TS101_HUMAN
ID TS101_HUMAN Reviewed; 390 AA.
AC Q99816; Q9BUM5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 232.
DE RecName: Full=Tumor susceptibility gene 101 protein;
DE AltName: Full=ESCRT-I complex subunit TSG101;
GN Name=TSG101;
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).
RC TISSUE=Placenta;
RX PubMed=9019400; DOI=10.1016/s0092-8674(00)81866-8;
RA Li L., Li X., Francke U., Cohen S.N.;
RT "The TSG101 tumor susceptibility gene is located in chromosome 11 band p15
RT and is mutated in human breast cancer.";
RL Cell 88:143-154(1997).
RN [2]
RP ERRATUM OF PUBMED:9019400, AND RETRACTION NOTICE OF PUBMED:9019400.
RX PubMed=9867424; DOI=10.1016/s0092-8674(00)89342-3;
RA Li L., Francke U., Cohen S.N.;
RL Cell 93:661-661(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [4]
RP ALTERNATIVE SPLICING (ISOFORM 2).
RX PubMed=9366528; DOI=10.1038/sj.onc.1201591;
RA Gayther S.A., Barski P., Batley S.J., Li L., de Foy K.A., Cohen S.N.,
RA Ponder B.A., Caldas C.;
RT "Aberrant splicing of the TSG101 and FHIT genes occurs frequently in
RT multiple malignancies and in normal tissues and mimics alterations
RT previously described in tumours.";
RL Oncogene 15:2119-2126(1997).
RN [5]
RP ALTERNATIVE SPLICING.
RX PubMed=9242438;
RA Lee M.P., Feinberg A.P.;
RT "Aberrant splicing but not mutations of TSG101 in human breast cancer.";
RL Cancer Res. 57:3131-3134(1997).
RN [6]
RP ALTERNATIVE SPLICING.
RX PubMed=9840940; DOI=10.1038/sj.onc.1202529;
RA Wagner K.-U., Dierisseau P., Rucker E.B. III, Robinson G.W.,
RA Hennighausen L.;
RT "Genomic architecture and transcriptional activation of the mouse and human
RT tumor susceptibility gene TSG101: common types of shorter transcripts are
RT true alternative splice variants.";
RL Oncogene 17:2761-2770(1998).
RN [7]
RP INTERACTION WITH DMAP1.
RX PubMed=10888872; DOI=10.1038/77023;
RA Rountree M.R., Bachman K.E., Baylin S.B.;
RT "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at
RT replication foci.";
RL Nat. Genet. 25:269-277(2000).
RN [8]
RP INTERACTION WITH HIV-1 P6 (MICROBIAL INFECTION) AND UBIQUITIN.
RX PubMed=11595185; DOI=10.1016/s0092-8674(01)00506-2;
RA Garrus J.E., von Schwedler U.K., Pornillos O.W., Morham S.G., Zavitz K.H.,
RA Wang H.E., Wettstein D.A., Stray K.M., Cote M., Rich R.L., Myszka D.G.,
RA Sundquist W.I.;
RT "Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1
RT budding.";
RL Cell 107:55-65(2001).
RN [9]
RP INTERACTION WITH HIV-1 P6 (MICROBIAL INFECTION).
RX PubMed=11427703; DOI=10.1073/pnas.131059198;
RA VerPlank L., Bouamr F., LaGrassa T.J., Agresta B., Kikonyogo A., Leis J.,
RA Carter C.A.;
RT "Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L
RT domain in HIV type 1 Pr55(Gag).";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7724-7729(2001).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11916981; DOI=10.1083/jcb.200112080;
RA Bishop N., Horman A., Woodman P.;
RT "Mammalian class E vps proteins recognize ubiquitin and act in the removal
RT of endosomal protein-ubiquitin conjugates.";
RL J. Cell Biol. 157:91-101(2002).
RN [11]
RP SELF-ASSOCIATION, INTERACTION WITH PDCD6IP; VPS28; SNF8 AND VPS36, AND
RP MUTAGENESIS OF MET-95.
