Details for: TJP1

Gene ID: 7082

Symbol: TJP1

Ensembl ID: ENSG00000104067

Description: tight junction protein 1

Associated with

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: GABAergic neuron (CL0000617)
    Fold Change: 4.41
    Marker Score: 18379
  • Cell Name: oligodendrocyte (CL0000128)
    Fold Change: 3.52
    Marker Score: 8419
  • Cell Name: vascular leptomeningeal cell (CL4023051)
    Fold Change: 3.51
    Marker Score: 4039
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: 3.43
    Marker Score: 7529
  • Cell Name: mature astrocyte (CL0002627)
    Fold Change: 3.19
    Marker Score: 2101
  • Cell Name: corneal endothelial cell (CL0000132)
    Fold Change: 3.17
    Marker Score: 1847
  • Cell Name: regular ventricular cardiac myocyte (CL0002131)
    Fold Change: 3.11
    Marker Score: 69597
  • Cell Name: astrocyte of the cerebral cortex (CL0002605)
    Fold Change: 3.06
    Marker Score: 65287
  • Cell Name: cerebral cortex endothelial cell (CL1001602)
    Fold Change: 2.89
    Marker Score: 1726
  • Cell Name: contractile cell (CL0000183)
    Fold Change: 2.88
    Marker Score: 1563
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: 2.83
    Marker Score: 24802
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: 2.7
    Marker Score: 3263
  • Cell Name: leptomeningeal cell (CL0000708)
    Fold Change: 2.69
    Marker Score: 1329
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: 2.65
    Marker Score: 1548
  • Cell Name: renal interstitial pericyte (CL1001318)
    Fold Change: 2.59
    Marker Score: 2474
  • Cell Name: sst GABAergic cortical interneuron (CL4023017)
    Fold Change: 2.57
    Marker Score: 51206
  • Cell Name: endothelial cell of vascular tree (CL0002139)
    Fold Change: 2.56
    Marker Score: 3727
  • Cell Name: cerebral cortex neuron (CL0010012)
    Fold Change: 2.56
    Marker Score: 7295
  • Cell Name: pyramidal neuron (CL0000598)
    Fold Change: 2.47
    Marker Score: 4155
  • Cell Name: taste receptor cell (CL0000209)
    Fold Change: 2.42
    Marker Score: 2093
  • Cell Name: vip GABAergic cortical interneuron (CL4023016)
    Fold Change: 2.39
    Marker Score: 90738
  • Cell Name: lamp5 GABAergic cortical interneuron (CL4023011)
    Fold Change: 2.39
    Marker Score: 35708
  • Cell Name: inhibitory interneuron (CL0000498)
    Fold Change: 2.37
    Marker Score: 10974
  • Cell Name: regular atrial cardiac myocyte (CL0002129)
    Fold Change: 2.37
    Marker Score: 8411
  • Cell Name: photoreceptor cell (CL0000210)
    Fold Change: 2.36
    Marker Score: 1779
  • Cell Name: astrocyte (CL0000127)
    Fold Change: 2.36
    Marker Score: 2047.5
  • Cell Name: podocyte (CL0000653)
    Fold Change: 2.35
    Marker Score: 867.5
  • Cell Name: kidney interstitial fibroblast (CL1000692)
    Fold Change: 2.33
    Marker Score: 4484.5
  • Cell Name: OFF retinal ganglion cell (CL4023033)
    Fold Change: 2.31
    Marker Score: 969
  • Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
    Fold Change: 2.28
    Marker Score: 84151
  • Cell Name: lung goblet cell (CL1000143)
    Fold Change: 2.26
    Marker Score: 652
  • Cell Name: mesangial cell (CL0000650)
    Fold Change: 2.24
    Marker Score: 2707
  • Cell Name: sncg GABAergic cortical interneuron (CL4023015)
    Fold Change: 2.24
    Marker Score: 17133
  • Cell Name: squamous epithelial cell (CL0000076)
    Fold Change: 2.23
    Marker Score: 1517
  • Cell Name: endothelial cell of uterus (CL0009095)
    Fold Change: 2.19
    Marker Score: 4369
  • Cell Name: cardiac neuron (CL0010022)
    Fold Change: 2.17
    Marker Score: 2708
  • Cell Name: conjunctival epithelial cell (CL1000432)
    Fold Change: 2.16
    Marker Score: 2274
  • Cell Name: near-projecting glutamatergic cortical neuron (CL4023012)
    Fold Change: 2.14
    Marker Score: 20153
  • Cell Name: lactocyte (CL0002325)
    Fold Change: 2.14
    Marker Score: 34355
  • Cell Name: corneal epithelial cell (CL0000575)
    Fold Change: 2.13
    Marker Score: 2351
  • Cell Name: alveolar type 2 fibroblast cell (CL4028006)
    Fold Change: 2.12
    Marker Score: 1181
  • Cell Name: epithelial cell of urethra (CL1000296)
    Fold Change: 2.12
    Marker Score: 1672
  • Cell Name: epithelial cell of prostate (CL0002231)
    Fold Change: 2.12
    Marker Score: 1473
  • Cell Name: oligodendrocyte precursor cell (CL0002453)
    Fold Change: 2.11
    Marker Score: 2611
  • Cell Name: chandelier pvalb GABAergic cortical interneuron (CL4023036)
    Fold Change: 2.1
    Marker Score: 8695
  • Cell Name: caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 2.1
    Marker Score: 8106
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 2.05
    Marker Score: 126338
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: 2.05
    Marker Score: 3024
  • Cell Name: mesothelial cell of epicardium (CL0011019)
    Fold Change: 2.01
