SKAP1_HUMAN
ID SKAP1_HUMAN Reviewed; 359 AA.
AC Q86WV1; D3DTV1; O15268;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Src kinase-associated phosphoprotein 1;
DE AltName: Full=Src family-associated phosphoprotein 1;
DE AltName: Full=Src kinase-associated phosphoprotein of 55 kDa;
DE Short=SKAP-55;
DE Short=pp55;
GN Name=SKAP1; Synonyms=SCAP1, SKAP55;
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), PROTEIN SEQUENCE OF 101-110;
RP 120-130 AND 153-158, PHOSPHORYLATION, INTERACTION WITH FYN, TISSUE
RP SPECIFICITY, AND VARIANT SER-161.
RC TISSUE=Blood;
RX PubMed=9195899; DOI=10.1074/jbc.272.26.16077;
RA Marie-Cardine A., Bruyns E., Eckerskorn C., Kirchgessner H., Meuer S.,
RA Schraven B.;
RT "Molecular cloning of SKAP55, a novel protein that associates with p59fyn
RT in human T-lymphocytes.";
RL J. Biol. Chem. 272:16077-16080(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH FYB1, AND MUTAGENESIS OF TRP-333.
RX PubMed=9748251; DOI=10.1074/jbc.273.40.25789;
RA Marie-Cardine A., Hendricks-Taylor L.R., Boerth N.J., Zhao H., Schraven B.,
RA Koretzky G.A.;
RT "Molecular interaction between the Fyn-associated protein SKAP55 and the
RT SLP-76-associated phosphoprotein SLAP-130.";
RL J. Biol. Chem. 273:25789-25795(1998).
RN [6]
RP INTERACTION WITH FYB1, AND SUBCELLULAR LOCATION.
RX PubMed=9671755; DOI=10.1073/pnas.95.15.8779;
RA Liu J., Kang H., Raab M., da Silva A.J., Kraeft S.-K., Rudd C.E.;
RT "FYB (FYN binding protein) serves as a binding partner for lymphoid protein
RT and FYN kinase substrate SKAP55 and a SKAP55-related protein in T cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8779-8784(1998).
RN [7]
RP INTERACTION WITH FYB1, MUTAGENESIS OF TYR-295 AND TYR-298, AND FUNCTION.
RX PubMed=10856234; DOI=10.1093/emboj/19.12.2889;
RA Kang H., Freund C., Duke-Cohan J.S., Musacchio A., Wagner G., Rudd C.E.;
RT "SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY
RT motif in immune cell adaptor SKAP55.";
RL EMBO J. 19:2889-2899(2000).
RN [8]
RP HOMODIMERIZATION, MUTAGENESIS OF TYR-219; TYR-232; TYR-271 AND TRP-333,
RP PHOSPHORYLATION, AND INTERACTION WITH GRB2.
RX PubMed=12171928; DOI=10.1074/jbc.m206023200;
RA Wu L., Yu Z., Shen S.-H.;
RT "SKAP55 recruits to lipid rafts and positively mediates the MAPK pathway
RT upon T cell receptor activation.";
RL J. Biol. Chem. 277:40420-40427(2002).
RN [9]
RP PHOSPHORYLATION AT TYR-219 AND TYR-232, DEPHOSPHORYLATION BY PTPRC,
RP MUTAGENESIS OF TYR-219; TYR-232 AND TYR-271, SUBCELLULAR LOCATION,
RP FUNCTION, AND INTERACTION WITH PTPRC.
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 [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12652296; DOI=10.1038/ni913;
RA Wang H., Moon E.-Y., Azouz A., Wu X., Smith A., Schneider H., Hogg N.,
RA Rudd C.E.;
RT "SKAP-55 regulates integrin adhesion and formation of T cell-APC
RT conjugates.";
RL Nat. Immunol. 4:366-374(2003).
RN [11]
RP INTERACTION WITH FYB1, AND MUTAGENESIS OF TRP-333.