RX PubMed=14505570; DOI=10.1016/s0092-8674(03)00714-1;
RA von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y.,
RA Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A.,
RA Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.;
RT "The protein network of HIV budding.";
RL Cell 114:701-713(2003).
RN [12]
RP INTERACTION WITH HIV-1 GAG (MICROBIAL INFECTION) AND HGS, AND
RP SELF-ASSOCIATION.
RX PubMed=12900394; DOI=10.1083/jcb.200302138;
RA Pornillos O., Higginson D.S., Stray K.M., Fisher R.D., Garrus J.E.,
RA Payne M., He G.P., Wang H.E., Morham S.G., Sundquist W.I.;
RT "HIV Gag mimics the Tsg101-recruiting activity of the human Hrs protein.";
RL J. Cell Biol. 162:425-434(2003).
RN [13]
RP INTERACTION WITH EBOLA VIRUS VP40 (MICROBIAL INFECTION).
RX PubMed=12559917; DOI=10.1016/s0022-2836(02)01406-7;
RA Timmins J., Schoehn G., Ricard-Blum S., Scianimanico S., Vernet T.,
RA Ruigrok R.W., Weissenhorn W.;
RT "Ebola virus matrix protein VP40 interaction with human cellular factors
RT Tsg101 and Nedd4.";
RL J. Mol. Biol. 326:493-502(2003).
RN [14]
RP INTERACTION WITH HTLV-1 GAG (MICROBIAL INFECTION).
RX PubMed=14581525; DOI=10.1128/jvi.77.22.11882-11895.2003;
RA Bouamr F., Melillo J.A., Wang M.Q., Nagashima K., de Los Santos M.,
RA Rein A., Goff S.P.;
RT "PPPYVEPTAP motif is the late domain of human T-cell leukemia virus type 1
RT Gag and mediates its functional interaction with cellular proteins Nedd4
RT and Tsg101.";
RL J. Virol. 77:11882-11895(2003).
RN [15]
RP MUTAGENESIS OF ASN-45 AND MET-95.
RX PubMed=12802020; DOI=10.1073/pnas.0932599100;
RA Lu Q., Hope L.W., Brasch M., Reinhard C., Cohen S.N.;
RT "TSG101 interaction with HRS mediates endosomal trafficking and receptor
RT down-regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7626-7631(2003).
RN [16]
RP SELF-ASSOCIATION, AND INTERACTION WITH PDCD6IP AND EIAV P9 (MICROBIAL
RP INFECTION).
RX PubMed=14519844; DOI=10.1073/pnas.2133846100;
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RT "Divergent retroviral late-budding domains recruit vacuolar protein sorting
RT factors by using alternative adaptor proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
RN [17]
RP ERRATUM OF PUBMED:14519844.
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RL Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
RN [18]
RP UBIQUITINATION BY LRSAM1.
RX PubMed=15256501; DOI=10.1101/gad.294904;
RA Amit I., Yakir L., Katz M., Zwang Y., Marmor M.D., Citri A., Shtiegman K.,
RA Alroy I., Tuvia S., Reiss Y., Roubini E., Cohen M., Wides R., Bacharach E.,
RA Schubert U., Yarden Y.;
RT "Tal, a Tsg101-specific E3 ubiquitin ligase, regulates receptor endocytosis
RT and retrovirus budding.";
RL Genes Dev. 18:1737-1752(2004).
RN [19]
RP INTERACTION WITH VPS37A AND VPS37B, AND MUTAGENESIS OF MET-95.
RX PubMed=15218037; DOI=10.1074/jbc.m405226200;
RA Stuchell M.D., Garrus J.E., Mueller B., Stray K.M., Ghaffarian S.,
RA McKinnon R., Kraeusslich H.-G., Morham S.G., Sundquist W.I.;
RT "The human endosomal sorting complex required for transport (ESCRT-I) and
RT its role in HIV-1 budding.";
RL J. Biol. Chem. 279:36059-36071(2004).
RN [20]
RP INTERACTION WITH GGA1.
RX PubMed=15143060; DOI=10.1074/jbc.m402183200;
RA Mattera R., Puertollano R., Smith W.J., Bonifacino J.S.;
RT "The trihelical bundle subdomain of the GGA proteins interacts with
RT multiple partners through overlapping but distinct sites.";
RL J. Biol. Chem. 279:31409-31418(2004).
