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Vinexin (SH3-containing adapter molecule 1) (SCAM-1) (Sorbin and SH3 domain-containing protein 3)

 VINEX_HUMAN             Reviewed;         671 AA.
O60504; Q5BJE4; Q6NX54; Q96FY4; Q9UQE4;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
22-NOV-2017, entry version 179.
RecName: Full=Vinexin;
AltName: Full=SH3-containing adapter molecule 1;
Short=SCAM-1;
AltName: Full=Sorbin and SH3 domain-containing protein 3;
Name=SORBS3; Synonyms=SCAM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA), ALTERNATIVE SPLICING,
MUTAGENESIS, AND VARIANT THR-556.
TISSUE=Placenta;
PubMed=9885244; DOI=10.1083/jcb.144.1.59;
Kioka N., Sakata S., Kawauchi T., Amachi T., Akiyama S.K., Okazaki K.,
Yaen C., Yamada K.M., Aota S.;
"Vinexin: a novel vinculin-binding protein with multiple SH3 domains
enhances actin cytoskeletal organization.";
J. Cell Biol. 144:59-69(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND VARIANT THR-556.
Her J.-H., Gorman D., Miyajima A., Bolen J.B.;
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-556.
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND BETA), AND
VARIANT THR-556.
TISSUE=PNS, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH SOS.
PubMed=10585480; DOI=10.1074/jbc.274.50.35933;
Akamatsu M., Aota S., Suwa A., Ueda K., Amachi T., Yamada K.M.,
Akiyama S.K., Kioka N.;
"Vinexin forms a signaling complex with Sos and modulates epidermal
growth factor-induced c-Jun N-terminal kinase/stress-activated protein
kinase activities.";
J. Biol. Chem. 274:35933-35937(1999).
[7]
INTERACTION WITH SAFB2.
PubMed=12660241; DOI=10.1074/jbc.M212988200;
Townson S.M., Dobrzycka K.M., Lee A.V., Air M., Deng W., Kang K.,
Jiang S., Kioka N., Michaelis K., Oesterreich S.;
"SAFB2, a new scaffold attachment factor homolog and estrogen receptor
corepressor.";
J. Biol. Chem. 278:20059-20068(2003).
[8]
INTERACTION WITH SOCS7.
PubMed=15242778; DOI=10.1016/j.yexcr.2004.04.002;
Martens N., Wery M., Wang P., Braet F., Gertler A., Hooghe R.,
Vandenhaute J., Hooghe-Peters E.L.;
"The suppressor of cytokine signaling (SOCS)-7 interacts with the
actin cytoskeleton through vinexin.";
Exp. Cell Res. 298:239-248(2004).
[9]
INTERACTION WITH INPPL1.
PubMed=16302969; DOI=10.1111/j.1742-4658.2005.04996.x;
Paternotte N., Zhang J., Vandenbroere I., Backers K., Blero D.,
Kioka N., Vanderwinden J.-M., Pirson I., Erneux C.;
"SHIP2 interaction with the cytoskeletal protein Vinexin.";
FEBS J. 272:6052-6066(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[12]
INTERACTION WITH SRCIN1.
PubMed=18662323; DOI=10.1111/j.1471-4159.2008.05585.x;
Ito H., Atsuzawa K., Sudo K., Di Stefano P., Iwamoto I., Morishita R.,
Takei S., Semba R., Defilippi P., Asano T., Usuda N., Nagata K.;
"Characterization of a multidomain adaptor protein, p140Cap, as part
of a pre-synaptic complex.";
J. Neurochem. 107:61-72(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530; SER-551 AND
SER-563, VARIANT [LARGE SCALE ANALYSIS] THR-556, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM BETA),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 (ISOFORM BETA),
VARIANT [LARGE SCALE ANALYSIS] THR-556, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM BETA), AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530 AND SER-563, VARIANT
[LARGE SCALE ANALYSIS] THR-556, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM BETA),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; SER-530; SER-545;
SER-551 AND SER-563, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6
(ISOFORM BETA), VARIANT [LARGE SCALE ANALYSIS] THR-556, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM BETA), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544; SER-545 AND
SER-563, VARIANT [LARGE SCALE ANALYSIS] THR-556, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM BETA), CLEAVAGE
OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM BETA), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM BETA), CLEAVAGE
OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM BETA), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348; SER-395; SER-530;
SER-544; SER-545 AND SER-563, VARIANT [LARGE SCALE ANALYSIS] THR-556,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348; SER-530; SER-547
AND SER-551, VARIANT [LARGE SCALE ANALYSIS] THR-556, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
STRUCTURE BY NMR OF 383-437 AND 615-671.
