SRBS1_HUMAN
ID SRBS1_HUMAN Reviewed; 1292 AA.
AC Q9BX66; A0AED4; A6NEK3; A6NID8; A6NJS4; A7MD40; D3DR42; O43857; Q5T923;
AC Q5T924; Q5T927; Q5T928; Q5T929; Q5T930; Q5T931; Q5T932; Q7LBE5; Q8IVK0;
AC Q8IVQ4; Q96KF3; Q96KF4; Q9BX64; Q9BX65; Q9P2Q0; Q9UFT2; Q9UHN7; Q9Y338;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Sorbin and SH3 domain-containing protein 1;
DE AltName: Full=Ponsin;
DE AltName: Full=SH3 domain protein 5;
DE AltName: Full=SH3P12;
DE AltName: Full=c-Cbl-associated protein;
DE Short=CAP;
GN Name=SORBS1 {ECO:0000312|HGNC:HGNC:14565};
GN Synonyms=KIAA0894, KIAA1296, SH3D5;
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] {ECO:0000305, ECO:0000312|EMBL:AAK37563.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY,
RP INTERACTION WITH ABL1 AND INSULIN RECEPTOR, AND VARIANT PRO-61.
RC TISSUE=Liver {ECO:0000312|EMBL:AAD27647.1}, and
RC Skeletal muscle {ECO:0000312|EMBL:AAK37563.1};
RX PubMed=11374898; DOI=10.1006/geno.2001.6541;
RA Lin W.-H., Huang C.-J., Liu M.-W., Chang H.-M., Chen Y.-J., Tai T.-Y.,
RA Chuang L.-M.;
RT "Cloning, mapping, and characterization of the human sorbin and SH3 domain
RT containing 1 (SORBS1) gene: a protein associated with c-Abl during insulin
RT signaling in the hepatoma cell line Hep3B.";
RL Genomics 74:12-20(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAK57480.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), SUBCELLULAR LOCATION, INTERACTION
RP WITH SCA7, AND VARIANT PRO-61.
RC TISSUE=Retina {ECO:0000312|EMBL:AAK57480.1};
RX PubMed=11371513; DOI=10.1093/hmg/10.11.1201;
RA Lebre A.-S., Jamot L., Takahashi J., Spassky N., Leprince C., Ravise N.,
RA Zander C., Fujigasaki H., Kussel-Andermann P., Duyckaerts C., Camonis J.H.,
RA Brice A.;
RT "Ataxin-7 interacts with a Cbl-associated protein that it recruits into
RT neuronal intranuclear inclusions.";
RL Hum. Mol. Genet. 10:1201-1213(2001).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAF22175.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND VARIANTS PRO-61; TRP-74 AND
RP ALA-237.
RC TISSUE=Skeletal muscle {ECO:0000312|EMBL:AAF22175.1};
RX PubMed=11532984; DOI=10.1093/hmg/10.17.1753;
RA Lin W.-H., Chiu K.C., Chang H.-M., Lee K.C., Tai T.-Y., Chuang L.-M.;
RT "Molecular scanning of the human sorbin and SH3-domain-containing-1
RT (SORBS1) gene: positive association of the T228A polymorphism with obesity
RT and type 2 diabetes.";
RL Hum. Mol. Genet. 10:1753-1760(2001).
RN [4] {ECO:0000305, ECO:0000312|EMBL:CAD34588.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), INTERACTION WITH INPPL1, AND
RP VARIANT PRO-61.
RC TISSUE=Brain {ECO:0000312|EMBL:CAD34588.1};
RX PubMed=12504111; DOI=10.1016/s0006-291x(02)02894-2;
RA Vandenbroere I., Paternotte N., Dumont J.E., Erneux C., Pirson I.;
RT "The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-
RT containing inositol polyphosphate 5-phosphatase SHIP2.";
RL Biochem. Biophys. Res. Commun. 300:494-500(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 11), INTERACTION WITH PXN, X-RAY
RP CRYSTALLOGRAPHY (0.83 ANGSTROMS) OF 870-930 IN COMPLEX WITH PXN PEPTIDE,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT PRO-61.
RC TISSUE=Skeletal muscle;
RX PubMed=17462669; DOI=10.1016/j.jmb.2007.03.050;
RA Gehmlich K., Pinotsis N., Hayess K., van der Ven P.F., Milting H.,
RA El Banayosy A., Korfer R., Wilmanns M., Ehler E., Furst D.O.;
RT "Paxillin and ponsin interact in nascent costameres of muscle cells.";
RL J. Mol. Biol. 369:665-682(2007).
