ID PTPRC_HUMAN Reviewed; 1306 AA. AC P08575; A0A0A0MT22; A8K7W6; Q16614; Q9H0Y6; X6R433; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 3. DT 27-MAR-2024, entry version 248. DE RecName: Full=Receptor-type tyrosine-protein phosphatase C {ECO:0000305}; DE EC=3.1.3.48; DE AltName: Full=Leukocyte common antigen; DE Short=L-CA; DE AltName: Full=T200; DE AltName: CD_antigen=CD45; DE Flags: Precursor; GN Name=PTPRC {ECO:0000312|HGNC:HGNC:9666}; Synonyms=CD45; 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), AND ALTERNATIVE SPLICING. RC TISSUE=Lymphocyte; RX PubMed=2824653; DOI=10.1084/jem.166.5.1548; RA Streuli M., Hall L.R., Saga Y., Schlossman S.F., Saito H.; RT "Differential usage of three exons generates at least five different mRNAs RT encoding human leukocyte common antigens."; RL J. Exp. Med. 166:1548-1566(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING. RX PubMed=2956090; DOI=10.1002/j.1460-2075.1987.tb02361.x; RA Ralph S.J., Thomas M.L., Morton C.C., Trowbridge I.S.; RT "Structural variants of human T200 glycoprotein (leukocyte-common RT antigen)."; RL EMBO J. 6:1251-1257(1987). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Synovium; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-194. RX PubMed=2531281; DOI=10.1128/mcb.9.10.4550-4555.1989; RA Tsai A.Y.M., Streuli M., Saito H.; RT "Integrity of the exon 6 sequence is essential for tissue-specific RT alternative splicing of human leukocyte common antigen pre-mRNA."; RL Mol. Cell. Biol. 9:4550-4555(1989). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 193-1306. RC TISSUE=Placenta; RX PubMed=2971730; RA Hall L.R., Streuli M., Schlossman S.F., Saito H.; RT "Complete exon-intron organization of the human leukocyte common antigen RT (CD45) gene."; RL J. Immunol. 141:2781-2787(1988). RN [8] RP FUNCTION. RX PubMed=2845400; DOI=10.1073/pnas.85.19.7182; RA Charbonneau H., Tonks N.K., Walsh K.A., Fischer E.H.; RT "The leukocyte common antigen (CD45): a putative receptor-linked protein RT tyrosine phosphatase."; RL Proc. Natl. Acad. Sci. U.S.A. 85:7182-7186(1988). RN [9] RP MUTAGENESIS. RX PubMed=1695146; DOI=10.1002/j.1460-2075.1990.tb07415.x; RA Streuli M., Krueger N.X., Thai T., Tang M., Saito H.; RT "Distinct functional roles of the two intracellular phosphatase like RT domains of the receptor-linked protein tyrosine phosphatases LCA and LAR."; RL EMBO J. 9:2399-2407(1990). RN [10] RP INVOLVEMENT IN IMD105. RX PubMed=10700239; DOI=10.1038/73208; RA Kung C., Pingel J.T., Heikinheimo M., Klemola T., Varkila K., Yoo L.I., RA Vuopala K., Poyhonen M., Uhari M., Rogers M., Speck S.H., Chatila T., RA Thomas M.L.; RT "Mutations in the tyrosine phosphatase CD45 gene in a child with severe RT combined immunodeficiency disease."; RL Nat. Med. 6:343-345(2000). RN [11] RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=11975983; DOI=10.1016/s0198-8859(02)00379-8; RA Fukuhara K., Okumura M., Shiono H., Inoue M., Kadota Y., Miyoshi S., RA Matsuda H.; RT "A study on CD45 isoform expression during T-cell development and selection RT events in the human thymus."; RL Hum. Immunol. 63:394-404(2002). RN [12] RP INTERACTION WITH SKAP1, MUTAGENESIS OF CYS-853, AND FUNCTION. RX PubMed=11909961; DOI=10.1128/mcb.22.8.2673-2686.2002; RA Wu L., Fu J., Shen S.-H.; RT "SKAP55 coupled with CD45 positively regulates T-cell receptor-mediated RT gene transcription."; RL Mol. Cell. Biol. 22:2673-2686(2002). RN [13] RP INTERACTION WITH DPP4, AND SUBCELLULAR LOCATION. RX PubMed=12676959; DOI=10.1074/jbc.m212978200; RA Salgado F.J., Lojo J., Alonso-Lebrero J.L., Lluis C., Franco R., RA Cordero O.J., Nogueira M.; RT "A role for interleukin-12 in the regulation of T cell plasma membrane RT compartmentation."; RL J. Biol. Chem. 278:24849-24857(2003). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-975, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-234 AND ASN-337. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [16] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-234; ASN-278; ASN-286; ASN-337; RP ASN-421 AND ASN-490. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-975 AND SER-1299, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [18] 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). RN [19] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HUMAN CYTOMEGALOVIRUS RP PROTEIN UL11, SUBCELLULAR LOCATION (MICROBIAL INFECTION), AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=22174689; DOI=10.1371/journal.ppat.1002432; RA Gabaev I., Steinbrueck L., Pokoyski C., Pich A., Stanton R.J., RA Schwinzer R., Schulz T.F., Jacobs R., Messerle M., Kay-Fedorov P.C.; RT "The human cytomegalovirus UL11 protein interacts with the receptor RT tyrosine phosphatase CD45, resulting in functional paralysis of T cells."; RL PLoS Pathog. 