RIKEN structural genomics initiative (RSGI);
"Solution structure of SH3 domains of human vinexin.";
Submitted (OCT-2006) to the PDB data bank.
[24]
VARIANT [LARGE SCALE ANALYSIS] THR-556, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[25]
VARIANT [LARGE SCALE ANALYSIS] THR-556, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[26]
VARIANT [LARGE SCALE ANALYSIS] THR-556, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
-!- FUNCTION: Vinexin alpha isoform promotes up-regulation of actin
stress fiber formation. Vinexin beta isoform plays a role in cell
spreading and enhances the activation of JNK/SAPK in response to
EGF stimulation by using its third SH3 domain.
-!- SUBUNIT: Interacts with DLG5 through its third SH3 domain (By
similarity). Interacts with vinculin by the first two SH3 domains
and the proline rich region of vinculin. Binds to SOS (guanine
nucleotide exchange factor of RAS and RAC), through its third SH3
domain. The formation of this complex is down-regulated by
phosphorylation of SOS. Interacts with INPPL1/SHIP2, SAFB2, SOCS7
and SRCIN1. Interacts with FASLG. Interacts with MAPK1/ERK2 (By
similarity). {ECO:0000250}.
-!- INTERACTION:
P00519:ABL1; NbExp=5; IntAct=EBI-1222956, EBI-375543;
P31751:AKT2; NbExp=4; IntAct=EBI-741237, EBI-296058;
Q8NEC5:CATSPER1; NbExp=4; IntAct=EBI-741237, EBI-744545;
Q96FN4:CPNE2; NbExp=5; IntAct=EBI-741237, EBI-7097057;
Q14689-6:DIP2A; NbExp=3; IntAct=EBI-741237, EBI-10233719;
Q6IB98:EIF3S3; NbExp=3; IntAct=EBI-741237, EBI-10184995;
Q8N4B1-4:FAM109A; NbExp=4; IntAct=EBI-741237, EBI-14131832;
Q7L5A3:FAM214B; NbExp=4; IntAct=EBI-741237, EBI-745689;
P52597:HNRNPF; NbExp=4; IntAct=EBI-741237, EBI-352986;
P61978:HNRNPK; NbExp=4; IntAct=EBI-741237, EBI-304185;
Q9BUJ2:HNRNPUL1; NbExp=3; IntAct=EBI-741237, EBI-1018153;
O15357:INPPL1; NbExp=2; IntAct=EBI-1222953, EBI-1384248;
Q6ZU52:KIAA0408; NbExp=4; IntAct=EBI-741237, EBI-739493;
Q9NZQ3:NCKIPSD; NbExp=3; IntAct=EBI-741237, EBI-745080;
Q13177:PAK2; NbExp=6; IntAct=EBI-741237, EBI-1045887;
Q9P286:PAK5; NbExp=3; IntAct=EBI-741237, EBI-741896;
P13631:RARG; NbExp=2; IntAct=EBI-1222956, EBI-2568901;
Q9BST9:RTKN; NbExp=3; IntAct=EBI-1222956, EBI-446694;
Q14151:SAFB2; NbExp=3; IntAct=EBI-1222956, EBI-352869;
Q8IYX7:SAXO1; NbExp=3; IntAct=EBI-741237, EBI-3957636;
Q9H788:SH2D4A; NbExp=5; IntAct=EBI-741237, EBI-747035;
Q9H788-2:SH2D4A; NbExp=3; IntAct=EBI-741237, EBI-10308083;
Q9QWI6-2:Srcin1 (xeno); NbExp=4; IntAct=EBI-1222956, EBI-775607;
Q9NU19:TBC1D22B; NbExp=3; IntAct=EBI-741237, EBI-8787464;
P36406:TRIM23; NbExp=5; IntAct=EBI-741237, EBI-740098;
P14373:TRIM27; NbExp=3; IntAct=EBI-741237, EBI-719493;
Q8WV44:TRIM41; NbExp=3; IntAct=EBI-741237, EBI-725997;