RN [6] {ECO:0000305, ECO:0000312|EMBL:BAA92534.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9), AND VARIANT PRO-61.
RC TISSUE=Brain {ECO:0000312|EMBL:BAA92534.1};
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [7] {ECO:0000305, ECO:0000312|EMBL:CAB55947.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10), AND VARIANT PRO-61.
RC TISSUE=Uterus {ECO:0000312|EMBL:CAB55947.1};
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [9]
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 [10] {ECO:0000305, ECO:0000312|EMBL:AAH42612.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9), AND VARIANT
RP PRO-61.
RC TISSUE=Testis {ECO:0000312|EMBL:AAH42612.1};
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 [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 752-888.
RC TISSUE=Placenta;
RA Hachiya T., Kobayasi A., Touji S., Tamai K.;
RT "A Fas-ligand associated factor 2, FLAF2, potentiates Fas-ligand
RT stability.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-89; SER-472; SER-665;
RP THR-862 AND SER-945, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478 AND
RP SER-735 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1213
RP (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346 AND SER-603
RP (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-923 (ISOFORM 5),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-765 (ISOFORM 6),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469 (ISOFORM 7),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730 (ISOFORM 8),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387 AND SER-700 (ISOFORM 9),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS 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).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-350 AND SER-665, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242; SER-259; SER-341;
RP SER-350; SER-556; SER-665; THR-708; THR-862 AND TYR-937, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-114 (ISOFORMS 12 AND 8), PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-105 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-137 AND SER-452 (ISOFORM 6), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-146 (ISOFORM 9), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 870-930.
RX PubMed=17784760; DOI=10.1021/ja073846c;
RA Margiolaki I., Wright J.P., Wilmanns M., Fitch A.N., Pinotsis N.;
RT "Second SH3 domain of ponsin solved from powder diffraction.";
RL J. Am. Chem. Soc. 129:11865-11871(2007).
RN [19]
RP STRUCTURE BY NMR OF 796-926.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of SH3 domains of human Sorbin and SH3 domain-
RT containing protein 1.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [20]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-195.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Plays a role in tyrosine phosphorylation of CBL by linking
CC CBL to the insulin receptor. Required for insulin-stimulated glucose
CC transport. Involved in formation of actin stress fibers and focal
CC adhesions (By similarity). {ECO:0000250|UniProtKB:Q62417}.
CC -!- SUBUNIT: Interacts (via third SH3 domain) with the Ten-1 ICD form of
CC TENM1; the interaction induces the translocation of SORBS1 to the
CC nucleus. Interacts with INSM1 (By similarity). Interacts with the long
CC isoform of AFDN and with VCL. AFDN and VCL bind to SORBS1 in a
CC competitive manner and do not form a ternary complex. Interacts with
CC ABL1, CBL, CBLB and INPPL1/SHIP2 through the third SH3 domain.
CC Interaction with ABL1 occurs only after insulin stimulation while this
CC has no effect on the interaction with INPPL1. Interacts with the
CC insulin receptor but dissociates from it following insulin stimulation.
CC Also interacts with SCA7, PTK2/FAK1 and flotillin. Interacts (via SH3
CC domain 2) with PXN. {ECO:0000250, ECO:0000269|PubMed:11371513,
CC ECO:0000269|PubMed:11374898, ECO:0000269|PubMed:12504111,
CC ECO:0000269|PubMed:17462669}.
CC -!- INTERACTION:
CC Q9BX66; P00519: ABL1; NbExp=2; IntAct=EBI-433642, EBI-375543;
CC Q9BX66; O15265: ATXN7; NbExp=15; IntAct=EBI-433642, EBI-708350;
CC Q9BX66; P42858: HTT; NbExp=4; IntAct=EBI-433642, EBI-466029;
CC Q9BX66; O15357: INPPL1; NbExp=5; IntAct=EBI-433642, EBI-1384248;
CC Q9BX66; Q13177: PAK2; NbExp=2; IntAct=EBI-433642, EBI-1045887;
CC Q9BX66; Q6NSK7: RIN3; NbExp=3; IntAct=EBI-433642, EBI-21369851;
CC Q9BX66; P39052: Dnm2; Xeno; NbExp=5; IntAct=EBI-433642, EBI-349613;
CC Q9BX66; A0A061I5T4: H671_4g13114; Xeno; NbExp=2; IntAct=EBI-433642, EBI-2504267;
CC Q9BX66-7; Q8WWV3: RTN4IP1; NbExp=3; IntAct=EBI-17775963, EBI-743502;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell membrane.
