Full text data of STAM
STAM
(STAM1)
[Confidence: low (only semi-automatic identification from reviews)]
Signal transducing adapter molecule 1; STAM-1
Signal transducing adapter molecule 1; STAM-1
UniProt
Q92783
ID STAM1_HUMAN Reviewed; 540 AA.
AC Q92783; B0YJ99; D3DRU5; Q8N6D9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 122.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-15;
RP 110-119; 137-154; 215-223; 233-247 AND 364-373, AND TISSUE
RP 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
RT SH3 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RP INITIATOR METHIONINE, PHOSPHORYLATION AT TYR-198, AND 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
RT receptor 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.,
RA Takeshita T., Endo Y., Fujita T., Sugamura K.;
RT "Hrs is associated with STAM, a signal-transducing adaptor molecule.
RT Its 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.,
RA Takeshita T., 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
RP 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
RT on 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION, AND INTERACTION WITH PDGFRB.
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
RT cell proliferation but not migration.";
RL Cell. Signal. 22:1363-1368(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 4-143 IN COMPLEX WITH
RP UBIQUITIN, 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 [14]
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Involved in intracellular signal transduction mediated
CC by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation,
CC it plays a role in signaling leading to DNA synthesis and MYC
CC induction. May also play a role in T-cell development. Involved in
CC down-regulation of receptor tyrosine kinase via multivesicular
CC body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0
CC complex binds ubiquitin and acts as sorting machinery that
CC recognizes ubiquitinated receptors and transfers them to further
CC sequential lysosomal sorting/trafficking processes.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of STAM or
CC STAM2 and HGS. Probably part of a complex at least composed of
CC HSG, STAM and EPS15. Interacts with STAMBP/AMSH. Interacts with
CC PDGFRB.
CC -!- INTERACTION:
CC Q13094:LCP2; NbExp=3; IntAct=EBI-752333, EBI-346946;
CC O95630:STAMBP; NbExp=6; IntAct=EBI-752333, EBI-396676;
CC P0CG53:UBB (xeno); NbExp=9; IntAct=EBI-752333, EBI-5333021;
CC P0CG48:UBC; NbExp=2; IntAct=EBI-752333, EBI-3390054;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). Early endosome
CC membrane; Peripheral membrane protein; Cytoplasmic side
CC (Probable).
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DOMAIN: The VHS domain mediates high-avidity binding to Lys63-
CC linked and Lys48-linked polyubiquitinated cargos.
CC -!- PTM: Phosphorylated on Tyr-198. Phosphorylated in response to IL2,
CC IL3, IL4, IL7, CSF2/GM-CSF, EGF and PDGFB. Phosphorylated by
CC activated PDGFRB.
CC -!- SIMILARITY: Belongs to the STAM family.
CC -!- SIMILARITY: Contains 1 ITAM domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- SIMILARITY: Contains 1 UIM (ubiquitin-interacting motif) repeat.
CC -!- SIMILARITY: Contains 1 VHS domain.
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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 PIR; JC4916; JC4916.
DR RefSeq; NP_003464.1; NM_003473.3.
DR UniGene; Hs.335391; -.
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 ProteinModelPortal; Q92783; -.
DR SMR; Q92783; 4-143, 211-267, 301-377.
DR DIP; DIP-37761N; -.
DR IntAct; Q92783; 12.
DR MINT; MINT-734093; -.
DR STRING; 9606.ENSP00000366746; -.
DR PhosphoSite; Q92783; -.
DR DMDM; 71153545; -.
DR PaxDb; Q92783; -.
DR PRIDE; Q92783; -.
DR Ensembl; ENST00000377524; ENSP00000366746; ENSG00000136738.
DR Ensembl; ENST00000565101; ENSP00000456885; ENSG00000260045.
DR GeneID; 8027; -.
DR KEGG; hsa:8027; -.
DR UCSC; uc001ipj.2; human.
DR CTD; 8027; -.
DR GeneCards; GC10P017686; -.
DR HGNC; HGNC:11357; STAM.
DR HPA; CAB034399; -.
DR MIM; 601899; gene.
DR neXtProt; NX_Q92783; -.
DR PharmGKB; PA36179; -.
DR eggNOG; NOG309509; -.
DR HOGENOM; HOG000231952; -.
DR HOVERGEN; HBG053175; -.
DR InParanoid; Q92783; -.
DR KO; K04705; -.
DR OMA; YYMQSPG; -.
DR PhylomeDB; Q92783; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR SignaLink; Q92783; -.
DR EvolutionaryTrace; Q92783; -.
DR GeneWiki; Signal_transducing_adaptor_molecule; -.
DR GenomeRNAi; 8027; -.
