHA-1B-2 OF Q00975 VOLTAGE-DEPENDENT N-TYPE CALCIUM CHANNEL ALPHA-1B SUBUNIT. 251759 8.59 1 1 0.49 1558 IPI00220573.1 MYOSIN REGULATORY LIGHT CHAIN MRCL3. 19794 4.4 1 1 6.43 1559 IPI00220617.1 HYPOTHETICAL PROTEIN. 90203 7.88 1 1 1.81 1560 IPI00220738.1 SPLICE ISOFORM CRK-I OF P46108 PROTO-ONCOGENE C-CRK. 22936 4.96 1 1 8.33 1561 IPI00220754.1 SPLICE ISOFORM 1 OF Q9UEY8 GAMMA ADDUCIN. 75671 6.8 1 1 1.78 1562 IPI00220791.1 SPLICE ISOFORM 2 OF P49418 AMPHIPHYSIN. 71929 4.37 1 1 1.53 1563 IPI00220918.1 SPLICE ISOFORM 2 OF P26358 DNA (CYTOSINE-5)-METHYLTRANSFERASE 1. 184819 7.92 1 1 0.37 1564 IPI00220919.1 SPLICE ISOFORM 3 OF P26358 DNA (CYTOSINE-5)-METHYLTRANSFERASE 1. 144465 7.48 1 1 0.47 1565 IPI00220993.1 SPLICE ISOFORM CNPI OF P09543 2',3'-CYCLIC NUCLEOTIDE 3'- PHOSPHODIESTERASE. 45099 8.76 1 1 2.74 1566 IPI00221088.1 RIBOSOMAL PROTEIN S9. 22591 11.32 1 1 5.67 1567 IPI00221089.1 RIBOSOMAL PROTEIN S13. 17222 11.19 1 1 9.93 1568 IPI00221092.1 RIBOSOMAL PROTEIN S16. 16445 10.81 1 1 7.53 1569 IPI00221225.1 ANNEXIN IV. 36085 5.9 1 1 2.18 1570 IPI00221286.1 SPLICE ISOFORM SRP40-2 OF Q13243 SPLICING FACTOR, ARGININE/SERINE-RICH 5. 12528 10.56 1 1 4.67 1571 IPI00221287.1 SPLICE ISOFORM SRP40-4 OF Q13243 SPLICING FACTOR, ARGININE/SERINE-RICH 5. 30663 12.18 1 1 1.86 1572 IPI00221354.1 SPLICE ISOFORM SHORT OF P35637 RNA-BINDING PROTEIN FUS. 53355 9.59 1 1 2.29 1573 IPI00221391.1 NADH DEHYDROGENASE SUBUNIT 5. 67012 9.32 1 1 1.16 1574 IPI00232416.2 SIMILAR TO TAU TUBULIN KINASE 2. 51904 8.27 1 1 1.95 1575 IPI00232533.2 EUKARYOTIC TRANSLATION INITIATION FACTOR 1A, X-CHROMOSOMAL. 22218 9.37 1 1 5.61 1576 IPI00232922.1 SPLICE ISOFORM 6 OF P07202 THYROID PEROXIDASE PRECURSOR. 67293 7.96 1 1 0.98 1577 IPI00232923.1 SPLICE ISOFORM 2-3 OF P07202 THYROID PEROXIDASE PRECURSOR. 96475 7.33 1 1 0.69 1578 IPI00232924.1 SPLICE ISOFORM 2-4 OF P07202 THYROID PEROXIDASE PRECURSOR. 92031 7.01 1 1 0.72 1579 IPI00233255.2 SIMILAR TO PROTEIN-TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 11 (PROTEIN-TYROSINE PHOSPHATASE 2C) (PTP-2C) (PTP-1D) (SH-PTP3) (SH- PTP2) (SHP-2). 64013 6.74 1 1 1.43 1580 IPI00233820.2 CATALASE. 59625 7.41 1 1 1.71 1581 IPI00234131.2 SIMILAR TO 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL PRECURSOR (HSP60) (60 KDA CHAPERONIN) (CPN60) (HEAT SHOCK PROTEIN 60) (HSP-60) (MITOCHONDRIAL MATRIX PROTEIN P1) (P60 LYMPHOCYTE PROTEIN) (HUCHA60). 61092 4.91 1 1 1.57 1582 IPI00235352.1 SIMILAR TO PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE, TYPE II, BETA. 32317 9.91 1 1 4.98 1583 IPI00235412.1 DYNAMIN 1-LIKE. 79442 6.92 1 1 0.99 1584 IPI00236274.2 SIMILAR TO KH-TYPE SPLICING REGULATORY PROTEIN (FUSE BINDING PROTEIN 2). 85529 10.18 1 1 1.25 1585 IPI00237806.1 SPLICE ISOFORM 3 OF P11277 SPECTRIN BETA CHAIN, ERYTHROCYTE. 