CC Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Nucleus
CC {ECO:0000250}. Nucleus matrix {ECO:0000250}. Note=Colocalizes with the
CC Ten-1 ICD form of TENM1 in the nucleus (By similarity). Colocalizes
CC with actin stress fibers. Also detected at the plasma membrane and in
CC neuronal intranuclear inclusions. Colocalized with PXN at focal
CC adhesions during myogenic differentiation. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=12;
CC Name=1 {ECO:0000269|PubMed:11374898};
CC IsoId=Q9BX66-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11374898};
CC IsoId=Q9BX66-2; Sequence=VSP_050902, VSP_050910;
CC Name=3 {ECO:0000269|PubMed:11374898};
CC IsoId=Q9BX66-3; Sequence=VSP_050898, VSP_050900, VSP_050906,
CC VSP_050912, VSP_050913;
CC Name=4 {ECO:0000269|PubMed:11374898};
CC IsoId=Q9BX66-4; Sequence=VSP_050895, VSP_050896, VSP_050899,
CC VSP_050900, VSP_050903, VSP_050907,
CC VSP_050911;
CC Name=5 {ECO:0000269|PubMed:11532984};
CC IsoId=Q9BX66-5; Sequence=VSP_050896, VSP_050901, VSP_050911;
CC Name=6 {ECO:0000269|PubMed:12504111};
CC IsoId=Q9BX66-6; Sequence=VSP_050896, VSP_050899, VSP_050905,
CC VSP_050911;
CC Name=7 {ECO:0000305};
CC IsoId=Q9BX66-7; Sequence=VSP_050895, VSP_050896, VSP_050900,
CC VSP_050903, VSP_050908, VSP_050909;
CC Name=8 {ECO:0000269|PubMed:11371513};
CC IsoId=Q9BX66-8; Sequence=VSP_050895, VSP_050899, VSP_050900,
CC VSP_050904, VSP_050911;
CC Name=9 {ECO:0000305};
CC IsoId=Q9BX66-9; Sequence=VSP_050899, VSP_050900, VSP_050903,
CC VSP_050911;
CC Name=10 {ECO:0000305};
CC IsoId=Q9BX66-10; Sequence=VSP_050895, VSP_050900, VSP_050903,
CC VSP_050907, VSP_050911;
CC Name=11;
CC IsoId=Q9BX66-11; Sequence=VSP_050900, VSP_039210;
CC Name=12;
CC IsoId=Q9BX66-12; Sequence=VSP_050895, VSP_050899, VSP_041193,
CC VSP_050900, VSP_050904, VSP_041194,
CC VSP_050911;
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle (at protein level).
CC Widely expressed with highest levels in heart and skeletal muscle.
CC {ECO:0000269|PubMed:11374898, ECO:0000269|PubMed:17462669}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 12]: Derived from mouse ortholog data.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB93496.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA92534.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF136380; AAD27647.1; -; mRNA.
DR EMBL; AF356525; AAK37563.1; -; mRNA.
DR EMBL; AF356526; AAK37564.1; -; mRNA.
DR EMBL; AF356527; AAK37565.1; -; mRNA.
DR EMBL; AF330623; AAK57479.1; -; mRNA.
DR EMBL; AF330624; AAK57480.1; -; mRNA.
DR EMBL; AF136381; AAF22175.1; -; mRNA.
DR EMBL; AJ489942; CAD34588.1; -; mRNA.
DR EMBL; AM260536; CAJ97431.1; -; mRNA.
DR EMBL; AB037717; BAA92534.1; ALT_INIT; mRNA.
DR EMBL; AL117472; CAB55947.1; -; mRNA.
DR EMBL; AL158165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49999.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW50007.1; -; Genomic_DNA.
DR EMBL; BC042612; AAH42612.1; -; mRNA.
DR EMBL; BC152463; AAI52464.1; -; mRNA.
DR EMBL; U70668; AAB93496.1; ALT_FRAME; mRNA.
DR CCDS; CCDS31252.1; -. [Q9BX66-4]
DR CCDS; CCDS31253.1; -. [Q9BX66-9]
DR CCDS; CCDS31254.1; -. [Q9BX66-2]
DR CCDS; CCDS31255.1; -. [Q9BX66-1]
DR CCDS; CCDS31256.1; -. [Q9BX66-3]
DR CCDS; CCDS73169.1; -. [Q9BX66-11]
DR CCDS; CCDS7442.1; -. [Q9BX66-10]
DR CCDS; CCDS76326.1; -. [Q9BX66-8]
DR CCDS; CCDS76327.1; -. [Q9BX66-5]
DR PIR; T17257; T17257.
