VINEX_HUMAN
ID VINEX_HUMAN Reviewed; 671 AA.
AC O60504; Q5BJE4; Q6NX54; Q96FY4; Q9UQE4;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Vinexin;
DE AltName: Full=SH3-containing adapter molecule 1;
DE Short=SCAM-1;
DE AltName: Full=Sorbin and SH3 domain-containing protein 3;
GN Name=SORBS3; Synonyms=SCAM1;
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 BETA), ALTERNATIVE SPLICING,
RP MUTAGENESIS, AND VARIANT THR-556.
RC TISSUE=Placenta;
RX PubMed=9885244; DOI=10.1083/jcb.144.1.59;
RA Kioka N., Sakata S., Kawauchi T., Amachi T., Akiyama S.K., Okazaki K.,
RA Yaen C., Yamada K.M., Aota S.;
RT "Vinexin: a novel vinculin-binding protein with multiple SH3 domains
RT enhances actin cytoskeletal organization.";
RL J. Cell Biol. 144:59-69(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND VARIANT THR-556.
RA Her J.-H., Gorman D., Miyajima A., Bolen J.B.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-556.
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND BETA), AND
RP VARIANT THR-556.
RC TISSUE=PNS, 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 INTERACTION WITH SOS.
RX PubMed=10585480; DOI=10.1074/jbc.274.50.35933;
RA Akamatsu M., Aota S., Suwa A., Ueda K., Amachi T., Yamada K.M.,
RA Akiyama S.K., Kioka N.;
RT "Vinexin forms a signaling complex with Sos and modulates epidermal growth
RT factor-induced c-Jun N-terminal kinase/stress-activated protein kinase
RT activities.";
RL J. Biol. Chem. 274:35933-35937(1999).
RN [7]
RP INTERACTION WITH SAFB2.
RX PubMed=12660241; DOI=10.1074/jbc.m212988200;
RA Townson S.M., Dobrzycka K.M., Lee A.V., Air M., Deng W., Kang K., Jiang S.,
RA Kioka N., Michaelis K., Oesterreich S.;
RT "SAFB2, a new scaffold attachment factor homolog and estrogen receptor
RT corepressor.";
RL J. Biol. Chem. 278:20059-20068(2003).
RN [8]
RP INTERACTION WITH SOCS7.
RX PubMed=15242778; DOI=10.1016/j.yexcr.2004.04.002;
RA Martens N., Wery M., Wang P., Braet F., Gertler A., Hooghe R.,
RA Vandenhaute J., Hooghe-Peters E.L.;
RT "The suppressor of cytokine signaling (SOCS)-7 interacts with the actin
RT cytoskeleton through vinexin.";
RL Exp. Cell Res. 298:239-248(2004).
RN [9]
RP INTERACTION WITH INPPL1.
RX PubMed=16302969; DOI=10.1111/j.1742-4658.2005.04996.x;
RA Paternotte N., Zhang J., Vandenbroere I., Backers K., Blero D., Kioka N.,
RA Vanderwinden J.-M., Pirson I., Erneux C.;
RT "SHIP2 interaction with the cytoskeletal protein Vinexin.";
RL FEBS J. 272:6052-6066(2005).
RN [10]
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP INTERACTION WITH SRCIN1.
RX PubMed=18662323; DOI=10.1111/j.1471-4159.2008.05585.x;
RA Ito H., Atsuzawa K., Sudo K., Di Stefano P., Iwamoto I., Morishita R.,
RA Takei S., Semba R., Defilippi P., Asano T., Usuda N., Nagata K.;
RT "Characterization of a multidomain adaptor protein, p140Cap, as part of a
RT pre-synaptic complex.";
RL J. Neurochem. 107:61-72(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530; SER-551 AND SER-563,
RP VARIANT [LARGE SCALE ANALYSIS] THR-556, AND IDENTIFICATION BY MASS
RP 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 [14]
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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM BETA), PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-6 (ISOFORM BETA), VARIANT [LARGE SCALE
RP ANALYSIS] THR-556, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]
RP (ISOFORM BETA), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530 AND SER-563, VARIANT
RP [LARGE SCALE ANALYSIS] THR-556, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM BETA), PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-395; SER-530; SER-545; SER-551 AND SER-563,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 (ISOFORM BETA), VARIANT
RP [LARGE SCALE ANALYSIS] THR-556, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS] (ISOFORM BETA), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544; SER-545 AND SER-563,
RP VARIANT [LARGE SCALE ANALYSIS] THR-556, AND IDENTIFICATION BY MASS
RP 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM BETA), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM BETA), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM BETA), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM BETA), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348; SER-395; SER-530;
RP SER-544; SER-545 AND SER-563, VARIANT [LARGE SCALE ANALYSIS] THR-556, AND
RP 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348; SER-530; SER-547 AND
RP SER-551, VARIANT [LARGE SCALE ANALYSIS] THR-556, AND IDENTIFICATION BY MASS
RP 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 [23]
RP STRUCTURE BY NMR OF 383-437 AND 615-671.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of SH3 domains of human vinexin.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [24]
RP VARIANT [LARGE SCALE ANALYSIS] THR-556, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [25]
RP VARIANT [LARGE SCALE ANALYSIS] THR-556, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [26]
RP VARIANT [LARGE SCALE ANALYSIS] THR-556, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
CC -!- FUNCTION: Vinexin alpha isoform promotes up-regulation of actin stress
CC fiber formation. Vinexin beta isoform plays a role in cell spreading
CC and enhances the activation of JNK/SAPK in response to EGF stimulation
CC by using its third SH3 domain.