    Marker Score: 644
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: 2
    Marker Score: 584
  • Cell Name: type EC enteroendocrine cell (CL0000577)
    Fold Change: 1.99
    Marker Score: 1877
  • Cell Name: epithelial cell of lower respiratory tract (CL0002632)
    Fold Change: 1.98
    Marker Score: 8247.5
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: 1.97
    Marker Score: 2652
  • Cell Name: Sertoli cell (CL0000216)
    Fold Change: 1.96
    Marker Score: 11615
  • Cell Name: pulmonary artery endothelial cell (CL1001568)
    Fold Change: 1.96
    Marker Score: 1683
  • Cell Name: endothelial cell (CL0000115)
    Fold Change: 1.95
    Marker Score: 1750
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: 1.91
    Marker Score: 19720
  • Cell Name: type I pneumocyte (CL0002062)
    Fold Change: 1.9
    Marker Score: 2291.5
  • Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
    Fold Change: 1.9
    Marker Score: 18033
  • Cell Name: capillary endothelial cell (CL0002144)
    Fold Change: 1.87
    Marker Score: 2014
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: 1.86
    Marker Score: 7779
  • Cell Name: L6b glutamatergic cortical neuron (CL4023038)
    Fold Change: 1.85
    Marker Score: 15933
  • Cell Name: ovarian surface epithelial cell (CL2000064)
    Fold Change: 1.84
    Marker Score: 5011
  • Cell Name: vein endothelial cell (CL0002543)
    Fold Change: 1.84
    Marker Score: 1661
  • Cell Name: endothelial cell of pericentral hepatic sinusoid (CL0019022)
    Fold Change: 1.83
    Marker Score: 1955
  • Cell Name: macroglial cell (CL0000126)
    Fold Change: 1.83
    Marker Score: 4195
  • Cell Name: smooth muscle cell of prostate (CL1000487)
    Fold Change: 1.82
    Marker Score: 462
  • Cell Name: male germ cell (CL0000015)
    Fold Change: 1.81
    Marker Score: 521
  • Cell Name: ON retinal ganglion cell (CL4023032)
    Fold Change: 1.81
    Marker Score: 494
  • Cell Name: neuron (CL0000540)
    Fold Change: 1.8
    Marker Score: 7347
  • Cell Name: luminal cell of prostate epithelium (CL0002340)
    Fold Change: 1.74
    Marker Score: 1012
  • Cell Name: neuronal brush cell (CL0000555)
    Fold Change: 1.73
    Marker Score: 5807
  • Cell Name: skeletal muscle satellite stem cell (CL0008011)
    Fold Change: 1.73
    Marker Score: 1849
  • Cell Name: kidney loop of Henle thin descending limb epithelial cell (CL1001111)
    Fold Change: 1.73
    Marker Score: 1863
  • Cell Name: epithelial cell of glomerular capsule (CL1000450)
    Fold Change: 1.72
    Marker Score: 440
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: 1.72
    Marker Score: 1786
  • Cell Name: cholangiocyte (CL1000488)
    Fold Change: 1.71
    Marker Score: 640
  • Cell Name: supporting cell (CL0000630)
    Fold Change: 1.69
    Marker Score: 3181
  • Cell Name: alveolar capillary type 2 endothelial cell (CL4028003)
    Fold Change: 1.69
    Marker Score: 2447
  • Cell Name: basal cell (CL0000646)
    Fold Change: 1.68
    Marker Score: 2170
  • Cell Name: renal principal cell (CL0005009)
    Fold Change: 1.67
    Marker Score: 1288.5
  • Cell Name: club cell (CL0000158)
    Fold Change: 1.66
    Marker Score: 1933
  • Cell Name: parietal epithelial cell (CL1000452)
    Fold Change: 1.64
    Marker Score: 596
  • Cell Name: primordial germ cell (CL0000670)
    Fold Change: 1.64
    Marker Score: 2052
  • Cell Name: fat cell (CL0000136)
    Fold Change: 1.63
    Marker Score: 913
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: 1.63
    Marker Score: 404
  • Cell Name: retinal blood vessel endothelial cell (CL0002585)
    Fold Change: 1.62
    Marker Score: 389
  • Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
    Fold Change: 1.62
    Marker Score: 2498
  • Cell Name: granulosa cell (CL0000501)
    Fold Change: 1.61
    Marker Score: 16200.5
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: 1.61
    Marker Score: 508.5
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: 1.61
    Marker Score: 3661
  • Cell Name: CNS interneuron (CL0000402)
    Fold Change: 1.61
    Marker Score: 772
  • Cell Name: basal epithelial cell of prostatic duct (CL0002236)
    Fold Change: 1.59
    Marker Score: 1413
  • Cell Name: kidney connecting tubule epithelial cell (CL1000768)
    Fold Change: 1.59
    Marker Score: 2247
  • Cell Name: keratinocyte (CL0000312)
    Fold Change: 1.59
    Marker Score: 1324
  • Cell Name: endothelial cell of lymphatic vessel (CL0002138)
    Fold Change: 1.56
    Marker Score: 971
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: 1.55
    Marker Score: 17493
  • Cell Name: malignant cell (CL0001064)
    Fold Change: 1.54
    Marker Score: 20745
  • Cell Name: oogonial cell (CL0000024)
    Fold Change: 1.54
    Marker Score: 2215
  • Cell Name: neural cell (CL0002319)
    Fold Change: 1.54
    Marker Score: 742