DR RefSeq; NP_001030126.1; NM_001034954.1. [Q9BX66-1]
DR RefSeq; NP_001030127.1; NM_001034955.1. [Q9BX66-2]
DR RefSeq; NP_001030128.1; NM_001034956.1. [Q9BX66-3]
DR RefSeq; NP_001030129.1; NM_001034957.1.
DR RefSeq; NP_001277223.1; NM_001290294.1. [Q9BX66-11]
DR RefSeq; NP_001277224.1; NM_001290295.1.
DR RefSeq; NP_001277225.1; NM_001290296.1. [Q9BX66-5]
DR RefSeq; NP_001277226.1; NM_001290297.1. [Q9BX66-8]
DR RefSeq; NP_001277227.1; NM_001290298.1. [Q9BX66-6]
DR RefSeq; NP_006425.2; NM_006434.2. [Q9BX66-4]
DR RefSeq; NP_056200.1; NM_015385.3. [Q9BX66-10]
DR RefSeq; NP_079267.1; NM_024991.2. [Q9BX66-9]
DR RefSeq; XP_006717652.1; XM_006717589.1. [Q9BX66-5]
DR PDB; 2DL3; NMR; -; A=796-850.
DR PDB; 2ECZ; NMR; -; A=870-926.
DR PDB; 2LJ0; NMR; -; A=1228-1292.
DR PDB; 2LJ1; NMR; -; A=1228-1291.
DR PDB; 2MOX; NMR; -; A=791-930.
DR PDB; 2O2W; X-ray; 2.27 A; A=870-930.
DR PDB; 2O31; X-ray; 1.50 A; A=870-930.
DR PDB; 2O9S; X-ray; 0.83 A; A=870-930.
DR PDB; 2O9V; X-ray; 1.63 A; A=870-930.
DR PDB; 4LN2; X-ray; 1.00 A; A=866-930.
DR PDB; 4LNP; X-ray; 1.41 A; A=794-854.
DR PDBsum; 2DL3; -.
DR PDBsum; 2ECZ; -.
DR PDBsum; 2LJ0; -.
DR PDBsum; 2LJ1; -.
DR PDBsum; 2MOX; -.
DR PDBsum; 2O2W; -.
DR PDBsum; 2O31; -.
DR PDBsum; 2O9S; -.
DR PDBsum; 2O9V; -.
DR PDBsum; 4LN2; -.
DR PDBsum; 4LNP; -.
DR AlphaFoldDB; Q9BX66; -.
DR BMRB; Q9BX66; -.
DR SMR; Q9BX66; -.
DR BioGRID; 115831; 72.
DR CORUM; Q9BX66; -.
DR IntAct; Q9BX66; 47.
DR MINT; Q9BX66; -.
DR STRING; 9606.ENSP00000360293; -.
DR GlyGen; Q9BX66; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q9BX66; -.
DR PhosphoSitePlus; Q9BX66; -.
DR BioMuta; SORBS1; -.
DR DMDM; 317373504; -.
DR EPD; Q9BX66; -.
DR jPOST; Q9BX66; -.
DR MassIVE; Q9BX66; -.
DR MaxQB; Q9BX66; -.
DR PaxDb; Q9BX66; -.
DR PeptideAtlas; Q9BX66; -.
DR PRIDE; Q9BX66; -.
DR ProteomicsDB; 79354; -. [Q9BX66-1]
DR ProteomicsDB; 79355; -. [Q9BX66-10]
DR ProteomicsDB; 79356; -. [Q9BX66-11]
DR ProteomicsDB; 79357; -. [Q9BX66-12]
DR ProteomicsDB; 79358; -. [Q9BX66-2]
DR ProteomicsDB; 79359; -. [Q9BX66-3]
DR ProteomicsDB; 79360; -. [Q9BX66-4]
DR ProteomicsDB; 79361; -. [Q9BX66-5]
DR ProteomicsDB; 79362; -. [Q9BX66-6]
DR ProteomicsDB; 79363; -. [Q9BX66-7]
DR ProteomicsDB; 79364; -. [Q9BX66-8]
DR ProteomicsDB; 79365; -. [Q9BX66-9]
DR ABCD; Q9BX66; 4 sequenced antibodies.
DR Antibodypedia; 30624; 260 antibodies from 31 providers.
DR DNASU; 10580; -.