7:E1002432-E1002432(2011). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-975 AND SER-994, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 624-1233 ALONE AND IN COMPLEX WITH RP PHOSPHOPEPTIDE. RX PubMed=15684325; DOI=10.1084/jem.20041890; RA Nam H.J., Poy F., Saito H., Frederick C.A.; RT "Structural basis for the function and regulation of the receptor protein RT tyrosine phosphatase CD45."; RL J. Exp. Med. 201:441-452(2005). RN [23] RP INVOLVEMENT IN SUSCEPTIBILITY TO MS. RX PubMed=11101853; DOI=10.1038/82659; RA Jacobsen M., Schweer D., Ziegler A., Gaber R., Schock S., Schwinzer R., RA Wonigeit K., Lindert R.-B., Kantarci O., Schaefer-Klein J., Schipper H.I., RA Oertel W.H., Heidenreich F., Weinshenker B.G., Sommer N., Hemmer B.; RT "A point mutation in PTPRC is associated with the development of multiple RT sclerosis."; RL Nat. Genet. 26:495-499(2000). RN [24] RP VARIANT IMD105 364-GLU-TYR-365 DEL, AND CHARACTERIZATION OF VARIANT IMD105 RP 364-GLU-TYR-365 DEL. RX PubMed=11145714; DOI=10.4049/jimmunol.166.2.1308; RA Tchilian E.Z., Wallace D.L., Wells R.S., Flower D.R., Morgan G., RA Beverley P.C.L.; RT "A deletion in the gene encoding the CD45 antigen in a patient with SCID."; RL J. Immunol. 166:1308-1313(2001). RN [25] RP VARIANTS [LARGE SCALE ANALYSIS] ALA-230 AND ARG-865. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [26] RP VARIANT IMD105 542-LYS--SER-1306 DEL. RX PubMed=22689986; DOI=10.1073/pnas.1202249109; RA Roberts J.L., Buckley R.H., Luo B., Pei J., Lapidus A., Peri S., Wei Q., RA Shin J., Parrott R.E., Dunbrack R.L. Jr., Testa J.R., Zhong X.P., RA Wiest D.L.; RT "CD45-deficient severe combined immunodeficiency caused by uniparental RT disomy."; RL Proc. Natl. Acad. Sci. U.S.A. 109:10456-10461(2012). CC -!- FUNCTION: Protein tyrosine-protein phosphatase required for T-cell CC activation through the antigen receptor. Acts as a positive regulator CC of T-cell coactivation upon binding to DPP4. The first PTPase domain CC has enzymatic activity, while the second one seems to affect the CC substrate specificity of the first one. Upon T-cell activation, CC recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and CC thereby modulates LYN activity (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:11909961, ECO:0000269|PubMed:2845400}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for human CC cytomegalovirus protein UL11 and mediates binding of UL11 to T-cells, CC leading to reduced induction of tyrosine phosphorylation of multiple CC signaling proteins upon T-cell receptor stimulation and impaired T-cell CC proliferation. {ECO:0000269|PubMed:22174689}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10044}; CC -!- SUBUNIT: Binds GANAB and PRKCSH (By similarity). Interacts with SKAP1 CC (PubMed:11909961). Interacts with DPP4; the interaction is enhanced in CC an interleukin-12-dependent manner in activated lymphocytes CC (PubMed:12676959). {ECO:0000250|UniProtKB:P06800, CC ECO:0000269|PubMed:11909961, ECO:0000269|PubMed:12676959}. CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus CC protein UL11; the interaction is required for binding of UL11 to T- CC cells. {ECO:0000269|PubMed:22174689}. CC -!- INTERACTION: CC P08575; P41240: CSK; NbExp=3; IntAct=EBI-1341, EBI-1380630; CC P08575; P35222: CTNNB1; NbExp=2; IntAct=EBI-1341, EBI-491549; CC P08575; P00533: EGFR; NbExp=2; IntAct=EBI-1341, EBI-297353; CC P08575; P04626: ERBB2; NbExp=2; IntAct=EBI-1341, EBI-641062; CC P08575; P20701: ITGAL; NbExp=2; IntAct=EBI-1341, EBI-961214; CC P08575; P06239: LCK; NbExp=7; IntAct=EBI-1341, EBI-1348; CC P08575; P09382: LGALS1; NbExp=2; IntAct=EBI-1341, EBI-1048875; CC P08575; Q02763: TEK; NbExp=3; IntAct=EBI-1341, EBI-2257090; CC P08575; P06240: Lck; Xeno; NbExp=2; IntAct=EBI-1341, EBI-1401; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12676959, CC ECO:0000269|PubMed:22174689}; Single-pass type I membrane protein CC {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:12676959}. CC Note=Colocalized with DPP4 in membrane rafts. CC {ECO:0000269|PubMed:12676959}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Name=1; Synonyms=CD45RABC {ECO:0000303|PubMed:11975983}; CC IsoId=P08575-3; Sequence=Displayed; CC Name=2; Synonyms=CD45R0 {ECO:0000303|PubMed:11975983}; CC IsoId=P08575-4; Sequence=VSP_059409; CC Name=3; Synonyms=CD45RAB {ECO:0000303|PubMed:11975983}; CC IsoId=P08575-5; Sequence=VSP_059837; CC Name=4; Synonyms=CD45RAC {ECO:0000303|PubMed:11975983}; CC IsoId=P08575-6; Sequence=VSP_059836; CC Name=5; Synonyms=CD45RBC {ECO:0000303|PubMed:11975983}; CC IsoId=P08575-7; Sequence=VSP_059834; CC Name=6; Synonyms=CD45RA {ECO:0000303|PubMed:11975983}; CC IsoId=P08575-8; Sequence=VSP_059835; CC Name=7; Synonyms=CD45RB {ECO:0000303|PubMed:11975983}; CC IsoId=P08575-9; Sequence=VSP_059834, VSP_059837; CC Name=8; Synonyms=CD45RC {ECO:0000303|PubMed:11975983}; CC IsoId=P08575-10; Sequence=VSP_059833; CC -!