SRBS1_MOUSE
ID SRBS1_MOUSE Reviewed; 1290 AA.
AC Q62417; Q80TF8; Q8BZI3; Q8K3Y2; Q921F8; Q9Z0Z8; Q9Z0Z9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 179.
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|MGI:MGI:700014};
GN Synonyms=Kiaa1296 {ECO:0000312|EMBL:BAC65769.2},
GN Sh3d5 {ECO:0000303|PubMed:9630982};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC TISSUE=Embryo {ECO:0000269|PubMed:9630982};
RX PubMed=9630982; DOI=10.1038/nbt0696-741;
RA Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT "Cloning of ligand targets: systematic isolation of SH3 domain-containing
RT proteins.";
RL Nat. Biotechnol. 14:741-744(1996).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH CBL AND INSULIN RECEPTOR.
RX PubMed=9447983; DOI=10.1128/mcb.18.2.872;
RA Ribon V., Printen J.A., Hoffman N.G., Kay B.K., Saltiel A.R.;
RT "A novel, multifunctional c-Cbl binding protein in insulin receptor
RT signaling in 3T3-L1 adipocytes.";
RL Mol. Cell. Biol. 18:872-879(1998).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAD16008.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH AFDN AND VCL.
RC TISSUE=Brain {ECO:0000269|PubMed:10085297};
RX PubMed=10085297; DOI=10.1083/jcb.144.5.1001;
RA Mandai K., Nakanishi H., Satoh A., Takahashi K., Satoh K., Nishioka H.,
RA Mizoguchi A., Takai Y.;
RT "Ponsin/SH3P12: an l-afadin- and vinculin-binding protein localized at
RT cell-cell and cell-matrix adherens junctions.";
RL J. Cell Biol. 144:1001-1017(1999).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=15047181; DOI=10.1016/j.bbrc.2004.03.038;
RA Alcazar O., Ho R.C., Fujii N., Goodyear L.J.;
RT "cDNA cloning and functional characterization of a novel splice variant of
RT c-Cbl-associated protein from mouse skeletal muscle.";
RL Biochem. Biophys. Res. Commun. 317:285-293(2004).
RN [5] {ECO:0000305, ECO:0000312|EMBL:BAC65769.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [6]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [8] {ECO:0000305, ECO:0000312|EMBL:AAH12703.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH12703.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH12703.1};
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 [9] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PTK2/FAK1.
RX PubMed=9461600; DOI=10.1074/jbc.273.7.4073;
RA Ribon V., Herrera R., Kay B.K., Saltiel A.R.;
RT "A role for CAP, a novel, multifunctional Src homology 3 domain-containing
RT protein in formation of actin stress fibers and focal adhesions.";
RL J. Biol. Chem. 273:4073-4080(1998).
RN [10] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FLOTILLIN.
RX PubMed=11001060; DOI=10.1038/35025089;
RA Baumann C.A., Ribon V., Kanzaki M., Thurmond D.C., Mora S., Shigematsu S.,
RA Bickel P.E., Pessin J.E., Saltiel A.R.;
RT "CAP defines a second signalling pathway required for insulin-stimulated
RT glucose transport.";
RL Nature 407:202-207(2000).
RN [11]
RP INTERACTION WITH INSM1.
RX PubMed=12079283; DOI=10.1006/geno.2002.6800;
RA Xie J., Cai T., Zhang H., Lan M.S., Notkins A.L.;
RT "The zinc-finger transcription factor INSM1 is expressed during embryo
RT development and interacts with the Cbl-associated protein.";
RL Genomics 80:54-61(2002).
RN [12]
RP INTERACTION WITH CBLB.
RX PubMed=12842890; DOI=10.1074/jbc.m300664200;
RA Liu J., DeYoung S.M., Hwang J.B., O'Leary E.E., Saltiel A.R.;
RT "The roles of Cbl-b and c-Cbl in insulin-stimulated glucose transport.";
RL J. Biol. Chem. 278:36754-36762(2003).