DR Ensembl; ENST00000277982.9; ENSP00000277982.5; ENSG00000095637.23. [Q9BX66-2]
DR Ensembl; ENST00000306402.10; ENSP00000302556.6; ENSG00000095637.23. [Q9BX66-9]
DR Ensembl; ENST00000354106.7; ENSP00000277984.4; ENSG00000095637.23. [Q9BX66-5]
DR Ensembl; ENST00000361941.7; ENSP00000355136.3; ENSG00000095637.23. [Q9BX66-1]
DR Ensembl; ENST00000371227.8; ENSP00000360271.3; ENSG00000095637.23. [Q9BX66-11]
DR Ensembl; ENST00000371239.5; ENSP00000360283.1; ENSG00000095637.23. [Q9BX66-8]
DR Ensembl; ENST00000371241.5; ENSP00000360285.1; ENSG00000095637.23. [Q9BX66-4]
DR Ensembl; ENST00000371245.7; ENSP00000360291.2; ENSG00000095637.23. [Q9BX66-3]
DR Ensembl; ENST00000371246.6; ENSP00000360292.2; ENSG00000095637.23. [Q9BX66-2]
DR Ensembl; ENST00000371247.7; ENSP00000360293.2; ENSG00000095637.23. [Q9BX66-1]
DR Ensembl; ENST00000371249.6; ENSP00000360295.2; ENSG00000095637.23. [Q9BX66-10]
DR Ensembl; ENST00000607232.5; ENSP00000475901.1; ENSG00000095637.23. [Q9BX66-12]
DR GeneID; 10580; -.
DR KEGG; hsa:10580; -.
DR MANE-Select; ENST00000371247.7; ENSP00000360293.2; NM_001034954.3; NP_001030126.2.
DR UCSC; uc001kko.4; human. [Q9BX66-1]
DR CTD; 10580; -.
DR DisGeNET; 10580; -.
DR GeneCards; SORBS1; -.
DR HGNC; HGNC:14565; SORBS1.
DR HPA; ENSG00000095637; Low tissue specificity.
DR MIM; 605264; gene.
DR neXtProt; NX_Q9BX66; -.
DR OpenTargets; ENSG00000095637; -.
DR PharmGKB; PA37899; -.
DR VEuPathDB; HostDB:ENSG00000095637; -.
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00940000158658; -.
DR HOGENOM; CLU_003951_1_1_1; -.
DR InParanoid; Q9BX66; -.
DR OMA; XTSRRTR; -.
DR OrthoDB; 228183at2759; -.
DR PhylomeDB; Q9BX66; -.
DR TreeFam; TF320680; -.
DR PathwayCommons; Q9BX66; -.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR SignaLink; Q9BX66; -.
DR SIGNOR; Q9BX66; -.
DR BioGRID-ORCS; 10580; 10 hits in 1078 CRISPR screens.
DR ChiTaRS; SORBS1; human.
DR EvolutionaryTrace; Q9BX66; -.
DR GeneWiki; SORBS1; -.
DR GenomeRNAi; 10580; -.
DR Pharos; Q9BX66; Tbio.
DR PRO; PR:Q9BX66; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9BX66; protein.
DR Bgee; ENSG00000095637; Expressed in blood vessel layer and 198 other tissues.
DR ExpressionAtlas; Q9BX66; baseline and differential.
DR Genevisible; Q9BX66; HS.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0030055; C:cell-substrate junction; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
DR GO; GO:0016600; C:flotillin complex; ISS:BHF-UCL.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0005915; C:zonula adherens; TAS:ProtInc.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0008092; F:cytoskeletal protein binding; TAS:ProtInc.
DR GO; GO:0005158; F:insulin receptor binding; IDA:UniProtKB.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IDA:BHF-UCL.
DR GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
DR GO; GO:0031589; P:cell-substrate adhesion; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:BHF-UCL.
DR GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; ISS:UniProtKB.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISS:BHF-UCL.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:BHF-UCL.
DR GO; GO:0043149; P:stress fiber assembly; ISS:UniProtKB.
DR CDD; cd11919; SH3_Sorbs1_1; 1.
DR CDD; cd11922; SH3_Sorbs1_2; 1.
DR CDD; cd11916; SH3_Sorbs1_3; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR003127; SoHo_dom.
DR InterPro; IPR035606; SORBS1_SH3.
DR InterPro; IPR035610; SORBS1_SH3_1.
DR InterPro; IPR035611; SORBS1_SH3_2.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF02208; Sorb; 1.
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; Alternative splicing; Cell junction; Cell membrane;
KW Cytoplasm; Cytoskeleton; Glycoprotein; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Transport.