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Other Information

**Key Characteristics** TJP1 is a member of the tight junction protein family and is composed of three main domains: the cytoplasmic domain, the transmembrane domain, and the extracellular domain. The cytoplasmic domain interacts with various signaling molecules, including calmodulin and runx1, to regulate tight junction function. The transmembrane domain spans the cell membrane, while the extracellular domain interacts with cadherin and other cell adhesion molecules. TJP1 is highly expressed in various cell types, including GABAergic neurons, oligodendrocytes, and vascular leptomeningeal cells. **Pathways and Functions** TJP1 is involved in various cellular processes, including: 1. **Actin Cytoskeleton Organization**: TJP1 interacts with actin-binding proteins to regulate cytoskeleton organization and cell migration. 2. **Adherens Junction Maintenance**: TJP1 is essential for maintaining adherens junctions, which are critical for cell-cell adhesion and tissue integrity. 3. **Apoptosis Regulation**: TJP1 negatively regulates apoptotic processes by interacting with pro-apoptotic proteins. 4. **Signaling by Hippo Pathway**: TJP1 is involved in the Hippo signaling pathway, which regulates cell growth and proliferation. 5. **Viral Infection Pathways**: TJP1 is a target of SARS-CoV-2, which can disrupt tight junctions and contribute to infection. **Clinical Significance** Dysregulation of TJP1 has been implicated in various diseases, including: 1. **Infectious Diseases**: TJP1 is a target of SARS-CoV-2, and its dysregulation can contribute to infection. 2. **Cancer**: TJP1 is often downregulated in cancer cells, leading to loss of cell-cell adhesion and increased tumor progression. 3. **Neurological Disorders**: TJP1 is involved in the maintenance of the blood-brain barrier and is dysregulated in neurological disorders, such as multiple sclerosis. 4. **Cardiovascular Diseases**: TJP1 is involved in the regulation of blood pressure and is dysregulated in cardiovascular diseases, such as hypertension. In conclusion, TJP1 is a multifunctional protein that plays a critical role in maintaining epithelial and endothelial cell layers. Its dysregulation has been implicated in various diseases, highlighting the importance of tight junctions in maintaining tissue integrity and function. Further research is needed to fully understand the mechanisms of TJP1 and its role in disease pathogenesis.

Genular Protein ID: 2392219501

Symbol: ZO1_HUMAN

Name: Tight junction protein ZO-1

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 8395056

Title: The tight junction protein ZO-1 is homologous to the Drosophila discs-large tumor suppressor protein of septate junctions.

PubMed ID: 8395056

DOI: 10.1073/pnas.90.16.7834

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16572171

Title: Analysis of the DNA sequence and duplication history of human chromosome 15.

PubMed ID: 16572171

DOI: 10.1038/nature04601

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 7798316

Title: Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions.

PubMed ID: 7798316

DOI: 10.1083/jcb.127.6.1617

PubMed ID: 7542259

Title: Epidermal growth factor induces tyrosine phosphorylation and reorganization of the tight junction protein ZO-1 in A431 cells.

PubMed ID: 7542259

DOI: 10.1242/jcs.108.4.1735

PubMed ID: 9792688

Title: The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton.

PubMed ID: 9792688

DOI: 10.1074/jbc.273.45.29745

PubMed ID: 11734628

Title: The coxsackievirus and adenovirus receptor is a transmembrane component of the tight junction.

PubMed ID: 11734628

DOI: 10.1073/pnas.261452898

PubMed ID: 12354695

Title: Isolation and functional characterization of the actin binding region in the tight junction protein ZO-1.

PubMed ID: 12354695

DOI: 10.1096/fj.02-0121fje

PubMed ID: 12023291

Title: Evidence for a functional interaction between cingulin and ZO-1 in cultured cells.

PubMed ID: 12023291

DOI: 10.1074/jbc.m203717200

PubMed ID: 12154091

Title: Molecular cloning, functional expression, and tissue distribution of a novel human gap junction-forming protein, connexin-31.9. Interaction with zona occludens protein-1.

PubMed ID: 12154091

DOI: 10.1074/jbc.m205348200

PubMed ID: 15183511

Title: Connexin47, connexin29 and connexin32 co-expression in oligodendrocytes and Cx47 association with zonula occludens-1 (ZO-1) in mouse brain.

PubMed ID: 15183511

DOI: 10.1016/j.neuroscience.2004.03.063

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: 17015620

Title: Cdc42 GEF Tuba regulates the junctional configuration of simple epithelial cells.

PubMed ID: 17015620

DOI: 10.1083/jcb.200605012

PubMed ID: 17897942

Title: Domain-swapped dimerization of the second PDZ domain of ZO2 may provide a structural basis for the polymerization of claudins.