RN [13]
RP INTERACTION WITH TENM1, AND SUBCELLULAR LOCATION.
RX PubMed=15777793; DOI=10.1016/j.yexcr.2004.12.020;
RA Nunes S.M., Ferralli J., Choi K., Brown-Luedi M., Minet A.D.,
RA Chiquet-Ehrismann R.;
RT "The intracellular domain of teneurin-1 interacts with MBD1 and CAP/ponsin
RT resulting in subcellular codistribution and translocation to the nuclear
RT matrix.";
RL Exp. Cell Res. 305:122-132(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200;
RA Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A.,
RA Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A.,
RA Schoepfer R., Burlingame A.L.;
RT "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT preparations using lectin weak affinity chromatography and mass
RT spectrometry.";
RL Mol. Cell. Proteomics 5:923-934(2006).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [18]
RP PHOSPHORYLATION AT TYR-325; TYR-421 AND TYR-1238.
RX PubMed=19891780; DOI=10.1186/1471-2121-10-80;
RA Fernow I., Tomasovic A., Siehoff-Icking A., Tikkanen R.;
RT "Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src
RT kinases.";
RL BMC Cell Biol. 10:80-80(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; SER-55; SER-58; SER-62;
RP THR-179; SER-185; SER-204; SER-209; SER-261; SER-270; SER-345; SER-376;
RP SER-407; SER-432; SER-969; THR-1189; TYR-1198; SER-1201 AND SER-1209,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND SER-346 (ISOFORMS 2
RP AND 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-376
RP (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175 AND SER-357
RP (ISOFORM 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288 AND SER-470
RP (ISOFORM 7), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. {ECO:0000269|PubMed:11001060, ECO:0000269|PubMed:9447983,
CC ECO:0000269|PubMed:9461600}.
CC -!- SUBUNIT: Interacts (via SH3 domain 2) with PXN (By similarity).
CC Interacts with the long isoform of AFDN and with VCL. AFDN and VCL bind
CC to SORBS1 in a competitive manner and do not form a ternary complex.
CC Interacts with ABL1, CBL, CBLB and INPPL1/SHIP2 through the third SH3
CC domain. Interaction with ABL1 occurs only after insulin stimulation
CC while this has no effect on the interaction with INPPL1. Interacts with
CC the insulin receptor but dissociates from it following insulin
CC stimulation. Also interacts with SCA7, PTK2/FAK1 and flotillin.
CC Interacts (via third SH3 domain) with the Ten-1 ICD form of TENM1; the
CC interaction induces the translocation of SORBS1 to the nucleus.
CC Interacts with INSM1. {ECO:0000250, ECO:0000269|PubMed:10085297,
CC ECO:0000269|PubMed:11001060, ECO:0000269|PubMed:12079283,
CC ECO:0000269|PubMed:12842890, ECO:0000269|PubMed:15777793,
CC ECO:0000269|PubMed:9447983, ECO:0000269|PubMed:9461600}.
CC -!- INTERACTION:
CC Q62417-2; P49023: PXN; Xeno; NbExp=8; IntAct=EBI-7072893, EBI-702209;
CC Q62417-2; P18206: VCL; Xeno; NbExp=3; IntAct=EBI-7072893, EBI-716775;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell membrane.
CC Cytoplasm, cytoskeleton. Cell junction, focal adhesion {ECO:0000250}.
