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 27-MAR-2024, entry version 207. 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 a 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 149. DR ComplexPortal; CPX-7143; ESCRT-0 complex, STAM2 variant. DR CORUM; O75886; -. DR IntAct; O75886; 193. DR MINT; O75886; -. DR STRING; 9606.ENSP00000263904; -. DR GlyGen; O75886; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000263904; -. DR PeptideAtlas; O75886; -. DR ProteomicsDB; 50243; -. [O75886-1] DR ProteomicsDB; 50244; -. [O75886-2] DR Pumba; O75886; -. DR Antibodypedia; 33682; 398 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 AGR; HGNC:11358; -. 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; CNTSEDW; -. DR OrthoDB; 620063at2759; -. 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; 18 hits in 1163 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 205 other cell types or tissues. 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; ISS:ComplexPortal. 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; NAS: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; NAS:ComplexPortal. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd21390; GAT_STAM2; 1. DR CDD; cd11963; SH3_STAM2; 1. DR CDD; cd16999; VHS_STAM2; 1. DR Gene3D; 1.20.5.1940; -; 1. DR Gene3D; 1.25.40.90; -; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 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 InterPro; IPR047493; VHS_STAM2. DR PANTHER; PTHR45929; JAK PATHWAY SIGNAL TRANSDUCTION ADAPTOR MOLECULE; 1. DR PANTHER; PTHR45929:SF1; SIGNAL TRANSDUCING ADAPTER MOLECULE 2; 1. DR Pfam; PF00018; SH3_1; 1. DR Pfam; PF02809; UIM; 1. DR Pfam; PF00790; VHS; 1. DR PRINTS; PR00499; P67PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00326; SH3; 1. DR SMART; SM00726; UIM; 1. DR SMART; SM00288; VHS; 1. DR SUPFAM; SSF48464; ENTH/VHS domain; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50002; SH3; 1. DR PROSITE; PS50330; UIM; 1. DR PROSITE; PS50179; VHS; 1. DR Genevisible; O75886; HS. 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 //