Details for: LMO7

Gene ID: 4008

Symbol: LMO7

Ensembl ID: ENSG00000136153

Description: LIM domain 7

Associated with

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: polychromatophilic erythroblast (CL0000550)
    Fold Change: 255.8741
    Cell Significance Index: -39.8000
  • Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
    Fold Change: 155.1785
    Cell Significance Index: -39.3600
  • Cell Name: smooth muscle fiber of ileum (CL1000278)
    Fold Change: 85.6769
    Cell Significance Index: -40.4500
  • Cell Name: mucosal type mast cell (CL0000485)
    Fold Change: 85.3647
    Cell Significance Index: -34.6800
  • Cell Name: ileal goblet cell (CL1000326)
    Fold Change: 60.1619
    Cell Significance Index: -40.3700
  • Cell Name: ciliated cell of the bronchus (CL0002332)
    Fold Change: 36.1459
    Cell Significance Index: -34.5100
  • Cell Name: orthochromatic erythroblast (CL0000552)
    Fold Change: 32.3815
    Cell Significance Index: -39.9300
  • Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
    Fold Change: 15.0213
    Cell Significance Index: -40.2400
  • Cell Name: stromal cell of bone marrow (CL0010001)
    Fold Change: 10.1798
    Cell Significance Index: -40.1700
  • Cell Name: epithelial cell of sweat gland (CL1000448)
    Fold Change: 8.1857
    Cell Significance Index: 5.8500
  • Cell Name: epidermal Langerhans cell (CL0002457)
    Fold Change: 5.7114
    Cell Significance Index: -12.5000
  • Cell Name: conjunctival epithelial cell (CL1000432)
    Fold Change: 5.4054
    Cell Significance Index: 73.7500
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: 5.3579
    Cell Significance Index: 411.1600
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: 3.6127
    Cell Significance Index: 187.6700
  • Cell Name: indirect pathway medium spiny neuron (CL4023029)
    Fold Change: 3.3353
    Cell Significance Index: 147.5300
  • Cell Name: direct pathway medium spiny neuron (CL4023026)
    Fold Change: 3.2120
    Cell Significance Index: 121.6300
  • Cell Name: paneth cell of colon (CL0009009)
    Fold Change: 2.9078
    Cell Significance Index: 43.5700
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: 2.6479
    Cell Significance Index: 120.0200
  • Cell Name: type I muscle cell (CL0002211)
    Fold Change: 2.5292
    Cell Significance Index: 61.7100
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 2.4368
    Cell Significance Index: 488.8300
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 2.3139
    Cell Significance Index: 459.2000
  • Cell Name: tuft cell of colon (CL0009041)
    Fold Change: 2.1340
    Cell Significance Index: 1926.8000
  • Cell Name: thyroid follicular cell (CL0002258)
    Fold Change: 1.9487
    Cell Significance Index: 20.7100
  • Cell Name: corneal epithelial cell (CL0000575)
    Fold Change: 1.8223
    Cell Significance Index: 25.9400
  • Cell Name: hippocampal granule cell (CL0001033)
    Fold Change: 1.7983
    Cell Significance Index: 120.9200
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: 1.6563
    Cell Significance Index: 180.1600
  • Cell Name: centrilobular region hepatocyte (CL0019029)
    Fold Change: 1.4874
    Cell Significance Index: 25.0600
  • Cell Name: cardiac muscle cell (CL0000746)
    Fold Change: 1.4048
    Cell Significance Index: 20.7400
  • Cell Name: hippocampal pyramidal neuron (CL1001571)
    Fold Change: 1.3870
    Cell Significance Index: 39.5800
  • Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 1.2141
    Cell Significance Index: 435.4800
  • Cell Name: type II muscle cell (CL0002212)
    Fold Change: 1.0146
    Cell Significance Index: 16.3700
  • Cell Name: odontoblast (CL0000060)
    Fold Change: 1.0099
    Cell Significance Index: 129.4600
  • Cell Name: umbrella cell of urothelium (CL4030056)
    Fold Change: 0.8345
    Cell Significance Index: 7.6900
  • Cell Name: luminal cell of prostate epithelium (CL0002340)
    Fold Change: 0.7001
    Cell Significance Index: 7.2500
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 0.6725
    Cell Significance Index: 367.2700
  • Cell Name: basal cell of urothelium (CL1000486)
    Fold Change: 0.6708
    Cell Significance Index: 82.4800
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: 0.6047
    Cell Significance Index: 16.9000
  • Cell Name: skeletal muscle fiber (CL0008002)
    Fold Change: 0.5836
    Cell Significance Index: 15.0000
  • Cell Name: small intestine goblet cell (CL1000495)
    Fold Change: 0.5497
    Cell Significance Index: 19.3200
  • Cell Name: colon goblet cell (CL0009039)
    Fold Change: 0.5320
    Cell Significance Index: 52.6300
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: 0.5142
    Cell Significance Index: 58.9200
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: 0.4442
    Cell Significance Index: 72.2500
  • Cell Name: intermediate cell of urothelium (CL4030055)
    Fold Change: 0.4277
    Cell Significance Index: 77.1000
  • Cell Name: forebrain neuroblast (CL1000042)
    Fold Change: 0.3843
    Cell Significance Index: 23.6200
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: 0.3726
    Cell Significance Index: 19.4100
  • Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
    Fold Change: 0.3353
    Cell Significance Index: 7.1400
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: 0.2593
    Cell Significance Index: 12.0900
  • Cell Name: hair follicular keratinocyte (CL2000092)
    Fold Change: 0.2352
    Cell Significance Index: 103.9900
  • Cell Name: GABAergic interneuron (CL0011005)
    Fold Change: 0.1921
    Cell Significance Index: 132.8700
  • Cell Name: enteroendocrine cell of colon (CL0009042)
