SH3K1_HUMAN
ID SH3K1_HUMAN Reviewed; 665 AA.
AC Q96B97; B7Z1D5; Q5JPT4; Q5JPT5; Q8IWX6; Q8IX98; Q96RN4; Q9NYR0;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=SH3 domain-containing kinase-binding protein 1;
DE AltName: Full=CD2-binding protein 3;
DE Short=CD2BP3;
DE AltName: Full=Cbl-interacting protein of 85 kDa;
DE AltName: Full=Human Src family kinase-binding protein 1;
DE Short=HSB-1;
GN Name=SH3KBP1; Synonyms=CIN85;
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 INTERACTION WITH CBL.
RX PubMed=10679202; DOI=10.1006/bbrc.2000.2147;
RA Take H., Watanabe S., Takeda K., Yu Z.-X., Iwata N., Kajigaya S.;
RT "Cloning and characterization of a novel adaptor protein, CIN85, that
RT interacts with c-Cbl.";
RL Biochem. Biophys. Res. Commun. 268:321-328(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=T-cell;
RX PubMed=12618476; DOI=10.1093/intimm/dxg032;
RA Tibaldi E.V., Reinherz E.L.;
RT "CD2BP3, CIN85 and the structurally related adaptor protein CMS bind to the
RT same CD2 cytoplasmic segment but elicit divergent functional activities.";
RL Int. Immunol. 15:313-329(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal cortex, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 262-665, AND VARIANT LEU-382.
RX PubMed=11474197; DOI=10.1159/000056966;
RA Narita T., Amano F., Yoshizaki K., Nishimoto N., Nishimura T., Tajima T.,
RA Namiki H., Taniyama T.;
RT "Assignment of SH3KBP1 to human chromosome band Xp22.1-->p21.3 by in situ
RT hybridization.";
RL Cytogenet. Cell Genet. 93:133-134(2001).
RN [7]
RP INTERACTION WITH BLNK; CRK; BCAR1; PIK3R3; GRB2 AND SOS1, AND
RP SELF-ASSOCIATION.
RX PubMed=11071869; DOI=10.1006/bbrc.2000.3760;
RA Watanabe S., Take H., Takeda K., Yu Z.X., Iwata N., Kajigaya S.;
RT "Characterization of the CIN85 adaptor protein and identification of
RT components involved in CIN85 complexes.";
RL Biochem. Biophys. Res. Commun. 278:167-174(2000).
RN [8]
RP INTERACTION WITH CBLB AND ENDOPHILINS, LACK OF INTERACTION WITH CBLC,
RP FUNCTION IN RECEPTOR INTERNALIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=12177062; DOI=10.1074/jbc.m205535200;
RA Szymkiewicz I., Kowanetz K., Soubeyran P., Dinarina A., Lipkowitz S.,
RA Dikic I.;
RT "CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine
RT kinases.";
RL J. Biol. Chem. 277:39666-39672(2002).
RN [9]
RP FUNCTION IN RECEPTOR INTERNALIZATION, INTERACTION WITH EGFR; SH3GL1;
RP SH3GL2; SH3GL3 AND CBL, AND SUBCELLULAR LOCATION.
RX PubMed=11894095; DOI=10.1038/416183a;
RA Soubeyran P., Kowanetz K., Szymkiewicz I., Langdon W.Y., Dikic I.;
RT "Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF
RT receptors.";
RL Nature 416:183-187(2002).
RN [10]
RP FUNCTION IN RECEPTOR INTERNALIZATION, AND INTERACTION WITH SH3GL1; SH3GL2;
RP SH3GL3; CBL AND MET.
RX PubMed=11894096; DOI=10.1038/416187a;
RA Petrelli A., Gilestro G.F., Lanzardo S., Comoglio P.M., Migone N.,
RA Giordano S.;
RT "The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation
RT of c-Met.";
RL Nature 416:187-190(2002).
RN [11]
RP UBIQUITINATION BY CBL AND CBLB.
RX PubMed=12218189; DOI=10.1073/pnas.192462299;
RA Haglund K., Shimokawa N., Szymkiewicz I., Dikic I.;
RT "Cbl-directed monoubiquitination of CIN85 is involved in regulation of
RT ligand-induced degradation of EGF receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12191-12196(2002).