CC Nucleus. Nucleus matrix. Note=Colocalized with PXN at focal adhesions
CC during myogenic differentiation (By similarity). Colocalizes with actin
CC stress fibers. Also detected at the plasma membrane and in neuronal
CC intranuclear inclusions. Colocalizes with the Ten-1 ICD form of TENM1
CC in the nucleus. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1 {ECO:0000305};
CC IsoId=Q62417-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15047181}; Synonyms=CAPsm
CC {ECO:0000303|PubMed:15047181};
CC IsoId=Q62417-2; Sequence=VSP_050886, VSP_050889, VSP_050890,
CC VSP_050892;
CC Name=3 {ECO:0000269|PubMed:10085297}; Synonyms=Ponsin-2
CC {ECO:0000303|PubMed:10085297};
CC IsoId=Q62417-3; Sequence=VSP_050886, VSP_050891, VSP_050892,
CC VSP_050893;
CC Name=4 {ECO:0000269|PubMed:10085297}; Synonyms=Ponsin-1
CC {ECO:0000303|PubMed:10085297};
CC IsoId=Q62417-4; Sequence=VSP_050885, VSP_050886, VSP_050889,
CC VSP_050890, VSP_050892, VSP_050893;
CC Name=5 {ECO:0000269|PubMed:9447983, ECO:0000269|PubMed:9630982};
CC IsoId=Q62417-5; Sequence=VSP_050886, VSP_050889, VSP_050890,
CC VSP_050892, VSP_050893;
CC Name=6 {ECO:0000305};
CC IsoId=Q62417-6; Sequence=VSP_050886, VSP_050887, VSP_050889,
CC VSP_050890, VSP_050892, VSP_050893;
CC Name=7 {ECO:0000305};
CC IsoId=Q62417-7; Sequence=VSP_050886, VSP_050888, VSP_050889,
CC VSP_050890, VSP_050892, VSP_050894;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested: heart, brain,
CC spleen, lung, liver, muscle, kidney and testis. Expressed in 3T3-L1
CC adipocytes but not in 3T3-L1 fibroblasts. {ECO:0000269|PubMed:10085297,
CC ECO:0000269|PubMed:9447983}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:16452088}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65769.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U58883; AAC71776.1; -; mRNA.
DR EMBL; AF078666; AAD16007.1; -; mRNA.
DR EMBL; AF078667; AAD16008.1; -; mRNA.
DR EMBL; AF521593; AAM77354.1; -; mRNA.
DR EMBL; AK122487; BAC65769.2; ALT_INIT; mRNA.
DR EMBL; AK035212; BAC28980.1; -; mRNA.
DR EMBL; BC012703; AAH12703.1; -; mRNA.
DR CCDS; CCDS37978.1; -. [Q62417-3]
DR CCDS; CCDS37979.1; -. [Q62417-2]
DR CCDS; CCDS37981.1; -. [Q62417-4]
DR CCDS; CCDS89388.1; -. [Q62417-5]
DR RefSeq; NP_001030134.1; NM_001034962.1.
DR RefSeq; NP_001030135.1; NM_001034963.1.
DR RefSeq; NP_001030136.1; NM_001034964.1.
DR AlphaFoldDB; Q62417; -.
DR SMR; Q62417; -.
DR BioGRID; 203213; 42.
DR IntAct; Q62417; 13.
DR MINT; Q62417; -.
DR iPTMnet; Q62417; -.
DR PhosphoSitePlus; Q62417; -.
DR SwissPalm; Q62417; -.
DR EPD; Q62417; -.
DR jPOST; Q62417; -.
DR MaxQB; Q62417; -.
DR PeptideAtlas; Q62417; -.
DR PRIDE; Q62417; -.
DR ProteomicsDB; 262681; -. [Q62417-1]
DR ProteomicsDB; 262682; -. [Q62417-2]
DR ProteomicsDB; 262683; -. [Q62417-3]
DR ProteomicsDB; 262684; -. [Q62417-4]
DR ProteomicsDB; 262685; -. [Q62417-5]
DR ProteomicsDB; 262686; -. [Q62417-6]
DR ProteomicsDB; 262687; -. [Q62417-7]
DR DNASU; 20411; -.
DR GeneID; 20411; -.
DR KEGG; mmu:20411; -.
DR UCSC; uc008hkr.1; mouse. [Q62417-1]
DR UCSC; uc008hks.1; mouse. [Q62417-6]
DR UCSC; uc008hkt.1; mouse. [Q62417-7]
DR CTD; 10580; -.