CC -!- SUBUNIT: Interacts with DLG5 through its third SH3 domain (By
CC similarity). Interacts with vinculin by the first two SH3 domains and
CC the proline rich region of vinculin. Binds to SOS (guanine nucleotide
CC exchange factor of RAS and RAC), through its third SH3 domain. The
CC formation of this complex is down-regulated by phosphorylation of SOS.
CC Interacts with INPPL1/SHIP2, SAFB2, SOCS7 and SRCIN1. Interacts with
CC FASLG. Interacts with MAPK1/ERK2 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O60504; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-741237, EBI-11096309;
CC O60504; Q96EY9: ADAT3; NbExp=3; IntAct=EBI-741237, EBI-3922811;
CC O60504; Q53H80: AKIRIN2; NbExp=3; IntAct=EBI-741237, EBI-742928;
CC O60504; P31751: AKT2; NbExp=3; IntAct=EBI-741237, EBI-296058;
CC O60504; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-741237, EBI-11954519;
CC O60504; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-741237, EBI-8643161;
CC O60504; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-741237, EBI-744545;
CC O60504; O43439-4: CBFA2T2; NbExp=3; IntAct=EBI-741237, EBI-11954144;
CC O60504; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-741237, EBI-10171570;
CC O60504; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-741237, EBI-744556;
CC O60504; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-741237, EBI-10961624;
CC O60504; Q16204: CCDC6; NbExp=3; IntAct=EBI-741237, EBI-1045350;
CC O60504; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-741237, EBI-10175300;
CC O60504; P51946: CCNH; NbExp=3; IntAct=EBI-741237, EBI-741406;
CC O60504; Q9UK58: CCNL1; NbExp=3; IntAct=EBI-741237, EBI-2836773;
CC O60504; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-741237, EBI-396137;
CC O60504; P42773: CDKN2C; NbExp=3; IntAct=EBI-741237, EBI-711290;
CC O60504; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-741237, EBI-749051;
CC O60504; Q8IWX8: CHERP; NbExp=3; IntAct=EBI-741237, EBI-2555370;
CC O60504; Q9H9E3: COG4; NbExp=3; IntAct=EBI-741237, EBI-368382;
CC O60504; Q99829: CPNE1; NbExp=3; IntAct=EBI-741237, EBI-1642542;
CC O60504; Q96FN4: CPNE2; NbExp=6; IntAct=EBI-741237, EBI-7097057;
CC O60504; Q86YQ8: CPNE8; NbExp=3; IntAct=EBI-741237, EBI-1642325;
CC O60504; Q9BSW2: CRACR2A; NbExp=3; IntAct=EBI-741237, EBI-739773;
CC O60504; P26196: DDX6; NbExp=3; IntAct=EBI-741237, EBI-351257;
CC O60504; Q14689-6: DIP2A; NbExp=3; IntAct=EBI-741237, EBI-10233719;
CC O60504; Q92997: DVL3; NbExp=3; IntAct=EBI-741237, EBI-739789;
CC O60504; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-741237, EBI-743105;
CC O60504; O15372: EIF3H; NbExp=3; IntAct=EBI-741237, EBI-709735;
CC O60504; Q6IB98: EIF3S3; NbExp=3; IntAct=EBI-741237, EBI-10184995;
CC O60504; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-741237, EBI-744099;
CC O60504; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-741237, EBI-745689;
CC O60504; Q9NYF3: FAM53C; NbExp=3; IntAct=EBI-741237, EBI-1644252;
CC O60504; Q6PCT2-2: FBXL19; NbExp=3; IntAct=EBI-741237, EBI-11959077;
CC O60504; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-741237, EBI-744935;
CC O60504; O95995: GAS8; NbExp=3; IntAct=EBI-741237, EBI-1052570;
CC O60504; P55040: GEM; NbExp=3; IntAct=EBI-741237, EBI-744104;