Q3SY00:TSGA10IP; NbExp=4; IntAct=EBI-741237, EBI-10241197;
Q5ST30-4:VARS2; NbExp=3; IntAct=EBI-741237, EBI-10244997;
Q9H9H4:VPS37B; NbExp=3; IntAct=EBI-741237, EBI-4400866;
A5D8V6:VPS37C; NbExp=5; IntAct=EBI-741237, EBI-2559305;
Q9Y6W5:WASF2; NbExp=3; IntAct=EBI-1222956, EBI-4290615;
O00401:WASL; NbExp=3; IntAct=EBI-1222956, EBI-957615;
Q8TF74:WIPF2; NbExp=4; IntAct=EBI-741237, EBI-2850112;
O15156:ZBTB7B; NbExp=3; IntAct=EBI-741237, EBI-740434;
Q9NQZ6:ZC4H2; NbExp=3; IntAct=EBI-741237, EBI-747993;
-!- SUBCELLULAR LOCATION: Isoform Alpha: Cell junction {ECO:0000250}.
Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized at cell-
extracellular matrix junctions (By similarity). Both isoforms were
localized at focal adhesion and cell-cell adhesion sites.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform Beta: Cell junction {ECO:0000250}.
Nucleus. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized at
cell-extracellular matrix junctions (By similarity). Both isoforms
were localized at focal adhesion and cell-cell adhesion sites,
vinexin beta was also found in the nucleus. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha;
IsoId=O60504-1; Sequence=Displayed;
Name=Beta;
IsoId=O60504-2; Sequence=VSP_004489;
Note=Contains a phosphoserine at position 6. Initiator Met-1 is
removed. Contains a N-acetylalanine at position 2.
{ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22223895, ECO:0000244|PubMed:22814378};
-!- TISSUE SPECIFICITY: Both isoforms are expressed in different
tissues like heart, placenta, brain, skeletal muscle and pancreas.
Isoform beta is especially found in liver.
-!- PTM: Phosphorylated at Ser-530 by MAPK1/ERK2 during cell
spreading. {ECO:0000250}.
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EMBL; AF064807; AAD32304.1; -; mRNA.
EMBL; AF037261; AAC09244.1; -; mRNA.
EMBL; AC037459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471080; EAW63675.1; -; Genomic_DNA.
EMBL; BC067260; AAH67260.2; -; mRNA.
EMBL; BC091514; AAH91514.1; -; mRNA.
EMBL; BC010146; AAH10146.1; -; mRNA.
CCDS; CCDS47824.1; -. [O60504-2]
CCDS; CCDS6031.1; -. [O60504-1]
RefSeq; NP_001018003.1; NM_001018003.2. [O60504-2]
RefSeq; NP_005766.3; NM_005775.4. [O60504-1]
RefSeq; XP_005273428.1; XM_005273371.1. [O60504-2]
RefSeq; XP_016868433.1; XM_017012944.1. [O60504-2]
RefSeq; XP_016868434.1; XM_017012945.1. [O60504-2]
RefSeq; XP_016868435.1; XM_017012946.1. [O60504-2]
UniGene; Hs.528572; -.
PDB; 2CT3; NMR; -; A=615-671.
PDB; 2DLM; NMR; -; A=383-437.
PDB; 2NWM; NMR; -; A=383-438.
PDB; 2YUP; NMR; -; A=447-523.
PDBsum; 2CT3; -.
PDBsum; 2DLM; -.
PDBsum; 2NWM; -.
PDBsum; 2YUP; -.
ProteinModelPortal; O60504; -.
