STAM2_HUMAN
ID STAM2_HUMAN Reviewed; 525 AA.
AC O75886; A8K8A0; D3DPA1; Q7LDQ0; Q9UF58;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Signal transducing adapter molecule 2;
DE Short=STAM-2;
DE AltName: Full=Hrs-binding protein;
GN Name=STAM2; Synonyms=HBP;
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] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP INTERACTION WITH JAK2 AND JAK3.
RC TISSUE=Fetal brain;
RX PubMed=10899310; DOI=10.1016/s0014-5793(00)01760-9;
RA Endo K., Takeshita T., Kasai H., Sasaki Y., Tanaka N., Asao H., Kikuchi K.,
RA Yamada M., Chenb M., O'Shea J.J., Sugamura K.;
RT "STAM2, a new member of the STAM family, binding to the Janus kinases.";
RL FEBS Lett. 477:55-61(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP INTERACTION WITH HGS AND UBIQUITIN, IDENTIFICATION IN A COMPLEX WITH HSG
RP AND EPS15, AND SUBCELLULAR LOCATION.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [9]
RP INTERACTION WITH CBX5.
RX PubMed=15882967; DOI=10.1016/j.bbrc.2005.04.016;
RA Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III;
RT "The mammalian heterochromatin protein 1 binds diverse nuclear proteins
RT through a common motif that targets the chromoshadow domain.";
RL Biochem. Biophys. Res. Commun. 331:929-937(2005).
RN [10]
RP INTERACTION WITH VPS37C.
RX PubMed=15509564; DOI=10.1074/jbc.m410384200;
RA Eastman S.W., Martin-Serrano J., Chung W., Zang T., Bieniasz P.D.;
RT "Identification of human VPS37C, a component of endosomal sorting complex
RT required for transport-I important for viral budding.";
RL J. Biol. Chem. 280:628-636(2005).
RN [11]
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 [12]
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 [13]
RP STRUCTURE BY NMR OF 1-269.
RG RIKEN structural genomics initiative (RSGI);
RT "The solution structure of the VHS and SH3 domains of human signal
RT transducing adaptor molecule 2.";
RL Submitted (NOV-2005) to the PDB data bank.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of STAM or STAM2 and
CC HGS. Part of a complex at least composed of HSG, STAM2 and EPS15.
CC Interacts with JAK2 and JAK3. Interacts with ubiquitinated proteins and
CC the deubiquitinating enzyme USP8/UBPY (By similarity). Interacts (via
CC the via the PxVxL motif) with CBX5; the interaction is direct.
CC Interacts with VPS37C. Interacts with ubiquitin; the interaction is
CC direct. Interacts (via UIM domain) with UBQLN1 (via ubiquitin-like
CC domain) (By similarity). {ECO:0000250|UniProtKB:O88811,
CC ECO:0000269|PubMed:10899310, ECO:0000269|PubMed:12551915,
CC ECO:0000269|PubMed:15509564, ECO:0000269|PubMed:15882967}.
CC -!- INTERACTION:
CC O75886; Q9NYB9: ABI2; NbExp=5; IntAct=EBI-373258, EBI-743598;
CC O75886; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-373258, EBI-11096309;
CC O75886; Q92870-2: APBB2; NbExp=3; IntAct=EBI-373258, EBI-21535880;
CC O75886; Q96B67: ARRDC3; NbExp=6; IntAct=EBI-373258, EBI-2875665;
CC O75886; P54253: ATXN1; NbExp=8; IntAct=EBI-373258, EBI-930964;
CC O75886; P48643: CCT5; NbExp=3; IntAct=EBI-373258, EBI-355710;
CC O75886; O00311: CDC7; NbExp=3; IntAct=EBI-373258, EBI-374980;
CC O75886; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-373258, EBI-21553822;
CC O75886; Q15038: DAZAP2; NbExp=7; IntAct=EBI-373258, EBI-724310;
CC O75886; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-373258, EBI-25840379;
CC O75886; G5E9A7: DMWD; NbExp=3; IntAct=EBI-373258, EBI-10976677;
CC O75886; P22607: FGFR3; NbExp=3; IntAct=EBI-373258, EBI-348399;
CC O75886; P01112: HRAS; NbExp=3; IntAct=EBI-373258, EBI-350145;
CC O75886; P42858: HTT; NbExp=6; IntAct=EBI-373258, EBI-466029;
CC O75886; O60333-2: KIF1B; NbExp=3; IntAct=EBI-373258, EBI-10975473;
CC O75886; Q9P2K6: KLHL42; NbExp=6; IntAct=EBI-373258, EBI-739890;
CC O75886; Q969R5: L3MBTL2; NbExp=4; IntAct=EBI-373258, EBI-739909;
CC O75886; Q13094: LCP2; NbExp=9; IntAct=EBI-373258, EBI-346946;
CC O75886; Q99732: LITAF; NbExp=11; IntAct=EBI-373258, EBI-725647;
