STAM1_HUMAN
ID STAM1_HUMAN Reviewed; 540 AA.
AC Q92783; B0YJ99; D3DRU5; Q8N6D9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Signal transducing adapter molecule 1;
DE Short=STAM-1;
GN Name=STAM; Synonyms=STAM1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-15; 110-119;
RP 137-154; 215-223; 233-247 AND 364-373, AND TISSUE SPECIFICITY.
RC TISSUE=T-cell;
RX PubMed=8780729; DOI=10.1006/bbrc.1996.1290;
RA Takeshita T., Arita T., Asao H., Tanaka N., Higuchi M., Kuroda H.,
RA Kaneko K., Munakata H., Endo Y., Fujita T., Sugamura K.;
RT "Cloning of a novel signal-transducing adaptor molecule containing an SH3
RT domain and ITAM.";
RL Biochem. Biophys. Res. Commun. 225:1035-1039(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [5]
RP PROTEIN SEQUENCE OF 189-213, INTERACTION WITH HGS, CLEAVAGE OF INITIATOR
RP METHIONINE, PHOSPHORYLATION AT TYR-198, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=11687594; DOI=10.1074/jbc.m109992200;
RA Steen H., Kuster B., Fernandez M., Pandey A., Mann M.;
RT "Tyrosine phosphorylation mapping of the epidermal growth factor receptor
RT signaling pathway.";
RL J. Biol. Chem. 277:1031-1039(2002).
RN [6]
RP INTERACTION WITH HGS.
RX PubMed=9407053; DOI=10.1074/jbc.272.52.32785;
RA Asao H., Sasaki Y., Arita T., Tanaka N., Endo K., Kasai H., Takeshita T.,
RA Endo Y., Fujita T., Sugamura K.;
RT "Hrs is associated with STAM, a signal-transducing adaptor molecule. Its
RT suppressive effect on cytokine-induced cell growth.";
RL J. Biol. Chem. 272:32785-32791(1997).
RN [7]
RP INTERACTION WITH STAMBP.
RX PubMed=10383417; DOI=10.1074/jbc.274.27.19129;
RA Tanaka N., Kaneko K., Asao H., Kasai H., Endo Y., Fujita T., Takeshita T.,
RA Sugamura K.;
RT "Possible involvement of a novel STAM-associated molecule 'AMSH' in
RT intracellular signal transduction mediated by cytokines.";
RL J. Biol. Chem. 274:19129-19135(1999).
RN [8]
RP INTERACTION WITH HGS, AND IDENTIFICATION IN A COMPLEX WITH HGS AND EPS15.
RX PubMed=12551915; DOI=10.1074/jbc.m210843200;
RA Bache K.G., Raiborg C., Mehlum A., Stenmark H.;
RT "STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on
RT early endosomes.";
RL J. Biol. Chem. 278:12513-12521(2003).
RN [9]
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 [10]
RP INTERACTION WITH PDGFRB, AND PHOSPHORYLATION AT TYR-381 AND TYR-384.
RX PubMed=20494825; DOI=10.1016/j.cellsig.2010.05.004;
RA Wardega P., Heldin C.H., Lennartsson J.;
RT "Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell
RT proliferation but not migration.";
RL Cell. Signal. 22:1363-1368(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND IDENTIFICATION BY
RP 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INTERACTION WITH LITAF, IDENTIFICATION IN A COMPLEX WITH HGS AND LITAF, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23166352; DOI=10.1083/jcb.201204137;
RA Lee S.M., Chin L.S., Li L.;
RT "Charcot-Marie-Tooth disease-linked protein SIMPLE functions with the ESCRT
RT machinery in endosomal trafficking.";
RL J. Cell Biol. 199:799-816(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP INTERACTION WITH DTX3L, IDENTIFICATION IN A COMPLEX WITH DTX3L; HGS AND
RP ITCH, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=24790097; DOI=10.1091/mbc.e13-10-0612;
RA Holleman J., Marchese A.;
RT "The ubiquitin ligase deltex-3l regulates endosomal sorting of the G
RT protein-coupled receptor CXCR4.";
RL Mol. Biol. Cell 25:1892-1904(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-276, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [18]
RP INTERACTION WITH HAVCR1, AND FUNCTION (MICROBIAL INFECTION).