RN [12]
RP INTERACTION WITH DAB2, AND IDENTIFICATION IN A COMPLEX WITH DAB2 AND
RP CLATHRIN.
RX PubMed=14596919; DOI=10.1016/s0014-5793(03)01111-6;
RA Kowanetz K., Terzic J., Dikic I.;
RT "Dab2 links CIN85 with clathrin-mediated receptor internalization.";
RL FEBS Lett. 554:81-87(2003).
RN [13]
RP FUNCTION IN CELL ADHESION, AND INTERACTION WITH PDCD6IP; PTK2/FAK1 AND
RP PTK2B/PYK2.
RX PubMed=12771190; DOI=10.1242/jcs.00522;
RA Schmidt M.H., Chen B., Randazzo L.M., Boegler O.;
RT "SETA/CIN85/Ruk and its binding partner AIP1 associate with diverse
RT cytoskeletal elements, including FAKs, and modulate cell adhesion.";
RL J. Cell Sci. 116:2845-2855(2003).
RN [14]
RP INTERACTION WITH CD2 AND F-ACTIN CAPPING PROTEIN.
RX PubMed=12690097; DOI=10.1074/jbc.m302540200;
RA Hutchings N.J., Clarkson N., Chalkley R., Barclay A.N., Brown M.H.;
RT "Linking the T cell surface protein CD2 to the actin-capping protein CAPZ
RT via CMS and CIN85.";
RL J. Biol. Chem. 278:22396-22403(2003).
RN [15]
RP FUNCTION IN RECEPTOR INTERNALIZATION.
RX PubMed=12734385; DOI=10.1073/pnas.1031790100;
RA Schmidt M.H., Furnari F.B., Cavenee W.K., Bogler O.;
RT "Epidermal growth factor receptor signaling intensity determines
RT intracellular protein interactions, ubiquitination, and internalization.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:6505-6510(2003).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [17]
RP FUNCTION IN RECEPTOR INTERNALIZATION, INTERACTION WITH ASAP1; ARAP3; HIP1R;
RP SYNJ2; INPP5D; STAP1 AND EGFR, IDENTIFICATION IN A COMPLEX WITH ASAP1 AND
RP ARAP3, AND SUBCELLULAR LOCATION.
RX PubMed=15090612; DOI=10.1091/mbc.e03-09-0683;
RA Kowanetz K., Husnjak K., Holler D., Kowanetz M., Soubeyran P., Hirsch D.,
RA Schmidt M.H., Pavelic K., De Camilli P., Randazzo P.A., Dikic I.;
RT "CIN85 associates with multiple effectors controlling intracellular
RT trafficking of epidermal growth factor receptors.";
RL Mol. Biol. Cell 15:3155-3166(2004).
RN [18]
RP INTERACTION WITH PDCD6IP; EGFR; CBL AND CBLB.
RX PubMed=15456872; DOI=10.1128/mcb.24.20.8981-8993.2004;
RA Schmidt M.H., Hoeller D., Yu J., Furnari F.B., Cavenee W.K., Dikic I.,
RA Bogler O.;
RT "Alix/AIP1 antagonizes epidermal growth factor receptor downregulation by
RT the Cbl-SETA/CIN85 complex.";
RL Mol. Cell. Biol. 24:8981-8993(2004).
RN [19]
RP FUNCTION, AND INTERACTION WITH MAP3K4.
RX PubMed=16256071; DOI=10.1016/j.bbrc.2005.10.032;
RA Aissouni Y., Zapart G., Iovanna J.L., Dikic I., Soubeyran P.;
RT "CIN85 regulates the ability of MEKK4 to activate the p38 MAP kinase
RT pathway.";
RL Biochem. Biophys. Res. Commun. 338:808-814(2005).
RN [20]
RP INTERACTION WITH SPRY2.
RX PubMed=15962011; DOI=10.1038/sj.embor.7400453;
RA Haglund K., Schmidt M.H., Wong E.S., Guy G.R., Dikic I.;
RT "Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth
RT factor receptor downregulation.";
RL EMBO Rep. 6:635-641(2005).
RN [21]
RP FUNCTION IN APOPTOSIS, AND INTERACTION WITH SRC; LCK; LYN; FGR; FYN; HCK;
RP TRADD; BIRC2; TRAF1; TRAF2 AND TNFR1.