DR NextBio; 30597; -.
DR PRO; PR:Q92783; -.
DR ArrayExpress; Q92783; -.
DR Bgee; Q92783; -.
DR CleanEx; HS_STAM; -.
DR Genevestigator; Q92783; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR003903; Ubiquitin-int_motif.
DR InterPro; IPR002014; VHS.
DR InterPro; IPR018205; VHS_subgr.
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; SM00726; UIM; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51055; ITAM_1; FALSE_NEG.
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; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Endosome; Membrane; Phosphoprotein;
KW Polymorphism; Protein transport; Reference proteome; SH3 domain;
KW Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 540 Signal transducing adapter molecule 1.
FT /FTId=PRO_0000190145.
FT DOMAIN 16 143 VHS.
FT REPEAT 171 190 UIM.
FT DOMAIN 210 269 SH3.
FT DOMAIN 370 387 ITAM.
FT MOD_RES 156 156 Phosphoserine.
FT MOD_RES 198 198 Phosphotyrosine.
FT MOD_RES 381 381 Phosphotyrosine.
FT MOD_RES 384 384 Phosphotyrosine.
FT VAR_SEQ 392 403 YYMQSSGVSGSQ -> GSGPTIRKPSPS (in isoform
FT 2).
FT /FTId=VSP_014846.
FT VAR_SEQ 404 540 Missing (in isoform 2).
FT /FTId=VSP_014847.
FT VARIANT 212 212 G -> D (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036348.
FT CONFLICT 267 267 D -> Y (in Ref. 4; AAH30586).
FT HELIX 10 16
FT STRAND 21 23
FT HELIX 26 36
FT HELIX 42 54
FT HELIX 59 75
FT HELIX 78 84
FT HELIX 87 99
FT HELIX 102 119
FT HELIX 123 125
FT HELIX 127 137
FT STRAND 213 219
FT STRAND 236 244
FT STRAND 247 251
FT STRAND 256 258
FT STRAND 264 266
FT HELIX 304 315
FT HELIX 327 375
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
//
ID STAM1_HUMAN Reviewed; 540 AA.
AC Q92783; B0YJ99; D3DRU5; Q8N6D9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 122.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-15;
RP 110-119; 137-154; 215-223; 233-247 AND 364-373, AND TISSUE
RP 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
RT SH3 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RP INITIATOR METHIONINE, PHOSPHORYLATION AT TYR-198, AND 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
RT receptor 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.,
RA Takeshita T., Endo Y., Fujita T., Sugamura K.;
RT "Hrs is associated with STAM, a signal-transducing adaptor molecule.
RT Its 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.,
RA Takeshita T., 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
RP 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
RT on 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION, AND INTERACTION WITH PDGFRB.
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
RT cell proliferation but not migration.";
RL Cell. Signal. 22:1363-1368(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 4-143 IN COMPLEX WITH
RP UBIQUITIN, 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 [14]
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Involved in intracellular signal transduction mediated
CC by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation,
CC it plays a role in signaling leading to DNA synthesis and MYC
CC induction. May also play a role in T-cell development. Involved in
CC down-regulation of receptor tyrosine kinase via multivesicular
CC body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0
CC complex binds ubiquitin and acts as sorting machinery that
CC recognizes ubiquitinated receptors and transfers them to further
CC sequential lysosomal sorting/trafficking processes.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of STAM or
CC STAM2 and HGS. Probably part of a complex at least composed of
CC HSG, STAM and EPS15. Interacts with STAMBP/AMSH. Interacts with
CC PDGFRB.
CC -!- INTERACTION:
CC Q13094:LCP2; NbExp=3; IntAct=EBI-752333, EBI-346946;
CC O95630:STAMBP; NbExp=6; IntAct=EBI-752333, EBI-396676;
CC P0CG53:UBB (xeno); NbExp=9; IntAct=EBI-752333, EBI-5333021;
CC P0CG48:UBC; NbExp=2; IntAct=EBI-752333, EBI-3390054;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). Early endosome
CC membrane; Peripheral membrane protein; Cytoplasmic side
CC (Probable).
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DOMAIN: The VHS domain mediates high-avidity binding to Lys63-
CC linked and Lys48-linked polyubiquitinated cargos.
CC -!- PTM: Phosphorylated on Tyr-198. Phosphorylated in response to IL2,
CC IL3, IL4, IL7, CSF2/GM-CSF, EGF and PDGFB. Phosphorylated by
CC activated PDGFRB.
CC -!- SIMILARITY: Belongs to the STAM family.
CC -!- SIMILARITY: Contains 1 ITAM domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- SIMILARITY: Contains 1 UIM (ubiquitin-interacting motif) repeat.