PubMed ID: 17897942

DOI: 10.1074/jbc.m703826200

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: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 18823282

Title: Characterization of the ubinuclein protein as a new member of the nuclear and adhesion complex components (NACos).

PubMed ID: 18823282

DOI: 10.1042/bc20080072

PubMed ID: 19332538

Title: Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells.

PubMed ID: 19332538

DOI: 10.1074/jbc.m901901200

PubMed ID: 20093627

Title: Myozap, a novel intercalated disc protein, activates serum response factor-dependent signaling and is required to maintain cardiac function in vivo.

PubMed ID: 20093627

DOI: 10.1161/circresaha.109.213256

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: 20930113

Title: Zona occludens proteins modulate podosome formation and function.

PubMed ID: 20930113

DOI: 10.1096/fj.10-155598

PubMed ID: 22016770

Title: Multi-tasking role of the mechanosensing protein Ankrd2 in the signaling network of striated muscle.

PubMed ID: 22016770

DOI: 10.1371/journal.pone.0025519

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: 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: 28169360

Title: Loss of DLG5 promotes breast cancer malignancy by inhibiting the Hippo signaling pathway.

PubMed ID: 28169360

DOI: 10.1038/srep42125

PubMed ID: 31473225

Title: Sperm Flagellar 1 Binds Actin in Intestinal Epithelial Cells and Contributes to Formation of Filopodia and Lamellipodia.

PubMed ID: 31473225

DOI: 10.1053/j.gastro.2019.08.031

PubMed ID: 16737969

Title: Comparative structural analysis of the erbin PDZ domain and the first PDZ domain of ZO-1. Insights into determinants of PDZ domain specificity.

PubMed ID: 16737969

DOI: 10.1074/jbc.m602901200

PubMed ID: 17928286

Title: Domain swapping within PDZ2 is responsible for dimerization of ZO proteins.

PubMed ID: 17928286

DOI: 10.1074/jbc.m707255200

PubMed ID: 18636092

Title: Domain-swapped dimerization of ZO-1 PDZ2 generates specific and regulatory connexin43-binding sites.

PubMed ID: 18636092

DOI: 10.1038/emboj.2008.138

PubMed ID: 20200156

Title: Insights into regulated ligand binding sites from the structure of ZO-1 Src homology 3-guanylate kinase module.

PubMed ID: 20200156

DOI: 10.1074/jbc.m109.093674

PubMed ID: 21240187

Title: Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge controls cell migration.

PubMed ID: 21240187

DOI: 10.1038/emboj.2010.353

PubMed ID: 21387411

Title: Solution structure of the second PDZ domain of Zonula Occludens 1.

PubMed ID: 21387411

DOI: 10.1002/prot.22955

Sequence Information:

  • Length: 1748
  • Mass: 195459
  • Checksum: 189E31617084C0CC
  • Sequence:
  • MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL 
    KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSRPD 
    PEPVSDNEED SYDEEIHDPR SGRSGVVNRR SEKIWPRDRS ASRERSLSPR SDRRSVASSQ 
    PAKPTKVTLV KSRKNEEYGL RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM 
    SLTDAKTLIE RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS 
    GRSHDRPPRR SRSRSPDQRS EPSDHSRHSP QQPSNGSLRS RDEERISKPG AVSTPVKHAD 
    DHTPKTVEEV TVERNEKQTP SLPEPKPVYA QVGQPDVDLP VSPSDGVLPN STHEDGILRP 
    SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV LEDSPAAKEG LEEGDQILRV NNVDFTNIIR 
    EEAVLFLLDL PKGEEVTILA QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG 
    EVFRVVDTLY NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD 
    FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF GPIADVAREK 
    LAREEPDIYQ IAKSEPRDAG TDQRSSGIIR LHTIKQIIDQ DKHALLDVTP NAVDRLNYAQ 
    WYPIVVFLNP DSKQGVKTMR MRLCPESRKS ARKLYERSHK LRKNNHHLFT TTINLNSMND 
    GWYGALKEAI QQQQNQLVWV SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT 
    SDYEDTDTEG GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP 
    QAQPQPIHRI DSPGFKPASQ QKAEASSPVP YLSPETNPAS STSAVNHNVN LTNVRLEEPT 
    PAPSTSYSPQ ADSLRTPSTE AAHIMLRDQE PSLSSHVDPT KVYRKDPYPE EMMRQNHVLK 
    QPAVSHPGHR PDKEPNLTYE PQLPYVEKQA SRDLEQPTYR YESSSYTDQF SRNYEHRLRY 
    EDRVPMYEEQ WSYYDDKQPY PSRPPFDNQH SQDLDSRQHP EESSERGYFP RFEEPAPLSY 
    DSRPRYEQAP RASALRHEEQ PAPGYDTHGR LRPEAQPHPS AGPKPAESKQ YFEQYSRSYE 
    QVPPQGFTSR AGHFEPLHGA AAVPPLIPSS QHKPEALPSN TKPLPPPPTQ TEEEEDPAMK 
    PQSVLTRVKM FENKRSASLE TKKDVNDTGS FKPPEVASKP SGAPIIGPKP TSQNQFSEHD 
    KTLYRIPEPQ KPQLKPPEDI VRSNHYDPEE DEEYYRKQLS YFDRRSFENK PPAHIAASHL 
    SEPAKPAHSQ NQSNFSSYSS KGKPPEADGV DRSFGEKRYE PIQATPPPPP LPSQYAQPSQ 
    PVTSASLHIH SKGAHGEGNS VSLDFQNSLV SKPDPPPSQN KPATFRPPNR EDTAQAAFYP 
    QKSFPDKAPV NGTEQTQKTV TPAYNRFTPK PYTSSARPFE RKFESPKFNH NLLPSETAHK 
    PDLSSKTPTS PKTLVKSHSL AQPPEFDSGV ETFSIHAEKP KYQINNISTV PKAIPVSPSA 
    VEEDEDEDGH TVVATARGIF NSNGGVLSSI ETGVSIIIPQ GAIPEGVEQE IYFKVCRDNS 
    ILPPLDKEKG ETLLSPLVMC GPHGLKFLKP VELRLPHCDP KTWQNKCLPG DPNYLVGANC 
    VSVLIDHF