RX PubMed=15707590; DOI=10.1016/j.yexcr.2004.11.005;
RA Narita T., Nishimura T., Yoshizaki K., Taniyama T.;
RT "CIN85 associates with TNF receptor 1 via Src and modulates TNF-alpha-
RT induced apoptosis.";
RL Exp. Cell Res. 304:256-264(2005).
RN [22]
RP FUNCTION IN RECEPTOR INTERNALIZATION.
RX PubMed=16177060; DOI=10.4049/jimmunol.175.7.4208;
RA Molfetta R., Belleudi F., Peruzzi G., Morrone S., Leone L., Dikic I.,
RA Piccoli M., Frati L., Torrisi M.R., Santoni A., Paolini R.;
RT "CIN85 regulates the ligand-dependent endocytosis of the IgE receptor: a
RT new molecular mechanism to dampen mast cell function.";
RL J. Immunol. 175:4208-4216(2005).
RN [23]
RP INTERACTION WITH ARHGAP17.
RX PubMed=16678097; DOI=10.1016/j.cell.2006.02.045;
RA Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M.,
RA Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K.,
RA Starostine A., Metalnikov P., Pawson T.;
RT "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
RT proteins in epithelial cells.";
RL Cell 125:535-548(2006).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [25]
RP INTERACTION WITH DDN AND MAGI2, AND SUBCELLULAR LOCATION.
RX PubMed=16751601; DOI=10.1093/jb/mvj105;
RA Kawata A., Iida J., Ikeda M., Sato Y., Mori H., Kansaku A., Sumita K.,
RA Fujiwara N., Rokukawa C., Hamano M., Hirabayashi S., Hata Y.;
RT "CIN85 is localized at synapses and forms a complex with S-SCAM via
RT dendrin.";
RL J. Biochem. 139:931-939(2006).
RN [26]
RP INTERACTION WITH MVB12A.
RX PubMed=16895919; DOI=10.1074/jbc.m605693200;
RA Konishi H., Tashiro K., Murata Y., Nabeshi H., Yamauchi E., Taniguchi H.;
RT "CFBP is a novel tyrosine-phosphorylated protein that might function as a
RT regulator of CIN85/CD2AP.";
RL J. Biol. Chem. 281:28919-28931(2006).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, 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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254; SER-436; SER-509;
RP SER-511; SER-521 AND SER-587, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, 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 [30]
RP INTERACTION WITH MAP3K4 AND ZFP36, AND SUBCELLULAR LOCATION.
RX PubMed=20221403; DOI=10.1371/journal.pone.0009588;
RA Kedar V.P., Darby M.K., Williams J.G., Blackshear P.J.;
RT "Phosphorylation of human tristetraprolin in response to its interaction
RT with the Cbl interacting protein CIN85.";
RL PLoS ONE 5:E9588-E9588(2010).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-436 AND SER-587, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [32]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
RN [33]
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 [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; THR-254; SER-436 AND
RP SER-587, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-509 AND SER-511, 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 [37]
RP FUNCTION, AND INVOLVEMENT IN IMD61.
RX PubMed=29636373; DOI=10.1084/jem.20170534;
RA Keller B., Shoukier M., Schulz K., Bhatt A., Heine I., Strohmeier V.,
RA Speckmann C., Engels N., Warnatz K., Wienands J.;
RT "Germline deletion of CIN85 in humans with X chromosome-linked antibody
RT deficiency.";
RL J. Exp. Med. 215:1327-1336(2018).
RN [38]
RP INTERACTION WITH CHIKUNGUNYA VIRUS NON-STRUCTURAL PROTEIN 3 (MICROBIAL
RP INFECTION).
RX PubMed=31493651; DOI=10.1016/j.virol.2019.08.022;
RA Agback P., Dominguez F., Pustovalova Y., Lukash T., Shiliaev N.,
RA Orekhov V.Y., Frolov I., Agback T., Frolova E.I.;
RT "Structural characterization and biological function of bivalent binding of
RT CD2AP to intrinsically disordered domain of chikungunya virus nsP3
RT protein.";
RL Virology 537:130-142(2019).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-58 IN COMPLEX WITH CBLB.
RX PubMed=16228008; DOI=10.1038/nsmb1000;
RA Jozic D., Cardenes N., Deribe Y.L., Moncalian G., Hoeller D., Groemping Y.,
RA Dikic I., Rittinger K., Bravo J.;
RT "Cbl promotes clustering of endocytic adaptor proteins.";
RL Nat. Struct. Mol. Biol. 12:972-979(2005).