CC O75886; P02545: LMNA; NbExp=3; IntAct=EBI-373258, EBI-351935;
CC O75886; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-373258, EBI-2811583;
CC O75886; Q96CS7: PLEKHB2; NbExp=6; IntAct=EBI-373258, EBI-373552;
CC O75886; O60260-5: PRKN; NbExp=3; IntAct=EBI-373258, EBI-21251460;
CC O75886; P60891: PRPS1; NbExp=3; IntAct=EBI-373258, EBI-749195;
CC O75886; Q13671: RIN1; NbExp=4; IntAct=EBI-373258, EBI-366017;
CC O75886; Q9Y3C5: RNF11; NbExp=4; IntAct=EBI-373258, EBI-396669;
CC O75886; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-373258, EBI-747035;
CC O75886; Q9H788-2: SH2D4A; NbExp=3; IntAct=EBI-373258, EBI-10308083;
CC O75886; P37840: SNCA; NbExp=3; IntAct=EBI-373258, EBI-985879;
CC O75886; O95630: STAMBP; NbExp=9; IntAct=EBI-373258, EBI-396676;
CC O75886; O60220: TIMM8A; NbExp=9; IntAct=EBI-373258, EBI-1049822;
CC O75886; P0CG47: UBB; NbExp=3; IntAct=EBI-373258, EBI-413034;
CC O75886; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-373258, EBI-741480;
CC O75886; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-373258, EBI-947187;
CC O75886; A5D8V6: VPS37C; NbExp=6; IntAct=EBI-373258, EBI-2559305;
CC O75886; O76024: WFS1; NbExp=3; IntAct=EBI-373258, EBI-720609;
CC O75886; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-373258, EBI-742550;
CC O75886; Q8WU02; NbExp=3; IntAct=EBI-373258, EBI-747182;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome membrane
CC {ECO:0000269|PubMed:12551915}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12551915}; Cytoplasmic side
CC {ECO:0000269|PubMed:12551915}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=STAM2A;
CC IsoId=O75886-1; Sequence=Displayed;
CC Name=2; Synonyms=STAM2B;
CC IsoId=O75886-2; Sequence=VSP_014848;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10899310}.
CC -!- DOMAIN: The VHS and UIM domains mediate the interaction with
CC ubiquitinated proteins.
CC -!- DOMAIN: The SH3 domain mediates the interaction with USP8.
CC -!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
CC required for interaction with chromoshadow domains. This motif requires
CC additional residues -7, -6, +4 and +5 of the central Val which contact
CC the chromoshadow domain.
CC -!- PTM: Phosphorylated in response to IL-2, GM-CSF, EGF and PDGF.
CC -!- SIMILARITY: Belongs to the STAM family. {ECO:0000305}.
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DR EMBL; AF042273; AAC63963.1; -; mRNA.
DR EMBL; AF042274; AAC63964.1; -; mRNA.
DR EMBL; AL133600; CAB63735.1; -; mRNA.
DR EMBL; AK292265; BAF84954.1; -; mRNA.
DR EMBL; AK292847; BAF85536.1; -; mRNA.
DR EMBL; AC079790; AAY14712.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11490.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11492.1; -; Genomic_DNA.
DR EMBL; BC028740; AAH28740.1; -; mRNA.
DR CCDS; CCDS2196.1; -. [O75886-1]
DR PIR; T43437; T43437.
DR RefSeq; NP_005834.4; NM_005843.5. [O75886-1]
DR PDB; 1X2Q; NMR; -; A=195-269.
DR PDB; 1X5B; NMR; -; A=1-150.
DR PDB; 2L0T; NMR; -; B=1-150.
DR PDB; 5CRV; X-ray; 2.00 A; C/D=350-370.
DR PDB; 5IXF; NMR; -; A=162-265.
DR PDBsum; 1X2Q; -.
DR PDBsum; 1X5B; -.
DR PDBsum; 2L0T; -.
DR PDBsum; 5CRV; -.
DR PDBsum; 5IXF; -.
DR AlphaFoldDB; O75886; -.
DR BMRB; O75886; -.
DR SMR; O75886; -.
DR BioGRID; 115548; 115.
DR ComplexPortal; CPX-7143; ESCRT-0 complex, STAM2 variant.
DR CORUM; O75886; -.
DR IntAct; O75886; 173.
DR MINT; O75886; -.
DR STRING; 9606.ENSP00000263904; -.
DR iPTMnet; O75886; -.
DR MetOSite; O75886; -.
DR PhosphoSitePlus; O75886; -.
DR BioMuta; STAM2; -.
DR EPD; O75886; -.
DR jPOST; O75886; -.
DR MassIVE; O75886; -.
DR MaxQB; O75886; -.
DR PaxDb; O75886; -.
DR PeptideAtlas; O75886; -.
DR PRIDE; O75886; -.
DR ProteomicsDB; 50243; -. [O75886-1]
DR ProteomicsDB; 50244; -. [O75886-2]
DR Antibodypedia; 33682; 369 antibodies from 36 providers.
DR DNASU; 10254; -.
DR Ensembl; ENST00000263904.5; ENSP00000263904.4; ENSG00000115145.10. [O75886-1]
DR GeneID; 10254; -.