DR MGI; MGI:700014; Sorbs1.
DR eggNOG; KOG4225; Eukaryota.
DR InParanoid; Q62417; -.
DR OrthoDB; 228183at2759; -.
DR PhylomeDB; Q62417; -.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR BioGRID-ORCS; 20411; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Sorbs1; mouse.
DR PRO; PR:Q62417; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q62417; protein.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0030055; C:cell-substrate junction; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0016600; C:flotillin complex; IDA:BHF-UCL.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0005158; F:insulin receptor binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IPI:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IGI:MGI.
DR GO; GO:0031589; P:cell-substrate adhesion; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
DR GO; GO:0048041; P:focal adhesion assembly; IDA:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; IDA:UniProtKB.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IMP:BHF-UCL.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:1904393; P:regulation of skeletal muscle acetylcholine-gated channel clustering; IGI:MGI.
DR GO; GO:0043149; P:stress fiber assembly; IDA: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 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 Alternative splicing; Cell junction; Cell membrane; Cytoplasm;
KW Cytoskeleton; Glycoprotein; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Transport.
FT CHAIN 1..1290
FT /note="Sorbin and SH3 domain-containing protein 1"
FT /id="PRO_0000072186"
FT DOMAIN 202..247
FT /note="SoHo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00195"
FT DOMAIN 1049..1108
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1123..1184
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1229..1290
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 179
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84109"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 325
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:19891780"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 421
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:19891780"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 475
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX66"
FT MOD_RES 969
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1189
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1193
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX66"
FT MOD_RES 1198
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1238
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:19891780"
FT VAR_SEQ 26
FT /note="K -> KADPFRARSISAVKIIPVKTVKSPSGLVLPP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10085297"
FT /id="VSP_050885"
FT VAR_SEQ 70..78
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10085297,
FT ECO:0000303|PubMed:15047181, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9447983,
FT ECO:0000303|PubMed:9630982"
FT /id="VSP_050886"
FT VAR_SEQ 117
FT /note="G -> GATSSSSAPSEG (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_050887"
FT VAR_SEQ 117
FT /note="G -> GATSSSSAPSEVIVVPLYLVNTDRGQGQEGTARTPASLGPLGCVHTV
FT PATTPAASPLTFPTLDDFIPPHLQRRPHHSQPASACGSLSPASQTSPPSPPPPLVPPVP
FT EDLHRGLEPDLPGAVSSTG (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_050888"
FT VAR_SEQ 163
FT /note="R -> REQQKRLSSLS (in isoform 2, isoform 4, isoform
FT 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10085297,
FT ECO:0000303|PubMed:15047181, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9447983,
