SKAP2_HUMAN
ID SKAP2_HUMAN Reviewed; 359 AA.
AC O75563; A4D173; Q53GP6; Q75MK6; Q75MZ4; Q9UBZ3; Q9UED8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Src kinase-associated phosphoprotein 2;
DE AltName: Full=Pyk2/RAFTK-associated protein;
DE AltName: Full=Retinoic acid-induced protein 70;
DE AltName: Full=SKAP55 homolog;
DE Short=SKAP-55HOM;
DE Short=SKAP-HOM;
DE AltName: Full=Src family-associated phosphoprotein 2;
DE AltName: Full=Src kinase-associated phosphoprotein 55-related protein;
DE AltName: Full=Src-associated adapter protein with PH and SH3 domains;
GN Name=SKAP2; Synonyms=PRAP, RA70, SAPS, SCAP2, SKAP55R;
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], TISSUE SPECIFICITY, INDUCTION, POSSIBLE
RP INTERACTION WITH FYN; HCK AND LYN, FUNCTION, AND VARIANT SER-202.
RC TISSUE=Testis;
RX PubMed=9837776; DOI=10.1006/bbrc.1998.9637;
RA Kouroku Y., Soyama A., Fujita E., Urase K., Tsukahara T., Momoi T.;
RT "RA70 is a src kinase-associated protein expressed ubiquitously.";
RL Biochem. Biophys. Res. Commun. 252:738-742(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, PHOSPHORYLATION,
RP INTERACTION WITH FYB1, AND VARIANT SER-202.
RC TISSUE=Leukocyte;
RX PubMed=9755858; DOI=10.1016/s0014-5793(98)01040-0;
RA Marie-Cardine A., Verhagen A.M., Eckerskorn C., Schraven B.;
RT "SKAP-HOM, a novel adaptor protein homologous to the FYN-associated protein
RT SKAP55.";
RL FEBS Lett. 435:55-60(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FYB1, AND PHOSPHORYLATION.
RC TISSUE=Lymphocyte;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PTK2B, PHOSPHORYLATION,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Hippocampus;
RX PubMed=12893833; DOI=10.1074/jbc.m213217200;
RA Takahashi T., Yamashita H., Nagano Y., Nakamura T., Ohmori H., Avraham H.,
RA Avraham S., Yasuda M., Matsumoto M.;
RT "Identification and characterization of a novel Pyk2/related adhesion focal
RT tyrosine kinase-associated protein that inhibits alpha-synuclein
RT phosphorylation.";
RL J. Biol. Chem. 278:42225-42233(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-202.
RC TISSUE=Pancreas;
RA Lee J.-S., Suh K.S., Burr J.G.;
RT "Src-associated adaptor protein with PH and SH3 domain.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Testis;
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 [12]
RP PHOSPHORYLATION, INTERACTION WITH FYB1; LAT AND GRB2, AND TISSUE
RP SPECIFICITY.
RX PubMed=10942756; DOI=10.1074/jbc.m001439200;
RA Asazuma N., Wilde J.I., Berlanga O., Leduc M., Leo A., Schweighoffer E.,
RA Tybulewicz V., Bon C., Liu S.K., McGlade C.J., Schraven B., Watson S.P.;
RT "Interaction of linker for activation of T cells with multiple adapter
RT proteins in platelets activated by the glycoprotein VI-selective ligand,
RT convulxin.";
RL J. Biol. Chem. 275:33427-33434(2000).
RN [13]
RP INDUCTION, AND INTERACTION WITH PRAM1.
RX PubMed=11301322; DOI=10.1074/jbc.m011683200;
RA Moog-Lutz C., Peterson E.J., Lutz P.G., Eliason S., Cave-Riant F.,
RA Singer A., Di Gioia Y., Dmovski S., Kamens J., Cayre Y.E., Koretzky G.;
RT "PRAM-1 is a novel adaptor protein regulated by retinoic acid (RA) and
RT promyelocytic leukemia (PML)-RA receptor alpha in acute promyelocytic
RT leukemia cells.";
RL J. Biol. Chem. 276:22375-22381(2001).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-6, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND TYR-197, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 71-79 IN COMPLEX WITH PTPN22, AND
RP PHOSPHORYLATION AT TYR-75.