242656 4.99 1 1 0.47 1586 IPI00237884.1 A-KINASE ANCHOR PROTEIN 12 ISOFORM 1. 191482 4.07 1 1 1.12 1587 IPI00239789.1 HYPOTHETICAL PROTEIN. 47921 6.91 1 1 2.82 1588 IPI00242253.4 SIMILAR TO RETICULOCALBIN 1 PRECURSOR. 36289 4.46 1 1 5.18 1589 IPI00243499.2 SIMILAR TO AMINOPEPTIDASE PUROMYCIN SENSITIVE. 30397 4.47 1 1 3.68 1590 IPI00243595.2 FLJ00153 PROTEIN. 54312 8.78 1 1 1.41 1591 IPI00243913.3 SIMILAR TO NEUROFILAMENT-LIKE PROTEIN. 115538 4.56 1 1 0.56 1592 IPI00244116.1 SIMILAR TO HYPOTHETICAL PROTEIN MGC27277. 50892 8.49 1 1 1.4 1593 IPI00244567.2 GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) GAMMA-2 SUBUNIT. 7719 8.22 1 1 22.86 1594 IPI00246067.2 SIMILAR TO KERATIN 8, TYPE II CYTOSKELETAL - HUMAN. 45740 5.03 1 1 2.13 1595 IPI00246556.2 --none found in database-- 17536 6.53 1 1 3.92 1596 IPI00246975.2 GLUTATHIONE S-TRANSFERASE MU 3. 26428 5.19 1 1 7.59 1597 IPI00247493.1 HYPOTHETICAL PROTEIN KIAA0679. 103071 4.56 1 1 0.65 122 1598 IPI00248099.2 SIMILAR TO CHROMATIN ASSEMBLY FACTOR 1 SUBUNIT C (CAF-1 SUBUNIT C) (CHROMATIN ASSEMBLY FACTOR I P48 SUBUNIT) (CAF-I 48 KDA SUBUNIT) (CAF- IP48) (RETINOBLASTOMA BINDING PROTEIN P48) (RETINOBLASTOMA-BINDING PROTEIN 4) (RBBP-4) (MSI1 PROTEIN HOMOLOG).... 48212 4.9 1 1 3.04 1599 IPI00248597.2 --none found in database-- 8151 4.52 1 1 6.85 1600 IPI00248708.3 --none found in database-- 148561 9.04 1 1 0.37 1601 IPI00248956.1 SPLICE ISOFORM A OF Q9UH03 NEURONAL-SPECIFIC SEPTIN 3. 39345 7.22 1 1 3.48 1602 IPI00249627.2 --none found in database-- 29061 8.71 1 1 3.37 1603 IPI00249656.1 SIMILAR TO RIKEN CDNA 2310039E09. 41899 8.64 1 1 2.75 1604 IPI00252153.1 HYPOTHETICAL PROTEIN FLJ33253. 63244 8.17 1 1 1.26 1605 IPI00254157.3 --none found in database-- 44064 5 1 1 3.33 1606 IPI00256143.2 --none found in database-- 27979 5.78 1 1 2.77 1607 IPI00256684.1 SPLICE ISOFORM B OF O95782 ADAPTER-RELATED PROTEIN COMPLEX 2 ALPHA 1 SUBUNIT. 105370 7.72 1 1 1.88 1608 IPI00257898.2 SIMILAR TO HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN G (HNRNP G) (RNA BINDING MOTIF PROTEIN, X CHROMOSOME) (GLYCOPROTEIN P43). 41987 9.61 1 1 2.56 1609 IPI00257932.1 SIMILAR TO HYPOTHETICAL PROTEIN MGC15737. 23307 4.45 1 1 4.37 1610 IPI00258370.2 SIMILAR TO CALCIUM-BINDING TRANSPORTER. 28389 6.99 1 1 1.95 1611 IPI00258514.2 SIMILAR TO 78 KDA GLUCOSE-REGULATED PROTEIN PRECURSOR (GRP 78) (IMMUNOGLOBULIN HEAVY CHAIN BINDING PROTEIN) (BIP) (ENDOPLASMIC RETICULUM LUMENAL CA(2+) BINDING PROTEIN GRP78). 67459 4.94 1 1 3.45 1612 IPI00258904.2 SIMILAR TO PEPTIDYL-PRO CIS TRANS ISOMERASE. 18513 8.01 1 1 2.91 1613 IPI00260715.2 SPLICE ISOFORM LONG OF P35637 RNA-BINDING PROTEIN FUS. 56239 9.49 1 1 2.17 1614 IPI00260755.2 SIMILAR TO DJ1100H13.4 (PUTATIVE RHOGAP DOMAIN CONTAINING PROTEIN). 