Genular Protein ID: 3205537733

Symbol: G5E9E7_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11181995

Title: The sequence of the human genome.

PubMed ID: 11181995

DOI: 10.1126/science.1058040

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: 16572171

Title: Analysis of the DNA sequence and duplication history of human chromosome 15.

PubMed ID: 16572171

DOI: 10.1038/nature04601

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: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

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: 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

Sequence Information:

  • Length: 1692
  • Mass: 189676
  • Checksum: A425468CB02037DD
  • Sequence:
  • MERNTFSMDC HSKSTAMEET AIWEQHTVTL HRAPGFGFGI AISGGRDNPH FQSGETSIVI 
    SDVLKGGPAE GQLQENDRVA MVNGVSMDNV EHAFAVQQLR KSGKNAKITI RRKKKVQIPV 
    SRPDPEPVSD NEEDSYDEEI HDPRSGRSGV VNRRSEKIWP RDRSASRERS LSPRSDRRSV 
    ASSQPAKPTK VTLVKSRKNE EYGLRLASHI FVKEISQDSL AARDGNIQEG DVVLKINGTV 
    TENMSLTDAK TLIERSKGKL KMVVQRDERA TLLNVPDLSD SIHSANASER DDISEIQSLA 
    SDHSGRSHDR PPRRSRSRSP DQRSEPSDHS RHSPQQPSNG SLRSRDEERI SKPGAVSTPV 
    KHADDHTPKT VEEVTVERNE KQTPSLPEPK PVYAQVGQPD VDLPVSPSDG VLPNSTHEDG 
    ILRPSMKLVK FRKGDSVGLR LAGGNDVGIF VAGVLEDSPA AKEGLEEGDQ ILRVNNVDFT 
    NIIREEAVLF LLDLPKGEEV TILAQKKKDV YRRIVESDVG DSFYIRTHFE YEKESPYGLS 
    FNKGEVFRVV DTLYNGKLGS WLAIRIGKNH KEVERGIIPN KNRAEQLASV QYTLPKTAGG 
    DRADFWRFRG LRSSKRNLRK SREDLSAQPV QTKFPAYERV VLREAGFLRP VTIFGPIADV 
    AREKLAREEP DIYQIAKSEP RDAGTDQRSS GIIRLHTIKQ IIDQDKHALL DVTPNAVDRL 
    NYAQWYPIVV FLNPDSKQGV KTMRMRLCPE SRKSARKLYE RSHKLRKNNH HLFTTTINLN 
    SMNDGWYGAL KEAIQQQQNQ LVWVSEGKAD GATSDDLDLH DDRLSYLSAP GSEYSMYSTD 
    SRHTSDYEDT DTEGGAYTDQ ELDETLNDEV GTPPESAITR SSEPVREDSS GMHHENQTYP 
    PYSPQAQPQP IHRIDSPGFK PASQQVYRKD PYPEEMMRQN HVLKQPAVSH PGHRPDKEPN 
    LTYEPQLPYV EKQASRDLEQ PTYRYESSSY TDQFSRNYEH RLRYEDRVPM YEEQWSYYDD 
    KQPYPSRPPF DNQHSQDLDS RQHPEESSER GYFPRFEEPA PLSYDSRPRY EQAPRASALR 
    HEEQPAPGYD THGRLRPEAQ PHPSAGPKPA ESKQYFEQYS RSYEQVPPQG FTSRAGHFEP 
    LHGAAAVPPL IPSSQHKPEA LPSNTKPLPP PPTQTEEEED PAMKPQSVLT RVKMFENKRS 
    ASLETKKDVN DTGSFKPPEV ASKPSGAPII GPKPTSQNQF SEHDKTLYRI PEPQKPQLKP 
    PEDIVRSNHY DPEEDEEYYR KQLSYFDRRS FENKPPAHIA ASHLSEPAKP AHSQNQSNFS 
    SYSSKGKPPE ADGVDRSFGE KRYEPIQATP PPPPLPSQYA QPSQPVTSAS LHIHSKGAHG 
    EGNSVSLDFQ NSLVSKPDPP PSQNKPATFR PPNREDTAQA AFYPQKSFPD KAPVNGTEQT 
    QKTVTPAYNR FTPKPYTSSA RPFERKFESP KFNHNLLPSE TAHKPDLSSK TPTSPKTLVK 
    SHSLAQPPEF DSGVETFSIH AEKPKYQINN ISTVPKAIPV SPSAVEEDED EDGHTVVATA 
    RGIFNSNGGV LSSIETGVSI IIPQGAIPEG VEQEIYFKVC RDNSILPPLD KEKGETLLSP 
    LVMCGPHGLK FLKPVELRLP HCASMTPDGW SFALKSSDSS SGDPKTWQNK CLPGDPNYLV 
    GANCVSVLID HF