RX PubMed=29742433; DOI=10.1016/j.celrep.2018.04.013;
RA Dejarnac O., Hafirassou M.L., Chazal M., Versapuech M., Gaillard J.,
RA Perera-Lecoin M., Umana-Diaz C., Bonnet-Madin L., Carnec X., Tinevez J.Y.,
RA Delaugerre C., Schwartz O., Roingeard P., Jouvenet N., Berlioz-Torrent C.,
RA Meertens L., Amara A.;
RT "TIM-1 Ubiquitination Mediates Dengue Virus Entry.";
RL Cell Rep. 23:1779-1793(2018).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 301-377 IN COMPLEX WITH STAM,
RP SUBUNIT, AND INTERACTION WITH STAM.
RX PubMed=19278655; DOI=10.1016/j.str.2009.01.012;
RA Ren X., Kloer D.P., Kim Y.C., Ghirlando R., Saidi L.F., Hummer G.,
RA Hurley J.H.;
RT "Hybrid structural model of the complete human ESCRT-0 complex.";
RL Structure 17:406-416(2009).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 4-143 IN COMPLEX WITH UBIQUITIN,
RP DOMAIN VHS, AND SUBUNIT.
RX PubMed=20150893; DOI=10.1038/emboj.2010.6;
RA Ren X., Hurley J.H.;
RT "VHS domains of ESCRT-0 cooperate in high-avidity binding to
RT polyubiquitinated cargo.";
RL EMBO J. 29:1045-1054(2010).
RN [21]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-212.
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: Involved in intracellular signal transduction mediated by
CC cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it
CC plays a role in signaling leading to DNA synthesis and MYC induction.
CC May also play a role in T-cell development. Involved in down-regulation
CC of receptor tyrosine kinase via multivesicular body (MVBs) when
CC complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds
CC ubiquitin and acts as sorting machinery that recognizes ubiquitinated
CC receptors and transfers them to further sequential lysosomal
CC sorting/trafficking processes.
CC -!- FUNCTION: (Microbial infection) Plays an important role in Dengue virus
CC entry. {ECO:0000269|PubMed:29742433}.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of STAM or STAM2 and
CC HGS (PubMed:11687594, PubMed:9407053, PubMed:19278655). Probably part
CC of a complex at least composed of HSG, STAM and EPS15
CC (PubMed:12551915). Found in a complex with HGS and E3 ligase ITCH and
CC DTX3L (PubMed:24790097). Interacts with E3 ligase DTX3L; the
CC interaction brings together STAM and HSG, promotes their recruitment to
CC early endosomes and decreases STAM and HGS ubiquitination by ITCH
CC (PubMed:24790097). Interacts with STAMBP/AMSH (PubMed:10383417).
CC Interacts with PDGFRB (PubMed:20494825). Interacts with LITAF; the
CC interaction is direct (PubMed:23166352). Identified in a complex with
CC HGS and LITAF (PubMed:23166352). Interacts with HAVCR1
CC (PubMed:29742433). {ECO:0000269|PubMed:10383417,
CC ECO:0000269|PubMed:11687594, ECO:0000269|PubMed:12551915,
CC ECO:0000269|PubMed:19278655, ECO:0000269|PubMed:20150893,
CC ECO:0000269|PubMed:20494825, ECO:0000269|PubMed:23166352,
CC ECO:0000269|PubMed:24790097, ECO:0000269|PubMed:29742433,
CC ECO:0000269|PubMed:9407053}.
CC -!- INTERACTION:
CC Q92783; O14964: HGS; NbExp=4; IntAct=EBI-752333, EBI-740220;
CC Q92783; Q13094: LCP2; NbExp=3; IntAct=EBI-752333, EBI-346946;
CC Q92783; O95630: STAMBP; NbExp=7; IntAct=EBI-752333, EBI-396676;
CC Q92783; P0CG48: UBC; NbExp=2; IntAct=EBI-752333, EBI-3390054;
CC Q92783; P0CG53: UBB; Xeno; NbExp=9; IntAct=EBI-752333, EBI-5333021;
CC Q92783-1; O14964: HGS; NbExp=5; IntAct=EBI-15763634, EBI-740220;
CC Q92783-1; Q99LI8: Hgs; Xeno; NbExp=4; IntAct=EBI-15763634, EBI-2119135;
CC Q92783-2; P28329-3: CHAT; NbExp=3; IntAct=EBI-12025738, EBI-25837549;
CC Q92783-2; P22607: FGFR3; NbExp=3; IntAct=EBI-12025738, EBI-348399;
CC Q92783-2; O14964: HGS; NbExp=3; IntAct=EBI-12025738, EBI-740220;
CC Q92783-2; P01112: HRAS; NbExp=3; IntAct=EBI-12025738, EBI-350145;
CC Q92783-2; Q13449: LSAMP; NbExp=3; IntAct=EBI-12025738, EBI-4314821;
CC Q92783-2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-12025738, EBI-2811583;
CC Q92783-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-12025738, EBI-396669;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Early endosome membrane
CC {ECO:0000269|PubMed:23166352, ECO:0000269|PubMed:24790097}; Peripheral
CC membrane protein {ECO:0000305|PubMed:23166352,
CC ECO:0000305|PubMed:24790097}; Cytoplasmic side
CC {ECO:0000305|PubMed:23166352, ECO:0000305|PubMed:24790097}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92783-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92783-2; Sequence=VSP_014846, VSP_014847;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:8780729}.