66290 8.46 1 1 0.84 1615 IPI00289348.1 HYPOTHETICAL PROTEIN FLJ30766. 27508 7.29 1 1 2.04 1616 IPI00289551.1 STEROL/RETINOL DEHYDROGENASE. 35645 8.77 1 1 1.89 1617 IPI00289572.1 SPLICE ISOFORM 1 OF P07202 THYROID PEROXIDASE PRECURSOR. 102931 6.75 1 1 0.64 1618 IPI00289573.3 SPLICE ISOFORM 2 OF P07202 THYROID PEROXIDASE PRECURSOR. 96667 6.79 1 1 0.68 1619 IPI00289575.1 SPLICE ISOFORM 4 OF P07202 THYROID PEROXIDASE PRECURSOR. 98295 6.94 1 1 0.67 1620 IPI00289576.3 SPLICE ISOFORM 5 OF P07202 THYROID PEROXIDASE PRECURSOR. 84549 6.33 1 1 0.79 1621 IPI00289819.2 CATION-INDEPENDENT MANNOSE-6-PHOSPHATE RECEPTOR PRECURSOR. 274966 5.82 1 1 0.24 1622 IPI00290461.1 EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT 1. 29062 4.45 1 1 4.26 1623 IPI00290462.3 CARBONYL REDUCTASE 3. 30850 6.06 1 1 5.78 1624 IPI00290557.1 SIMILAR TO UBIQUITIN UBF-FL. 65644 9.19 1 1 1.04 1625 IPI00290842.2 MICROTUBULE-ASSOCIATED PROTEIN 4 ISOFORM 4. 109619 4.82 1 1 1.06 1626 IPI00290857.1 KERATIN, TYPE II CYTOSKELETAL 3. 64511 6.41 1 1 1.59 1627 IPI00291165.2 POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1. 86456 7.86 1 1 0.89 1628 IPI00291579.4 KINESIN FAMILY MEMBER 23 ISOFORM 1. 112994 8.84 1 1 0.71 1629 IPI00291922.2 PROTEASOME SUBUNIT ALPHA TYPE 5. 26411 4.45 1 1 5.39 1630 IPI00291993.1 SPLICE ISOFORM M4 OF P52272 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN M. 77469 9.29 1 1 2.19 1631 IPI00292434.3 SPLICE ISOFORM M1-M2 OF P52272 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN M. 73575 9.45 1 1 2.32 1632 IPI00292776.1 HYPOTHETICAL PROTEIN KIAA1508. 65597 8.95 1 1 0.7 1633 IPI00293080.1 HYPOTHETICAL PROTEIN. 140183 8.58 1 1 0.39 1634 IPI00293338.5 SMC5 PROTEIN. 131136 8.53 1 1 0.62 1635 IPI00293380.2 SUPERFAST MYOSIN REGULATORY LIGHT CHAIN 2. 21332 4.43 1 1 3.14 1636 IPI00293884.4 KINESIN-LIKE PROTEIN KIF23. 101041 8.83 1 1 0.79 1637 IPI00293975.1 GLUTATHIONE PEROXIDASE 1. 21899 6.5 1 1 8.96 1638 IPI00294158.1 BILIVERDIN REDUCTASE A PRECURSOR. 33428 6.41 1 1 4.73 1639 IPI00294566.1 HYPOTHETICAL PROTEIN. 55210 7.23 1 1 1.98 1640 IPI00294632.1 PUTATIVE DYNEIN LIGHT CHAIN PROTEIN DJ8B22.1. 10535 6.93 1 1 5.62 1641 IPI00294980.1 PEPSINOGEN. 8716 10.47 1 1 5.48 1642 IPI00295386.3 CARBONYL REDUCTASE 1. 30375 8.49 1 1 5.78 1643 IPI00295392.3 60S RIBOSOMAL PROTEIN L3. 45978 10.89 1 1 2.99 1644 IPI00295461.1 SPLICE ISOFORM 1 OF Q12884 SEPRASE. 87821 6.87 1 1 0.66 1645 IPI00295589.1 EUKARYOTIC TRANSLATION INITIATION FACTOR 4GI. 175535 5.01 1 1 0.63 1646 IPI00296191.1 VACUOLAR ATP SYNTHASE SUBUNIT H. 55883 6.44 1 1 4.76 1647 IPI00296241.3 HISTO-BLOOD GROUP ABO SYSTEM TRANSFERASE (NAGAT) [Includes: GLYCOPROTEIN-FUCOSYLGALACTOSIDE ALPHA-N- ACETYLGALACTOSAMINYLTRANSFERASE (EC 2.4.1.40) (FUCOSYLGLYCOPROTEIN ALPHA-N-ACETYLGALACTOSAMINYLTRANSFERASE) (HISTO-BLOOD GROUP A 40934 9.24 1 1 1.41 123 TRANSFERASE) (A TRANSFERA 1648 IPI00296291.1 HP1-BP74 PROTEIN. 