CC -!- FUNCTION: Adapter protein involved in regulating diverse signal
CC transduction pathways. Involved in the regulation of endocytosis and
CC lysosomal degradation of ligand-induced receptor tyrosine kinases,
CC including EGFR and MET/hepatocyte growth factor receptor, through an
CC association with CBL and endophilins. The association with CBL, and
CC thus the receptor internalization, may be inhibited by an interaction
CC with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent
CC endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-
CC kinase activity by interaction with its regulatory subunit (By
CC similarity). May be involved in regulation of cell adhesion; promotes
CC the interaction between TTK2B and PDCD6IP. May be involved in the
CC regulation of cellular stress response via the MAPK pathways through
CC its interaction with MAP3K4. Is involved in modulation of tumor
CC necrosis factor mediated apoptosis. Plays a role in the regulation of
CC cell morphology and cytoskeletal organization. Required in the control
CC of cell shape and migration. Has an essential role in the stimulation
CC of B cell activation (PubMed:29636373). {ECO:0000250,
CC ECO:0000269|PubMed:11894095, ECO:0000269|PubMed:11894096,
CC ECO:0000269|PubMed:12177062, ECO:0000269|PubMed:12734385,
CC ECO:0000269|PubMed:12771190, ECO:0000269|PubMed:15090612,
CC ECO:0000269|PubMed:15707590, ECO:0000269|PubMed:16177060,
CC ECO:0000269|PubMed:16256071, ECO:0000269|PubMed:21834987,
CC ECO:0000269|PubMed:29636373}.
CC -!- SUBUNIT: Can self-associate and form homotetramers. Interacts with CD2,
CC F-actin capping protein, PIK3R3, GRB2, EGFR, MET, BLNK, MAP3K4,
CC PDCD6IP, SPRY2, ARHGAP17, ARHGAP27, MAGI2, CRK, BCAR1, SOS1, ASAP1,
CC ARAP3, HIP1R, SYNJ2, INPP5D and STAP1. Interacts with CBL and CBLB, but
CC does not interact with CBLC. Two molecules of SH3KBP1 seem to bind
CC through their respective SH3 1 domain to one molecule of CBLB. The
CC interaction with CBL or CBLB and EGFR is increased upon EGF
CC stimulation. The interaction with CBL is attenuated by PDCD6IP.
CC Interacts through its proline-rich region with the SH3 domain of
CC endophilins SH3GL1, SH3GL2 and SH3GL3. The SH3KBP1-endophilin complex
CC seems to associate with a complex containing the phosphorylated
CC receptor (EGFR or MET) and phosphorylated CBL. Probably associates with
CC ASAP1 and phosphorylated EGFR. Probably part of a complex consisting of
CC at least SH3KBP1, ASAP1 and ARAP3. Interacts with focal adhesion
CC kinases PTK2/FAK1 AND PTK2B/PYK2, probably as a dimer. Interacts with
CC DAB2 and probably associates with chathrin through its interaction with
CC DAB2. Part of a complex consisting of SH3KBP1, DAB2, and clathrin heavy
CC chain. DAB2 and clathrin dissociate from SH3KBP1 following growth
CC factor treatment, enabling interaction with CBL. Interacts with DDN and
CC probably associates with MAGI2 through its interaction with DDN.
CC Interacts with the SH3 domains of SRC tyrosine-protein kinases SRC,
CC LCK, LYN, FGR, FYN and HCK. Interacts with TRADD, BIRC2, TRAF1, TRAF2
CC and TNFR1, and the association with a TNFR1-associated complex upon
CC stimulation with TNF-alpha seems to be mediated by SRC. Interacts (via
CC SH3 domains) with SHKBP1 (via PXXXPR motifs) (By similarity).
CC Interaction with CBL is abolished in the presence of SHKBP1 (By
CC similarity). Interacts (via SH3 domains) with ZFP36 (via extreme C-
CC terminal region) (PubMed:20221403). Interacts with MAP3K4; this
CC interaction enhances the association with ZFP36 (PubMed:20221403).