CC O60504; P23415: GLRA1; NbExp=3; IntAct=EBI-741237, EBI-12020340;
CC O60504; O95872: GPANK1; NbExp=3; IntAct=EBI-741237, EBI-751540;
CC O60504; Q92917: GPKOW; NbExp=3; IntAct=EBI-741237, EBI-746309;
CC O60504; P13807: GYS1; NbExp=3; IntAct=EBI-741237, EBI-740553;
CC O60504; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-741237, EBI-14103818;
CC O60504; O14964: HGS; NbExp=3; IntAct=EBI-741237, EBI-740220;
CC O60504; P52597: HNRNPF; NbExp=3; IntAct=EBI-741237, EBI-352986;
CC O60504; P61978: HNRNPK; NbExp=4; IntAct=EBI-741237, EBI-304185;
CC O60504; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-741237, EBI-7060731;
CC O60504; Q9BUJ2: HNRNPUL1; NbExp=3; IntAct=EBI-741237, EBI-1018153;
CC O60504; Q9NV31: IMP3; NbExp=3; IntAct=EBI-741237, EBI-747481;
CC O60504; Q1MX18: INSC; NbExp=3; IntAct=EBI-741237, EBI-12081118;
CC O60504; Q8NA54: IQUB; NbExp=3; IntAct=EBI-741237, EBI-10220600;
CC O60504; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-741237, EBI-2556193;
CC O60504; Q6ZU52: KIAA0408; NbExp=4; IntAct=EBI-741237, EBI-739493;
CC O60504; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-741237, EBI-14069005;
CC O60504; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-741237, EBI-14086479;
CC O60504; Q13064: MKRN3; NbExp=3; IntAct=EBI-741237, EBI-2340269;
CC O60504; Q15742: NAB2; NbExp=3; IntAct=EBI-741237, EBI-8641936;
CC O60504; Q96HR8: NAF1; NbExp=3; IntAct=EBI-741237, EBI-2515597;
CC O60504; A0A0S2Z4D7: NCK1; NbExp=3; IntAct=EBI-741237, EBI-16429340;
CC O60504; Q9NZQ3: NCKIPSD; NbExp=3; IntAct=EBI-741237, EBI-745080;
CC O60504; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-741237, EBI-11750983;
CC O60504; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-741237, EBI-10271199;
CC O60504; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-741237, EBI-2859639;
CC O60504; Q9UHY1: NRBP1; NbExp=3; IntAct=EBI-741237, EBI-749731;
CC O60504; O43482: OIP5; NbExp=3; IntAct=EBI-741237, EBI-536879;
CC O60504; Q9UJX0: OSGIN1; NbExp=3; IntAct=EBI-741237, EBI-9057006;
CC O60504; Q13177: PAK2; NbExp=6; IntAct=EBI-741237, EBI-1045887;
CC O60504; Q9P286: PAK5; NbExp=3; IntAct=EBI-741237, EBI-741896;
CC O60504; Q8N4B1-4: PHETA1; NbExp=3; IntAct=EBI-741237, EBI-14131832;
CC O60504; O43189: PHF1; NbExp=3; IntAct=EBI-741237, EBI-530034;
CC O60504; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-741237, EBI-14066006;
CC O60504; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-741237, EBI-12014286;
CC O60504; O60568: PLOD3; NbExp=3; IntAct=EBI-741237, EBI-741582;
CC O60504; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-741237, EBI-10171633;
CC O60504; P56282: POLE2; NbExp=3; IntAct=EBI-741237, EBI-713847;
CC O60504; O15160: POLR1C; NbExp=3; IntAct=EBI-741237, EBI-1055079;
CC O60504; O75145: PPFIA3; NbExp=3; IntAct=EBI-741237, EBI-1763225;
CC O60504; Q8IXY8: PPIL6; NbExp=3; IntAct=EBI-741237, EBI-12226639;
CC O60504; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-741237, EBI-2557469;
CC O60504; P47897: QARS1; NbExp=3; IntAct=EBI-741237, EBI-347462;
CC O60504; O75771: RAD51D; NbExp=3; IntAct=EBI-741237, EBI-1055693;
CC O60504; Q13671: RIN1; NbExp=3; IntAct=EBI-741237, EBI-366017;
CC O60504; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-741237, EBI-1378139;