61436 10.26 1 1 0.72 1649 IPI00297587.1 HYPOTHETICAL PROTEIN FLJ25874. 32161 8.14 1 1 1.71 1650 IPI00297597.1 NUCLEAR RNA HELICASE. 49078 5.67 1 1 2.34 1651 IPI00298237.1 TRIPEPTIDYL-PEPTIDASE I PRECURSOR. 61229 6.42 1 1 2.49 1652 IPI00298347.1 PROTEIN-TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 11. 68011 7.31 1 1 1.35 1653 IPI00298394.2 SIMILAR TO HYPOTHETICAL PROTEIN. 123425 6.65 1 1 0.54 1654 IPI00298497.3 FIBRINOGEN BETA CHAIN PRECURSOR [Contains: FIBRINOPEPTIDE B]. 55928 8.38 1 1 3.05 1655 IPI00299000.1 PROLIFERATION-ASSOCIATED PROTEIN 2G4. 43787 6.52 1 1 4.31 1656 IPI00299155.3 PROTEASOME SUBUNIT ALPHA TYPE 4. 29484 7.86 1 1 8.43 1657 IPI00299608.2 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 1. 108488 5.06 1 1 1.94 1658 IPI00299755.1 PHOSPHATIDYLINOSITOL 3-KINASE. 100988 6.7 1 1 0.68 1659 IPI00300285.2 HYPOTHETICAL PROTEIN DKFZP564D1378. 29776 6.17 1 1 7.78 1660 IPI00300587.2 SIMILAR TO HP4 OLFACTORY RECEPTOR. 38231 8.89 1 1 1.46 1661 IPI00301023.3 SPLICE ISOFORM 1 OF O75781 PARALEMMIN. 42076 4.64 1 1 3.62 1662 IPI00301154.1 POLYADENYLATE-BINDING PROTEIN 3. 70031 10.2 1 1 1.74 1663 IPI00301288.2 HYPOTHETICAL PROTEIN FLJ90754. 178834 5.11 1 1 0.31 1664 IPI00301610.3 HYPOTHETICAL PROTEIN KIAA1994. 113760 5.47 1 1 1.07 1665 IPI00302227.3 HYPOTHETICAL PROTEIN FLJ23447. 56555 10.15 1 1 1.17 1666 IPI00302309.2 HYPOTHETICAL PROTEIN FLJ10890. 108741 5.79 1 1 0.52 1667 IPI00302966.2 HYPOTHETICAL PROTEIN FLJ10890. 129687 6.56 1 1 0.44 1668 IPI00303335.1 NEBULIN. 773214 9.49 1 1 0.1 1669 IPI00304111.1 EXTRACELLULAR SIGNAL-RELATED KINASE 1C. 38249 6.14 1 1 4.48 1670 IPI00304577.3 SPLICE ISOFORM A OF O95782 ADAPTER-RELATED PROTEIN COMPLEX 2 ALPHA 1 SUBUNIT. 107555 7.06 1 1 1.84 1671 IPI00304911.3 VACUOLAR ATP SYNTHASE SUBUNIT B, KIDNEY ISOFORM. 56980 5.52 1 1 3.9 1672 IPI00305092.2 PYM PROTEIN. 28286 10.71 1 1 3.13 1673 IPI00305461.1 INTER-ALPHA-TRYPSIN INHIBITOR HEAVY CHAIN H2 PRECURSOR. 106596 6.94 1 1 0.63 1674 IPI00305469.1 SIMILAR TO V-CRK AVIAN SARCOMA VIRUS CT10 ONCOGENE HOMOLOG. 22906 5.13 1 1 8.33 1675 IPI00305486.1 SPLICE ISOFORM 1 OF P49418 AMPHIPHYSIN. 76257 4.28 1 1 1.44 1676 IPI00305491.3 HYPOTHETICAL SERINE/THREONINE PROTEIN PHOSPHATASE. 58129 6.97 1 1 1.76 1677 IPI00306667.2 SPLICE ISOFORM CNPII OF P09543 2',3'-CYCLIC NUCLEOTIDE 3'- PHOSPHODIESTERASE. 51085 9.59 1 1 2.4 1678 IPI00306840.1 SPHINGOSINE-1-PHOSPHATE PHOSPHATASE 1. 48889 9.18 1 1 1.36 1679 IPI00306870.1 DJ148E22.2 (NOVEL PABPC1. 33332 9.29 1 1 3.77 1680 IPI00306929.4 SPLICE ISOFORM 1 OF Q8IUG5 MYOSIN XVIIIB. 