RN [21]
RP INTERACTION WITH GGA3.
RX PubMed=15039775; DOI=10.1038/ncb1106;
RA Puertollano R., Bonifacino J.S.;
RT "Interactions of GGA3 with the ubiquitin sorting machinery.";
RL Nat. Cell Biol. 6:244-251(2004).
RN [22]
RP INTERACTION WITH VPS37C, AND MUTAGENESIS OF 368-ARG--PHE-371.
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 [23]
RP INTERACTION WITH HUMAN SPUMARETROVIRUS GAG (MICROBIAL INFECTION).
RX PubMed=15858022; DOI=10.1128/jvi.79.10.6392-6399.2005;
RA Patton G.S., Morris S.A., Chung W., Bieniasz P.D., McClure M.O.;
RT "Identification of domains in gag important for prototypic foamy virus
RT egress.";
RL J. Virol. 79:6392-6399(2005).
RN [24]
RP INTERACTION WITH LASSA VIRUS RING FINGER PROTEIN Z (MICROBIAL INFECTION).
RX PubMed=16571837; DOI=10.1128/jvi.80.8.4191-4195.2006;
RA Urata S., Noda T., Kawaoka Y., Yokosawa H., Yasuda J.;
RT "Cellular factors required for Lassa virus budding.";
RL J. Virol. 80:4191-4195(2006).
RN [25]
RP INTERACTION WITH VPS28; VPS37A; VPS37B; VPS37C; VPS37D; MVB12A AND MVB12B,
RP AND RECONSTITUTION OF THE ESCRT-I COMPLEX.
RX PubMed=18005716; DOI=10.1016/j.chom.2007.06.003;
RA Morita E., Sandrin V., Alam S.L., Eckert D.M., Gygi S.P., Sundquist W.I.;
RT "Identification of human MVB12 proteins as ESCRT-I subunits that function
RT in HIV budding.";
RL Cell Host Microbe 2:41-53(2007).
RN [26]
RP FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH CEP55;
RP CD2AP; IQGAP1 AND ROCK1, AND MUTAGENESIS OF 158-PRO--ASN-160.
RX PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
RA Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K.,
RA Sundquist W.I.;
RT "Human ESCRT and ALIX proteins interact with proteins of the midbody and
RT function in cytokinesis.";
RL EMBO J. 26:4215-4227(2007).
RN [27]
RP INTERACTION WITH MGRN1, UBIQUITINATION BY MGRN1, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ASN-45 AND MET-95.
RX PubMed=17229889; DOI=10.1091/mbc.e06-09-0787;
RA Kim B.Y., Olzmann J.A., Barsh G.S., Chin L.S., Li L.;
RT "Spongiform neurodegeneration-associated E3 ligase Mahogunin ubiquitylates
RT TSG101 and regulates endosomal trafficking.";
RL Mol. Biol. Cell 18:1129-1142(2007).
RN [28]
RP FUNCTION IN CYTOKINESIS, FUNCTION IN HIV-1 BUDDING, SUBCELLULAR LOCATION,
RP SELF-ASSOCIATION, INTERACTION WITH CEP55; HSG; VPS28; VPS37A; VPS37B;
RP VPS37C; VPS37D; PDCD6IP; LRSAM1; HIV-1 GAG AND EBOLA VIRUS VP40, AND
RP MUTAGENESIS OF 158-PRO--SER-162.
RX PubMed=17556548; DOI=10.1126/science.1143422;
RA Carlton J.G., Martin-Serrano J.;
RT "Parallels between cytokinesis and retroviral budding: a role for the ESCRT
RT machinery.";
RL Science 316:1908-1912(2007).
RN [29]
RP INTERACTION WITH PDCD6.
RX PubMed=18256029; DOI=10.1074/jbc.m800717200;
RA Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T.,
RA Maki M.;
RT "Identification of Alix-type and non-Alix-type ALG-2-binding sites in human
RT phospholipid scramblase 3: differential binding to an alternatively spliced
RT isoform and amino acid-substituted mutants.";
RL J. Biol. Chem. 283:9623-9632(2008).