    Fold Change: 0.1691
    Cell Significance Index: 32.1800
  • Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
    Fold Change: 0.1362
    Cell Significance Index: 10.1500
  • Cell Name: pulmonary alveolar epithelial cell (CL0000322)
    Fold Change: 0.1154
    Cell Significance Index: 87.3800
  • Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
    Fold Change: 0.1107
    Cell Significance Index: 81.2000
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: 0.1005
    Cell Significance Index: 63.8400
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: 0.0562
    Cell Significance Index: 6.6300
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: 0.0096
    Cell Significance Index: 1.3200
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: 0.0084
    Cell Significance Index: 1.4400
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: 0.0049
    Cell Significance Index: 0.1300
  • Cell Name: pancreatic A cell (CL0000171)
    Fold Change: -0.0092
    Cell Significance Index: -6.7800
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: -0.0102
    Cell Significance Index: -19.1200
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: -0.0182
    Cell Significance Index: -33.5700
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: -0.0237
    Cell Significance Index: -36.4100
  • Cell Name: pancreatic PP cell (CL0002275)
    Fold Change: -0.0251
    Cell Significance Index: -15.7000
  • Cell Name: enterocyte of epithelium of small intestine (CL1000334)
    Fold Change: -0.0260
    Cell Significance Index: -0.7500
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: -0.0311
    Cell Significance Index: -42.2600
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: -0.0372
    Cell Significance Index: -16.8700
  • Cell Name: type B pancreatic cell (CL0000169)
    Fold Change: -0.0445
    Cell Significance Index: -25.1200
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: -0.0595
    Cell Significance Index: -1.6200
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: -0.0913
    Cell Significance Index: -9.3300
  • Cell Name: pancreatic endocrine cell (CL0008024)
    Fold Change: -0.0930
    Cell Significance Index: -10.6200
  • Cell Name: pancreatic D cell (CL0000173)
    Fold Change: -0.0998
    Cell Significance Index: -21.0200
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: -0.1160
    Cell Significance Index: -33.3800
  • Cell Name: retinal progenitor cell (CL0002672)
    Fold Change: -0.1249
    Cell Significance Index: -7.0100
  • Cell Name: cortical interneuron (CL0008031)
    Fold Change: -0.1557
    Cell Significance Index: -3.7400
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: -0.1592
    Cell Significance Index: -3.4500
  • Cell Name: L6b glutamatergic cortical neuron (CL4023038)
    Fold Change: -0.1622
    Cell Significance Index: -5.3100
  • Cell Name: enteroendocrine cell of small intestine (CL0009006)
    Fold Change: -0.1730
    Cell Significance Index: -4.3300
  • Cell Name: Purkinje cell (CL0000121)
    Fold Change: -0.2005
    Cell Significance Index: -4.3900
  • Cell Name: epithelial cell of stomach (CL0002178)
    Fold Change: -0.2021
    Cell Significance Index: -23.5500
  • Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
    Fold Change: -0.2031
    Cell Significance Index: -6.4700
  • Cell Name: periportal region hepatocyte (CL0019026)
    Fold Change: -0.2154
    Cell Significance Index: -3.1800
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: -0.2205
    Cell Significance Index: -32.0600
  • Cell Name: lactocyte (CL0002325)
    Fold Change: -0.2430
    Cell Significance Index: -31.3900
  • Cell Name: transit amplifying cell of colon (CL0009011)
    Fold Change: -0.3166
    Cell Significance Index: -10.1400
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: -0.3783
    Cell Significance Index: -39.3900
  • Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
    Fold Change: -0.4130
    Cell Significance Index: -32.7100
  • Cell Name: intestinal tuft cell (CL0019032)
    Fold Change: -0.4141
    Cell Significance Index: -25.3900
  • Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
    Fold Change: -0.4172
    Cell Significance Index: -19.6100
  • Cell Name: respiratory goblet cell (CL0002370)
    Fold Change: -0.4280
    Cell Significance Index: -4.4200
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: -0.4594
    Cell Significance Index: -29.6400
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: -0.4738
    Cell Significance Index: -29.8600
  • Cell Name: near-projecting glutamatergic cortical neuron (CL4023012)
    Fold Change: -0.4779
    Cell Significance Index: -11.9200
  • Cell Name: microfold cell of epithelium of small intestine (CL1000353)
    Fold Change: -0.4912
    Cell Significance Index: -33.9700
  • Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
    Fold Change: -0.4928
    Cell Significance Index: -10.4600
  • Cell Name: transit amplifying cell of small intestine (CL0009012)
    Fold Change: -0.5532
    Cell Significance Index: -11.4800
  • Cell Name: sebum secreting cell (CL0000317)
    Fold Change: -0.5567
    Cell Significance Index: -39.3700
  • Cell Name: regular ventricular cardiac myocyte (CL0002131)
    Fold Change: -0.5942
    Cell Significance Index: -7.6200
  • Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
    Fold Change: -0.6306
    Cell Significance Index: -22.0900
  • Cell Name: leptomeningeal cell (CL0000708)
    Fold Change: -0.6370
    Cell Significance Index: -13.6200
  • Cell Name: stratified epithelial cell (CL0000079)
    Fold Change: -0.6407
    Cell Significance Index: -23.5200