285185 6.88 1 1 0.19 1681 IPI00307219.2 --none found in database-- 52180 9.67 1 1 1.27 1682 IPI00307516.4 HYPOTHETICAL PROTEIN FLJ32752. 122765 7.23 1 1 0.54 1683 IPI00307702.1 H53_GS1. 58017 8.33 1 1 1.12 1684 IPI00328268.5 EIF4GII. 176652 5.02 1 1 0.63 1685 IPI00328319.4 CHROMATIN ASSEMBLY FACTOR 1 SUBUNIT C. 50614 4.65 1 1 2.86 1686 IPI00329276.1 B-CELL NOVEL PROTEIN ISOFORM 3. 77401 8.71 1 1 0.86 1687 IPI00329389.2 60S RIBOSOMAL PROTEIN L6. 32597 11.29 1 1 2.79 1688 IPI00329391.1 SIMILAR TO DIHYDROLIPOAMIDE S-ACETYLTRANSFERASE PRECURSOR. 68997 7.94 1 1 2.32 1689 IPI00329442.1 FIBROBLAST ACTIVATION PROTEIN, ALPHA. 87713 6.63 1 1 0.66 1690 IPI00329607.5 ZINC FINGER PROTEIN 93 (ZINC FINGER PROTEIN HTF34). 53858 10.26 1 1 1.06 1691 IPI00329633.3 THREONYL-TRNA SYNTHETASE. 83435 6.64 1 1 1.24 1692 IPI00332047.1 --none found in database-- 10605 4.79 1 1 8.51 1693 IPI00332128.1 --none found in database-- 48426 4.7 1 1 2.3 1694 IPI00332371.1 6-PHOSPHOFRUCTOKINASE, LIVER TYPE. 85048 7.38 1 1 1.92 1695 IPI00332570.3 POLYADENYLATE-BINDING PROTEIN 2. 58518 9.77 1 1 2.11 1696 IPI00332604.1 FLJ00140 PROTEIN. 64716 10.19 1 1 1.04 1697 IPI00333134.2 SPLICE ISOFORM 2 OF O43426 SYNAPTOJANIN 1. 144887 7.34 1 1 0.99 1698 IPI00333196.1 --none found in database-- 56744 8.49 1 1 1.19 124 1699 IPI00333323.1 --none found in database-- 45158 10.72 1 1 3.4 1700 IPI00333763.5 SIMILAR TO RIKEN CDNA 2900070E19 GENE. 16628 6.78 1 1 8.92 1701 IPI00334255.1 HYPOTHETICAL PROTEIN FLJ39802. 69109 8 1 1 0.97 1702 IPI00334272.2 SIMILAR TO MYOSIN:SUBUNIT=REGULATORY LIGHT CHAIN. 31859 6.24 1 1 3.91 1703 IPI00334324.1 --none found in database-- 26794 10.04 1 1 3.69 1704 IPI00334763.1 --none found in database-- 42146 8.37 1 1 2.9 1705 IPI00334877.1 --none found in database-- 15754 10.25 1 1 7.97 1706 IPI00335168.4 SMOOTH MUSCLE AND NON-MUSCLE MYOSIN ALKALI LIGHT CHAIN ISOFORM 1. 16930 4.29 1 1 8.61 1707 IPI00335186.3 SPLICE ISOFORM 3 OF P07202 THYROID PEROXIDASE PRECURSOR. 102739 7.25 1 1 0.65 1708 IPI00335929.1 SERUM/GLUCOCORTICOID REGULATED KINASE-LIKE ISOFORM 2. 53306 7.24 1 1 1.08 1709 IPI00337584.1 SCAVENGER RECEPTOR CLASS A, MEMBER 3 ISOFORM 1. 70062 6.66 1 1 0.92 1710 IPI00337806.1 --none found in database-- 153097 4.94 1 1 0.72 1711 IPI00337814.1 HYPOTHETICAL PROTEIN. 55244 7.23 1 1 1.98 1712 IPI00373980.1 SIMILAR TO CG11206-PA. 71306 7.2 1 1 0.77 1713 IPI00373982.1 SIMILAR TO 40S RIBOSOMAL PROTEIN S16. 14346 10.41 1 1 8.53 1714 IPI00374005.1 SIMILAR TO TRIOSEPHOSPHATE ISOMERASE 1. 10312 10.22 1 1 8.51 1715 IPI00374119.1 SMOOTH MUSCLE AND NON-MUSCLE MYOSIN ALKALI LIGHT CHAIN ISOFORM 3. 17557 4.24 1 1 8.28 1716 IPI00374239.1 SIMILAR TO 40S RIBOSOMAL PROTEIN S3. 