ID CDCP1_HUMAN Reviewed; 836 AA. AC Q9H5V8; Q49UB4; Q6NT71; Q6U9Y2; Q8WU91; Q96QU7; Q9H676; Q9H8C2; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 3. DT 24-JAN-2024, entry version 159. DE RecName: Full=CUB domain-containing protein 1; DE AltName: Full=Membrane glycoprotein gp140; DE AltName: Full=Subtractive immunization M plus HEp3-associated 135 kDa protein; DE Short=SIMA135; DE AltName: Full=Transmembrane and associated with src kinases; DE AltName: CD_antigen=CD318; DE Flags: Precursor; GN Name=CDCP1; Synonyms=TRASK; ORFNames=UNQ2486/PRO5773; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND RP VARIANT GLY-709. RX PubMed=11466621; DOI=10.1038/sj.onc.1204566; RA Scherl-Mostageer M., Sommergruber W., Abseher R., Hauptmann R., Ambros P., RA Schweifer N.; RT "Identification of a novel gene, CDCP1, overexpressed in human colorectal RT cancer."; RL Oncogene 20:4402-4408(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 30-48; 281-293 RP AND 427-438, GLYCOSYLATION, PHOSPHORYLATION, SHEDDING, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND VARIANTS ARG-525 AND GLY-709. RX PubMed=12660814; DOI=10.1038/sj.onc.1206220; RA Hooper J.D., Zijlstra A., Aimes R.T., Liang H., Claassen G.F., Tarin D., RA Testa J.E., Quigley J.P.; RT "Subtractive immunization using highly metastatic human tumor cells RT identifies SIMA135/CDCP1, a 135 kDa cell surface phosphorylated RT glycoprotein antigen."; RL Oncogene 22:1783-1794(2003). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 30-34 AND RP 369-375, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION, RP GLYCOSYLATION, TISSUE SPECIFICITY, INTERACTION WITH CDH2; CDH3; SDC1; SDC4 RP AND ST14, AND FUNCTION. RX PubMed=16007225; DOI=10.1038/sj.onc.1208582; RA Bhatt A.S., Erdjument-Bromage H., Tempst P., Craik C.S., Moasser M.M.; RT "Adhesion signaling by a novel mitotic substrate of src kinases."; RL Oncogene 24:5333-5343(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS RP ARG-525 AND GLY-709. RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-697 (ISOFORM 1), AND VARIANT VAL-673. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-691 (ISOFORM 1), IDENTIFICATION BY MASS RP SPECTROMETRY, PHOSPHORYLATION AT TYR-734, GLYCOSYLATION, TRYPTIC CLEAVAGE, RP AND VARIANT ARG-525. RC TISSUE=Epidermis; RX PubMed=14739293; DOI=10.1074/jbc.m309678200; RA Brown T.A., Yang T.M., Zaitsevskaia T., Xia Y., Dunn C.A., Sigle R.O., RA Knudsen B., Carter W.G.; RT "Adhesion or plasmin regulates tyrosine phosphorylation of a novel membrane RT glycoprotein p80/gp140/CUB domain-containing protein 1 in epithelia."; RL J. Biol. Chem. 279:14772-14783(2004). RN [9] RP FUNCTION, AND PHOSPHORYLATION. RC TISSUE=Epidermis; RX PubMed=8647901; DOI=10.1083/jcb.132.4.727; RA Xia Y., Gil S.G., Carter W.G.; RT "Anchorage mediated by integrin alpha6beta4 to laminin 5 (epiligrin) RT regulates tyrosine phosphorylation of a membrane-associated 80-kD RT protein."; RL J. Cell Biol. 132:727-740(1996). RN [10] RP FUNCTION. RX PubMed=12799299; DOI=10.1111/j.1749-6632.2003.tb03249.x; RA Conze T., Lammers R., Kuci S., Scherl-Mostageer M., Schweifer N., Kanz L., RA Buehring H.-J.; RT "CDCP1 is a novel marker for hematopoietic stem cells."; RL Ann. N. Y. Acad. Sci. 996:222-226(2003). RN [11] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=15153610; DOI=10.1634/stemcells.22-3-334; RA Buehring H.-J., Kuci S., Conze T., Rathke G., Bartolovic K., Gruenebach F., RA Scherl-Mostageer M., Bruemmendorf T.H., Schweifer N., Lammers R.; RT "CDCP1 identifies a broad spectrum of normal and malignant stem/progenitor RT cell subsets of hematopoietic and nonhematopoietic origin."; RL Stem Cells 22:334-343(2004). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SRC AND PRKCG, AND RP MUTAGENESIS OF TYR-734 AND TYR-762. RX PubMed=15851033; DOI=10.1016/j.cell.2005.02.019; RA Benes C.H., Wu N., Elia A.E.H., Dharia T., Cantley L.C., Soltoff S.P.; RT "The C2 domain of PKCdelta is a phosphotyrosine binding domain."; RL Cell 121:271-280(2005). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION. RX PubMed=16404722; DOI=10.1002/pmic.200500180; RA Andre M., Le Caer J.-P., Greco C., Planchon S., El Nemer W., Boucheix C., RA Rubinstein E., Chamot-Rooke J., Le Naour F.; RT "Proteomic analysis of the tetraspanin web using LC-ESI-MS/MS and MALDI- RT FTICR-MS."; RL Proteomics 6:1437-1449(2006). RN [14] RP SUBCELLULAR LOCATION. RX PubMed=17335815; DOI=10.1016/j.febslet.2007.02.025; RA Perry S.E., Robinson P., Melcher A., Quirke P., Buehring H.-J., Cook G.P., RA Blair G.E.; RT "Expression of the CUB domain containing protein 1 (CDCP1) gene in RT colorectal tumour cells."; RL FEBS Lett. 581:1137-1142(2007). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: May be involved in cell adhesion and cell matrix association. CC May play a role in the regulation of anchorage versus migration or CC proliferation versus differentiation via its phosphorylation. May be a CC novel marker for leukemia diagnosis and for immature hematopoietic stem CC cell subsets. Belongs to the tetraspanin web involved in tumor CC progression and metastasis. {ECO:0000269|PubMed:11466621, CC ECO:0000269|PubMed:12799299, ECO:0000269|PubMed:15153610, CC ECO:0000269|PubMed:16007225, ECO:0000269|PubMed:16404722, CC ECO:0000269|PubMed:8647901}. CC -!- SUBUNIT: Interacts with CDH2/N-cadherin, CDH3/P-cadherin, CC SDC1/syndecan-1, SDC4/syndecan-4 and the serine protease ST14/MT-SP1. CC Also interacts with SRC and PRKCG/protein kinase C gamma. CC {ECO:0000269|PubMed:15851033, ECO:0000269|PubMed:16007225}. CC -!- INTERACTION: CC Q9H5V8; O00560: SDCBP; NbExp=6; IntAct=EBI-1019736, EBI-727004; CC Q9H5V8; P12931: SRC; NbExp=3; IntAct=EBI-1019736, EBI-621482; CC Q9H5V8; P07947: YES1; NbExp=2; IntAct=EBI-1019736, EBI-515331; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305}; Single- CC pass membrane protein {ECO:0000305}. Note=Shedding may also lead to a CC soluble peptide. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9H5V8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H5V8-2; Sequence=VSP_017432; CC Name=3; CC IsoId=Q9H5V8-3; Sequence=VSP_017433, VSP_017434; CC -!- TISSUE SPECIFICITY: Highly expressed in mitotic cells with low CC expression during interphase. Detected at highest levels in skeletal CC muscle and colon with lower levels in kidney, small intestine, placenta CC and lung. Up-regulated in a number of human tumor cell lines, as well CC as in colorectal cancer, breast carcinoma and lung cancer. Also CC expressed in cells with phenotypes reminiscent of mesenchymal stem CC cells and neural stem cells. {ECO:0000269|PubMed:11466621, CC ECO:0000269|PubMed:12660814, ECO:0000269|PubMed:15153610, CC ECO:0000269|PubMed:16007225}. CC -!- PTM: Phosphorylated on tyrosine by kinases of the SRC family such as CC SRC and YES as well as by the protein kinase C gamma/PRKCG. CC Dephosphorylated by phosphotyrosine phosphatases. Also phosphorylated CC by suramin, a heparin analog. Tyrosine phosphorylated in response to CC dissociation of integrin alpha-6 beta-4 from laminin-5. CC {ECO:0000269|PubMed:12660814, ECO:0000269|PubMed:14739293, CC ECO:0000269|PubMed:16007225, ECO:0000269|PubMed:8647901}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12660814, CC ECO:0000269|PubMed:14739293, ECO:0000269|PubMed:16007225}. CC -!