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**Key Characteristics:** 1. **LIM domain**: LMO7 contains a LIM domain, a type of protein-protein interaction domain that is involved in protein-protein interactions and protein modification. 2. **Ubiquitination activity**: LMO7 exhibits ubiquitin ligase activity, which is essential for protein modification, degradation, and regulation of cellular processes. 3. **Cellular localization**: LMO7 is predominantly found in the cytoplasm, nucleus, and plasma membrane, indicating its involvement in various cellular processes. 4. **Expression patterns**: LMO7 is highly expressed in epithelial cells, cardiac myocytes, and immune cells, suggesting its role in maintaining tissue homeostasis and immune function. **Pathways and Functions:** 1. **Adaptive immune system**: LMO7 is involved in the regulation of adaptive immune responses, including antigen processing and presentation by MHC class I molecules. 2. **Antigen processing: ubiquitination & proteasome degradation**: LMO7's ubiquitin ligase activity is crucial for the degradation of antigens by the proteasome, allowing for efficient presentation by MHC class I molecules. 3. **Apical plasma membrane**: LMO7 is involved in the regulation of cell adhesion at the apical plasma membrane, which is essential for maintaining epithelial barrier function. 4. **Cell surface**: LMO7's presence at the cell surface allows it to interact with other proteins and regulate signaling pathways. 5. **Cytoplasm**: LMO7's ubiquitin ligase activity in the cytoplasm is involved in protein modification and degradation, regulating various cellular processes. **Clinical Significance:** 1. **Immune disorders**: Dysregulation of LMO7 has been implicated in autoimmune diseases, such as rheumatoid arthritis and lupus, highlighting its importance in maintaining immune homeostasis. 2. **Cancer**: LMO7's involvement in signaling pathways and protein modification suggests its potential role in cancer development and progression. 3. **Cardiac disease**: LMO7's expression in cardiac myocytes suggests its involvement in cardiac function and disease, including hypertrophic cardiomyopathy. 4. **Respiratory disease**: LMO7's expression in epithelial cells of the lower respiratory tract highlights its potential role in respiratory disease, such as asthma and chronic obstructive pulmonary disease (COPD). In conclusion, LMO7 is a multifunctional protein that plays a crucial role in regulating immune responses, cell adhesion, and protein modification pathways. Its dysregulation has been implicated in various diseases, highlighting the importance of further research into its mechanisms of action and clinical significance.

Genular Protein ID: 286314314

Symbol: LMO7_HUMAN

Name: LIM domain only protein 7

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11935316

Title: A genomic map of a 6-Mb region at 13q21-q22 implicated in cancer development: identification and characterization of candidate genes.

PubMed ID: 11935316

DOI: 10.1007/s00439-001-0646-6

PubMed ID: 15057823

Title: The DNA sequence and analysis of human chromosome 13.