13211 5.17 1 1 10.74 1717 IPI00374318.1 SIMILAR TO 60S RIBOSOMAL PROTEIN L27A. 12538 12.1 1 1 9.73 1718 IPI00374566.1 SIMILAR TO PROTEIN 40KD. 17755 4.47 1 1 6.1 1719 IPI00374734.1 SIMILAR TO MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM22 HOMOLOG (TRANSLOCASE OF OUTER MEMBRANE 22 KDA SUBUNIT HOMOLOG) (HTOM22) (1C9-2). 32926 4.63 1 1 1.68 1720 IPI00374918.1 HYPOTHETICAL PROTEIN XP_353349. 10953 9.56 1 1 4.95 1721 IPI00374976.1 ELKS DELTA. 124904 5.91 1 1 0.83 1722 IPI00375145.1 SPLICE ISOFORM SHORT OF P45974 UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 5. 93308 4.71 1 1 1.92 1723 IPI00375210.1 SIMILAR TO RIBOSE-PHOSPHATE PYROPHOSPHOKINASE III (PHOSPHORIBOSYL PYROPHOSPHATE SYNTHETASE III) (PRS-III). 38356 6.7 1 1 3.72 1724 IPI00375223.1 HYPOTHETICAL PROTEIN LOC255743. 55697 8.61 1 1 0.98 1725 IPI00375731.1 HYPOTHETICAL PROTEIN DKFZP686E2459. 110338 6.12 1 1 1.31 1726 IPI00375802.1 HYPOTHETICAL PROTEIN DKFZP781B1340. 65111 5.4 1 1 0.86 1727 IPI00375907.2 HYPOTHETICAL PROTEIN LOC200186. 74180 7.01 1 1 0.71 1728 IPI00375927.1 HYPOTHETICAL PROTEIN DKFZP686F07114. 123331 6.7 1 1 0.54 1729 IPI00376018.1 CYTOPLASMIC DYNEIN LIGHT CHAIN 2A ISOFORM B. 7342 7.53 1 1 19.05 1730 IPI00376108.1 SIMILAR TO AMINOPEPTIDASE PUROMYCIN SENSITIVE. 46093 4.66 1 1 2.44 1731 IPI00376139.1 PHOSPHOINOSITIDE-3-KINASE, CLASS 3. 101549 6.79 1 1 0.68 1732 IPI00376426.1 SIMILAR TO HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 (HELIX- DESTABILIZING PROTEIN) (SINGLE-STRAND BINDING PROTEIN) (HNRNP CORE PROTEIN A1) (HDP-1) (TOPOISOMERASE-INHIBITOR SUPPRESSED). 21265 6.25 1 1 5.82 1733 IPI00376452.1 SIMILAR TO 40S RIBOSOMAL PROTEIN S20. 14339 10.53 1 1 9.45 1734 IPI00376740.1 SIMILAR TO GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE. 26342 8.9 1 1 2.48 1735 IPI00376747.1 SIMILAR TO HYPOTHETICAL PROTEIN. 232554 6.84 1 1 0.28 1736 IPI00376825.1 SIMILAR TO DJ834A16.1 (SIMILAR TO PGAM). 14527 4.64 1 1 7.75 1737 IPI00376841.1 SIMILAR TO GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE, LIVER (GAPDH). 21168 7.66 1 1 3.63 1738 IPI00376910.1 HYPOTHETICAL PROTEIN XP_352987. 15467 10.35 1 1 3.6 1739 IPI00376992.1 MLL/SEPTIN6 FUSION PROTEIN. 63143 8.15 1 1 1.79 1740 IPI00377006.1 SODIUM CHANNEL PROTEIN TYPE V ALPHA SUBUNIT. 227485 5.18 1 1 0.45 1741 IPI00377087.1 GELSOLIN ISOFORM B. 80641 5.6 1 1 1.78 1742 IPI00377132.1 BH3 INTERACTING DOMAIN DEATH AGONIST ISOFORM 3. 11263 10.22 1 1 15.15 1743 IPI00377238.1 TITIN ISOFORM N2-A. 3.82E+06 6.25 1 1 0.01 1744 IPI00382569.1 --none found in database-- 25911 8.95 1 1 2.2 1745 IPI00382574.1 --none found in database-- 13463 5.56 1 1 10.17 1746 IPI00382629.2 --none found in database-- 158768 7.09 1 1 0.44 1747 IPI00382632.1 --none found in database-- 18183 5.68 1 1 6.13 1748 IPI00382644.1 PUTATIVE EUKARYOTIC TRANSLATION INITIATION FACTOR 1A. 16329 4.73 1 1 7.69 1749 IPI00382716.1 --none found in database-- 11418 9.85 1 1 6.86 125 1750 IPI00382803.2 SPLICE ISOFORM 1 OF P27816 MICROTUBULE-ASSOCIATED PROTEIN 4. 