SMR; O60504; -.
BioGrid; 115475; 65.
CORUM; O60504; -.
IntAct; O60504; 148.
MINT; MINT-262486; -.
STRING; 9606.ENSP00000240123; -.
iPTMnet; O60504; -.
PhosphoSitePlus; O60504; -.
BioMuta; SORBS3; -.
EPD; O60504; -.
MaxQB; O60504; -.
PaxDb; O60504; -.
PeptideAtlas; O60504; -.
PRIDE; O60504; -.
Ensembl; ENST00000240123; ENSP00000240123; ENSG00000120896. [O60504-1]
Ensembl; ENST00000523965; ENSP00000429764; ENSG00000120896. [O60504-2]
GeneID; 10174; -.
KEGG; hsa:10174; -.
UCSC; uc003xbv.4; human. [O60504-1]
CTD; 10174; -.
DisGeNET; 10174; -.
EuPathDB; HostDB:ENSG00000120896.13; -.
GeneCards; SORBS3; -.
H-InvDB; HIX0201306; -.
HGNC; HGNC:30907; SORBS3.
HPA; HPA015849; -.
HPA; HPA048034; -.
MIM; 610795; gene.
neXtProt; NX_O60504; -.
OpenTargets; ENSG00000120896; -.
PharmGKB; PA128394570; -.
eggNOG; ENOG410IPNP; Eukaryota.
eggNOG; ENOG410XP8Q; LUCA.
GeneTree; ENSGT00760000119190; -.
HOGENOM; HOG000294090; -.
HOVERGEN; HBG054842; -.
InParanoid; O60504; -.
OMA; NTLNFQF; -.
OrthoDB; EOG091G039F; -.
PhylomeDB; O60504; -.
TreeFam; TF320680; -.
Reactome; R-HSA-445355; Smooth Muscle Contraction.
SignaLink; O60504; -.
SIGNOR; O60504; -.
ChiTaRS; SORBS3; human.
EvolutionaryTrace; O60504; -.
GeneWiki; SORBS3; -.
GenomeRNAi; 10174; -.
PRO; PR:O60504; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000120896; -.
CleanEx; HS_SORBS3; -.
ExpressionAtlas; O60504; baseline and differential.
Genevisible; O60504; HS.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0017166; F:vinculin binding; IPI:UniProtKB.
GO; GO:0007015; P:actin filament organization; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
GO; GO:0006936; P:muscle contraction; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0051495; P:positive regulation of cytoskeleton organization; NAS:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB.
CDD; cd11921; SH3_Vinexin_1; 1.
CDD; cd11924; SH3_Vinexin_2; 1.
CDD; cd11918; SH3_Vinexin_3; 1.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR003127; SoHo_dom.
InterPro; IPR028510; Vinexin.
InterPro; IPR035609; Vinexin_SH3_1.
InterPro; IPR035608; Vinexin_SH3_2.
InterPro; IPR035607; Vinexin_SH3_3.
PANTHER; PTHR44972; PTHR44972; 1.
Pfam; PF00018; SH3_1; 1.
Pfam; PF14604; SH3_9; 2.
Pfam; PF02208; Sorb; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 3.
SMART; SM00459; Sorb; 1.
SUPFAM; SSF50044; SSF50044; 3.
PROSITE; PS50002; SH3; 3.
PROSITE; PS50831; SOHO; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell adhesion;
Cell junction; Complete proteome; Cytoplasm; Cytoskeleton; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain.
CHAIN 1 671 Vinexin.
/FTId=PRO_0000065830.
DOMAIN 115 187 SoHo. {ECO:0000255|PROSITE-
ProRule:PRU00195}.
DOMAIN 380 439 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 454 515 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 612 671 SH3 3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 380 515 Binds to vinculin.
REGION 612 671 Binds to SOS.
MOD_RES 348 348 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 530 530 Phosphoserine; by MAPK1.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 544 544 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 545 545 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 547 547 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 551 551 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 563 563 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 342 Missing (in isoform Beta).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9885244}.
/FTId=VSP_004489.