PubMed ID: 15057823

DOI: 10.1038/nature02379

PubMed ID: 10048485

Title: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.

PubMed ID: 10048485

DOI: 10.1093/dnares/5.6.355

PubMed ID: 12168954

Title: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.

PubMed ID: 12168954

DOI: 10.1093/dnares/9.3.99

PubMed ID: 10531035

Title: Identification of a family of human F-box proteins.

PubMed ID: 10531035

DOI: 10.1016/s0960-9822(00)80020-2

PubMed ID: 9826547

Title: Analysis of a human cDNA containing a tissue-specific alternatively spliced LIM domain.

PubMed ID: 9826547

DOI: 10.1006/bbrc.1998.9656

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17924679

Title: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 16959974

Title: The consensus coding sequences of human breast and colorectal cancers.

PubMed ID: 16959974

DOI: 10.1126/science.1133427

Sequence Information:

  • Length: 1683
  • Mass: 192696
  • Checksum: 3E79B2AEAC67F6F5
  • Sequence:
  • MKKIRICHIF TFYSWMSYDV LFQRTELGAL EIWRQLICAH VCICVGWLYL RDRVCSKKDI 
    ILRTEQNSGR TILIKAVTEK NFETKDFRAS LENGVLLCDL INKLKPGVIK KINRLSTPIA 
    GLDNINVFLK ACEQIGLKEA QLFHPGDLQD LSNRVTVKQE ETDRRVKNVL ITLYWLGRKA 
    QSNPYYNGPH LNLKAFENLL GQALTKALED SSFLKRSGRD SGYGDIWCPE RGEFLAPPRH 
    HKREDSFESL DSLGSRSLTS CSSDITLRGG REGFESDTDS EFTFKMQDYN KDDMSYRRIS 
    AVEPKTALPF NRFLPNKSRQ PSYVPAPLRK KKPDKHEDNR RSWASPVYTE ADGTFSSNQR 
    RIWGTNVENW PTVQGTSKSS CYLEEEKAKT RSIPNIVKDD LYVRKLSPVM PNPGNAFDQF 
    LPKCWTPEDV NWKRIKRETY KPWYKEFQGF SQFLLLQALQ TYSDDILSSE THTKIDPTSG 
    PRLITRRKNL SYAPGYRRDD LEMAALDPDL ENDDFFVRKT GVFHANPYVL RAFEDFRKFS 
    EQDDSVERDI ILQCREGELV LPDLEKDDMI VRRIPAQKKE VPLSGAPDRY HPVPFPEPWT 
    LPPEIQAKFL CVFERTCPSK EKSNSCRILV PSYRQKKDDM LTRKIQSWKL GTTVPPISFT 
    PGPCSEADLK RWEAIREASR LRHKKRLMVE RLFQKIYGEN GSKSMSDVSA EDVQNLRQLR 
    YEEMQKIKSQ LKEQDQKWQD DLAKWKDRRK SYTSDLQKKK EEREEIEKQA LEKSKRSSKT 
    FKEMLQDRES QNQKSTVPSR RRMYSFDDVL EEGKRPPTMT VSEASYQSER VEEKGATYPS 
    EIPKEDSTTF AKREDRVTTE IQLPSQSPVE EQSPASLSSL RSRSTQMEST RVSASLPRSY 
    RKTDTVRLTS VVTPRPFGSQ TRGISSLPRS YTMDDAWKYN GDVEDIKRTP NNVVSTPAPS 
    PDASQLASSL SSQKEVAATE EDVTRLPSPT SPFSSLSQDQ AATSKATLSS TSGLDLMSES 
    GEGEISPQRE VSRSQDQFSD MRISINQTPG KSLDFGFTIK WDIPGIFVAS VEAGSPAEFS 
    QLQVDDEIIA INNTKFSYND SKEWEEAMAK AQETGHLVMD VRRYGKAGSP ETKWIDATSG 
    IYNSEKSSNL SVTTDFSESL QSSNIESKEI NGIHDESNAF ESKASESISL KNLKRRSQFF 
    EQGSSDSVVP DLPVPTISAP SRWVWDQEEE RKRQERWQKE QDRLLQEKYQ REQEKLREEW 
    QRAKQEAERE NSKYLDEELM VLSSNSMSLT TREPSLATWE ATWSEGSKSS DREGTRAGEE 
    ERRQPQEEVV HEDQGKKPQD QLVIERERKW EQQLQEEQEQ KRLQAEAEEQ KRPAEEQKRQ 
    AEIERETSVR IYQYRRPVDS YDIPKTEEAS SGFLPGDRNK SRSTTELDDY STNKNGNNKY 
    LDQIGNMTSS QRRSKKEQVP SGAELERQQI LQEMRKRTPL HNDNSWIRQR SASVNKEPVS 
    LPGIMRRGES LDNLDSPRSN SWRQPPWLNQ PTGFYASSSV QDFSRPPPQL VSTSNRAYMR 
    NPSSSVPPPS AGSVKTSTTG VATTQSPTPR SHSPSASQSG SQLRNRSVSG KRICSYCNNI 
    LGKGAAMIIE SLGLCYHLHC FKCVACECDL GGSSSGAEVR IRNHQLYCND CYLRFKSGRP 
    TAM