RX PubMed=21719704; DOI=10.1074/jbc.m111.254722;
RA Yu X., Chen M., Zhang S., Yu Z.H., Sun J.P., Wang L., Liu S., Imasaki T.,
RA Takagi Y., Zhang Z.Y.;
RT "Substrate specificity of lymphoid-specific tyrosine phosphatase (Lyp) and
RT identification of Src kinase-associated protein of 55 kDa homolog (SKAP-
RT HOM) as a Lyp substrate.";
RL J. Biol. Chem. 286:30526-30534(2011).
CC -!- FUNCTION: May be involved in B-cell and macrophage adhesion processes.
CC In B-cells, may act by coupling the B-cell receptor (BCR) to integrin
CC activation. May play a role in src signaling pathway.
CC {ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:9837776}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with PTPNS1. Part of a
CC complex consisting of SKAP2, FYB1 and PTPNS1. Part of a complex
CC consisting of SKAP2, FYB1 and LILRB3. May interact with actin (By
CC similarity). Interacts with FYB1, which is required for SKAP2 protein
CC stability. Interacts with LAT, GRB2, PTK2B and PRAM1. May interact with
CC FYN, HCK and LYN. Interacts with FASLG. {ECO:0000250,
CC ECO:0000269|PubMed:10942756, ECO:0000269|PubMed:11301322,
CC ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:19807924,
CC ECO:0000269|PubMed:21719704, ECO:0000269|PubMed:9671755,
CC ECO:0000269|PubMed:9755858}.
CC -!- INTERACTION:
CC O75563; Q9Y2R2: PTPN22; NbExp=3; IntAct=EBI-2483161, EBI-1211241;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12893833}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Present in platelets (at
CC protein level). {ECO:0000269|PubMed:10942756,
CC ECO:0000269|PubMed:9755858, ECO:0000269|PubMed:9837776}.
CC -!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:11301322,
CC ECO:0000269|PubMed:9837776}.
CC -!- DOMAIN: The SH3 domain interacts with FYB1 and PTK2B.
CC -!- PTM: Phosphorylated in resting platelets. Phosphorylated by FYN on Tyr-
CC 261 upon T-cell activation (Probable). Dephosphorylated on Tyr-75 by
CC PTPN22. {ECO:0000269|PubMed:10942756, ECO:0000269|PubMed:12893833,
CC ECO:0000269|PubMed:21719704, ECO:0000269|PubMed:9671755,
CC ECO:0000269|PubMed:9755858, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SKAP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB014486; BAA36194.1; -; mRNA.
DR EMBL; AJ004886; CAA06193.1; -; mRNA.
DR EMBL; AF072166; AAC39924.1; -; mRNA.
DR EMBL; AF051323; AAC99296.1; -; mRNA.
DR EMBL; AK313209; BAG36025.1; -; mRNA.
DR EMBL; AK222885; BAD96605.1; -; mRNA.
DR EMBL; AC003999; AAS02033.1; -; Genomic_DNA.
DR EMBL; AC011299; AAS07536.1; -; Genomic_DNA.
DR EMBL; CH236948; EAL24231.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93859.1; -; Genomic_DNA.
DR EMBL; BC002893; AAH02893.1; -; mRNA.
DR EMBL; BC036044; AAH36044.1; -; mRNA.
DR CCDS; CCDS5400.1; -.
DR RefSeq; NP_001290397.1; NM_001303468.1.
DR RefSeq; NP_003921.2; NM_003930.4.
DR RefSeq; XP_016868260.1; XM_017012771.1.
DR PDB; 3OMH; X-ray; 2.90 A; E/F/G/H=71-79.
DR PDBsum; 3OMH; -.
DR AlphaFoldDB; O75563; -.
DR SMR; O75563; -.
DR BioGRID; 114448; 43.
DR IntAct; O75563; 12.
DR STRING; 9606.ENSP00000005587; -.
DR iPTMnet; O75563; -.
DR PhosphoSitePlus; O75563; -.
DR BioMuta; SKAP2; -.
DR OGP; O75563; -.