RX PubMed=15849195; DOI=10.1074/jbc.m413201200;
RA Huang Y., Norton D.D., Precht P., Martindale J.L., Burkhardt J.K.,
RA Wange R.L.;
RT "Deficiency of ADAP/Fyb/SLAP-130 destabilizes SKAP55 in Jurkat T cells.";
RL J. Biol. Chem. 280:23576-23583(2005).
RN [12]
RP FUNCTION.
RX PubMed=15939789; DOI=10.1084/jem.20042577;
RA Jo E.-K., Wang H., Rudd C.E.;
RT "An essential role for SKAP-55 in LFA-1 clustering on T cells that cannot
RT be substituted by SKAP-55R.";
RL J. Exp. Med. 201:1733-1739(2005).
RN [13]
RP PHOSPHORYLATION, AND INTERACTION WITH FYB1.
RX PubMed=16461356; DOI=10.1074/jbc.m508774200;
RA Duke-Cohan J.S., Kang H., Liu H., Rudd C.E.;
RT "Regulation and function of SKAP-55 non-canonical motif binding to the SH3c
RT domain of adhesion and degranulation-promoting adaptor protein.";
RL J. Biol. Chem. 281:13743-13750(2006).
RN [14]
RP FUNCTION.
RX PubMed=16980616; DOI=10.1128/mcb.00331-06;
RA Kliche S., Breitling D., Togni M., Pusch R., Heuer K., Wang X., Freund C.,
RA Kasirer-Friede A., Menasche G., Koretzky G.A., Schraven B.;
RT "The ADAP/SKAP55 signaling module regulates T-cell receptor-mediated
RT integrin activation through plasma membrane targeting of Rap1.";
RL Mol. Cell. Biol. 26:7130-7144(2006).
RN [15]
RP INTERACTION WITH RASGRP1.
RX PubMed=17658605; DOI=10.1016/j.molimm.2007.05.024;
RA Kosco K.A., Cerignoli F., Williams S., Abraham R.T., Mustelin T.;
RT "SKAP55 modulates T cell antigen receptor-induced activation of the Ras-
RT Erk-AP1 pathway by binding RasGRP1.";
RL Mol. Immunol. 45:510-522(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-271, AND IDENTIFICATION BY
RP 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 INTERACTION WITH FYB2 AND FYB1.
RX PubMed=27335501; DOI=10.4049/jimmunol.1501913;
RA Jung S.H., Yoo E.H., Yu M.J., Song H.M., Kang H.Y., Cho J.Y., Lee J.R.;
RT "ARAP, a novel adaptor protein, is required for TCR signaling and integrin-
RT mediated adhesion.";
RL J. Immunol. 197:942-952(2016).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 108-213.
RA Tang Y., Swanson K.D., Neel B.G., Eck M.J.;
RT "Structural basis for the dimerization and phosphoinositide specificity of
RT the Src kinase-associated phosphoproteins SKAP55 and SKAP-HOM.";
RL Submitted (JUL-2005) to the PDB data bank.
CC -!- FUNCTION: Positively regulates T-cell receptor signaling by enhancing
CC the MAP kinase pathway. Required for optimal conjugation between T-
CC cells and antigen-presenting cells by promoting the clustering of
CC integrin ITGAL on the surface of T-cells. May be involved in high
CC affinity immunoglobulin epsilon receptor signaling in mast cells.
CC {ECO:0000269|PubMed:10856234, ECO:0000269|PubMed:11909961,
CC ECO:0000269|PubMed:12652296, ECO:0000269|PubMed:15939789,
CC ECO:0000269|PubMed:16980616}.
CC -!- SUBUNIT: Homodimer (PubMed:9195899). Interacts with FYN
CC (PubMed:9195899). Interacts with PTPRC (PubMed:11909961). Interacts
CC with GRB2 when phosphorylated on Tyr-271 (PubMed:12171928). Interacts
CC with FYB1, which is required for SKAP2 protein stability
CC (PubMed:9748251, PubMed:9671755, PubMed:10856234, PubMed:15849195,
CC PubMed:16461356, PubMed:27335501). Part of a complex consisting of
CC SKAP1, FYB1 and CLNK (By similarity). Interacts with RASGRP1
CC (PubMed:17658605). Interacts with FYB2 (PubMed:27335501).