- TISSUE SPECIFICITY: Isoform 1: Detected in thymocytes. Isoform 2: CC Detected in thymocytes. Isoform 3: Detected in thymocytes. Isoform 4: CC Not detected in thymocytes. Isoform 5: Detected in thymocytes. Isoform CC 6: Not detected in thymocytes. Isoform 7: Detected in thymocytes. CC Isoform 8: Not detected in thymocytes. {ECO:0000269|PubMed:11975983}. CC -!- DEVELOPMENTAL STAGE: Isoform 1: During T-cell development, expressed at CC the CD3-CD4-CD8- and CD3+CD4+CD8- stages but barely detectable at the CC CD3-CD4+CD8+ stage. Isoform 2: During T-cell development, expressed at CC low levels at the CD3-CD4-CD8- and CD3-CD4+CD8- stages but up-regulated CC at the CD3+CD4+CD8+ and CD3+CD4+CD8- stages. Isoform 3: During T-cell CC development, expressed at the CD3-CD4-CD8- and CD3+CD4+CD8- stages but CC barely detectable at the CD3-CD4+CD8+ stage. Isoform 5: During T-cell CC development, expressed at the CD3-CD4-CD8- and CD3+CD4+CD8- stages but CC barely detectable at the CD3-CD4+CD8+ stage. Isoform 7: Consistently CC expressed at high levels at all stages of T-cell development. CC {ECO:0000269|PubMed:11975983}. CC -!- DOMAIN: The first PTPase domain interacts with SKAP1. CC -!- PTM: Heavily N- and O-glycosylated. {ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:19349973}. CC -!- DISEASE: Multiple sclerosis (MS) [MIM:126200]: A multifactorial, CC inflammatory, demyelinating disease of the central nervous system. CC Sclerotic lesions are characterized by perivascular infiltration of CC monocytes and lymphocytes and appear as indurated areas in pathologic CC specimens (sclerosis in plaques). The pathological mechanism is CC regarded as an autoimmune attack of the myelin sheath, mediated by both CC cellular and humoral immunity. Clinical manifestations include visual CC loss, extra-ocular movement disorders, paresthesias, loss of sensation, CC weakness, dysarthria, spasticity, ataxia and bladder dysfunction. CC Genetic and environmental factors influence susceptibility to the CC disease. {ECO:0000269|PubMed:11101853}. Note=Disease susceptibility may CC be associated with variants affecting the gene represented in this CC entry. CC -!- DISEASE: Immunodeficiency 105 (IMD105) [MIM:619924]: An autosomal CC recessive disorder characterized by recurrent infections in early CC infancy, decreased or absent numbers of non-functional T cells, normal CC or increased levels of B cells, hypogammaglobulinemia, and normal or CC low NK cells. Clinical manifestations may include pneumonia, CC dermatitis, and lymphadenopathy. {ECO:0000269|PubMed:10700239, CC ECO:0000269|PubMed:11145714, ECO:0000269|PubMed:22689986}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC Receptor class 1/6 subfamily. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAF84820.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA68269.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA68669.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=PTPRCbase; Note=PTPRC mutation db; CC URL="http://structure.bmc.lu.se/idbase/PTPRCbase/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=CD45 entry; CC URL="https://en.wikipedia.org/wiki/CD45"; 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; Y00638; CAA68669.1; ALT_INIT; mRNA. DR EMBL; Y00062; CAA68269.1; ALT_INIT; mRNA. DR EMBL; AK292131; BAF84820.1; ALT_INIT; mRNA. DR EMBL; AL157402; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL355988; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF510707; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471067; EAW91303.1; -; Genomic_DNA. DR EMBL; M23492; AAD15273.2; -; Genomic_DNA. DR