DR EPD; O75563; -.
DR MassIVE; O75563; -.
DR MaxQB; O75563; -.
DR PaxDb; O75563; -.
DR PeptideAtlas; O75563; -.
DR PRIDE; O75563; -.
DR ProteomicsDB; 50086; -.
DR Antibodypedia; 25901; 233 antibodies from 33 providers.
DR DNASU; 8935; -.
DR Ensembl; ENST00000345317.7; ENSP00000005587.2; ENSG00000005020.13.
DR GeneID; 8935; -.
DR KEGG; hsa:8935; -.
DR MANE-Select; ENST00000345317.7; ENSP00000005587.2; NM_003930.5; NP_003921.2.
DR UCSC; uc003syc.4; human.
DR CTD; 8935; -.
DR DisGeNET; 8935; -.
DR GeneCards; SKAP2; -.
DR HGNC; HGNC:15687; SKAP2.
DR HPA; ENSG00000005020; Low tissue specificity.
DR MIM; 605215; gene.
DR neXtProt; NX_O75563; -.
DR OpenTargets; ENSG00000005020; -.
DR PharmGKB; PA162403393; -.
DR VEuPathDB; HostDB:ENSG00000005020; -.
DR eggNOG; ENOG502QVFD; Eukaryota.
DR GeneTree; ENSGT00390000017856; -.
DR HOGENOM; CLU_062032_0_0_1; -.
DR InParanoid; O75563; -.
DR OMA; KQGFPQD; -.
DR OrthoDB; 767446at2759; -.
DR PhylomeDB; O75563; -.
DR TreeFam; TF331055; -.
DR PathwayCommons; O75563; -.
DR Reactome; R-HSA-391160; Signal regulatory protein family interactions.
DR SignaLink; O75563; -.
DR BioGRID-ORCS; 8935; 77 hits in 1066 CRISPR screens.
DR ChiTaRS; SKAP2; human.
DR GeneWiki; SKAP2; -.
DR GenomeRNAi; 8935; -.
DR Pharos; O75563; Tbio.
DR PRO; PR:O75563; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O75563; protein.
DR Bgee; ENSG00000005020; Expressed in sperm and 209 other tissues.
DR ExpressionAtlas; O75563; baseline and differential.
DR Genevisible; O75563; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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; 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; B-cell activation; Cytoplasm; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..359
FT /note="Src kinase-associated phosphoprotein 2"
FT /id="PRO_0000270179"
FT DOMAIN 116..219
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 297..358
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 14..64
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 66..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT MOD_RES 75
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:21719704"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT MOD_RES 151
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q3UND0"
FT MOD_RES 197
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT MOD_RES 261
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q3UND0"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT VARIANT 202
FT /note="A -> S (in dbSNP:rs1129771)"
FT /evidence="ECO:0000269|PubMed:9755858,
FT ECO:0000269|PubMed:9837776, ECO:0000269|Ref.5"
FT /id="VAR_029812"
FT VARIANT 253
FT /note="S -> T (in dbSNP:rs17154402)"
FT /id="VAR_029813"
FT CONFLICT 6
FT /note="S -> C (in Ref. 1; BAA36194)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="Y -> H (in Ref. 7; BAD96605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 41217 MW; 65F266535A89281E CRC64;
MPNPSSTSSP YPLPEEIRNL LADVETFVAD ILKGENLSKK AKEKRESLIK KIKDVKSIYL
QEFQDKGDAE DGEEYDDPFA GPPDTISLAS ERYDKDDEAP SDGAQFPPIA AQDLPFVLKA
GYLEKRRKDH SFLGFEWQKR WCALSKTVFY YYGSDKDKQQ KGEFAIDGYS VRMNNTLRKD
GKKDCCFEIS APDKRIYQFT AASPKDAEEW VQQLKFVLQD MESDIIPEDY DERGELYDDV
DHPLPISNPL TSSQPIDDEI YEELPEEEED SAPVKVEEQR KMSQDSVHHT SGDKSTDYAN
FYQGLWDCTG AFSDELSFKR GDVIYILSKE YNRYGWWVGE MKGAIGLVPK AYIMEMYDI