CC -!- DOMAIN: The VHS domain mediates high-avidity binding to Lys63-linked
CC and Lys48-linked polyubiquitinated cargos.
CC {ECO:0000269|PubMed:20150893}.
CC -!- PTM: Phosphorylated on Tyr-198. Phosphorylated in response to IL2, IL3,
CC IL4, IL7, CSF2/GM-CSF, EGF and PDGFB. Phosphorylated by activated
CC PDGFRB. {ECO:0000269|PubMed:11687594, ECO:0000269|PubMed:20494825}.
CC -!- PTM: Ubiquitinated by ITCH. {ECO:0000269|PubMed:24790097}.
CC -!- SIMILARITY: Belongs to the STAM family. {ECO:0000305}.
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DR EMBL; U43899; AAC50734.1; -; mRNA.
DR EMBL; EF445033; ACA06077.1; -; Genomic_DNA.
DR EMBL; EF445033; ACA06078.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86207.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86209.1; -; Genomic_DNA.
DR EMBL; BC030586; AAH30586.1; -; mRNA.
DR CCDS; CCDS7122.1; -. [Q92783-1]
DR PIR; JC4916; JC4916.
DR RefSeq; NP_003464.1; NM_003473.3. [Q92783-1]
DR PDB; 2L0A; NMR; -; A=207-267.
DR PDB; 3F1I; X-ray; 2.30 A; C/S=301-377.
DR PDB; 3LDZ; X-ray; 2.60 A; A/B/C/D=4-143.
DR PDBsum; 2L0A; -.
DR PDBsum; 3F1I; -.
DR PDBsum; 3LDZ; -.
DR AlphaFoldDB; Q92783; -.
DR BMRB; Q92783; -.
DR SMR; Q92783; -.
DR BioGRID; 113722; 133.
DR ComplexPortal; CPX-2825; ESCRT-0 complex, STAM variant.
DR CORUM; Q92783; -.
DR DIP; DIP-37761N; -.
DR IntAct; Q92783; 35.
DR MINT; Q92783; -.
DR STRING; 9606.ENSP00000366746; -.
DR GlyGen; Q92783; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92783; -.
DR PhosphoSitePlus; Q92783; -.
DR SwissPalm; Q92783; -.
DR BioMuta; STAM; -.
DR DMDM; 71153545; -.
DR EPD; Q92783; -.
DR jPOST; Q92783; -.
DR MassIVE; Q92783; -.
DR MaxQB; Q92783; -.
DR PaxDb; Q92783; -.
DR PeptideAtlas; Q92783; -.
DR PRIDE; Q92783; -.
DR ProteomicsDB; 75463; -. [Q92783-1]
DR ProteomicsDB; 75464; -. [Q92783-2]
DR Antibodypedia; 25306; 349 antibodies from 33 providers.
DR DNASU; 8027; -.
DR Ensembl; ENST00000377524.8; ENSP00000366746.3; ENSG00000136738.15. [Q92783-1]
DR GeneID; 8027; -.
DR KEGG; hsa:8027; -.
DR MANE-Select; ENST00000377524.8; ENSP00000366746.3; NM_003473.4; NP_003464.1.
DR UCSC; uc001ipj.3; human. [Q92783-1]
DR CTD; 8027; -.
DR DisGeNET; 8027; -.
DR GeneCards; STAM; -.
DR HGNC; HGNC:11357; STAM.
DR HPA; ENSG00000136738; Tissue enhanced (bone).
DR MIM; 601899; gene.
DR neXtProt; NX_Q92783; -.
DR OpenTargets; ENSG00000136738; -.
DR PharmGKB; PA36179; -.
DR VEuPathDB; HostDB:ENSG00000136738; -.
DR eggNOG; KOG2199; Eukaryota.
DR GeneTree; ENSGT00940000157171; -.
DR HOGENOM; CLU_010104_0_2_1; -.
DR InParanoid; Q92783; -.
DR OMA; AHALCQN; -.