CC -!- SIMILARITY: Contains 1 VHS domain.
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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 PIR; JC4916; JC4916.
DR RefSeq; NP_003464.1; NM_003473.3.
DR UniGene; Hs.335391; -.
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 ProteinModelPortal; Q92783; -.
DR SMR; Q92783; 4-143, 211-267, 301-377.
DR DIP; DIP-37761N; -.
DR IntAct; Q92783; 12.
DR MINT; MINT-734093; -.
DR STRING; 9606.ENSP00000366746; -.
DR PhosphoSite; Q92783; -.
DR DMDM; 71153545; -.
DR PaxDb; Q92783; -.
DR PRIDE; Q92783; -.
DR Ensembl; ENST00000377524; ENSP00000366746; ENSG00000136738.
DR Ensembl; ENST00000565101; ENSP00000456885; ENSG00000260045.
DR GeneID; 8027; -.
DR KEGG; hsa:8027; -.
DR UCSC; uc001ipj.2; human.
DR CTD; 8027; -.
DR GeneCards; GC10P017686; -.
DR HGNC; HGNC:11357; STAM.
DR HPA; CAB034399; -.
DR MIM; 601899; gene.
DR neXtProt; NX_Q92783; -.
DR PharmGKB; PA36179; -.
DR eggNOG; NOG309509; -.
DR HOGENOM; HOG000231952; -.
DR HOVERGEN; HBG053175; -.
DR InParanoid; Q92783; -.
DR KO; K04705; -.
DR OMA; YYMQSPG; -.
DR PhylomeDB; Q92783; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR SignaLink; Q92783; -.
DR EvolutionaryTrace; Q92783; -.
DR GeneWiki; Signal_transducing_adaptor_molecule; -.
DR GenomeRNAi; 8027; -.
DR NextBio; 30597; -.
DR PRO; PR:Q92783; -.
DR ArrayExpress; Q92783; -.
DR Bgee; Q92783; -.
DR CleanEx; HS_STAM; -.
DR Genevestigator; Q92783; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR003903; Ubiquitin-int_motif.
DR InterPro; IPR002014; VHS.
DR InterPro; IPR018205; VHS_subgr.
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; SM00726; UIM; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51055; ITAM_1; FALSE_NEG.
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; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Endosome; Membrane; Phosphoprotein;
KW Polymorphism; Protein transport; Reference proteome; SH3 domain;
KW Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 540 Signal transducing adapter molecule 1.
FT /FTId=PRO_0000190145.
FT DOMAIN 16 143 VHS.
FT REPEAT 171 190 UIM.
FT DOMAIN 210 269 SH3.
FT DOMAIN 370 387 ITAM.
FT MOD_RES 156 156 Phosphoserine.
FT MOD_RES 198 198 Phosphotyrosine.
FT MOD_RES 381 381 Phosphotyrosine.
FT MOD_RES 384 384 Phosphotyrosine.
FT VAR_SEQ 392 403 YYMQSSGVSGSQ -> GSGPTIRKPSPS (in isoform
FT 2).
FT /FTId=VSP_014846.
FT VAR_SEQ 404 540 Missing (in isoform 2).
FT /FTId=VSP_014847.
FT VARIANT 212 212 G -> D (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036348.
FT CONFLICT 267 267 D -> Y (in Ref. 4; AAH30586).
FT HELIX 10 16
FT STRAND 21 23
FT HELIX 26 36
FT HELIX 42 54
FT HELIX 59 75
FT HELIX 78 84
FT HELIX 87 99
FT HELIX 102 119
FT HELIX 123 125
FT HELIX 127 137
FT STRAND 213 219
FT STRAND 236 244
FT STRAND 247 251
FT STRAND 256 258
FT STRAND 264 266
FT HELIX 304 315
FT HELIX 327 375
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
//
MIM
601899
*RECORD*
*FIELD* NO
601899
*FIELD* TI
*601899 SIGNAL-TRANSDUCING ADAPTOR MOLECULE 1; STAM
;;SIGNAL-TRANSDUCING ADAPTOR MOLECULE;;
read moreSTAM1
*FIELD* TX
CLONING
Stimulation of cells with cytokines results in a signal transduction
cascade involving cytokine receptors, Janus kinases (JAKs) and signal
transducers and activators of transcription (STATs). In order to
investigate signal transduction downstream of JAK3 (600173), Takeshita
et al. (1996) screened for molecules induced after stimulation of cells
with the cytokine IL2 (147680). Their screen identified a novel
molecule, which they named STAM for 'signal-transducing adaptor
molecule.' They cloned the human STAM cDNA from a T-cell cDNA library
and found that it encodes a 540-amino acid polypeptide. The
approximately 70-kD protein product was precipitated by
anti-phosphotyrosine. Northern blot analysis indicated that STAM was
expressed as a 2.9-kb message in all tissue and cell types examined. The
STAM sequence contains a Src-homology 3 (SH3) domain and an
immunoreceptor tyrosine-based activation motif (ITAM). Takeshita et al.