FT CHAIN 1..1292
FT /note="Sorbin and SH3 domain-containing protein 1"
FT /id="PRO_0000072185"
FT DOMAIN 366..469
FT /note="SoHo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00195"
FT DOMAIN 793..852
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 867..928
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1231..1292
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62417"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 344
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62417"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62417"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62417"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84109"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 536
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q62417"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62417"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62417"
FT MOD_RES 654
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q62417"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 708
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62417"
FT MOD_RES 862
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 937
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 945
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62417"
FT MOD_RES 1240
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q62417"
FT VAR_SEQ 26..57
FT /note="Missing (in isoform 4, isoform 7, isoform 8, isoform
FT 10 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:11371513, ECO:0000303|PubMed:11374898,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_050895"
FT VAR_SEQ 101..109
FT /note="Missing (in isoform 4, isoform 5, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:11374898,
FT ECO:0000303|PubMed:11532984, ECO:0000303|PubMed:12504111,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_050896"
FT VAR_SEQ 147..215
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11374898"
FT /id="VSP_050898"
FT VAR_SEQ 148..270
FT /note="Missing (in isoform 4, isoform 6, isoform 8, isoform
FT 9 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:10718198,
FT ECO:0000303|PubMed:11371513, ECO:0000303|PubMed:11374898,
FT ECO:0000303|PubMed:12504111, ECO:0000303|PubMed:15489334"
FT /id="VSP_050899"
FT VAR_SEQ 319..328
FT /note="Missing (in isoform 12)"
FT /evidence="ECO:0000305"
FT /id="VSP_041193"
FT VAR_SEQ 408..453
FT /note="Missing (in isoform 3, isoform 4, isoform 7, isoform
FT 8, isoform 9, isoform 10, isoform 11 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:10718198,
FT ECO:0000303|PubMed:11230166, ECO:0000303|PubMed:11371513,
FT ECO:0000303|PubMed:11374898, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17462669"
FT /id="VSP_050900"
FT VAR_SEQ 431..451
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11371513,
FT ECO:0000303|PubMed:11374898, ECO:0000303|PubMed:11532984"
FT /id="VSP_050901"
FT VAR_SEQ 434..453
FT /note="DNPYTPTYQFPASTPSPKSE -> TKSCSVMSPRLECSGTVIAHCSLKLLDS
FT SNPPTSASQVAGTA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11374898"
FT /id="VSP_050902"
FT VAR_SEQ 552..635
FT /note="Missing (in isoform 4, isoform 7, isoform 9 and
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:10718198,
FT ECO:0000303|PubMed:11230166, ECO:0000303|PubMed:11374898,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_050903"
FT VAR_SEQ 580..635
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:12504111"
FT /id="VSP_050905"
FT VAR_SEQ 580..601
FT /note="Missing (in isoform 8 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:11371513"
FT /id="VSP_050904"
FT VAR_SEQ 602..635
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11374898"
FT /id="VSP_050906"
FT VAR_SEQ 709
FT /note="K -> KVDRKGGNAHMISSSSVHSRTFNTSNALGPVCKHKKPLSAAKACISE
FT ILPSKFKPRLSAPSALLQEQKSILLPSEKAQSCENLCVSGSLNDSKRGLPLQVGGSIEN
FT LLMRSRRDYDSKSSSTMSLQEYSTSGRRPCPLSRKAGMQFTMLYRDMHQINRSGLFLGS
FT ISSSSSVRDLASHFEKSSLALSRGELGPSQEGSEHIPKHTVSSRITAFEQLIQRSRSMP
FT SLDLSGRLSKSPTPVLSRGSLTSARSAESLLESTKLHPKEMDGMNSSGVYASPTCSNMA
FT HHALSFRGLVPSEPLSTCSDDVDRCSNISTDSREGSGGSVHGDFPKHRLNKCKGTCPAS