CC O60504; Q9BST9: RTKN; NbExp=3; IntAct=EBI-741237, EBI-446694;
CC O60504; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-741237, EBI-11984663;
CC O60504; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-741237, EBI-3957636;
CC O60504; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-741237, EBI-748391;
CC O60504; Q9C0A6-3: SETD5; NbExp=3; IntAct=EBI-741237, EBI-12233047;
CC O60504; Q9H788: SH2D4A; NbExp=6; IntAct=EBI-741237, EBI-747035;
CC O60504; Q9H788-2: SH2D4A; NbExp=3; IntAct=EBI-741237, EBI-10308083;
CC O60504; O14512: SOCS7; NbExp=3; IntAct=EBI-741237, EBI-1539606;
CC O60504; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-741237, EBI-742688;
CC O60504; Q9H987-2: SYNPO2L; NbExp=3; IntAct=EBI-741237, EBI-12082116;
CC O60504; Q9NU19: TBC1D22B; NbExp=4; IntAct=EBI-741237, EBI-8787464;
CC O60504; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-741237, EBI-11955057;
CC O60504; Q15561: TEAD4; NbExp=3; IntAct=EBI-741237, EBI-747736;
CC O60504; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-741237, EBI-11139477;
CC O60504; Q63HR2: TNS2; NbExp=3; IntAct=EBI-741237, EBI-949753;
CC O60504; P36406: TRIM23; NbExp=6; IntAct=EBI-741237, EBI-740098;
CC O60504; P14373: TRIM27; NbExp=3; IntAct=EBI-741237, EBI-719493;
CC O60504; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-741237, EBI-725997;
CC O60504; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-741237, EBI-744794;
CC O60504; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-741237, EBI-10241197;
CC O60504; P40222: TXLNA; NbExp=3; IntAct=EBI-741237, EBI-359793;
CC O60504; O75604: USP2; NbExp=3; IntAct=EBI-741237, EBI-743272;
CC O60504; Q5ST30: VARS2; NbExp=3; IntAct=EBI-741237, EBI-2116622;
CC O60504; Q5ST30-4: VARS2; NbExp=3; IntAct=EBI-741237, EBI-10244997;
CC O60504; P18206-2: VCL; NbExp=3; IntAct=EBI-741237, EBI-11027067;
CC O60504; Q9H9H4: VPS37B; NbExp=3; IntAct=EBI-741237, EBI-4400866;
CC O60504; A5D8V6: VPS37C; NbExp=6; IntAct=EBI-741237, EBI-2559305;
CC O60504; Q8TF74: WIPF2; NbExp=3; IntAct=EBI-741237, EBI-2850112;
CC O60504; O15156: ZBTB7B; NbExp=3; IntAct=EBI-741237, EBI-740434;
CC O60504; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-741237, EBI-14104088;
CC O60504; Q9NQZ6: ZC4H2; NbExp=3; IntAct=EBI-741237, EBI-747993;
CC O60504; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-741237, EBI-744257;
CC O60504-1; O15357: INPPL1; NbExp=2; IntAct=EBI-1222953, EBI-1384248;
CC O60504-2; P00519: ABL1; NbExp=5; IntAct=EBI-1222956, EBI-375543;
CC O60504-2; P13631: RARG; NbExp=2; IntAct=EBI-1222956, EBI-2568901;
CC O60504-2; Q9BST9: RTKN; NbExp=3; IntAct=EBI-1222956, EBI-446694;
CC O60504-2; Q14151: SAFB2; NbExp=3; IntAct=EBI-1222956, EBI-352869;
CC O60504-2; Q9Y6W5: WASF2; NbExp=3; IntAct=EBI-1222956, EBI-4290615;
CC O60504-2; O00401: WASL; NbExp=3; IntAct=EBI-1222956, EBI-957615;
CC O60504-2; Q9QWI6-2: Srcin1; Xeno; NbExp=4; IntAct=EBI-1222956, EBI-775607;
CC -!- SUBCELLULAR LOCATION: [Isoform Alpha]: Cell junction {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized at cell-
CC extracellular matrix junctions (By similarity). Both isoforms were
CC localized at focal adhesion and cell-cell adhesion sites.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform Beta]: Cell junction {ECO:0000250}.