Genular Protein ID: 1068293739

Symbol: F8WD26_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11237011

Title: Initial sequencing and analysis of the human genome.

PubMed ID: 11237011

DOI: 10.1038/35057062

PubMed ID: 15057823

Title: The DNA sequence and analysis of human chromosome 13.

PubMed ID: 15057823

DOI: 10.1038/nature02379

PubMed ID: 15496913

Title: Finishing the euchromatic sequence of the human genome.

PubMed ID: 15496913

DOI: 10.1038/nature03001

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17924679

Title: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

Sequence Information:

  • Length: 1631
  • Mass: 186179
  • Checksum: FAB88F8504297121
  • Sequence:
  • MEGLEEAEAN CSVAFAEAQR WVEAVTEKNF ETKDFRASLE NGVLLCDLIN KLKPGVIKKI 
    NRLSTPIAGL DNINVFLKAC EQIGLKEAQL FHPGDLQDLS NRVTVKQEET DRRVKNVLIT 
    LYWLGRKAQS NPYYNGPHLN LKAFENLLGQ ALTKALEDSS FLKRSGRDSG YGDIWCPERG 
    EFLAPPRHHK REDSFESLDS LGSRSLTSCS SDITLRGGRE GFESDTDSEF TFKMQDYNKD 
    DMSYRRISAV EPKTALPFNR FLPNKSRQPS YVPAPLRKKK PDKHEDNRRS WASPVYTEAD 
    GTFSSNQRRI WGTNVENWPT VQGTSKSSCY LEEEKAKTRS IPNIVKDDLY VRKLSPVMPN 
    PGNAFDQFLP KCWTPEDVNW KRIKRETYKP WYKEFQGFSQ FLLLQALQTY SDDILSSETH 
    TKIDPTSGPR LITRRKNLSY APGYRRDDLE MAALDPDLEN DDFFVRKTGA FHANPYVLRA 
    FEDFRKFSEQ DDSVERDIIL QCREGELVLP DLEKDDMIVR RIPAQKKEVP LSGAPDRYHP 
    VPFPEPWTLP PEIQAKFLCV LERTCPSKEK SNSCRILVPS YRQKKDDMLT RKIQSWKLGT 
    TVPPISFTPG PCSEADLKRW EAIREASRLR HKKRLMVERL FQKIYGENGS KSMSDVSAED 
    VQNLRQLRYE EMQKIKSQLK EQDQKWQDDL AKWKDRRKSY TSDLQKKKEE REEIEKQALE 
    KSKRSSKTFK EMLQDRESQN QKSTVPSRRR MYSFDDVLEE GKRPPTMTVS EASYQSERVE 
    EKGATYPSEI PKEDSTTFAK REDRVTTEIQ LPSQSPVEEQ SPASLSSLRS RSTQMESTRV 
    SASLPRSYRK TDTVRLTSVV TPRPFGSQTR GISSLPRSYT MDDAWKYNGD VEDIKRTPNN 
    VVSTPAPSPD ASQLASSLSS QKEVAATEED VTRLPSPTSP FSSLSQDQAA TSKATLSSTS 
    GLDLMSESGE GEISPQREVS RSQDQFSDMR ISINQTPGKS LDFGFTIKWD IPGIFVASVE 
    AGSPAEFSQL QVDDEIIAIN NTKFSYNDSK EWEEAMAKAQ ETGHLVMDVR RYGKAGSPET 
    KWIDATSGIY NSEKSSNLSV TTDFSESLQS SNIESKEING IHDESNAFES KASESISLKN 
    LKRRSQFFEQ GSSDSVVPDL PVPTISAPSR WVWDQEEERK RQERWQKEQD RLLQEKYQRE 
    QEKLREEWQR AKQEAERENS KYLDEELMVL SSNSMSLTTR EPSLATWEAT WSEGSKSSDR 
    EGTRAGEEER RQPQEEVVHE DQGKKPQDQL VIERERKWEQ QLQEEQEQKR LQAEAEEQKR 
    PAEEQKRQAE IERETSVRIY QYRRPVDSYD IPKTEEASSG FLPGDRNKSR STTELDDYST 
    NKNGNNKYLD QIGNMTSSQR RSKKEQVPSG AELERQQILQ EMRKRTPLHN DNSWIRQRSA 
    SVNKEPVSLP GIMRRGESLD NLDSPRSNSW RQPPWLNQPT GFYASSSVQD FSRPPPQLVS 
    TSNRAYMRNP SSSVPPPSAG SVKTSTTGVA TTQSPTPRSH SPSASQSGSQ LRNRSVSGKR 
    ICSYCNNILG KGAAMIIESL GLCYHLHCFK CVACECDLGG SSSGAEVRIR NHQLYCNDCY 
    LRFKSGRPTA M