FT YTRFTTIRKHEQQQTSRQPEWRLDARGDKSTLLRNIYLMSPLPFRLKKPLHHHPRQPSP
FT GDSSGLLVGQKPDLPSQPHQDQPPSGGKPVVPTRLSSRHTMARLSRSSEPSQERPTALE
FT DYPRAINNGNSVPYSDHSLDRNNNPQSELAPSRG (in isoform 12)"
FT /evidence="ECO:0000305"
FT /id="VSP_041194"
FT VAR_SEQ 738..793
FT /note="Missing (in isoform 4 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:11374898"
FT /id="VSP_050907"
FT VAR_SEQ 795..799
FT /note="MRPAR -> KYDWA (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_050908"
FT VAR_SEQ 800..1292
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_050909"
FT VAR_SEQ 955..1212
FT /note="Missing (in isoform 4, isoform 5, isoform 6, isoform
FT 8, isoform 9, isoform 10 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:10718198,
FT ECO:0000303|PubMed:11230166, ECO:0000303|PubMed:11371513,
FT ECO:0000303|PubMed:11374898, ECO:0000303|PubMed:11532984,
FT ECO:0000303|PubMed:12504111, ECO:0000303|PubMed:15489334"
FT /id="VSP_050911"
FT VAR_SEQ 955..1117
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11374898"
FT /id="VSP_050910"
FT VAR_SEQ 956..975
FT /note="FSSHSKLITPAPSSLPHSRR -> LSHHSLRAGPDLTESEKSYV (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11374898"
FT /id="VSP_050912"
FT VAR_SEQ 976..1213
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11374898"
FT /id="VSP_050913"
FT VAR_SEQ 1213
FT /note="Q -> QLSHHSLRAGPDLTESEKSYV (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:17462669"
FT /id="VSP_039210"
FT VARIANT 61
FT /note="L -> P (in dbSNP:rs943542)"
FT /evidence="ECO:0000269|PubMed:10718198,
FT ECO:0000269|PubMed:11230166, ECO:0000269|PubMed:11371513,
FT ECO:0000269|PubMed:11374898, ECO:0000269|PubMed:11532984,
FT ECO:0000269|PubMed:12504111, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17462669"
FT /id="VAR_047652"
FT VARIANT 74
FT /note="R -> W (in dbSNP:rs757431022)"
FT /evidence="ECO:0000269|PubMed:11532984"
FT /id="VAR_019653"
FT VARIANT 175
FT /note="G -> V (in dbSNP:rs7081076)"
FT /id="VAR_047653"
FT VARIANT 195
FT /note="T -> A (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035661"
FT VARIANT 237
FT /note="T -> A (has a protective role in both obesity and
FT diabetes; dbSNP:rs2281939)"
FT /evidence="ECO:0000269|PubMed:11532984"
FT /id="VAR_019654"
FT VARIANT 485
FT /note="Y -> C (in dbSNP:rs35808802)"
FT /id="VAR_047654"
FT CONFLICT 9
FT /note="S -> P (in Ref. 5; CAJ97431)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="P -> S (in Ref. 1; AAD27647 and 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="D -> G (in Ref. 1; AAD27647 and 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="R -> K (in Ref. 1; AAD27647 and 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="A -> V (in Ref. 1; AAD27647 and 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="Y -> S (in Ref. 1; AAD27647 and 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 226..228
FT /note="RAS -> SAC (in Ref. 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="T -> P (in Ref. 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 292..295
FT /note="PSVS -> SSEC (in Ref. 1; AAD27647 and 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="S -> R (in Ref. 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="E -> V (in Ref. 1; AAD27647 and 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="D -> E (in Ref. 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="L -> F (in Ref. 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="E -> G (in Ref. 1; AAD27647 and 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="R -> S (in Ref. 1; AAD27647 and 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="D -> V (in Ref. 1; AAD27647 and 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="Q -> R (in Ref. 5; CAJ97431)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="G -> D (in Ref. 1; AAD27647 and 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="D -> N (in Ref. 1; AAD27647 and 3; AAF22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 1156
FT /note="V -> G (in Ref. 1; AAK37563/AAK37564)"
FT /evidence="ECO:0000305"
FT STRAND 796..802
FT /evidence="ECO:0007829|PDB:4LNP"
FT STRAND 808..811