DR KEGG; hsa:10254; -.
DR MANE-Select; ENST00000263904.5; ENSP00000263904.4; NM_005843.6; NP_005834.4.
DR UCSC; uc002tyc.4; human. [O75886-1]
DR CTD; 10254; -.
DR DisGeNET; 10254; -.
DR GeneCards; STAM2; -.
DR HGNC; HGNC:11358; STAM2.
DR HPA; ENSG00000115145; Low tissue specificity.
DR MIM; 606244; gene.
DR neXtProt; NX_O75886; -.
DR OpenTargets; ENSG00000115145; -.
DR PharmGKB; PA36180; -.
DR VEuPathDB; HostDB:ENSG00000115145; -.
DR eggNOG; KOG2199; Eukaryota.
DR GeneTree; ENSGT00940000157055; -.
DR HOGENOM; CLU_010104_0_2_1; -.
DR InParanoid; O75886; -.
DR OMA; FASEVRV; -.
DR OrthoDB; 906159at2759; -.
DR PhylomeDB; O75886; -.
DR TreeFam; TF315007; -.
DR PathwayCommons; O75886; -.
DR Reactome; R-HSA-182971; EGFR downregulation.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
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; O75886; -.
DR SIGNOR; O75886; -.
DR BioGRID-ORCS; 10254; 16 hits in 1077 CRISPR screens.
DR ChiTaRS; STAM2; human.
DR EvolutionaryTrace; O75886; -.
DR GeneWiki; STAM2; -.
DR GenomeRNAi; 10254; -.
DR Pharos; O75886; Tbio.
DR PRO; PR:O75886; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O75886; protein.
DR Bgee; ENSG00000115145; Expressed in tendon of biceps brachii and 203 other tissues.
DR Genevisible; O75886; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0033565; C:ESCRT-0 complex; TAS:ParkinsonsUK-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
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:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IC:ComplexPortal.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd11963; SH3_STAM2; 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; IPR035675; STAM2_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; SM00726; UIM; 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; Endosome; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; SH3 domain;
KW Transport.
FT CHAIN 1..525
FT /note="Signal transducing adapter molecule 2"
FT /id="PRO_0000190147"
FT DOMAIN 16..144
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 165..184
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 202..261
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 360..377
FT /note="ITAM"
FT REGION 143..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..220
FT /note="Interaction with USP8"
FT /evidence="ECO:0000250"
FT REGION 334..368
FT /note="Interaction with HGS"
FT /evidence="ECO:0000250"
FT MOTIF 54..67
FT /note="PxVxL motif"
FT COMPBIAS 145..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 343..525
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10899310"
FT /id="VSP_014848"
FT CONFLICT 81..83
FT /note="HLE -> RLG (in Ref. 2; CAB63735)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="N -> D (in Ref. 2; CAB63735)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="A -> V (in Ref. 2; CAB63735)"
FT /evidence="ECO:0000305"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:1X5B"
FT HELIX 26..38
FT /evidence="ECO:0007829|PDB:1X5B"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1X5B"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:1X5B"
FT HELIX 59..75
FT /evidence="ECO:0007829|PDB:1X5B"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:1X5B"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:1X5B"
FT HELIX 103..119
FT /evidence="ECO:0007829|PDB:1X5B"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1X5B"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:2L0T"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:1X5B"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1X5B"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:5IXF"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:1X2Q"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1X2Q"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:1X2Q"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:1X2Q"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:1X2Q"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:1X2Q"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:1X2Q"
FT HELIX 352..357
FT /evidence="ECO:0007829|PDB:5CRV"
FT HELIX 359..365
FT /evidence="ECO:0007829|PDB:5CRV"
SQ SEQUENCE 525 AA; 58164 MW; 408D484544DD9403 CRC64;
MPLFTANPFE QDVEKATNEY NTTEDWSLIM DICDKVGSTP NGAKDCLKAI MKRVNHKVPH
VALQALTLLG ACVANCGKIF HLEVCSRDFA TEVRAVIKNK AHPKVCEKLK SLMVEWSEEF
QKDPQFSLIS ATIKSMKEEG ITFPPAGSQT VSAAAKNGTS SNKNKEDEDI AKAIELSLQE
QKQQHTETKS LYPSSEIQLN NKVARKVRAL YDFEAVEDNE LTFKHGEIII VLDDSDANWW
KGENHRGIGL FPSNFVTTNL NIETEAAAVD KLNVIDDDVE EIKKSEPEPV YIDEDKMDRA
LQVLQSIDPT DSKPDSQDLL DLEDICQQMG PMIDEKLEEI DRKHSELSEL NVKVLEALEL
YNKLVNEAPV YSVYSKLHPP AHYPPASSGV PMQTYPVQSH GGNYMGQSIH QVTVAQSYSL
GPDQIGPLRS LPPNVNSSVT AQPAQTSYLS TGQDTVSNPT YMNQNSNLQS ATGTTAYTQQ
MGMSVDMSSY QNTTSNLPQL AGFPVTVPAH PVAQQHTNYH QQPLL