CC {ECO:0000250|UniProtKB:Q8R550, ECO:0000269|PubMed:10679202,
CC ECO:0000269|PubMed:11071869, ECO:0000269|PubMed:11894095,
CC ECO:0000269|PubMed:11894096, ECO:0000269|PubMed:12177062,
CC ECO:0000269|PubMed:12690097, ECO:0000269|PubMed:12771190,
CC ECO:0000269|PubMed:14596919, ECO:0000269|PubMed:15090612,
CC ECO:0000269|PubMed:15456872, ECO:0000269|PubMed:15707590,
CC ECO:0000269|PubMed:15962011, ECO:0000269|PubMed:16228008,
CC ECO:0000269|PubMed:16256071, ECO:0000269|PubMed:16678097,
CC ECO:0000269|PubMed:16751601, ECO:0000269|PubMed:16895919,
CC ECO:0000269|PubMed:20221403}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via SH3 domains) with
CC Chikungunya virus non-structural protein 3 (via C-terminus); this
CC interaction plays a role in initiation of viral replication.
CC {ECO:0000269|PubMed:31493651}.
CC -!- INTERACTION:
CC Q96B97; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-346595, EBI-11954519;
CC Q96B97; Q8WWN8: ARAP3; NbExp=4; IntAct=EBI-346595, EBI-4402732;
CC Q96B97; Q9ULH1: ASAP1; NbExp=11; IntAct=EBI-346595, EBI-346622;
CC Q96B97; O43150: ASAP2; NbExp=3; IntAct=EBI-346595, EBI-310968;
CC Q96B97; Q6PI77: BHLHB9; NbExp=5; IntAct=EBI-346595, EBI-11519926;
CC Q96B97; P52907: CAPZA1; NbExp=5; IntAct=EBI-346595, EBI-355586;
CC Q96B97; P22681: CBL; NbExp=20; IntAct=EBI-346595, EBI-518228;
CC Q96B97; Q13191: CBLB; NbExp=22; IntAct=EBI-346595, EBI-744027;
CC Q96B97; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-346595, EBI-10961624;
CC Q96B97; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-346595, EBI-347573;
CC Q96B97; P06729: CD2; NbExp=3; IntAct=EBI-346595, EBI-3912464;
CC Q96B97; Q9Y5K6: CD2AP; NbExp=4; IntAct=EBI-346595, EBI-298152;
CC Q96B97; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-346595, EBI-3867333;
CC Q96B97; O94850: DDN; NbExp=5; IntAct=EBI-346595, EBI-5240523;
CC Q96B97; Q9ULE3-2: DENND2A; NbExp=3; IntAct=EBI-346595, EBI-13305669;
CC Q96B97; P50570: DNM2; NbExp=5; IntAct=EBI-346595, EBI-346547;
CC Q96B97; Q86UU5: GGN; NbExp=3; IntAct=EBI-346595, EBI-10259069;
CC Q96B97; Q92835: INPP5D; NbExp=6; IntAct=EBI-346595, EBI-1380477;
CC Q96B97; O60333-2: KIF1B; NbExp=3; IntAct=EBI-346595, EBI-10975473;
CC Q96B97; Q5T749: KPRP; NbExp=5; IntAct=EBI-346595, EBI-10981970;
CC Q96B97; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-346595, EBI-741037;
CC Q96B97; Q9Y6R4: MAP3K4; NbExp=5; IntAct=EBI-346595, EBI-448104;
CC Q96B97; Q9H3P2: NELFA; NbExp=3; IntAct=EBI-346595, EBI-5461341;
CC Q96B97; P07237: P4HB; NbExp=3; IntAct=EBI-346595, EBI-395883;
CC Q96B97; P53803: POLR2K; NbExp=3; IntAct=EBI-346595, EBI-395357;
CC Q96B97; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-346595, EBI-396669;
CC Q96B97; P78314: SH3BP2; NbExp=8; IntAct=EBI-346595, EBI-727062;
CC Q96B97; Q99962: SH3GL2; NbExp=2; IntAct=EBI-346595, EBI-77938;
CC Q96B97; O43597: SPRY2; NbExp=2; IntAct=EBI-346595, EBI-742487;
CC Q96B97; Q13501: SQSTM1; NbExp=4; IntAct=EBI-346595, EBI-307104;
CC Q96B97; Q9ULZ2: STAP1; NbExp=5; IntAct=EBI-346595, EBI-6083058;
CC Q96B97; O15056: SYNJ2; NbExp=5; IntAct=EBI-346595, EBI-310513;
CC Q96B97; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-346595, EBI-11952721;
CC Q96B97; P0CG48: UBC; NbExp=6; IntAct=EBI-346595, EBI-3390054;
CC Q96B97; O76024: WFS1; NbExp=3; IntAct=EBI-346595, EBI-720609;
CC Q96B97; O15156-2: ZBTB7B; NbExp=3; IntAct=EBI-346595, EBI-11522250;
CC Q96B97; Q7Z783; NbExp=3; IntAct=EBI-346595, EBI-9088990;
CC Q96B97; P98078: Dab2; Xeno; NbExp=9; IntAct=EBI-346595, EBI-1391846;
CC Q96B97; P39052: Dnm2; Xeno; NbExp=4; IntAct=EBI-346595, EBI-349613;
CC Q96B97; Q9JKY5: Hip1r; Xeno; NbExp=3; IntAct=EBI-346595, EBI-642457;
CC Q96B97-1; Q13191-1: CBLB; NbExp=3; IntAct=EBI-7585212, EBI-15555129;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20221403}.