CC Nucleus. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized at cell-
CC extracellular matrix junctions (By similarity). Both isoforms were
CC localized at focal adhesion and cell-cell adhesion sites, vinexin beta
CC was also found in the nucleus. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=O60504-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=O60504-2; Sequence=VSP_004489;
CC -!- TISSUE SPECIFICITY: Both isoforms are expressed in different tissues
CC like heart, placenta, brain, skeletal muscle and pancreas. Isoform beta
CC is especially found in liver.
CC -!- PTM: Phosphorylated at Ser-530 by MAPK1/ERK2 during cell spreading.
CC {ECO:0000250}.
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DR EMBL; AF064807; AAD32304.1; -; mRNA.
DR EMBL; AF037261; AAC09244.1; -; mRNA.
DR EMBL; AC037459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63675.1; -; Genomic_DNA.
DR EMBL; BC067260; AAH67260.2; -; mRNA.
DR EMBL; BC091514; AAH91514.1; -; mRNA.
DR EMBL; BC010146; AAH10146.1; -; mRNA.
DR CCDS; CCDS47824.1; -. [O60504-2]
DR CCDS; CCDS6031.1; -. [O60504-1]
DR RefSeq; NP_001018003.1; NM_001018003.2. [O60504-2]
DR RefSeq; NP_005766.3; NM_005775.4. [O60504-1]
DR RefSeq; XP_005273428.1; XM_005273371.1. [O60504-2]
DR RefSeq; XP_016868433.1; XM_017012944.1. [O60504-2]
DR RefSeq; XP_016868434.1; XM_017012945.1. [O60504-2]
DR RefSeq; XP_016868435.1; XM_017012946.1. [O60504-2]
DR PDB; 2CT3; NMR; -; A=615-671.
DR PDB; 2DLM; NMR; -; A=383-437.
DR PDB; 2NWM; NMR; -; A=383-438.
DR PDB; 2YUP; NMR; -; A=447-523.
DR PDBsum; 2CT3; -.
DR PDBsum; 2DLM; -.
DR PDBsum; 2NWM; -.
DR PDBsum; 2YUP; -.
DR AlphaFoldDB; O60504; -.
DR SMR; O60504; -.
DR BioGRID; 115475; 179.
DR CORUM; O60504; -.
DR IntAct; O60504; 158.
DR MINT; O60504; -.
DR STRING; 9606.ENSP00000240123; -.
DR GlyGen; O60504; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60504; -.
DR MetOSite; O60504; -.
DR PhosphoSitePlus; O60504; -.
DR BioMuta; SORBS3; -.
DR EPD; O60504; -.
DR jPOST; O60504; -.
DR MassIVE; O60504; -.
DR MaxQB; O60504; -.
DR PaxDb; O60504; -.
DR PeptideAtlas; O60504; -.
DR PRIDE; O60504; -.
DR ProteomicsDB; 49442; -. [O60504-1]
DR ProteomicsDB; 49443; -. [O60504-2]
DR Antibodypedia; 2849; 87 antibodies from 18 providers.
DR DNASU; 10174; -.
DR Ensembl; ENST00000240123.12; ENSP00000240123.7; ENSG00000120896.14. [O60504-1]
DR Ensembl; ENST00000523965.5; ENSP00000429764.2; ENSG00000120896.14. [O60504-2]
DR GeneID; 10174; -.
DR KEGG; hsa:10174; -.
DR MANE-Select; ENST00000240123.12; ENSP00000240123.7; NM_005775.5; NP_005766.3.
DR UCSC; uc003xbv.4; human. [O60504-1]
DR CTD; 10174; -.
DR DisGeNET; 10174; -.
DR GeneCards; SORBS3; -.
DR HGNC; HGNC:30907; SORBS3.
DR HPA; ENSG00000120896; Low tissue specificity.
DR MIM; 610795; gene.
DR neXtProt; NX_O60504; -.
DR OpenTargets; ENSG00000120896; -.
DR PharmGKB; PA128394570; -.
DR VEuPathDB; HostDB:ENSG00000120896; -.
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00940000160558; -.
DR HOGENOM; CLU_026296_0_0_1; -.
DR InParanoid; O60504; -.
DR OMA; QVHREPR; -.