Genular Protein ID: 1742725041

Symbol: B4DZK4_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Sequence Information:

  • Length: 757
  • Mass: 84771
  • Checksum: 0840537F0C1836DE
  • Sequence:
  • MMRQNHVLKQ PAVSHPGHRP DKEPNLTYEP QLPYVEKQAS RDLEQPTYRY ESSSYTDQFS 
    RNYEHRLRYE DRVPMYEEQW SYYDDKQPYP SRPPFDNQHS QDLDSRQHPE ESSERGYFPR 
    FEEPAPLSYD SRPRYEQAPR ASALRHEEQP APGYDTHGRL RPEAQPHPSA GPKPAESKQY 
    FEQYSRSYEQ VPPQGFTSRA GHFEPLHGAA AVPPLIPSSQ HKPEALPSNT KPLPPPPTQT 
    EEEEDPAMKP QSVLTRVKMF ENKRSASLET KKDVNDTGSF KPPEVASKPS GAPIIGPKPT 
    SQNQFSEHDK TLYRIPEPQK PQLKPPEDIV RSNHYDPEED EEYYRKQLSY FDRRSFENKP 
    PAHIAASHLS EPAKPAHSQN QSNFSSYSSK GKPPEADGVD RSFGEKRYEP IQATPPPPPL 
    PSQYAQPSQP VTSASLHIHS KGAHGEGNSV SLDFQNSLVS KPDPPPSQNK PATFRPPNRE 
    DTAQAAFYPQ KSFPDKAPVN GTEQTQKTVT PAYNRFTPKP YTSSARPFER KFESPKFNHN 
    LLPSETAHKP DLSSKTPTSP KTLVKSHSLA QPPEFDSGVE TFSIHAEKPK YQINNISTVP 
    KAIPVSPSAV EEDEDEDGHT VVATARGIFN SNGGVLSSIE TGVSIIIPQG AIPEGVEQEI 
    YFKVCRDNSI LPPLDKEKGE TLLSPLVMCG PHGLKFLKPV ELRLPHCASM TPDGWSFALK 
    SSDSSSGDPK TWQNKCLPGD PNYLVGANCV SVLIDHF

Genular Protein ID: 1388967868

Symbol: A9CQZ8_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Sequence Information:

  • Length: 1761
  • Mass: 196815
  • Checksum: 49CB477755EE15D7
  • Sequence:
  • LTSTAMEETA IWEQHTVTLH RAPGFGFGIA ISGGRDNPHF QSGETSIVIS DVLKGGPAEG 
    QLQENDRVAM VNGVSMDNVE HAFAVQQLRK SGKNAKITIR RKKKVQIPVS RPDPEPVSDN 
    EEDSYDEEIH DPRSGRSGVV NRRSEKIWPR DRSASRERSL SPRSDRRSVA SSQPAKPTKV 
    TLVKSRKNEE YGLRLASHIF VKEISQDSLA ARDGNIQEGD VVLKINGTVT ENMSLTDAKT 
    LIERSKGKLK MVVQRDERAT LLNVPDLSDS IHSANASERD DISEIQSLAS DHSGRSHDRP 
    PRRSRSRSPD QRSEPSDHSR HSPQQPSNGS LRSRDEERIS KPGAVSTPVK HADDHTPKTV 
    EEVTVERNEK QTPSLPEPKP VYAQVGQPDV DLPVSPSDGV LPNSTHEDGI LRPSMKLVKF 
    RKGDSVGLRL AGGNDVGIFV AGVLEDSPAA KEGLEEGDQI LRVNNVDFTN IIREEAVLFL 
    LDLPKGEEVT ILAQKKKDVY RRIVESDVGD SFYIRTHFEY EKESPYGLSF NKGEVFRVVD 
    TLYNGKLGSW LAIRIGKNHK EVERGIIPNK NRAEQLASVQ YTLPKTAGGD RADFWRFRGL 
    RSSKRNLRKS REDLSAQPVQ TKFPAYERVV LREAGFLRPV TIFGPIADVA REKLAREEPD 
    IYQIAKSEPR DAGTDQRSSG IIRLHTIKQI IDQDKHALLD VTPNAVDRLN YAQWYPIVVF 
    LNPDSKQGVK TMRMRLCPES RKSARKLYER SHKLRKNNHH LFTTTINLNS MNDGWYGALK 
    EAIQQQQNQL VWVSEGKADG ATSDDLDLHD DRLSYLSAPG SEYSMYSTDS RHTSDYEDTD 
    TEGGAYTDQE LDETLNDEVG TPPESAITRS SEPVREDSSG MHHENQTYPP YSPQAQPQPI 
    HRIDSPGFKP ASQQKAEASS PVPYLSPETN PASSTSAVNH NVNLTNVRLE EPTPAPSTSY 
    SPQADSLRTP STEAAHIMLR DQEPSLSSHV DPTKVYRKDP YPEEMMRQNH VLKQPAVSHP 
    GHRPDKEPNL TYEPQLPYVE KQASRDLEQP TYRYESSSYT DQFSRNYEHR LRYEDRVPMY 
    EEQWSYYDDK QPYPSRPPFD NQHSQDLDSR QHPEESSERG YFPRFEEPAP LSYDSRPRYE 
    QAPRASALRH EEQPAPGYDT HGRLRPEAQP HPSAGPKPAE SKQYFEQYSR SYEQVPPQGF 
    TSRAGHFEPL HGAAAVPPLI PSSQHKPEAL PSNTKPLPPP PTQTEEEEDP AMKPQSVLTR 
    VKMFENKRSA SLETKKDVND TGSFKPPEVA SKPSGAPIIG PKPTSQNQFS EHDKTLYRIP 
    EPQKPQLKPP EDIVRSNHYD PEEDEEYYRK QLSYFDRRSF ENKPPAHIAA SHLSEPAKPA 
    HSQNQSNFSS YSSKGKPPEA DGVDRSFGEK RYEPIQATPP PPPLPSQYAQ PSQPVTSASL 
    HIHSKGAHGE GNSVSLDFQN SLVSKPDPPP SQNKPATFRP PNREDTAQAA FYPQKSFPDK 
    APVNGTEQTQ KTVTPAYNRF TPKPYTSSAR PFERKFESPK FNHNLLPSET AHKPDLSSKT 
    PTSPKTLVKS HSLAQPPEFD SGVETFSIHA EKPKYQINNI STVPKAIPVS PSAVEEDEDE 
    DGHTVVATAR GIFNSNGGVL SSIETGVSII IPQGAIPEGV EQEIYFKVCR DNSILPPLDK 
    EKGETLLSPL VMCGPHGLKF LKPVELRLPH CASMTPDGWS FALKSSDSSS GDPKTWQNKC 
    LPGDPNYLVG ANCVSVLIDH F