CC Cytoplasm, cytoskeleton. Cytoplasmic vesicle membrane; Peripheral
CC membrane protein. Synapse, synaptosome. Cell junction, focal adhesion
CC {ECO:0000250}. Note=Localized in endocytic vesicles containing
CC clustered receptors. Colocalizes with ASAP1 in vesicular structures.
CC Colocalized with actin microfilaments and focal adhesions (By
CC similarity). Colocalized with MAGI2 in synaptosomes. Translocation to
CC EGFR containing vesicles upon EGF stimulation is inhibited in the
CC presence of SH3KBP1 (By similarity). Colocalizes with ZFP36 in the
CC cytoplasm (PubMed:20221403). {ECO:0000250|UniProtKB:Q8R550,
CC ECO:0000269|PubMed:20221403}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96B97-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96B97-2; Sequence=VSP_007504;
CC Name=3;
CC IsoId=Q96B97-3; Sequence=VSP_044655, VSP_044656;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Also expressed in some
CC cancer cell lines.
CC -!- PTM: Monoubiquitinated by CBL and CBLB after EGF stimulation; probably
CC on its C-terminus.
CC -!- DISEASE: Immunodeficiency 61 (IMD61) [MIM:300310]: An X-linked
CC recessive primary immunologic disorder characterized by recurrent
CC infections due to impaired antibody production. Affected individuals
CC have normal numbers of circulating B and T cells, but B cells have an
CC intrinsic defect in antibody production. Disease severity is variable
CC and onset is in early childhood. {ECO:0000269|PubMed:29636373}.
CC Note=The disease may be caused by variants affecting the gene
CC represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 1]: Interacts with CBL.
CC -!- MISCELLANEOUS: [Isoform 2]: Interacts with CD2 cytoplasmic tail and
CC does not interact with F-actin. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50663.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF230904; AAF37854.1; -; mRNA.
DR EMBL; AF542051; AAN77231.1; -; mRNA.
DR EMBL; AK293234; BAH11470.1; -; mRNA.
DR EMBL; AK293237; BAH11471.1; -; mRNA.
DR EMBL; AL732423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL772197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015806; AAH15806.1; -; mRNA.
DR EMBL; BC050663; AAH50663.1; ALT_SEQ; mRNA.
DR EMBL; AF329267; AAK95587.1; -; mRNA.
DR EMBL; AF329268; AAO13348.1; -; mRNA.
DR CCDS; CCDS14193.1; -. [Q96B97-1]
DR CCDS; CCDS35213.1; -. [Q96B97-2]
DR CCDS; CCDS55383.1; -. [Q96B97-3]
DR PIR; JC7191; JC7191.
DR RefSeq; NP_001019837.1; NM_001024666.2. [Q96B97-2]
DR RefSeq; NP_001171889.1; NM_001184960.1. [Q96B97-3]
DR RefSeq; NP_114098.1; NM_031892.2. [Q96B97-1]
DR RefSeq; XP_016884958.1; XM_017029469.1.
DR PDB; 2BZ8; X-ray; 2.00 A; A/B=1-58.
DR PDB; 2K6D; NMR; -; A=267-328.