Genular Protein ID: 3653551670

Symbol: E9PMT2_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11237011

Title: Initial sequencing and analysis of the human genome.

PubMed ID: 11237011

DOI: 10.1038/35057062

PubMed ID: 15057823

Title: The DNA sequence and analysis of human chromosome 13.

PubMed ID: 15057823

DOI: 10.1038/nature02379

PubMed ID: 15496913

Title: Finishing the euchromatic sequence of the human genome.

PubMed ID: 15496913

DOI: 10.1038/nature03001

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17924679

Title: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

Sequence Information:

  • Length: 1398
  • Mass: 160022
  • Checksum: 1F6FF3E6124190AF
  • Sequence:
  • MQDYNKDDMS YRRISAVEPK TALPFNRFLP NKSRQPSYVP APLRKKKPDK HEDNRRSWAS 
    PVYTEADGTF SSNQRRIWGT NVENWPTVQG TSKSSCYLEE EKAKTRSIPN IVKDDLYVRK 
    LSPVMPNPGN AFDQFLPKCW TPEDVNWKRI KRETYKPWYK EFQGFSQFLL LQALQTYSDD 
    ILSSETHTKI DPTSGPRLIT RRKNLSYAPG YRRDDLEMAA LDPDLENDDF FVRKTGAFHA 
    NPYVLRAFED FRKFSEQDDS VERDIILQCR EGELVLPDLE KDDMIVRRIP AQKKEVPLSG 
    APDRYHPVPF PEPWTLPPEI QAKFLCVLER TCPSKEKSNS CRILVPSYRQ KKDDMLTRKI 
    QSWKLGTTVP PISFTPGPCS EADLKRWEAI REASRLRHKK RLMVERLFQK IYGENGSKSM 
    SDVSAEDVQN LRQLRYEEMQ KIKSQLKEQD QKWQDDLAKW KDRRKSYTSD LQKKKEEREE 
    IEKQALEKSK RSSKTFKEML QDRESQNQKS TVPSRRRMYS FDDVLEEGKR PPTMTVSEAS 
    YQSERVEEKG ATYPSEIPKE DSTTFAKRED RVTTEIQLPS QSPVEEQSPA SLSSLRSRST 
    QMESTRVSAS LPRSYRKTDT VRLTSVVTPR PFGSQTRGIS SLPRSYTMDD AWKYNGDVED 
    IKRTPNNVVS TPAPSPDASQ LASSLSSQKE VAATEEDVTR LPSPTSPFSS LSQDQAATSK 
    ATLSSTSGLD LMSESGEGEI SPQREVSRSQ DQFSDMRISI NQTPGKSLDF GFTIKWDIPG 
    IFVASVEAGS PAEFSQLQVD DEIIAINNTK FSYNDSKEWE EAMAKAQETG HLVMDVRRYG 
    KAGSPETKWI DATSGIYNSE KSSNLSVTTD FSESLQSSNI ESKEINGIHD ESNAFESKAS 
    ESISLKNLKR RSQFFEQGSS DSVVPDLPVP TISAPSRWVW DQEEERKRQE RWQKEQDRLL 
    QEKYQREQEK LREEWQRAKQ EAERENSKYL DEELMVLSSN SMSLTTREPS LATWEATWSE 
    GSKSSDREGT RAGEEERRQP QEEVVHEDQG KKPQDQLVIE RERKWEQQLQ EEQEQKRLQA 
    EAEEQKRPAE EQKRQAEIER ETSVRIYQYR RPVDSYDIPK TEEASSGFLP GDRNKSRSTT 
    ELDDYSTNKN GNNKYLDQIG NMTSSQRRSK KEQVPSGAEL ERQQILQEMR KRTPLHNDNS 
    WIRQRSASVN KEPVSLPGIM RRGESLDNLD SPRSNSWRQP PWLNQPTGFY ASSSVQDFSR 
    PPPQLVSTSN RAYMRNPSSS VPPPSAGSVK TSTTGVATTQ SPTPRSHSPS ASQSGSQLRN 
    RSVSGKRICS YCNNILGKGA AMIIESLGLC YHLHCFKCVA CECDLGGSSS GAEVRIRNHQ 
    LYCNDCYLRF KSGRPTAM

Genular Protein ID: 849257810

Symbol: A0A0A0MTE2_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11237011

Title: Initial sequencing and analysis of the human genome.