126443 5.39 1 1 0.91 1751 IPI00382869.1 FARNESYL PYROPHOSPHATE SYNTHETASE LIKE-4 PROTEIN. 39750 4.61 1 1 3.45 1752 IPI00383134.1 SIMILAR TO BA92K2.2 (SIMILAR TO UBIQUITIN). 16874 9.67 1 1 3.36 1753 IPI00383234.1 AMPHIPHYSIN I VARIANT CT2. 60634 3.81 1 1 1.76 1754 IPI00383296.1 RIBONUCLEOPROTEIN. 73621 9.29 1 1 2.32 1755 IPI00383323.1 --none found in database-- 35570 10.05 1 1 5.97 1756 IPI00383607.1 HYPOTHETICAL PROTEIN. 200087 6.54 1 1 0.28 1757 IPI00383660.2 KIAA1508 PROTEIN. 68838 8.74 1 1 0.67 1758 IPI00383752.1 DELTA 3, DELTA 2-ENOYL-COA ISOMERASE. 12656 8.51 1 1 3.45 1759 IPI00383786.1 NEBULIN. 111660 9.61 1 1 0.72 1760 IPI00383911.1 HYPOTHETICAL PROTEIN FLJ36307. 20450 10.4 1 1 8.6 1761 IPI00384065.1 HYPOTHETICAL PROTEIN FLJ90034. 58059 6.94 1 1 0.79 1762 IPI00384187.1 HYPOTHETICAL PROTEIN. 40100 6.8 1 1 3.43 1763 IPI00384282.1 CYTOVILLIN 2. 16302 9.83 1 1 6.38 1764 IPI00384366.1 SIMILAR TO RIKEN CDNA 5133400G04 GENE. 20847 10.09 1 1 2.66 1765 IPI00384463.1 EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA. 153361 4.9 1 1 0.72 1766 IPI00384476.1 E74-LIKE FACTOR 1. 67498 4.84 1 1 0.81 1767 IPI00384504.1 SIMILAR TO BCL-2-ASSOCIATED TRANSCRIPTION FACTOR. 57763 11.73 1 1 3.55 1768 IPI00384544.1 MYOSIN REGULATORY LIGHT CHAIN. 19779 4.44 1 1 6.4 1769 IPI00384582.2 SIMILAR TO MICROTUBULE-ASSOCIATED PROTEIN 4. 89580 10.27 1 1 1.28 1770 IPI00384584.1 B-CELL NOVEL PROTEIN ISOFORM 2. 72185 8.11 1 1 0.92 1771 IPI00384585.1 B-CELL NOVEL PROTEIN ISOFORM 1. 73779 8.4 1 1 0.9 1772 IPI00384758.1 HYPOTHETICAL PROTEIN FLJ39514. 69992 6.76 1 1 0.94 1773 IPI00385001.1 HYPOTHETICAL PROTEIN DKFZP686L1653. 182480 6.89 1 1 0.37 1774 IPI00385055.1 HYPOTHETICAL PROTEIN. 100447 5.72 1 1 0.55 1775 IPI00385120.1 HYPOTHETICAL PROTEIN. 6196 10.36 1 1 16.67 1776 IPI00385347.1 HYPOTHETICAL PROTEIN DKFZP779O048. 12455 8.75 1 1 10 1777 IPI00385371.1 B-IND1 PROTEIN. 43543 8.19 1 1 5.68 1778 IPI00385399.1 MITOGEN-ACTIVATED PROTEIN KINASE 3. 43109 6.74 1 1 3.96 1779 IPI00385414.1 HYPOTHETICAL PROTEIN. 66055 7.28 1 1 1.01 1780 IPI00385659.1 HYPOTHETICAL PROTEIN. 16156 8.48 1 1 5.84 1781 IPI00385699.1 NUCLEASE SENSITIVE ELEMENT BINDING PROTEIN 1. 35369 9.5 1 1 5.94 1782 IPI00385860.1 GPR18-ISO. 38034 9.75 1 1 1.2 1783 IPI00386245.1 AMPHIPHYSIN I VARIANT NC1. 62173 3.83 1 1 1.72 1784 IPI00386350.1 HYPOTHETICAL PROTEIN FLJ13874. 19784 9.33 1 1 5.52 1785 IPI00386445.1 RIBOSOMAL PROTEIN S2. 21721 11.51 1 1 6.4 1786 IPI00386533.1 EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA, 1 ISOFORM 3. 