FT ECO:0000303|PubMed:9630982"
FT /id="VSP_050889"
FT VAR_SEQ 341..402
FT /note="Missing (in isoform 2, isoform 4, isoform 5, isoform
FT 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10085297,
FT ECO:0000303|PubMed:15047181, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9447983,
FT ECO:0000303|PubMed:9630982"
FT /id="VSP_050890"
FT VAR_SEQ 369..402
FT /note="TNLEKDLSFCQAELEADLEKVETVNKSPSANSPQ -> PPKKIWDYTPGDCS
FT ILPREDRK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10085297"
FT /id="VSP_050891"
FT VAR_SEQ 477..965
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10085297,
FT ECO:0000303|PubMed:15047181, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9447983,
FT ECO:0000303|PubMed:9630982"
FT /id="VSP_050892"
FT VAR_SEQ 994..1049
FT /note="Missing (in isoform 3, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:10085297,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9447983,
FT ECO:0000303|PubMed:9630982"
FT /id="VSP_050893"
FT VAR_SEQ 1212..1290
FT /note="QPQAQQRRVTPDRSQPSLDLCSYQALYSYVPQNDDELELRDGDIVDVMEKCD
FT DGWFVGTSRRTRQFGTFPGNYVKPLYL -> VSKLSNSACSFHPQLCQRHTALLGLLFH
FT ALIKSYLEQAGWEFFSYMSVAFS (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_050894"
FT CONFLICT 205
FT /note="A -> T (in Ref. 7; BAC28980)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="L -> P (in Ref. 7; BAC28980)"
FT /evidence="ECO:0000305"
FT CONFLICT 1004
FT /note="K -> M (in Ref. 4; AAM77354)"
FT /evidence="ECO:0000305"
FT MOD_RES Q62417-2:164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q62417-2:346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q62417-4:194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q62417-4:376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q62417-5:164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q62417-5:346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q62417-6:175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q62417-6:357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q62417-7:288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q62417-7:470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1290 AA; 143070 MW; 07C9A74BD794E390 CRC64;
MSSECDVGSS KAVVNGLASG NHGPDKDMDP TKICTGKGTV TLRASSSYRG TPSSSPVSPQ
ESPKHESKSG LEPEDPSADE WKLSSSADTN GNAQPSPLAA KGYRSVHPSL SADKPQGSPL
LNEVSSSHIE TDSQDFPPTS RPSSAYPSTT IVNPTIVLLQ HNRDPASERR AGEQDPVPTP
AELTSPGRAS ERRAKDASRR VVRSAQDLSD VSTDEVGIPL RNTERSKDWY KTMFKQIHKL
NRDDDSDVHS PRYSFSDDTK SPLSVPRSKS EMNYIEGEKV VKRSATLPLP ARSSSLKSSP
ERNDWEPLDK KVDTRKYRAE PKSIYEYQPG KSSVLTNEKM SRDISPEEID LKNEPWYKFF
SELEFGRPTN LEKDLSFCQA ELEADLEKVE TVNKSPSANS PQSSAVSPTP DITSEPPGYI
YSSNFHAVKR ESDGTPGGLA SLENERQIYK SVLEGGDIPL QGLSGLKRPS SSASTKVDRK
GGNAHMISSS SVHSRTFHTS NALGPGCKHK KPLSAAKACI SEILPSKFKP RLSAPSALLQ
EQKSVLLPSE KAQSCENLCV SLNDSKRGLP LRVGGSIENL LMRSRRDYDS KSSSTMSLQE
YGTSSRRPCP LSRKAGLHFS MFYRDMHQIN RAGLSLGSIS SSSVRDLASH FERSSLTLAR
GELGASQEGS EHIPKHTVSS RITAFEQLIQ RSRSMPSLDF SGRLSKSPTP VLSRSGLTSA
RSAESLLEST KLRPREMDGM DSGGVYASPT CSNMADHALS FRSLVPSEPL SICSDELDHC
SNVSNDSREG SGGSVHGDFP KHRLNKCKGT CPASYTRFTT IRKHEQQSSR QSDWRSDSRG
DKNSLLRNIH LMSPLPFRLK KPLQQHPRQP PPSDSSESPA GQKADLPCHD PQDQPHSAGK
PQVPTRLSSR HTMARLSHNS EPPLDRPAGL EDCTRAINNG NPVPYSDHGL DRNNNPQSEL
AAAHGDSESP RHFIPADYLE STEEFIRRRH DDKEKLLADQ RRLKREQEEA DIAARRHTGV
IPTHHQFITN ERFGDLLNID DTAKRKSGLE MRPARAKFDF KAQTLKELPL QKGDVVYIYR
QIDQNWYEGE HHGRVGIFPR TYIELLPPAE KAQPRKLAPV QVLEYGEAIA KFNFNGDTQV
EMSFRKGERI TLLRQVDENW YEGRIPGTSR QGIFPITYVD VLKRPLVKTP VDYIDLPYSS
SPSRSATVSP QQPQAQQRRV TPDRSQPSLD LCSYQALYSY VPQNDDELEL RDGDIVDVME
KCDDGWFVGT SRRTRQFGTF PGNYVKPLYL