CC {ECO:0000250|UniProtKB:Q4V7G1, ECO:0000269|PubMed:10856234,
CC ECO:0000269|PubMed:11909961, ECO:0000269|PubMed:12171928,
CC ECO:0000269|PubMed:15849195, ECO:0000269|PubMed:16461356,
CC ECO:0000269|PubMed:17658605, ECO:0000269|PubMed:27335501,
CC ECO:0000269|PubMed:9195899, ECO:0000269|PubMed:9671755,
CC ECO:0000269|PubMed:9748251}.
CC -!- INTERACTION:
CC Q86WV1; P62952: BLCAP; NbExp=3; IntAct=EBI-2477305, EBI-3895726;
CC Q86WV1; Q5T9C2: FAM102A; NbExp=4; IntAct=EBI-2477305, EBI-10246318;
CC Q86WV1; O15117: FYB1; NbExp=6; IntAct=EBI-2477305, EBI-1753267;
CC Q86WV1; Q96QH2: PRAM1; NbExp=4; IntAct=EBI-2477305, EBI-2860740;
CC Q86WV1; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-2477305, EBI-747035;
CC Q86WV1; Q9H788-2: SH2D4A; NbExp=3; IntAct=EBI-2477305, EBI-10308083;
CC Q86WV1-2; P55210: CASP7; NbExp=3; IntAct=EBI-11995314, EBI-523958;
CC Q86WV1-2; P07237: P4HB; NbExp=3; IntAct=EBI-11995314, EBI-395883;
CC Q86WV1-2; P60201-2: PLP1; NbExp=3; IntAct=EBI-11995314, EBI-12188331;
CC Q86WV1-2; Q96QH2: PRAM1; NbExp=3; IntAct=EBI-11995314, EBI-2860740;
CC Q86WV1-2; Q9P1I4: ST13; NbExp=3; IntAct=EBI-11995314, EBI-25892254;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11909961,
CC ECO:0000269|PubMed:9671755}. Nucleus {ECO:0000269|PubMed:11909961,
CC ECO:0000269|PubMed:9671755}. Cell membrane
CC {ECO:0000269|PubMed:11909961, ECO:0000269|PubMed:9671755}. Note=Upon T-
CC cell stimulation, translocates to lipid rafts at the cell membrane.
CC {ECO:0000269|PubMed:9671755}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86WV1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86WV1-2; Sequence=VSP_022179;
CC -!- TISSUE SPECIFICITY: Highly expressed in thymocytes and peripheral blood
CC lymphocytes. Also expressed in spleen cells and testis. Present in T-
CC cells (at protein level). {ECO:0000269|PubMed:9195899}.
CC -!- DOMAIN: The SH3 domain interacts with FYB1.
CC -!- PTM: Phosphorylated on tyrosines. Phosphorylation by FYN on Tyr-271 is
CC required for GRB2 interaction. Phosphorylation by FYN on Tyr-295
CC abolishes interaction with FYB1. Tyr-232 is dephosphorylated by PTPRC
CC (Probable). {ECO:0000305|PubMed:11909961, ECO:0000305|PubMed:12171928,
CC ECO:0000305|PubMed:16461356, ECO:0000305|PubMed:9195899}.
CC -!- SIMILARITY: Belongs to the SKAP family. {ECO:0000305}.
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DR EMBL; Y11215; CAA72101.1; -; mRNA.
DR EMBL; AC006468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC036222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94749.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94750.1; -; Genomic_DNA.
DR EMBL; BC047870; AAH47870.1; -; mRNA.
DR CCDS; CCDS32674.1; -. [Q86WV1-1]
DR RefSeq; NP_001068567.1; NM_001075099.1. [Q86WV1-2]
DR RefSeq; NP_003717.3; NM_003726.3. [Q86WV1-1]
DR PDB; 1U5D; X-ray; 1.70 A; A/B/C/D=108-213.