- PTM: A soluble form may also be produced by proteolytic cleavage at the CC cell surface (shedding). Another peptide of 80 kDa (p80) is present in CC cultured keratinocytes probably due to tryptic cleavage at an CC unidentified site on its N-terminal side. Converted to p80 by plasmin, CC a trypsin-like protease. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15388.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY026461; AAK02058.1; -; mRNA. DR EMBL; AF468010; AAO33397.1; -; mRNA. DR EMBL; AY167484; AAO34538.1; -; mRNA. DR EMBL; AY358779; AAQ89139.1; -; mRNA. DR EMBL; AK023834; BAB14695.1; -; mRNA. DR EMBL; AK026187; BAB15388.1; ALT_INIT; mRNA. DR EMBL; AK026622; BAB15511.1; -; mRNA. DR EMBL; AC104165; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105902; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC021099; AAH21099.1; -; mRNA. DR EMBL; BC069254; AAH69254.1; -; mRNA. DR EMBL; AY375452; AAR21289.1; -; mRNA. DR CCDS; CCDS2727.1; -. [Q9H5V8-1] DR CCDS; CCDS46812.1; -. [Q9H5V8-3] DR RefSeq; NP_073753.3; NM_022842.4. [Q9H5V8-1] DR RefSeq; NP_835488.1; NM_178181.2. [Q9H5V8-3] DR AlphaFoldDB; Q9H5V8; -. DR SASBDB; Q9H5V8; -. DR BioGRID; 122336; 21. DR CORUM; Q9H5V8; -. DR DIP; DIP-33861N; -. DR IntAct; Q9H5V8; 27. DR MINT; Q9H5V8; -. DR STRING; 9606.ENSP00000296129; -. DR GlyConnect; 1160; 13 N-Linked glycans (8 sites). DR GlyCosmos; Q9H5V8; 9 sites, 12 glycans. DR GlyGen; Q9H5V8; 11 sites, 12 N-linked glycans (8 sites), 1 O-linked glycan (1 site). DR iPTMnet; Q9H5V8; -. DR PhosphoSitePlus; Q9H5V8; -. DR SwissPalm; Q9H5V8; -. DR BioMuta; CDCP1; -. DR DMDM; 317373455; -. DR CPTAC; CPTAC-2211; -. DR EPD; Q9H5V8; -. DR jPOST; Q9H5V8; -. DR MassIVE; Q9H5V8; -. DR MaxQB; Q9H5V8; -. DR PaxDb; 9606-ENSP00000296129; -. DR PeptideAtlas; Q9H5V8; -. DR ProteomicsDB; 80933; -. [Q9H5V8-1] DR ProteomicsDB; 80934; -. [Q9H5V8-2] DR ProteomicsDB; 80935; -. [Q9H5V8-3] DR Pumba; Q9H5V8; -. DR ABCD; Q9H5V8; 13 sequenced antibodies. DR Antibodypedia; 2564; 990 antibodies from 44 providers. DR DNASU; 64866; -. DR Ensembl; ENST00000296129.6; ENSP00000296129.1; ENSG00000163814.8. [Q9H5V8-1] DR Ensembl; ENST00000425231.2; ENSP00000399342.2; ENSG00000163814.8. [Q9H5V8-3] DR GeneID; 64866; -. DR KEGG; hsa:64866; -. DR MANE-Select; ENST00000296129.6; ENSP00000296129.1; NM_022842.5; NP_073753.3. DR UCSC; uc003com.5; human. [Q9H5V8-1] DR AGR; HGNC:24357; -. DR CTD; 64866; -. DR DisGeNET; 64866; -. DR GeneCards; CDCP1; -. DR HGNC; HGNC:24357; CDCP1. DR HPA; ENSG00000163814; Tissue enhanced (esophagus). DR MIM; 611735; gene. DR neXtProt; NX_Q9H5V8; -. DR OpenTargets; ENSG00000163814; -. DR PharmGKB; PA142672140; -. DR VEuPathDB; HostDB:ENSG00000163814; -. DR eggNOG; ENOG502QVKN; Eukaryota. DR GeneTree; ENSGT00390000010209; -. DR HOGENOM; CLU_007498_0_0_1; -. DR InParanoid; Q9H5V8; -. DR OMA; IACETGR; -. DR OrthoDB; 4272077at2759; -. DR PhylomeDB; Q9H5V8; -. DR TreeFam; TF331392; -. DR PathwayCommons; Q9H5V8; -. DR SignaLink; Q9H5V8; -. DR SIGNOR; Q9H5V8; -. DR BioGRID-ORCS; 64866; 11 hits in 1169 CRISPR screens. DR ChiTaRS; CDCP1; human. DR GeneWiki; CDCP1; -. DR GenomeRNAi; 64866; -. DR Pharos; Q9H5V8; Tbio. DR PRO; PR:Q9H5V8; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9H5V8; Protein. DR Bgee; ENSG00000163814; Expressed in gingival epithelium and 135 other cell types or tissues. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR038811; CDCP1. DR InterPro; IPR035914; Sperma_CUB_dom_sf. DR PANTHER; PTHR14477; CUB DOMAIN-CONTAINING PROTEIN 1; 1. DR PANTHER; PTHR14477:SF1; CUB DOMAIN-CONTAINING PROTEIN 1; 1. DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1. DR Genevisible; Q9H5V8; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Reference proteome; KW Secreted; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..29 FT /evidence="ECO:0000269|PubMed:12660814, FT ECO:0000269|PubMed:16007225" FT CHAIN 30..836 FT /note="CUB domain-containing protein 1" FT /id="PRO_0000226249" FT TOPO_DOM 30..667 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 668..688 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 689..836 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 417..544 FT /note="CUB" FT REGION 776..836 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 802..825 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 368..369 FT /note="Cleavage; by ST14/MT-SP1" FT MOD_RES 734 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:14739293" FT CARBOHYD 39 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 122 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 180 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 205 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 270 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 310 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 386 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 476..499 FT /evidence="ECO:0000250" FT VAR_SEQ 1..187 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_017432" FT VAR_SEQ 342..343 FT /note="NK -> SE (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12975309, FT ECO:0000303|PubMed:15489334" FT /id="VSP_017433" FT VAR_SEQ 344..836 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12975309, FT ECO:0000303|PubMed:15489334" FT /id="VSP_017434" FT VARIANT 525 FT /note="Q -> R (in dbSNP:rs3749191)" FT /evidence="ECO:0000269|PubMed:12660814, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:14739293" FT /id="VAR_025498" FT VARIANT 673 FT /note="A -> V (in dbSNP:rs35428731)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_055095" FT VARIANT 709 FT /note="D -> G (in dbSNP:rs9874077)" FT /evidence="ECO:0000269|PubMed:11466621, FT ECO:0000269|PubMed:12660814, ECO:0000269|PubMed:14702039" FT /id="VAR_025499" FT MUTAGEN 734 FT /note="Y->F: Impaired association with SRC." FT /evidence="ECO:0000269|PubMed:15851033" FT MUTAGEN 762 FT /note="Y->F: Impaired association with protein kinase PRKCG FT but not with SRC." FT /evidence="ECO:0000269|PubMed:15851033" FT CONFLICT 252 FT /note="W -> C (in Ref. 5; BAB14695)" FT /evidence="ECO:0000305" FT CONFLICT 284 FT /note="Y -> D (in Ref. 5; BAB15388)" FT /evidence="ECO:0000305" FT CONFLICT 434 FT /note="S -> G (in Ref. 5; BAB14695)" FT /evidence="ECO:0000305" FT CONFLICT 466 FT /note="K -> R (in Ref. 5; BAB15388)" FT /evidence="ECO:0000305" FT CONFLICT 827 FT /note="N -> S (in Ref. 2; AAO33397 and 5; BAB15511)" FT /evidence="ECO:0000305" SQ SEQUENCE 836 AA; 92932 MW; 544FFDBBDD371518 CRC64; MAGLNCGVSI ALLGVLLLGA ARLPRGAEAF EIALPRESNI TVLIKLGTPT LLAKPCYIVI SKRHITMLSI KSGERIVFTF SCQSPENHFV IEIQKNIDCM SGPCPFGEVQ LQPSTSLLPT LNRTFIWDVK AHKSIGLELQ FSIPRLRQIG PGESCPDGVT HSISGRIDAT VVRIGTFCSN GTVSRIKMQE GVKMALHLPW FHPRNVSGFS IANRSSIKRL CIIESVFEGE GSATLMSANY PEGFPEDELM TWQFVVPAHL RASVSFLNFN LSNCERKEER VEYYIPGSTT NPEVFKLEDK QPGNMAGNFN LSLQGCDQDA QSPGILRLQF QVLVQHPQNE SNKIYVVDLS NERAMSLTIE PRPVKQSRKF VPGCFVCLES RTCSSNLTLT SGSKHKISFL CDDLTRLWMN VEKTISCTDH RYCQRKSYSL QVPSDILHLP VELHDFSWKL LVPKDRLSLV LVPAQKLQQH THEKPCNTSF SYLVASAIPS QDLYFGSFCP GGSIKQIQVK QNISVTLRTF APSFQQEASR QGLTVSFIPY FKEEGVFTVT PDTKSKVYLR TPNWDRGLPS LTSVSWNISV PRDQVACLTF FKERSGVVCQ TGRAFMIIQE QRTRAEEIFS LDEDVLPKPS FHHHSFWVNI SNCSPTSGKQ LDLLFSVTLT PRTVDLTVIL IAAVGGGVLL LSALGLIICC VKKKKKKTNK GPAVGIYNDN INTEMPRQPK KFQKGRKDND SHVYAVIEDT MVYGHLLQDS SGSFLQPEVD TYRPFQGTMG VCPPSPPTIC SRAPTAKLAT EEPPPRSPPE SESEPYTFSH PNNGDVSSKD TDIPLLNTQE PMEPAE //