EMBL; M23496; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23466; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23467; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23468; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23469; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23470; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23471; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23472; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23473; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23474; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23475; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23476; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23477; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23478; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23479; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23480; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23481; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23482; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23483; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23484; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23485; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23486; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23487; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23488; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23489; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23490; AAD15273.2; JOINED; Genomic_DNA. DR EMBL; M23491; AAD15273.2; JOINED; Genomic_DNA. DR CCDS; CCDS1397.2; -. [P08575-3] DR CCDS; CCDS1398.2; -. [P08575-4] DR PIR; A46546; A46546. DR RefSeq; NP_002829.3; NM_002838.4. [P08575-3] DR RefSeq; NP_563578.2; NM_080921.3. [P08575-4] DR RefSeq; XP_006711535.1; XM_006711472.3. [P08575-5] DR RefSeq; XP_006711536.1; XM_006711473.3. [P08575-7] DR RefSeq; XP_006711537.1; XM_006711474.3. [P08575-9] DR PDB; 1YGR; X-ray; 2.90 A; A/B=624-1233. DR PDB; 1YGU; X-ray; 2.90 A; A/B=624-1233. DR PDB; 5FMV; X-ray; 2.90 A; A/B=225-573. DR PDB; 5FN6; X-ray; 3.30 A; A=225-481. DR PDB; 5FN7; X-ray; 2.30 A; A/B=225-394. DR PDBsum; 1YGR; -. DR PDBsum; 1YGU; -. DR PDBsum; 5FMV; -. DR PDBsum; 5FN6; -. DR PDBsum; 5FN7; -. DR AlphaFoldDB; P08575; -. DR SMR; P08575; -. DR BioGRID; 111752; 34. DR DIP; DIP-224N; -. DR IntAct; P08575; 90. DR MINT; P08575; -. DR STRING; 9606.ENSP00000411355; -. DR BindingDB; P08575; -. DR ChEMBL; CHEMBL3243; -. DR TCDB; 8.A.128.1.11; the signaling adaptor protein karap/dap12/tyrobp (sap) family. DR DEPOD; PTPRC; -. DR GlyConnect; 339; 63 N-Linked glycans (9 sites), 15 O-Linked glycans (2 sites). DR GlyCosmos; P08575; 25 sites, 100 glycans. DR GlyGen; P08575; 39 sites, 76 N-linked glycans (10 sites), 26 O-linked glycans (7 sites). DR iPTMnet; P08575; -. DR MetOSite; P08575; -. DR PhosphoSitePlus; P08575; -. DR SwissPalm; P08575; -. DR BioMuta; PTPRC; -. DR DMDM; 33112650; -. DR CPTAC; CPTAC-1172; -. DR CPTAC; CPTAC-5846; -. DR CPTAC; CPTAC-5847; -. DR CPTAC; CPTAC-5871; -. DR CPTAC; CPTAC-5872; -. DR CPTAC; CPTAC-5945; -. DR CPTAC; CPTAC-5946; -. DR EPD; P08575; -. DR jPOST; P08575; -. DR MassIVE; P08575; -. DR MaxQB; P08575; -. DR PaxDb; 9606-ENSP00000411355; -. DR PeptideAtlas; P08575; -. DR Pumba; P08575; -. DR ABCD; P08575; 10 sequenced antibodies. DR Antibodypedia; 737; 11100 antibodies from 55 providers. DR CPTC; P08575; 2 antibodies. DR DNASU; 5788; -. DR Ensembl; ENST00000348564.11; ENSP00000306782.7; ENSG00000081237.21. [P08575-4] DR Ensembl; ENST00000442510.8; ENSP00000411355.3; ENSG00000081237.21. [P08575-3] DR Ensembl; ENST00000573477.5; ENSP00000461074.2; ENSG00000262418.5. DR Ensembl; ENST00000573679.5; ENSP00000458322.2; ENSG00000262418.5. DR Ensembl; ENST00000697631.1; ENSP00000513363.1; ENSG00000081237.21. [P08575-8] DR GeneID; 5788; -. DR KEGG; hsa:5788; -. DR MANE-Select; ENST00000442510.8; ENSP00000411355.3; NM_002838.5; NP_002829.3. DR UCSC; uc001gur.3; human. DR UCSC; uc061fse.1; human. [P08575-3] DR AGR; HGNC:9666; -. DR CTD; 5788; -. DR DisGeNET; 5788; -. DR GeneCards; PTPRC; -. DR HGNC; HGNC:9666; PTPRC. DR HPA; ENSG00000081237; Tissue enhanced (lymphoid). DR MalaCards; PTPRC; -. DR MIM; 126200; phenotype. DR MIM; 151460; gene. DR MIM; 619924; phenotype. DR neXtProt; NX_P08575; -. DR OpenTargets; ENSG00000081237; -. DR Orphanet; 169157; T-B+ severe combined immunodeficiency due to CD45 deficiency. DR PharmGKB; PA34011; -. DR VEuPathDB; HostDB:ENSG00000081237; -. DR eggNOG; KOG4228; Eukaryota. DR GeneTree; ENSGT00940000159457; -. DR InParanoid; P08575; -. DR OMA; ISANKPC; -. DR OrthoDB; 2875525at2759; -. DR PhylomeDB; P08575; -. DR TreeFam; TF351829; -. DR PathwayCommons; P08575; -. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-416700; Other semaphorin interactions. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; P08575; -. DR SIGNOR; P08575; -. DR BioGRID-ORCS; 5788; 20 hits in 1177 CRISPR screens. DR ChiTaRS; PTPRC; human. DR EvolutionaryTrace; P08575; -. DR GeneWiki; PTPRC; -. DR GenomeRNAi; 5788; -. DR Pharos; P08575; Tchem. DR PRO; PR:P08575; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P08575; Protein. DR Bgee; ENSG00000081237; Expressed in monocyte and 197 other cell types or tissues. DR ExpressionAtlas; P08575; baseline and differential. DR GO; GO:0032059; C:bleb; IDA:ARUK-UCL. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; NAS:ARUK-UCL. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0098857; C:membrane microdomain; ISS:ARUK-UCL. DR GO; GO:0045121; C:membrane raft; ISS:ARUK-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0030506; F:ankyrin binding; IPI:ARUK-UCL. DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IEA:Ensembl. DR GO; GO:0008201; F:heparin binding; IEA:Ensembl. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; ISS:ARUK-UCL. DR GO; GO:0030507; F:spectrin binding; IDA:ARUK-UCL. DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ARUK-UCL. DR GO; GO:0046633; P:alpha-beta T cell proliferation; IEA:Ensembl. DR GO; GO:0030183; P:B cell differentiation; ISS:ARUK-UCL. DR GO; GO:0042100; P:B cell proliferation; ISS:UniProtKB. DR GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0048539; P:bone marrow development; IMP:UniProtKB. DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISS:ARUK-UCL. DR GO; GO:0044770; P:cell cycle phase transition; IMP:UniProtKB. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc. DR GO; GO:0031668; P:cellular response to extracellular stimulus; ISS:ARUK-UCL. DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB. DR GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB. DR GO; GO:1904155; P:DN2 thymocyte differentiation; TAS:ARUK-UCL. DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0042492; P:gamma-delta T cell differentiation; IEA:Ensembl. DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:UniProtKB. DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IEA:Ensembl. DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IEA:Ensembl. DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl. DR GO; GO:0001779; P:natural killer cell differentiation; ISS:ARUK-UCL. DR GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IMP:UniProtKB. DR GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; ISS:UniProtKB. DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:ARUK-UCL. DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISS:ARUK-UCL. DR GO; GO:1903979; P:negative regulation of microglial cell activation; TAS:ARUK-UCL. DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; IEA:Ensembl. DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB. DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; ISS:ARUK-UCL. DR GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; ISS:UniProtKB. DR GO; GO:0045060; P:negative thymic T cell selection; IEA:Ensembl. DR GO; GO:0044855; P:plasma membrane raft distribution; ISS:ARUK-UCL. DR GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IEA:Ensembl. DR GO; GO:0050857; P:positive regulation of antigen receptor-mediated signaling pathway; ISS:UniProtKB. DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:ARUK-UCL. DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0060369; P:positive regulation of Fc receptor mediated stimulatory signaling pathway; ISS:ARUK-UCL. DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IEA:Ensembl. DR GO; GO:2000473; P:positive regulation of hematopoietic stem cell migration; IMP:UniProtKB. DR GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IEA:Ensembl. DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IMP:UniProtKB. DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISS:ARUK-UCL. DR GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IEA:Ensembl. DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:ARUK-UCL. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:ARUK-UCL. DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:ARUK-UCL. DR GO; GO:0045860; P:positive regulation of protein kinase activity; NAS:UniProtKB. DR GO; GO:1903615; P:positive regulation of protein tyrosine phosphatase activity; ISS:ARUK-UCL. DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:UniProtKB. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:Ensembl. DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:ARUK-UCL. DR GO; GO:0045059; P:positive thymic T cell selection; IEA:Ensembl. DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB. DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB. DR GO; GO:0010468; P:regulation of gene expression; ISS:ARUK-UCL. DR GO; GO:0032677; P:regulation of interleukin-8 production; IDA:ARUK-UCL. DR GO; GO:0050764; P:regulation of phagocytosis; IDA:ARUK-UCL. DR GO; GO:0061097; P:regulation of protein tyrosine kinase activity; IDA:ARUK-UCL. DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; IGI:ARUK-UCL. DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB. DR GO; GO:1904044; P:response to aldosterone; IEA:Ensembl. DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl. DR GO; GO:0048864; P:stem cell development; IMP:UniProtKB. DR GO; GO:0042110; P:T cell activation; TAS:ARUK-UCL. DR GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB. DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB. DR CDD; cd00063; FN3; 2. DR CDD; cd14558; R-PTP-C-2; 1. DR CDD; cd14557; R-PTPc-C-1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2. DR IDEAL; IID00537; -. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000242; PTP_cat. DR InterPro; IPR024739; PTP_recept_N. DR InterPro; IPR016335; Ptprc. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR InterPro; IPR000387; Tyr_Pase_dom. DR PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR19134:SF539; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE C; 1. DR Pfam; PF12567; CD45; 1. DR Pfam; PF00041; fn3; 2. DR Pfam; PF12453; PTP_N; 1. DR Pfam; PF00102; Y_phosphatase; 2. DR PIRSF; PIRSF002004; Leukocyte_common_antigen; 1. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00060; FN3; 2. DR SMART; SM00194; PTPc; 2. DR SMART; SM00404; PTPc_motif; 2. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR PROSITE; PS50853; FN3; 2. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disease variant; KW Glycoprotein; Host-virus interaction; Hydrolase; Membrane; Phosphoprotein; KW Protein phosphatase; Reference proteome; Repeat; SCID; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..25 FT CHAIN 26..1306 FT /note="Receptor-type tyrosine-protein phosphatase C" FT /id="PRO_0000025470" FT TOPO_DOM 26..577 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 578..598 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 599..1306 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 391..483 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 484..576 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 653..912 FT /note="Tyrosine-protein phosphatase 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT DOMAIN 944..1228 FT /note="Tyrosine-protein phosphatase 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT REGION 28..163 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 993..1014 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1261..1306 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1280..1306 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 853 FT /note="Phosphocysteine intermediate" FT ACT_SITE 1169 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000250" FT BINDING 821 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 853..859 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 897 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 683 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P04157" FT MOD_RES 975 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19367720, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 994 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 997 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04157" FT MOD_RES 1001 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04157" FT MOD_RES 1004 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04157" FT MOD_RES 1005 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06800" FT MOD_RES 1009 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04157" FT MOD_RES 1299 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT CARBOHYD 80 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 92 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 97 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 186 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 192 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 199 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 234 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19349973" FT CARBOHYD 262 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 272 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 278 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 