Genular Protein ID: 307590623

Symbol: A0A087X0K9_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11181995

Title: The sequence of the human genome.

PubMed ID: 11181995

DOI: 10.1126/science.1058040

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: 16572171

Title: Analysis of the DNA sequence and duplication history of human chromosome 15.

PubMed ID: 16572171

DOI: 10.1038/nature04601

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: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

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: 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

Sequence Information:

  • Length: 1768
  • Mass: 197459
  • Checksum: 859D325A088B366C
  • Sequence:
  • MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL 
    KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSRPD 
    PEPVSDNEED SYDEEIHDPR SGRSGVVNRR SEKIWPRDRS ASRERSLSPR SDRRSVASSQ 
    PAKPTKVTLV KSRKNEEYGL RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM 
    SLTDAKTLIE RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS 
    GRSHDRPPRR SRSRSPDQRS EPSDHSRHSP QQPSNGSLRS RDEERISKPG AVSTPVKHAD 
    DHTPKTVEEV TVERNEKQTP SLPEPKPVYA QVGQPDVDLP VSPSDGVLPN STHEDGILRP 
    SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV LEDSPAAKEG LEEGDQILRV NNVDFTNIIR 
    EEAVLFLLDL PKGEEVTILA QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG 
    EVFRVVDTLY NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD 
    FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF GPIADVAREK 
    LAREEPDIYQ IAKSEPRDAG TDQRSSGIIR LHTIKQIIDQ DKHALLDVTP NAVDRLNYAQ 
    WYPIVVFLNP DSKQGVKTMR MRLCPESRKS ARKLYERSHK LRKNNHHLFT TTINLNSMND 
    GWYGALKEAI QQQQNQLVWV SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT 
    SDYEDTDTEG GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP 
    QAQPQPIHRI DSPGFKPASQ QKAEASSPVP YLSPETNPAS STSAVNHNVN LTNVRLEEPT 
    PAPSTSYSPQ ADSLRTPSTE AAHIMLRDQE PSLSSHVDPT KVYRKDPYPE EMMRQNHVLK 
    QPAVSHPGHR PDKEPNLTYE PQLPYVEKQA SRDLEQPTYR YESSSYTDQF SRNYEHRLRY 
    EDRVPMYEEQ WSYYDDKQPY PSRPPFDNQH SQDLDSRQHP EESSERGYFP RFEEPAPLSY 
    DSRPRYEQAP RASALRHEEQ PAPGYDTHGR LRPEAQPHPS AGPKPAESKQ YFEQYSRSYE 
    QVPPQGFTSR AGHFEPLHGA AAVPPLIPSS QHKPEALPSN TKPLPPPPTQ TEEEEDPAMK 
    PQSVLTRVKM FENKRSASLE TKKDVNDTGS FKPPEVASKP SGAPIIGPKP TSQNQFSEHD 
    KTLYRIPEPQ KPQLKPPEDI VRSNHYDPEE DEEYYRKQLS YFDRRSFENK PPAHIAASHL 
    SEPAKPAHSQ NQSNFSSYSS KGKPPEADGV DRSFGEKRYE PIQATPPPPP LPSQYAQPSQ 
    PVTSASLHIH SKGAHGEGNS VSLDFQNSLV SKPDPPPSQN KPATFRPPNR EDTAQAAFYP 
    QKSFPDKAPV NGTEQTQKTV TPAYNRFTPK PYTSSARPFE RKFESPKFNH NLLPSETAHK 
    PDLSSKTPTS PKTLVKSHSL AQPPEFDSGV ETFSIHAEKP KYQINNISTV PKAIPVSPSA 
    VEEDEDEDGH TVVATARGIF NSNGGVLSSI ETGVSIIIPQ GAIPEGVEQE IYFKVCRDNS 
    ILPPLDKEKG ETLLSPLVMC GPHGLKFLKP VELRLPHCAS MTPDGWSFAL KSSDSSSGDP 
    KTWQNKCLPG DPNYLVGANC VSVLIDHF