PubMed ID: 11237011

DOI: 10.1038/35057062

PubMed ID: 15057823

Title: The DNA sequence and analysis of human chromosome 13.

PubMed ID: 15057823

DOI: 10.1038/nature02379

PubMed ID: 15496913

Title: Finishing the euchromatic sequence of the human genome.

PubMed ID: 15496913

DOI: 10.1038/nature03001

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17924679

Title: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

Sequence Information:

  • Length: 1385
  • Mass: 158203
  • Checksum: 885B4564E783EB43
  • Sequence:
  • MQDYNKDDMS YRRISAVEPK TALPFNRFLP NKSRQPSYVP APLRKKKPDK HEDNRRSWAS 
    PVYTEADGTF SSNQRRIWGT NVENWPTVQG TSKSSCYLEE EKAKTRSIPN IVKDDLYVRK 
    LSPVMPNPGN AFDQFLPKCW TPEDVNWKRI KRETYKPWYK EFQGFSQFLL LQALQTYSDD 
    ILSSETHTKI DPTSGPRLIT RRKNLSYAPG YRRDDLEMAA LDPDLENDDF FVRKTGAFHA 
    NPYVLRAFED FRKFSEQDDS VERDIILQCR EGELVLPDLE KDDMIVRRIP AQKKEVPLSG 
    APDRYHPVPF PEPWTLPPEI QAKFLCVLER TCPSKEKSNS CRILVPSYRQ KKDDMLTRKI 
    QSWKLGTTVP PISFTPGPCS EADLKRWEAI REASRLRHKK RLMVERLFQK IYGENGSKSM 
    SDVSAEDVQN LRQLRYEEMQ KIKSQLKEQD QKWQDDLAKW KDRRKSYTSD LQKKKEEREE 
    IEKQALEKSK RSSKTFKEML QDRESQNQKS TVPSRRRMYS FDDVLEEGKR PPTMTVSEAS 
    YQSERVEEKG ATYPSEIPKE DSTTFAKRED RVTTEIQLPS QSPVEEQSPA SLSSLRSRST 
    QMESTRVSAS LPRSYRKTDT VRLTSVVTPR PFGSQTRGIS SLPRSYTMDD AWKYNGDVED 
    IKRTPNNVVS TPAPSPDASQ LASSLSSQKE VAATEEDVTR LPSPTSPFSS LSQDQAATSK 
    ATLSSTSGLD LMSESGEGEI SPQREVSRSQ DQFSDMRISI NQTPGKSLDF GFTIKWDIPG 
    IFVASVEAGS PAEFSQLQVD DEIIAINNTK FSYNDSKEWE EAMAKAQETG HLVMDVRRYG 
    KAGSPETKWI DATSGIYNSE KSSNLSVTTD FSESLQSSNI ESKEINGIHD ESNAFESKAS 
    ESISLKNLKR RSQFFEQGSS DSVVPDLPVP TISAPSRWVW DQEEERKRQE RWQKEQDRLL 
    QEKYQREQEK LREEWQRAKQ EAERENSKYL DEELMVLSSN SMSLTTREPS LATWEATWSE 
    GSKSSDREGT RAGEEERRQP QEEVVHEDQG KKPQDQLVIE RERKWEQQLQ EEQEQKRLQA 
    EAEEQKRPAE EQKRQAEIER ETSVRIYQYR RPVDSYDIPK TEEASSGFLP GDRNKSRSTT 
    ELDDYSTNKN GNNKYLDQIG NMTSSQRRSK KEQVPSGAEL ERQQILQEMR KRTPLHNDNS 
    WIRQRSASVN KEPVSLPGIM RRGESLDNLD SPRSNSWRQP PWLNQPTGFY ASSSVQDFSR 
    PPPQLVSTSN RAYMRNPSSS VPPPSAGSVK TSTTGVATTQ SPTPRSHSPS ASQSGSQLRN 
    SVLPVSVTSE ALPQELKSGS ETTNCTATTA ISDSNLDGQP PCDVSLHTKA LLQIEEEVVA 
    AHVDL

Genular Protein ID: 1348366939

Symbol: F8J2B5_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 21670154

Title: LMO7 mediates cell-specific activation of the Rho-myocardin-related transcription factor-serum response factor pathway and plays an important role in breast cancer cell migration.