286 FT /note="N-linked (GlcNAc...) asparagine; atypical" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 337 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19349973" FT CARBOHYD 380 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 421 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 470 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 490 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 531 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 34..194 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000269|PubMed:2956090" FT /id="VSP_059409" FT VAR_SEQ 34..146 FT /note="Missing (in isoform 8)" FT /evidence="ECO:0000269|PubMed:11975983" FT /id="VSP_059833" FT VAR_SEQ 34..99 FT /note="Missing (in isoform 5 and isoform 7)" FT /evidence="ECO:0000269|PubMed:11975983, FT ECO:0000269|PubMed:2824653" FT /id="VSP_059834" FT VAR_SEQ 100..194 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000269|PubMed:2824653" FT /id="VSP_059835" FT VAR_SEQ 100..146 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000269|PubMed:2824653" FT /id="VSP_059836" FT VAR_SEQ 147..194 FT /note="Missing (in isoform 3 and isoform 7)" FT /evidence="ECO:0000269|PubMed:11975983, FT ECO:0000269|PubMed:2824653" FT /id="VSP_059837" FT VARIANT 193 FT /note="T -> A (in dbSNP:rs4915154)" FT /id="VAR_036860" FT VARIANT 230 FT /note="E -> A (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035653" FT VARIANT 296 FT /note="I -> L (in dbSNP:rs2230606)" FT /id="VAR_051763" FT VARIANT 364..365 FT /note="Missing (in IMD105; associated with lack of surface FT expression)" FT /evidence="ECO:0000269|PubMed:11145714" FT /id="VAR_021205" FT VARIANT 423 FT /note="T -> I (in dbSNP:rs6696162)" FT /id="VAR_051764" FT VARIANT 542..1306 FT /note="Missing (in IMD105)" FT /evidence="ECO:0000269|PubMed:22689986" FT /id="VAR_087537" FT VARIANT 570 FT /note="H -> Q (in dbSNP:rs12136658)" FT /id="VAR_051765" FT VARIANT 865 FT /note="G -> R (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035654" FT VARIANT 1285 FT /note="S -> R (in dbSNP:rs2298872)" FT /id="VAR_020303" FT MUTAGEN 853 FT /note="C->S: Loss of activity. Abolishes interaction with FT SKAP1." FT /evidence="ECO:0000269|PubMed:11909961" FT CONFLICT 652 FT /note="L -> P (in Ref. 1; CAA68669)" FT /evidence="ECO:0000305" FT CONFLICT 1209 FT /note="P -> L (in Ref. 1; CAA68669)" FT /evidence="ECO:0000305" FT HELIX 228..231 FT /evidence="ECO:0007829|PDB:5FN7" FT TURN 232..234 FT /evidence="ECO:0007829|PDB:5FN7" FT STRAND 237..242 FT /evidence="ECO:0007829|PDB:5FN7" FT TURN 243..246 FT /evidence="ECO:0007829|PDB:5FN7" FT STRAND 247..252 FT /evidence="ECO:0007829|PDB:5FN7" FT STRAND 259..263 FT /evidence="ECO:0007829|PDB:5FN7" FT HELIX 266..268 FT /evidence="ECO:0007829|PDB:5FN7" FT STRAND 269..273 FT /evidence="ECO:0007829|PDB:5FN7" FT STRAND 278..284 FT /evidence="ECO:0007829|PDB:5FN7" FT STRAND 288..291 FT /evidence="ECO:0007829|PDB:5FN7" FT STRAND 293..298 FT /evidence="ECO:0007829|PDB:5FN7" FT HELIX 303..305 FT /evidence="ECO:0007829|PDB:5FN7" FT STRAND 306..310 FT /evidence="ECO:0007829|PDB:5FN7" FT HELIX 314..316 FT /evidence="ECO:0007829|PDB:5FN7" FT TURN 317..319 FT /evidence="ECO:0007829|PDB:5FN7" FT STRAND 321..327 FT /evidence="ECO:0007829|PDB:5FN7" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:5FN7" FT STRAND 338..344 FT /evidence="ECO:0007829|PDB:5FN7" FT STRAND 347..356 FT /evidence="ECO:0007829|PDB:5FN7" FT STRAND 364..373 FT /evidence="ECO:0007829|PDB:5FN7" FT STRAND 376..388 FT /evidence="ECO:0007829|PDB:5FN7" FT STRAND 396..401 FT /evidence="ECO:0007829|PDB:5FMV" FT STRAND 403..406 FT /evidence="ECO:0007829|PDB:5FMV" FT STRAND 408..413 FT /evidence="ECO:0007829|PDB:5FMV" FT STRAND 420..427 FT /evidence="ECO:0007829|PDB:5FMV" FT STRAND 429..438 FT /evidence="ECO:0007829|PDB:5FMV" FT STRAND 443..446 FT /evidence="ECO:0007829|PDB:5FMV" FT STRAND 454..470 FT /evidence="ECO:0007829|PDB:5FMV" FT STRAND 474..479 FT /evidence="ECO:0007829|PDB:5FMV" FT STRAND 489..499 FT /evidence="ECO:0007829|PDB:5FMV" FT STRAND 501..506 FT /evidence="ECO:0007829|PDB:5FMV" FT STRAND 518..541 FT /evidence="ECO:0007829|PDB:5FMV" FT STRAND 549..557 FT /evidence="ECO:0007829|PDB:5FMV" FT STRAND 566..571 FT /evidence="ECO:0007829|PDB:5FMV" FT TURN 635..637 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 638..658 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 665..667 FT /evidence="ECO:0007829|PDB:1YGR" FT TURN 670..672 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 675..680 FT /evidence="ECO:0007829|PDB:1YGR" FT