(1996) suggested that STAM acts as an adaptor molecule in signal
transduction pathways from cytokine receptors.
GENE FUNCTION
Asao et al. (1997) showed that HGS (604375) binds to STAM via
coiled-coil sequences and appears to regulate proliferation in response
to cytokines.
MAPPING
Takeshita et al. (1996) used fluorescence in situ hybridization to map
the STAM gene to human chromosome 10p14-p13.
*FIELD* RF
1. Asao, H.; Sasaki, Y.; Arita, T.; Tanaka, N.; Endo, K.; Kasai, H.;
Takeshita, T; Endo, Y.; Fujita, T.; Sugamura, K.: Hrs is associated
with STAM, a signal-transducing adaptor molecule: its suppressive
effect on cytokine-induced cell growth. J. Biol. Chem. 272: 32785-32791,
1997.
2. Takeshita, T.; Arita, T.; Asao, H.; Tanaka, N.; Higuchi, M.; Kuroda,
H.; Kaneko, K.; Munakata, H.; Endo, Y.; Fujita, T.; Sugamura, K.:
Cloning of a novel signal-transducing adaptor molecule containing
an SH3 domain and ITAM. Biochem. Biophys. Res. Commun. 225: 1035-1039,
1996.
*FIELD* CN
Paul J. Converse - updated: 12/28/1999
*FIELD* CD
Jennifer P. Macke: 5/16/1997
*FIELD* ED
mgross: 08/31/2001
carol: 12/28/1999
carol: 12/27/1999
alopez: 7/18/1997
*RECORD*
*FIELD* NO
601899
*FIELD* TI
*601899 SIGNAL-TRANSDUCING ADAPTOR MOLECULE 1; STAM
;;SIGNAL-TRANSDUCING ADAPTOR MOLECULE;;
read moreSTAM1
*FIELD* TX
CLONING
Stimulation of cells with cytokines results in a signal transduction
cascade involving cytokine receptors, Janus kinases (JAKs) and signal
transducers and activators of transcription (STATs). In order to
investigate signal transduction downstream of JAK3 (600173), Takeshita
et al. (1996) screened for molecules induced after stimulation of cells
with the cytokine IL2 (147680). Their screen identified a novel
molecule, which they named STAM for 'signal-transducing adaptor
molecule.' They cloned the human STAM cDNA from a T-cell cDNA library
and found that it encodes a 540-amino acid polypeptide. The
approximately 70-kD protein product was precipitated by
anti-phosphotyrosine. Northern blot analysis indicated that STAM was
expressed as a 2.9-kb message in all tissue and cell types examined. The
STAM sequence contains a Src-homology 3 (SH3) domain and an
immunoreceptor tyrosine-based activation motif (ITAM). Takeshita et al.
(1996) suggested that STAM acts as an adaptor molecule in signal
transduction pathways from cytokine receptors.
GENE FUNCTION
Asao et al. (1997) showed that HGS (604375) binds to STAM via
coiled-coil sequences and appears to regulate proliferation in response
to cytokines.
MAPPING
Takeshita et al. (1996) used fluorescence in situ hybridization to map
the STAM gene to human chromosome 10p14-p13.
*FIELD* RF
1. Asao, H.; Sasaki, Y.; Arita, T.; Tanaka, N.; Endo, K.; Kasai, H.;
Takeshita, T; Endo, Y.; Fujita, T.; Sugamura, K.: Hrs is associated
with STAM, a signal-transducing adaptor molecule: its suppressive
effect on cytokine-induced cell growth. J. Biol. Chem. 272: 32785-32791,
1997.
2. Takeshita, T.; Arita, T.; Asao, H.; Tanaka, N.; Higuchi, M.; Kuroda,
H.; Kaneko, K.; Munakata, H.; Endo, Y.; Fujita, T.; Sugamura, K.:
Cloning of a novel signal-transducing adaptor molecule containing
an SH3 domain and ITAM. Biochem. Biophys. Res. Commun. 225: 1035-1039,
1996.
*FIELD* CN
Paul J. Converse - updated: 12/28/1999
*FIELD* CD
Jennifer P. Macke: 5/16/1997
*FIELD* ED
mgross: 08/31/2001
carol: 12/28/1999
carol: 12/27/1999
alopez: 7/18/1997