DR PDBsum; 1U5D; -.
DR AlphaFoldDB; Q86WV1; -.
DR SMR; Q86WV1; -.
DR BioGRID; 114184; 103.
DR IntAct; Q86WV1; 60.
DR MINT; Q86WV1; -.
DR STRING; 9606.ENSP00000338171; -.
DR iPTMnet; Q86WV1; -.
DR PhosphoSitePlus; Q86WV1; -.
DR BioMuta; SKAP1; -.
DR DMDM; 269849660; -.
DR jPOST; Q86WV1; -.
DR MassIVE; Q86WV1; -.
DR MaxQB; Q86WV1; -.
DR PaxDb; Q86WV1; -.
DR PeptideAtlas; Q86WV1; -.
DR PRIDE; Q86WV1; -.
DR ProteomicsDB; 70207; -. [Q86WV1-1]
DR ProteomicsDB; 70208; -. [Q86WV1-2]
DR Antibodypedia; 1187; 257 antibodies from 32 providers.
DR DNASU; 8631; -.
DR Ensembl; ENST00000336915.11; ENSP00000338171.6; ENSG00000141293.16. [Q86WV1-1]
DR Ensembl; ENST00000584924.5; ENSP00000464311.1; ENSG00000141293.16. [Q86WV1-1]
DR GeneID; 8631; -.
DR KEGG; hsa:8631; -.
DR MANE-Select; ENST00000336915.11; ENSP00000338171.6; NM_003726.4; NP_003717.3.
DR UCSC; uc002ini.2; human. [Q86WV1-1]
DR CTD; 8631; -.
DR DisGeNET; 8631; -.
DR GeneCards; SKAP1; -.
DR HGNC; HGNC:15605; SKAP1.
DR HPA; ENSG00000141293; Tissue enhanced (lymphoid).
DR MIM; 604969; gene.
DR neXtProt; NX_Q86WV1; -.
DR OpenTargets; ENSG00000141293; -.
DR PharmGKB; PA162403362; -.
DR VEuPathDB; HostDB:ENSG00000141293; -.
DR eggNOG; ENOG502QSSU; Eukaryota.
DR GeneTree; ENSGT00390000017856; -.
DR HOGENOM; CLU_062032_0_0_1; -.
DR InParanoid; Q86WV1; -.
DR OMA; IFYYYSN; -.
DR OrthoDB; 767446at2759; -.
DR PhylomeDB; Q86WV1; -.
DR TreeFam; TF331055; -.
DR PathwayCommons; Q86WV1; -.
DR SignaLink; Q86WV1; -.
DR SIGNOR; Q86WV1; -.
DR BioGRID-ORCS; 8631; 20 hits in 1076 CRISPR screens.
DR ChiTaRS; SKAP1; human.
DR EvolutionaryTrace; Q86WV1; -.
DR GeneWiki; SKAP1; -.
DR GenomeRNAi; 8631; -.
DR Pharos; Q86WV1; Tbio.
DR PRO; PR:Q86WV1; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q86WV1; protein.
DR Bgee; ENSG00000141293; Expressed in granulocyte and 123 other tissues.
DR ExpressionAtlas; Q86WV1; baseline and differential.
DR Genevisible; Q86WV1; HS.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001772; C:immunological synapse; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0044853; C:plasma membrane raft; IDA:BHF-UCL.
DR GO; GO:0042101; C:T cell receptor complex; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; TAS:BHF-UCL.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0002821; P:positive regulation of adaptive immune response; IDA:BHF-UCL.
DR GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; IGI:BHF-UCL.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IGI:BHF-UCL.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0033625; P:positive regulation of integrin activation; IDA:BHF-UCL.
DR GO; GO:1903039; P:positive regulation of leukocyte cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
DR CDD; cd12044; SH3_SKAP1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035765; SKAP1_SH3.
DR InterPro; IPR037781; SKAP_fam.