Genular Protein ID: 1959931507

Symbol: Q6MZU1_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Sequence Information:

  • Length: 1692
  • Mass: 189618
  • Checksum: E117187B0B6BA309
  • Sequence:
  • MERNTFSMDC HSKSTAMEET AIWEQHTVTL HRAPGFGFGI AISGGRDNPH FQSGETSIVI 
    SDVLKGGPAE GQLQENDRVA MVNGVSMDNV EHAFAVQQLR KSGKNAKITI RRKKKVQIPV 
    SRPDPEPVSD NEEDSYDEEI HDPRSGRSGV VNRRSEKIWP RDRSASRERS LSPRSDRRSV 
    ASSQPAKPTK VTLVKSRKNE EYGLRLASHI FVKEISQDSL AARDGNIQEG DVVLKINGTV 
    TENMSLTDAK TLIERSKGKL KMVVQRDERA TLLNVPDLSD SIHSANASER DDISEIQSLA 
    SDHSGRSHDR PPRRSRSRSP DQRSEPSDHS RHSPQQPSNG SLRSRDEERI SKPGAVSTPV 
    KHADDHTPKT VEEVTVERNE KQTPSLPEPK PVYAQVGQPD VDLPVSPSDG VLPNSTHEDG 
    ILRPSMKLVK FRKGDSVGLR LAGGNDVGIF VAGVLEDSPA AKEGLEEGDQ ILRVSNVDFT 
    NIIREEAVLF LLDLPKGEEV TILAQKKKDV YRRIVESDVG DSFYIRTHFE YEKESPYGLS 
    FNKGEVFRVV DTLYNGKLGS WLAIRIGKNH KEVERGIIPN KNRAEQLASV QYTLPKTAGG 
    DRADFWRFRG LRSSKRNLRK SREDLSAQPV QTKFPAYERV VLREAGFLRP VTIFGPIADV 
    AREKLAREEP DIYQIAKSEP RDAGTDQRSS GIIRLHTIKQ IIDQGKHALL DVTPNAVDRL 
    NYAQWYPIVV FLNPDSKQGV KTMRMRLCLE SRKSARKLYE RSHKLRKNNH HLFTTTINLN 
    SMNDGWYGAL KEAIQQQQNQ LVWVSEGKAD GATSDDLDLH DDRLSYLSAP GSEYSMYSTD 
    SRHTSDYEDT DTEGGAYTDQ ELDETLNDEV GTPPESAITR SSEPVREDSS GMHHENQTYP 
    PYSPQAQPQP IHRIDSPGFK PASQQVYRKD PYPEEMMRQN HVLKQPAVSH PGHRPDKEPN 
    LTYEPQLPYV EKQASRDLEQ PTYRYESSSY TDQFSRNYEH RLRYEDRVPM YEEQWSYYDD 
    KQPYPSRPPF DNQHSQDLDS RQHPEESSER GYFPRFEEPA PLSYDSRPRY EQAPRASALR 
    HEEQPAPGYD THGRLRPEAQ PHPSAGPKPA ESKQYFEQYS RSYEQVPPQG FTSRAGHFEP 
    LHGAAAVPPL IPSSQHKPEA LPSNTKPLPP PPTQTEEEED PAMKPQSVLT RVKMFENKRS 
    ASLETKKDVN DTGSFKPPEV ASKPSGAPII GPKPTSQNQF SEHDKTLYRV PEPQKPQLKP 
    PEDIVRSNHY DPEEDEEYYR KQLSYFDRRS FENKPPAHIA ASHLSEPAKL AHSQNQSNFS 
    SYSSKGKPPE ADGVDRSFGE KRYEPIQATP PPPPLPSQYA QPSQPVTSAS LHIHSKGAHG 
    EGNSVSLDFQ NSLVSKPDPP PSQNKPATFR PPNREDTAQA AFYPQKSFPD KAPVNGTEQT 
    QKTVTPAYNR FTPKPYTSSA RPFERKFESP KFNHNLLPSE TAHKPDLSSK TPTSPKTLVK 
    SHSLAQPPEF DSGVETFSIH AEKPKYQINN ISTVPKAIPV SPSAVEEDED EDGHTVVATA 
    RGIFNSNGGV LSSIETGVSI IIPQGAIPEG VEQEIYFKVC RDNSILPPLD KEKGETLLSP 
    LVMCGPHGLK FLKPVELRLP HCASMTPAGW SFALKSSDSS SGDPKTWQNK RLPGDPNYLV 
    GANCVSVLID HF

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. For the full schema, download it here.