PTPRC_HUMAN
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 03-AUG-2022, entry version 239.
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 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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
RP VARIANT T(-)B(+)NK(+) SCID 364-GLU--TYR-365 DEL, AND CHARACTERIZATION OF
RP VARIANT T(-)B(+)NK(+) SCID 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 [24]
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).
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: Severe combined immunodeficiency autosomal recessive T-cell-
CC negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+) SCID)
CC [MIM:608971]: A form of severe combined immunodeficiency (SCID), a
CC genetically and clinically heterogeneous group of rare congenital
CC disorders characterized by impairment of both humoral and cell-mediated
CC immunity, leukopenia, and low or absent antibody levels. Patients
CC present in infancy recurrent, persistent infections by opportunistic
CC organisms. The common characteristic of all types of SCID is absence of
CC T-cell-mediated cellular immunity due to a defect in T-cell
CC development. {ECO:0000269|PubMed:11145714}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
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 -!- 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";
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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; 88.
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 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 EPD; P08575; -.
DR jPOST; P08575; -.
DR MassIVE; P08575; -.
DR MaxQB; P08575; -.
DR PaxDb; P08575; -.
DR PeptideAtlas; P08575; -.
DR PRIDE; P08575; -.
DR ABCD; P08575; 10 sequenced antibodies.
DR Antibodypedia; 737; 9482 antibodies from 54 providers.
DR CPTC; P08575; 2 antibodies.
DR DNASU; 5788; -.
DR Ensembl; ENST00000348564.11; ENSP00000306782.7; ENSG00000081237.20. [P08575-4]
DR Ensembl; ENST00000442510.8; ENSP00000411355.3; ENSG00000081237.20. [P08575-3]
DR Ensembl; ENST00000573477.5; ENSP00000461074.2; ENSG00000262418.5.
DR Ensembl; ENST00000573679.5; ENSP00000458322.2; ENSG00000262418.5.
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 CTD; 5788; -.
DR DisGeNET; 5788; -.
DR GeneCards; PTPRC; -.
DR HGNC; HGNC:9666; PTPRC.
DR HPA; ENSG00000081237; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; PTPRC; -.
DR MIM; 126200; phenotype.
DR MIM; 151460; gene.
DR MIM; 608971; 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; IFRKCFH; -.
DR OrthoDB; 411281at2759; -.
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; 11 hits in 1078 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 195 other 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:0016021; C:integral component of membrane; TAS:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; 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:0018108; P:peptidyl-tyrosine phosphorylation; 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:1905451; P:positive regulation of Fc-gamma receptor signaling pathway involved in phagocytosis; 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:0043406; P:positive regulation of MAP kinase activity; 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: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:0046777; P:protein autophosphorylation; 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: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 Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.90.190.10; -; 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 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; SSF49265; SSF49265; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
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 T(-)B(+)NK(+) SCID; associated with lack
FT of surface 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 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