TURN 690..692 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 693..695 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 700..702 FT /evidence="ECO:0007829|PDB:1YGR" FT TURN 703..706 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 707..713 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 716..718 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 722..725 FT /evidence="ECO:0007829|PDB:1YGR" FT TURN 730..732 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 733..742 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 747..750 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 754..756 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 759..761 FT /evidence="ECO:0007829|PDB:1YGR" FT TURN 769..771 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 773..776 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 779..788 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 790..804 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 809..816 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 828..838 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 849..852 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 854..857 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 858..871 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 873..876 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 877..879 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 881..889 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 899..915 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 922..924 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 925..932 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 943..950 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 962..964 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 968..970 FT /evidence="ECO:0007829|PDB:1YGR" FT TURN 981..983 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 1020..1024 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 1031..1036 FT /evidence="ECO:0007829|PDB:1YGR" FT TURN 1040..1042 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 1043..1052 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 1057..1060 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 1064..1066 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 1069..1072 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 1090..1095 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 1097..1107 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 1115..1122 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 1127..1129 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 1134..1145 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 1165..1173 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 1176..1191 FT /evidence="ECO:0007829|PDB:1YGR" FT STRAND 1192..1194 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 1197..1207 FT /evidence="ECO:0007829|PDB:1YGR" FT TURN 1209..1212 FT /evidence="ECO:0007829|PDB:1YGR" FT HELIX 1215..1227 FT /evidence="ECO:0007829|PDB:1YGR" SQ SEQUENCE 1306 AA; 147486 MW; 6E942E2BF6B17AC5 CRC64; MTMYLWLKLL AFGFAFLDTE VFVTGQSPTP SPTGLTTAKM PSVPLSSDPL PTHTTAFSPA STFERENDFS ETTTSLSPDN TSTQVSPDSL DNASAFNTTG VSSVQTPHLP THADSQTPSA GTDTQTFSGS AANAKLNPTP GSNAISDVPG ERSTASTFPT DPVSPLTTTL SLAHHSSAAL PARTSNTTIT ANTSDAYLNA SETTTLSPSG SAVISTTTIA TTPSKPTCDE KYANITVDYL YNKETKLFTA KLNVNENVEC GNNTCTNNEV HNLTECKNAS VSISHNSCTA PDKTLILDVP PGVEKFQLHD CTQVEKADTT ICLKWKNIET FTCDTQNITY RFQCGNMIFD NKEIKLENLE PEHEYKCDSE ILYNNHKFTN ASKIIKTDFG SPGEPQIIFC RSEAAHQGVI TWNPPQRSFH NFTLCYIKET EKDCLNLDKN LIKYDLQNLK PYTKYVLSLH AYIIAKVQRN GSAAMCHFTT KSAPPSQVWN MTVSMTSDNS MHVKCRPPRD RNGPHERYHL EVEAGNTLVR NESHKNCDFR VKDLQYSTDY TFKAYFHNGD YPGEPFILHH STSYNSKALI AFLAFLIIVT SIALLVVLYK IYDLHKKRSC NLDEQQELVE RDDEKQLMNV EPIHADILLE TYKRKIADEG RLFLAEFQSI PRVFSKFPIK EARKPFNQNK NRYVDILPYD YNRVELSEIN GDAGSNYINA SYIDGFKEPR KYIAAQGPRD ETVDDFWRMI WEQKATVIVM VTRCEEGNRN KCAEYWPSME EGTRAFGDVV VKINQHKRCP DYIIQKLNIV NKKEKATGRE VTHIQFTSWP DHGVPEDPHL LLKLRRRVNA FSNFFSGPIV VHCSAGVGRT GTYIGIDAML EGLEAENKVD VYGYVVKLRR QRCLMVQVEA QYILIHQALV EYNQFGETEV NLSELHPYLH NMKKRDPPSE PSPLEAEFQR LPSYRSWRTQ HIGNQEENKS KNRNSNVIPY DYNRVPLKHE LEMSKESEHD SDESSDDDSD SEEPSKYINA SFIMSYWKPE VMIAAQGPLK ETIGDFWQMI FQRKVKVIVM LTELKHGDQE ICAQYWGEGK QTYGDIEVDL KDTDKSSTYT LRVFELRHSK RKDSRTVYQY QYTNWSVEQL PAEPKELISM IQVVKQKLPQ KNSSEGNKHH KSTPLLIHCR DGSQQTGIFC ALLNLLESAE TEEVVDIFQV VKALRKARPG MVSTFEQYQF LYDVIASTYP AQNGQVKKNN HQEDKIEFDN EVDKVKQDAN CVNPLGAPEK LPEAKEQAEG SEPTSGTEGP EHSVNGPASP ALNQGS //