DR PANTHER; PTHR15129; PTHR15129; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00233; PH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Cytoplasm; Direct protein sequencing; Immunity; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..359
FT /note="Src kinase-associated phosphoprotein 1"
FT /id="PRO_0000270173"
FT DOMAIN 107..210
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 294..355
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 219..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..295
FT /note="Interaction with FYB1"
FT COMPBIAS 219..236
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 142
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q3UUV5"
FT MOD_RES 219
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:11909961"
FT MOD_RES 232
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:11909961"
FT MOD_RES 271
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 295
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000305"
FT VAR_SEQ 293
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022179"
FT VARIANT 161
FT /note="G -> S (in dbSNP:rs2278868)"
FT /evidence="ECO:0000269|PubMed:9195899"
FT /id="VAR_029811"
FT VARIANT 242
FT /note="S -> G (in dbSNP:rs35288886)"
FT /id="VAR_035343"
FT MUTAGEN 219
FT /note="Y->F: Impairs interaction with PTPRC. No effect on
FT interaction with FYN or GRB2."
FT /evidence="ECO:0000269|PubMed:11909961,
FT ECO:0000269|PubMed:12171928"
FT MUTAGEN 232
FT /note="Y->F: Abolishes interaction with PTPRC,
FT translocation to cell membrane upon T-cell stimulation and
FT activation of the MAP kinase pathway. No effect on
FT interaction with FYN or GRB2."
FT /evidence="ECO:0000269|PubMed:11909961,
FT ECO:0000269|PubMed:12171928"
FT MUTAGEN 271
FT /note="Y->F: No effect on interaction with PTPRC and
FT translocation to cell membrane upon T-cell stimulation.
FT Abolishes interaction with FYN and GRB2 and activation of
FT the MAP kinase pathway."
FT /evidence="ECO:0000269|PubMed:11909961,
FT ECO:0000269|PubMed:12171928"
FT MUTAGEN 295
FT /note="Y->F: Abolishes FYB1-dependent activation of ITGAL
FT clustering."
FT /evidence="ECO:0000269|PubMed:10856234"
FT MUTAGEN 298
FT /note="Y->F: Impairs interaction with FYB1."
FT /evidence="ECO:0000269|PubMed:10856234"
FT MUTAGEN 333
FT /note="W->R: Abolishes homodimerization, interaction with
FT FYB1 and activation of the MAP kinase pathway."
FT /evidence="ECO:0000269|PubMed:12171928,
FT ECO:0000269|PubMed:15849195, ECO:0000269|PubMed:9748251"
FT CONFLICT 187
FT /note="S -> T (in Ref. 1; CAA72101)"
FT /evidence="ECO:0000305"
FT STRAND 108..119
FT /evidence="ECO:0007829|PDB:1U5D"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1U5D"
FT STRAND 126..136
FT /evidence="ECO:0007829|PDB:1U5D"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:1U5D"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:1U5D"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:1U5D"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1U5D"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:1U5D"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1U5D"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1U5D"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1U5D"
FT HELIX 195..212
FT /evidence="ECO:0007829|PDB:1U5D"
SQ SEQUENCE 359 AA; 41432 MW; 630FE4C17295BD6D CRC64;
MQAAALPEEI RWLLEDAEEF LAEGLRNENL SAVARDHRDH ILRGFQQIKA RYYWDFQPQG
GDIGQDSSDD NHSGTLGLSL TSDAPFLSDY QDEGMEDIVK GAQELDNVIK QGYLEKKSKD
HSFFGSEWQK RWCVVSRGLF YYYANEKSKQ PKGTFLIKGY GVRMAPHLRR DSKKESCFEL
TSQDRRSYEF TATSPAEARD WVDQISFLLK DLSSLTIPYE EDEEEEEKEE TYDDIDGFDS
PSCGSQCRPT ILPGSVGIKE PTEEKEEEDI YEVLPDEEHD LEEDESGTRR KGVDYASYYQ
GLWDCHGDQP DELSFQRGDL IRILSKEYNM YGWWVGELNS LVGIVPKEYL TTAFEVEER