VARIANT 255 255 P -> L (in dbSNP:rs3758036).
/FTId=VAR_057019.
VARIANT 556 556 I -> T (in dbSNP:rs2449331).
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16421571,
ECO:0000269|PubMed:9885244,
ECO:0000269|Ref.2}.
/FTId=VAR_055019.
VARIANT 573 573 T -> A (in dbSNP:rs1047030).
/FTId=VAR_055020.
MUTAGEN 649 649 W->F: Loss of SOS-binding ability.
{ECO:0000269|PubMed:9885244}.
MUTAGEN 667 667 Y->V: Loss of SOS-binding ability.
{ECO:0000269|PubMed:9885244}.
CONFLICT 583 583 L -> F (in Ref. 1; AAD32304).
{ECO:0000305}.
STRAND 385 389 {ECO:0000244|PDB:2DLM}.
STRAND 395 398 {ECO:0000244|PDB:2DLM}.
STRAND 406 414 {ECO:0000244|PDB:2DLM}.
STRAND 417 422 {ECO:0000244|PDB:2DLM}.
STRAND 425 435 {ECO:0000244|PDB:2DLM}.
HELIX 453 455 {ECO:0000244|PDB:2YUP}.
STRAND 456 461 {ECO:0000244|PDB:2YUP}.
STRAND 469 472 {ECO:0000244|PDB:2YUP}.
STRAND 480 485 {ECO:0000244|PDB:2YUP}.
STRAND 489 495 {ECO:0000244|PDB:2YUP}.
TURN 497 499 {ECO:0000244|PDB:2YUP}.
STRAND 502 506 {ECO:0000244|PDB:2YUP}.
HELIX 507 509 {ECO:0000244|PDB:2YUP}.
STRAND 510 514 {ECO:0000244|PDB:2YUP}.
STRAND 615 621 {ECO:0000244|PDB:2CT3}.
STRAND 637 644 {ECO:0000244|PDB:2CT3}.
STRAND 646 648 {ECO:0000244|PDB:2CT3}.
STRAND 650 657 {ECO:0000244|PDB:2CT3}.
STRAND 660 663 {ECO:0000244|PDB:2CT3}.
TURN 665 667 {ECO:0000244|PDB:2CT3}.
STRAND 668 670 {ECO:0000244|PDB:2CT3}.
SEQUENCE 671 AA; 75341 MW; 2D8A8718E0367BE9 CRC64;
MQGPPRSLRA GLSLDDFIPG HLQSHIGSSS RGTRVPVIRN GGSNTLNFQF HDPAPRTVCN
GGYTPRRDAS QHPDPAWYQT WPGPGSKPSA STKIPASQHT QNWSATWTKD SKRRDKRWVK
YEGIGPVDES GMPIAPRSSV DRPRDWYRRM FQQIHRKMPD LQLDWTFEEP PRDPRHLGAQ
QRPAHRPGPA TSSSGRSWDH SEELPRSTFN YRPGAFSTVL QPSNQVLRRR EKVDNVWTEE
SWNQFLQELE TGQRPKKPLV DDPGEKPSQP IEVLLERELA ELSAELDKDL RAIETRLPSP
KSSPAPRRAP EQRPPAGPAS AWSSSYPHAP YLGSARSLSP HKMADGGSPF LGRRDFVYPS
STRDPSASNG GGSPARREEK KRKAARLKFD FQAQSPKELT LQKGDIVYIH KEVDKNWLEG
EHHGRLGIFP ANYVEVLPAD EIPKPIKPPT YQVLEYGEAV AQYTFKGDLE VELSFRKGEH
ICLIRKVNEN WYEGRITGTG RQGIFPASYV QVSREPRLRL CDDGPQLPTS PRLTAAARSA
RHPSSPSALR SPADPIDLGG QTSPRRTGFS FPTQEPRPQT QNLGTPGPAL SHSRGPSHPL
DLGTSSPNTS QIHWTPYRAM YQYRPQNEDE LELREGDRVD VMQQCDDGWF VGVSRRTQKF
GTFPGNYVAP V


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