DR PDB; 2K9G; NMR; -; A=262-333.
DR PDB; 2N64; NMR; -; A/B/C=594-665.
DR PDB; 2O2O; NMR; -; A=92-168.
DR PDB; 2YDL; X-ray; 2.05 A; A=270-328.
DR PDB; 5ABS; X-ray; 1.74 A; A=599-662.
DR PDBsum; 2BZ8; -.
DR PDBsum; 2K6D; -.
DR PDBsum; 2K9G; -.
DR PDBsum; 2N64; -.
DR PDBsum; 2O2O; -.
DR PDBsum; 2YDL; -.
DR PDBsum; 5ABS; -.
DR AlphaFoldDB; Q96B97; -.
DR SMR; Q96B97; -.
DR BioGRID; 119029; 353.
DR CORUM; Q96B97; -.
DR DIP; DIP-31803N; -.
DR IntAct; Q96B97; 124.
DR MINT; Q96B97; -.
DR STRING; 9606.ENSP00000380921; -.
DR GlyGen; Q96B97; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q96B97; -.
DR MetOSite; Q96B97; -.
DR PhosphoSitePlus; Q96B97; -.
DR BioMuta; SH3KBP1; -.
DR DMDM; 31077034; -.
DR EPD; Q96B97; -.
DR jPOST; Q96B97; -.
DR MassIVE; Q96B97; -.
DR MaxQB; Q96B97; -.
DR PaxDb; Q96B97; -.
DR PeptideAtlas; Q96B97; -.
DR PRIDE; Q96B97; -.
DR ProteomicsDB; 63029; -.
DR ProteomicsDB; 76057; -. [Q96B97-1]
DR ProteomicsDB; 76058; -. [Q96B97-2]
DR Antibodypedia; 521; 216 antibodies from 32 providers.
DR DNASU; 30011; -.
DR Ensembl; ENST00000379698.8; ENSP00000369020.4; ENSG00000147010.18. [Q96B97-2]
DR Ensembl; ENST00000379716.5; ENSP00000369039.1; ENSG00000147010.18. [Q96B97-3]
DR Ensembl; ENST00000397821.8; ENSP00000380921.3; ENSG00000147010.18. [Q96B97-1]
DR GeneID; 30011; -.
DR KEGG; hsa:30011; -.
DR MANE-Select; ENST00000397821.8; ENSP00000380921.3; NM_031892.3; NP_114098.1.
DR UCSC; uc004czl.4; human. [Q96B97-1]
DR CTD; 30011; -.
DR DisGeNET; 30011; -.
DR GeneCards; SH3KBP1; -.
DR HGNC; HGNC:13867; SH3KBP1.
DR HPA; ENSG00000147010; Low tissue specificity.
DR MalaCards; SH3KBP1; -.
DR MIM; 300310; phenotype.
DR MIM; 300374; gene.
DR neXtProt; NX_Q96B97; -.
DR OpenTargets; ENSG00000147010; -.
DR PharmGKB; PA37822; -.
DR VEuPathDB; HostDB:ENSG00000147010; -.
DR eggNOG; KOG4348; Eukaryota.
DR GeneTree; ENSGT00940000155886; -.
DR HOGENOM; CLU_024255_1_0_1; -.
DR InParanoid; Q96B97; -.
DR OMA; PNSCHRS; -.
DR OrthoDB; 1577081at2759; -.
DR PhylomeDB; Q96B97; -.
DR TreeFam; TF350191; -.
DR PathwayCommons; Q96B97; -.
DR Reactome; R-HSA-182971; EGFR downregulation.
DR Reactome; R-HSA-6807004; Negative regulation of MET activity.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8866376; Reelin signalling pathway.
DR Reactome; R-HSA-8875360; InlB-mediated entry of Listeria monocytogenes into host cell.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; Q96B97; -.
DR SIGNOR; Q96B97; -.
DR BioGRID-ORCS; 30011; 12 hits in 699 CRISPR screens.
DR ChiTaRS; SH3KBP1; human.
DR EvolutionaryTrace; Q96B97; -.
DR GeneWiki; SH3KBP1; -.
DR GenomeRNAi; 30011; -.
DR Pharos; Q96B97; Tbio.
DR PRO; PR:Q96B97; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q96B97; protein.
DR Bgee; ENSG00000147010; Expressed in secondary oocyte and 188 other tissues.