DR OrthoDB; 906159at2759; -.
DR PhylomeDB; Q92783; -.
DR TreeFam; TF315007; -.
DR PathwayCommons; Q92783; -.
DR Reactome; R-HSA-182971; EGFR downregulation.
DR Reactome; R-HSA-5689901; Metalloprotease DUBs.
DR Reactome; R-HSA-6807004; Negative regulation of MET activity.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8875360; InlB-mediated entry of Listeria monocytogenes into host cell.
DR Reactome; R-HSA-9013420; RHOU GTPase cycle.
DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR SignaLink; Q92783; -.
DR SIGNOR; Q92783; -.
DR BioGRID-ORCS; 8027; 28 hits in 1078 CRISPR screens.
DR ChiTaRS; STAM; human.
DR EvolutionaryTrace; Q92783; -.
DR GeneWiki; Signal_transducing_adaptor_molecule; -.
DR GenomeRNAi; 8027; -.
DR Pharos; Q92783; Tbio.
DR PRO; PR:Q92783; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q92783; protein.
DR Bgee; ENSG00000136738; Expressed in calcaneal tendon and 203 other tissues.
DR ExpressionAtlas; Q92783; baseline and differential.
DR Genevisible; Q92783; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033565; C:ESCRT-0 complex; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IPI:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0036258; P:multivesicular body assembly; TAS:ParkinsonsUK-UCL.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:1903551; P:regulation of extracellular exosome assembly; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd11964; SH3_STAM1; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035657; STAM1_SH3.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002014; VHS_dom.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF02809; UIM; 1.
DR Pfam; PF00790; VHS; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50179; VHS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Endosome; Isopeptide bond; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; SH3 domain; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11687594,
FT ECO:0000269|PubMed:8780729"
FT CHAIN 2..540
FT /note="Signal transducing adapter molecule 1"
FT /id="PRO_0000190145"
FT DOMAIN 16..143
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 171..190
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 210..269
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 370..387
FT /note="ITAM"
FT REGION 500..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 198
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11687594"
FT MOD_RES 381
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:20494825"
FT MOD_RES 384
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:20494825"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 392..403
FT /note="YYMQSSGVSGSQ -> GSGPTIRKPSPS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014846"
FT VAR_SEQ 404..540
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014847"
FT VARIANT 212
FT /note="G -> D (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1554827317)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036348"
FT CONFLICT 267
FT /note="D -> Y (in Ref. 4; AAH30586)"
FT /evidence="ECO:0000305"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:3LDZ"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3LDZ"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:3LDZ"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:3LDZ"
FT HELIX 59..75
FT /evidence="ECO:0007829|PDB:3LDZ"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:3LDZ"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:3LDZ"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:3LDZ"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3LDZ"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:3LDZ"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:2L0A"
FT STRAND 236..244
FT /evidence="ECO:0007829|PDB:2L0A"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:2L0A"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:2L0A"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:2L0A"
FT HELIX 304..315
FT /evidence="ECO:0007829|PDB:3F1I"
FT HELIX 327..375
FT /evidence="ECO:0007829|PDB:3F1I"
SQ SEQUENCE 540 AA; 59180 MW; 8D6F07FAE538F36F CRC64;
MPLFATNPFD QDVEKATSEM NTAEDWGLIL DICDKVGQSR TGPKDCLRSI MRRVNHKDPH
VAMQALTLLG ACVSNCGKIF HLEVCSRDFA SEVSNVLNKG HPKVCEKLKA LMVEWTDEFK
NDPQLSLISA MIKNLKEQGV TFPAIGSQAA EQAKASPALV AKDPGTVANK KEEEDLAKAI
ELSLKEQRQQ STTLSTLYPS TSSLLTNHQH EGRKVRAIYD FEAAEDNELT FKAGEIITVL
DDSDPNWWKG ETHQGIGLFP SNFVTADLTA EPEMIKTEKK TVQFSDDVQV ETIEPEPEPA
FIDEDKMDQL LQMLQSTDPS DDQPDLPELL HLEAMCHQMG PLIDEKLEDI DRKHSELSEL
NVKVMEALSL YTKLMNEDPM YSMYAKLQNQ PYYMQSSGVS GSQVYAGPPP SGAYLVAGNA
QMSHLQSYSL PPEQLSSLSQ AVVPPSANPA LPSQQTQAAY PNTMVSSVQG NTYPSQAPVY
SPPPAATAAA ATADVTLYQN AGPNMPQVPN YNLTSSTLPQ PGGSQQPPQP QQPYSQKALL