FT /evidence="ECO:0007829|PDB:2MOX"
FT STRAND 819..825
FT /evidence="ECO:0007829|PDB:4LNP"
FT STRAND 827..835
FT /evidence="ECO:0007829|PDB:4LNP"
FT STRAND 838..843
FT /evidence="ECO:0007829|PDB:4LNP"
FT HELIX 844..846
FT /evidence="ECO:0007829|PDB:4LNP"
FT STRAND 847..849
FT /evidence="ECO:0007829|PDB:4LNP"
FT STRAND 863..865
FT /evidence="ECO:0007829|PDB:2MOX"
FT STRAND 870..874
FT /evidence="ECO:0007829|PDB:2O9S"
FT STRAND 882..885
FT /evidence="ECO:0007829|PDB:2MOX"
FT STRAND 893..899
FT /evidence="ECO:0007829|PDB:2O9S"
FT STRAND 901..908
FT /evidence="ECO:0007829|PDB:2O9S"
FT TURN 910..912
FT /evidence="ECO:0007829|PDB:2ECZ"
FT STRAND 915..919
FT /evidence="ECO:0007829|PDB:2O9S"
FT HELIX 920..922
FT /evidence="ECO:0007829|PDB:2O9S"
FT STRAND 923..927
FT /evidence="ECO:0007829|PDB:2O9S"
FT STRAND 1230..1233
FT /evidence="ECO:0007829|PDB:2LJ0"
FT STRAND 1235..1240
FT /evidence="ECO:0007829|PDB:2LJ0"
FT STRAND 1257..1263
FT /evidence="ECO:0007829|PDB:2LJ0"
FT STRAND 1267..1273
FT /evidence="ECO:0007829|PDB:2LJ0"
FT TURN 1274..1276
FT /evidence="ECO:0007829|PDB:2LJ0"
FT STRAND 1279..1283
FT /evidence="ECO:0007829|PDB:2LJ0"
FT STRAND 1286..1289
FT /evidence="ECO:0007829|PDB:2LJ0"
FT CONFLICT Q9BX66-2:435
FT /note="K -> E (in Ref. 1; AAK37564)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9BX66-2:452..455
FT /note="AHCS -> SRCG (in Ref. 1; AAK37564)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9BX66-2:463
FT /note="N -> D (in Ref. 1; AAK37564)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9BX66-4:105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q9BX66-4:346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9BX66-4:603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9BX66-5:923
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9BX66-6:137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q9BX66-6:452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q9BX66-6:765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9BX66-7:469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9BX66-8:114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q9BX66-8:730
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9BX66-9:146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q9BX66-9:387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9BX66-9:700
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9BX66-10:478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9BX66-10:735
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9BX66-12:114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q9BX66-12:1213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
SQ SEQUENCE 1292 AA; 142513 MW; 70DA4169B6D82F06 CRC64;
MSSECDGGSK AVMNGLAPGS NGQDKATADP LRARSISAVK IIPVKTVKNA SGLVLPTDMD
LTKICTGKGA VTLRASSSYR ETPSSSPASP QETRQHESKP GLEPEPSSAD EWRLSSSADA
NGNAQPSSLA AKGYRSVHPN LPSDKSQDAT SSSAAQPEVI VVPLYLVNTD RGQEGTARPP
TPLGPLGCVP TIPATASAAS PLTFPTLDDF IPPHLQRWPH HSQPARASGS FAPISQTPPS
FSPPPPLVPP APEDLRRVSE PDLTGAVSST DSSPLLNEVS SSLIGTDSQA FPSVSKPSSA
YPSTTIVNPT IVLLQHNREQ QKRLSSLSDP VSERRVGEQD SAPTQEKPTS PGKAIEKRAK
DDSRRVVKST QDLSDVSMDE VGIPLRNTER SKDWYKTMFK QIHKLNRDTP EENPYFPTYK
FPELPEIQQT SEEDNPYTPT YQFPASTPSP KSEDDDSDLY SPRYSFSEDT KSPLSVPRSK
SEMSYIDGEK VVKRSATLPL PARSSSLKSS SERNDWEPPD KKVDTRKYRA EPKSIYEYQP
GKSSVLTNEK MSRDISPEEI DLKNEPWYKF FSELEFGKPP PKKIWDYTPG DCSILPREDR
KTNLDKDLSL CQTELEADLE KMETLNKAPS ANVPQSSAIS PTPEISSETP GYIYSSNFHA
VKRESDGAPG DLTSLENERQ IYKSVLEGGD IPLQGLSGLK RPSSSASTKD SESPRHFIPA
DYLESTEEFI RRRHDDKEKL LADQRRLKRE QEEADIAARR HTGVIPTHHQ FITNERFGDL
LNIDDTAKRK SGSEMRPARA KFDFKAQTLK ELPLQKGDIV YIYKQIDQNW YEGEHHGRVG
IFPRTYIELL PPAEKAQPKK LTPVQVLEYG EAIAKFNFNG DTQVEMSFRK GERITLLRQV
DENWYEGRIP GTSRQGIFPI TYVDVIKRPL VKNPVDYMDL PFSSSPSRSA TASPQFSSHS
KLITPAPSSL PHSRRALSPE MHAVTSEWIS LTVGVPGRRS LALTPPLPPL PEASIYNTDH
LALSPRASPS LSLSLPHLSW SDRPTPRSVA SPLALPSPHK TYSLAPTSQA SLHMNGDGGV
HTPSSGIHQD SFLQLPLGSS DSVISQLSDA FSSQSKRQPW REESGQYERK AERGAGERGP
GGPKISKKSC LKPSDVVRCL STEQRLSDLN TPEESRPGKP LGSAFPGSEA EQTERHRGGE
QAGRKAARRG GSQQPQAQQR RVTPDRSQTS QDLFSYQALY SYIPQNDDEL ELRDGDIVDV
MEKCDDGWFV GTSRRTKQFG TFPGNYVKPL YL