DR ExpressionAtlas; Q96B97; baseline and differential.
DR Genevisible; Q96B97; HS.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; NAS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0050871; P:positive regulation of B cell activation; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR CDD; cd12052; SH3_CIN85_1; 1.
DR CDD; cd12055; SH3_CIN85_2; 1.
DR CDD; cd12057; SH3_CIN85_3; 1.
DR InterPro; IPR035770; CIN85_SH3_1.
DR InterPro; IPR035771; CIN85_SH3_2.
DR InterPro; IPR035772; CIN85_SH3_3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR028506; Sorbin_SH3.
DR PANTHER; PTHR14167:SF6; PTHR14167:SF6; 2.
DR Pfam; PF14604; SH3_9; 3.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF50044; SSF50044; 3.
DR PROSITE; PS50002; SH3; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cell junction; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endocytosis;
KW Host-virus interaction; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain; SH3-binding; Synapse; Synaptosome; Ubl conjugation.
FT CHAIN 1..665
FT /note="SH3 domain-containing kinase-binding protein 1"
FT /id="PRO_0000097728"
FT DOMAIN 1..58
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 98..157
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 267..328
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 159..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 602..664
FT /evidence="ECO:0000255"
FT COMPBIAS 162..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R550"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R550"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..54
FT /note="MVEAIVEFDYQAQHDDELTISVGEIITNIRKEDGGWWEGQINGRRGLFPDNF
FT VR -> MEVSAAKAPSAADLSEI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12618476,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_007504"
FT VAR_SEQ 1..4
FT /note="MVEA -> MGEE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044655"
FT VAR_SEQ 5..242
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044656"
FT VARIANT 382
FT /note="P -> L (in dbSNP:rs1310665369)"
FT /evidence="ECO:0000269|PubMed:11474197"
FT /id="VAR_015667"
FT CONFLICT 288
FT /note="I -> T (in Ref. 3; BAH11471)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="V -> A (in Ref. 3; BAH11471)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="A -> V (in Ref. 5; AAH15806)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:2BZ8"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2BZ8"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2BZ8"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2BZ8"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:2BZ8"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2BZ8"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2BZ8"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:2O2O"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2O2O"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2O2O"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2O2O"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:2O2O"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:2O2O"
FT STRAND 270..276
FT /evidence="ECO:0007829|PDB:2YDL"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2K6D"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:2YDL"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:2K9G"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:2YDL"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:2YDL"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:2YDL"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:2YDL"
FT HELIX 605..661
FT /evidence="ECO:0007829|PDB:5ABS"
SQ SEQUENCE 665 AA; 73126 MW; 3BD350FCDB14BD4C CRC64;
MVEAIVEFDY QAQHDDELTI SVGEIITNIR KEDGGWWEGQ INGRRGLFPD NFVREIKKEM
KKDPLTNKAP EKPLHEVPSG NSLLSSETIL RTNKRGERRR RRCQVAFSYL PQNDDELELK
VGDIIEVVGE VEEGWWEGVL NGKTGMFPSN FIKELSGESD ELGISQDEQL SKSSLRETTG
SESDGGDSSS TKSEGANGTV ATAAIQPKKV KGVGFGDIFK DKPIKLRPRS IEVENDFLPV
EKTIGKKLPA TTATPDSSKT EMDSRTKSKD YCKVIFPYEA QNDDELTIKE GDIVTLINKD
CIDVGWWEGE LNGRRGVFPD NFVKLLPPDF EKEGNRPKKP PPPSAPVIKQ GAGTTERKHE
IKKIPPERPE MLPNRTEEKE RPEREPKLDL QKPSVPAIPP KKPRPPKTNS LSRPGALPPR
RPERPVGPLT HTRGDSPKID LAGSSLSGIL DKDLSDRSND IDLEGFDSVV SSTEKLSHPT
TSRPKATGRR PPSQSLTSSS LSSPDIFDSP SPEEDKEEHI SLAHRGVDAS KKTSKTVTIS
QVSDNKASLP PKPGTMAAGG GGPAPLSSAA PSPLSSSLGT AGHRANSPSL FGTEGKPKME
PAASSQAAVE ELRTQVRELR SIIETMKDQQ KREIKQLLSE LDEEKKIRLR LQMEVNDIKK
ALQSK