DR OrthoDB; 228183at2759; -.
DR PhylomeDB; O60504; -.
DR TreeFam; TF320680; -.
DR PathwayCommons; O60504; -.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR SignaLink; O60504; -.
DR SIGNOR; O60504; -.
DR BioGRID-ORCS; 10174; 12 hits in 1083 CRISPR screens.
DR ChiTaRS; SORBS3; human.
DR EvolutionaryTrace; O60504; -.
DR GeneWiki; SORBS3; -.
DR GenomeRNAi; 10174; -.
DR Pharos; O60504; Tbio.
DR PRO; PR:O60504; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O60504; protein.
DR Bgee; ENSG00000120896; Expressed in right testis and 197 other tissues.
DR ExpressionAtlas; O60504; baseline and differential.
DR Genevisible; O60504; HS.
DR GO; GO:0030055; C:cell-substrate junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0017166; F:vinculin binding; IPI:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0031589; P:cell-substrate adhesion; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB.
DR CDD; cd11921; SH3_Vinexin_1; 1.
DR CDD; cd11924; SH3_Vinexin_2; 1.
DR CDD; cd11918; SH3_Vinexin_3; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR003127; SoHo_dom.
DR InterPro; IPR028510; Vinexin.
DR InterPro; IPR035609; Vinexin_SH3_1.
DR InterPro; IPR035608; Vinexin_SH3_2.
DR InterPro; IPR035607; Vinexin_SH3_3.
DR PANTHER; PTHR14167:SF54; PTHR14167:SF54; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF14604; SH3_9; 2.
DR Pfam; PF02208; Sorb; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 3.
DR SMART; SM00459; Sorb; 1.
DR SUPFAM; SSF50044; SSF50044; 3.
DR PROSITE; PS50002; SH3; 3.
DR PROSITE; PS50831; SOHO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell adhesion;
KW Cell junction; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..671
FT /note="Vinexin"
FT /id="PRO_0000065830"
FT DOMAIN 115..187
FT /note="SoHo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00195"
FT DOMAIN 380..439
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 454..515
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 612..671
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 46..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..515
FT /note="Binds to vinculin"
FT REGION 519..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..671
FT /note="Binds to SOS"
FT COMPBIAS 84..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 530
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..342
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9885244"
FT /id="VSP_004489"
FT VARIANT 255
FT /note="P -> L (in dbSNP:rs3758036)"
FT /id="VAR_057019"
FT VARIANT 556
FT /note="I -> T (in dbSNP:rs2449331)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16421571, ECO:0000269|PubMed:9885244,
FT ECO:0000269|Ref.2, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT /id="VAR_055019"
FT VARIANT 573
FT /note="T -> A (in dbSNP:rs1047030)"
FT /id="VAR_055020"
FT MUTAGEN 649
FT /note="W->F: Loss of SOS-binding ability."
FT /evidence="ECO:0000269|PubMed:9885244"
FT MUTAGEN 667
FT /note="Y->V: Loss of SOS-binding ability."
FT /evidence="ECO:0000269|PubMed:9885244"
FT CONFLICT 583
FT /note="L -> F (in Ref. 1; AAD32304)"
FT /evidence="ECO:0000305"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:2DLM"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:2DLM"
FT STRAND 406..414
FT /evidence="ECO:0007829|PDB:2DLM"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:2DLM"
FT STRAND 425..435
FT /evidence="ECO:0007829|PDB:2DLM"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:2YUP"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:2YUP"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:2YUP"
FT STRAND 480..485
FT /evidence="ECO:0007829|PDB:2YUP"
FT STRAND 489..495
FT /evidence="ECO:0007829|PDB:2YUP"
FT TURN 497..499
FT /evidence="ECO:0007829|PDB:2YUP"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:2YUP"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:2YUP"
FT STRAND 510..514
FT /evidence="ECO:0007829|PDB:2YUP"
FT STRAND 615..621
FT /evidence="ECO:0007829|PDB:2CT3"
FT STRAND 637..644
FT /evidence="ECO:0007829|PDB:2CT3"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:2CT3"
FT STRAND 650..657
FT /evidence="ECO:0007829|PDB:2CT3"
FT STRAND 660..663
FT /evidence="ECO:0007829|PDB:2CT3"
FT TURN 665..667
FT /evidence="ECO:0007829|PDB:2CT3"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:2CT3"
FT INIT_MET O60504-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES O60504-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES O60504-2:6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231"
SQ 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