PubMed ID: 21670154

DOI: 10.1128/MCB.01365-10

Sequence Information:

  • Length: 1631
  • Mass: 186241
  • Checksum: 5FC1483913806856
  • Sequence:
  • MEGLEEAEAN CSVAFAEAQR WVEAVTEKNF ETKDFRASLE NGVLLCDLIN KLKPGVIKKI 
    NRLSTPIAGL DNINVFLKAC EQIGLKEAQL FHPGDLQDLS NRVTVKQEET DRRVKNVLIT 
    LYWLGRKAQS NPYYNGPHLN LKAFENLLGQ ALTKALEDSS FLKRSGRDSG YGDIWCPERG 
    EFLAPPRHHK REDSFESLDS LGSRSLTSCS SDITLRGGRE GFESDTDSEF TFKMQDYNKD 
    DMSYRRISAV EPKTALPFNR FLPNKSRQPS YVPAPLRKKK PDKHEDNRRS WASPVYTEAD 
    GTFSSNQRRI WGTNVENWPT VQGTSKSSCY LEEEKAKTRS IPNIVKDDLY VRKLSPVMPN 
    PGNAFDQFLP KCWTPEDVNW KRIKRETYKP WYKEFQGFSQ FLLLQALQTY SDDILSSETH 
    TKIDPTSGPR LITRRKNLSY APGYRRDDLE MAALDPDLEN DDFFVRKTGV FHANPYVLRA 
    FEDFRKFSEQ DDSVERDIIL QCREGELVLP DLEKDDMIVR RIPAQKKEVP LSGAPDRYHP 
    VPFPEPWTLP PEIQAKFLCV FERTCPSKEK SNSCRILVPS YRQKKDDMLT RKIQSWKLGT 
    TVPPISFTPG PCSEADLKRW EAIREASRLR HKKRLMVERL FQKIYGENGS KSMSDVSAED 
    VQNLRQLRYE EMQKIKSQLK EQDQKWQDDL AKWKDRRKSY TSDLQKKKEE REEIEKQALE 
    KSKRSSKTFK EMLQDRESQN QKSTVPSRRR MYSFDDVLEE GKRPPTMTVS EASYQSERVE 
    EKGATYPSEI PKEDSTTFAK REDRVTTEIQ LPSQSPVEEQ SPASLSSLRS RSTQMESTRV 
    SASLPRSYRK TDTVRLTSVV TPRPFGSQTR GISSLPRSYT MDDAWKYNGD VEDIKRTPNN 
    VVSTPAPSPD ASQLASSLSS QKEVAATEED VTRLPSPTSP FSSLSQDQAA TSKATLSSTS 
    GLDLMSESGE GEISPQREVS RSQDQFSDMR ISINQTPGKS LDFGFTIKWD IPGIFVASVE 
    AGSPAEFSQL QVDDEIIAIN NTKFSYNDSK EWEEAMAKAQ ETGHLVMDVR RYGKAGSPET 
    KWIDATSGIY NSEKSSNLSV TTDFSESLQS SNIESKEING IHDESNAFES KASESISLKN 
    LKRRSQFFEQ GSSDSVVPDL PVPTISAPSR WVWDQEEERK RQERWQKEQD RLLQEKYQRE 
    QEKLREEWQR AKQEAERENS KYLDEELMVL SSNSMSLTTR EPSLATWEAT WSEGSKSSDR 
    EGTRAGEEER RQPQEEVVHE DQGKKPQDQL VIERERKWEQ QLQEEQEQKR LQAEAEEQKR 
    PAEEQKRQAE IERETSVRIY QYRRPVDSYD IPKTEEASSG FLPGDRNKSR STTELDDYST 
    NKNGNNKYLD QIGNMTSSQR RSKKEQVPSG AELERQQILQ EMRKRTPLHN DNSWIRQRSA 
    SVNKEPVSLP GIMRRGESLD NLDSPRSNSW RQPPWLNQPT GFYASSSVQD FSRPPPQLVS 
    TSNRAYMRNP SSSVPPPSAG SVKTSTTGVA TTQSPTPRSH SPSASQSGSQ LRNRSVSGKR 
    ICSYCNNILG KGAAMIIESL GLCYHLHCFK CVACECDLGG SSSGAEVRIR NHQLYCNDCY 
    LRFKSGRPTA M

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.