158517 4.86 1 1 0.7 1787 IPI00386534.1 EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA, 1 ISOFORM 2. 166589 4.86 1 1 0.66 1788 IPI00386623.1 HYPOTHETICAL PROTEIN. 34580 7.23 1 1 6.71 1789 IPI00386631.1 HYPOTHETICAL PROTEIN KIAA0910. 145331 7.69 1 1 0.99 1790 IPI00386639.1 ELASTIC TITIN. 883025 5.19 1 1 0.06 1791 IPI00386795.1 SIMILAR TO DIFFERENTIALLY EXPRESSED IN FDCP (MOUSE HOMOLOG) 6. 69043 5.65 1 1 1.69 1792 IPI00387125.1 BA196N14.4.2 (PRO1085 PROTEIN, ISOFORM 2, SIMILAR TO PROTEIN SERINE/THREONINE PHOSPHATASE 4 REGULATORY SUBUNIT 1. 38508 6.05 1 1 1.5 1793 IPI00395423.1 HYPOTHETICAL PROTEIN FLJ14719. 94705 6.77 1 1 0.72 1794 IPI00395469.1 SPLICE ISOFORM 3 OF O00154 CYTOSOLIC ACYL COENZYME A THIOESTER HYDROLASE. 42728 10.1 1 1 3.02 1795 IPI00395532.1 PRO3063. 26233 4.53 1 1 4.7 1796 IPI00395643.1 REGULATOR OF G-PROTEIN SIGNALLING 14. 61575 8.47 1 1 0.71 1797 IPI00395748.1 SPLICE ISOFORM 4 OF O00154 CYTOSOLIC ACYL COENZYME A THIOESTER HYDROLASE. 49170 10.05 1 1 2.65 1798 IPI00395750.1 SPLICE ISOFORM LONG OF O75083 WD-REPEAT PROTEIN 1. 67541 6.67 1 1 2.58 1799 IPI00395788.1 BH3 INTERACTING DOMAIN DEATH AGONIST. 26556 6.78 1 1 6.28 1800 IPI00395835.1 PUTATIVE C-MYC-RESPONSIVE ISOFORM 2. 16187 6.79 1 1 11.49 1801 IPI00395865.1 HISTONE ACETYLTRANSFERASE TYPE B SUBUNIT 2. 51576 5.07 1 1 2.84 126 1802 IPI00395972.1 --none found in database-- 152969 4.94 1 1 0.72 1803 IPI00395982.1 --none found in database-- 55277 8.31 1 1 1.22 1804 IPI00395998.1 RIBOSOMAL PROTEIN L32. 15860 11.9 1 1 9.63 1805 IPI00396023.1 COMPLEXIN 1. 15030 4.63 1 1 10.45 1806 IPI00396111.1 CYLD PROTEIN. 107316 5.27 1 1 0.52 1807 IPI00396152.1 MICROTUBULE-ASSOCIATED PROTEIN 4 ISOFORM 3. 119232 4.94 1 1 0.97 1808 IPI00396171.1 MICROTUBULE-ASSOCIATED PROTEIN 4 ISOFORM 2. 122596 5.14 1 1 0.94 1809 IPI00396265.1 NERF-1B. 57389 9.43 1 1 0.94 1810 IPI00396293.1 PMEPA1 VARIANT A PROTEIN. 26201 6.85 1 1 2.11 1811 IPI00396344.1 --none found in database-- 41771 7.8 1 1 1.25 1812 IPI00396426.1 HYPOTHETICAL PROTEIN. 33285 7.08 1 1 1.71 1813 IPI00396437.1 SIMILAR TO SRC HOMOLOGY 3 DOMAIN-CONTAINING PROTEIN HIP-55. 48294 4.72 1 1 2.55 1814 IPI00396482.1 --none found in database-- 24793 9.8 1 1 5.43 1815 IPI00396485.1 --none found in database-- 50183 7.42 1 1 2.41 1816 IPI00396508.1 DNAJ (HSP40) HOMOLOG, SUBFAMILY C, MEMBER 6. 102814 8.08 1 1 0.64 1817 IPI00396540.1 SCAVENGER RECEPTOR CLASS A, MEMBER 3 ISOFORM 2. 57359 6.11 1 1 1.17 1818 IPI00396558.1 SIMILAR TO MEMBRANE PROTEIN OF CHOLINERGIC SYNAPTIC VESICLES. 32559 6.72 1 1 4.67 1819 IPI00396589.1 INTERLEUKIN ENHANCER BINDING FACTOR 2, 45KD. 43062 4.93 1 1 2.82 1820 IPI00396653.1 SEX COMB ON MIDLEG HOMOLOG 1. 68325 9.91 1 1 0.81 127 REFERENCES 1. 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