RN [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [31]
RP INTERACTION WITH PDCD6IP.
RX PubMed=19520058; DOI=10.1016/j.bbrc.2009.06.015;
RA Okumura M., Ichioka F., Kobayashi R., Suzuki H., Yoshida H., Shibata H.,
RA Maki M.;
RT "Penta-EF-hand protein ALG-2 functions as a Ca2+-dependent adaptor that
RT bridges Alix and TSG101.";
RL Biochem. Biophys. Res. Commun. 386:237-241(2009).
RN [32]
RP INTERACTION WITH MGRN1, AND UBIQUITINATION BY MGRN1.
RX PubMed=19703557; DOI=10.1016/j.bbadis.2009.08.009;
RA Jiao J., Sun K., Walker W.P., Bagher P., Cota C.D., Gunn T.M.;
RT "Abnormal regulation of TSG101 in mice with spongiform neurodegeneration.";
RL Biochim. Biophys. Acta 1792:1027-1035(2009).
RN [33]
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 [34]
RP FUNCTION, SUBUNIT, AND IDENTIFICATION IN AN ESCRT-I COMPLEX WITH UBAP1.
RX PubMed=21757351; DOI=10.1016/j.cub.2011.06.028;
RA Stefani F., Zhang L., Taylor S., Donovan J., Rollinson S., Doyotte A.,
RA Brownhill K., Bennion J., Pickering-Brown S., Woodman P.;
RT "UBAP1 is a component of an endosome-specific ESCRT-I complex that is
RT essential for MVB sorting.";
RL Curr. Biol. 21:1245-1250(2011).
RN [35]
RP INTERACTION WITH HEPATITIS E VIRUS PROTEIN ORF3.
RX PubMed=21068219; DOI=10.1099/vir.0.025791-0;
RA Nagashima S., Takahashi M., Jirintai S., Tanaka T., Yamada K.,
RA Nishizawa T., Okamoto H.;
RT "A PSAP motif in the ORF3 protein of hepatitis E virus is necessary for
RT virion release from infected cells.";
RL J. Gen. Virol. 92:269-278(2011).
RN [36]
RP INTERACTION WITH ARRDC1.
RX PubMed=21191027; DOI=10.1128/jvi.02045-10;
RA Rauch S., Martin-Serrano J.;
RT "Multiple interactions between the ESCRT machinery and arrestin-related
RT proteins: implications for PPXY-dependent budding.";
RL J. Virol. 85:3546-3556(2011).
RN [37]
RP INTERACTION WITH LITAF, AND 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 [38]
RP FUNCTION.
RX PubMed=22660413; DOI=10.1038/ncb2502;
RA Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G., Geeraerts A.,
RA Ivarsson Y., Depoortere F., Coomans C., Vermeiren E., Zimmermann P.,
RA David G.;
RT "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.";
RL Nat. Cell Biol. 14:677-685(2012).
RN [39]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [40]
RP FUNCTION, INTERACTION WITH ARRDC1, AND MUTAGENESIS OF MET-95.
RX PubMed=22315426; DOI=10.1073/pnas.1200448109;
RA Nabhan J.F., Hu R., Oh R.S., Cohen S.N., Lu Q.;
RT "Formation and release of arrestin domain-containing protein 1-mediated
RT microvesicles (ARMMs) at plasma membrane by recruitment of TSG101
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:4146-4151(2012).
RN [41]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [42]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [43]
RP STRUCTURE BY NMR OF 1-145, INTERACTION WITH HIV-1 P6 (MICROBIAL INFECTION)
RP AND UBIQUITIN, AND MUTAGENESIS OF VAL-43; ASN-45; ASP-46; TYR-63; PHE-88;
RP VAL-89; MET-95 AND VAL-141.
RX PubMed=12006492; DOI=10.1093/emboj/21.10.2397;
RA Pornillos O.W., Alam S.L., Rich R.L., Myszka D.G., Davis D.R.,
RA Sundquist W.I.;
RT "Structure and functional interactions of the Tsg101 UEV domain.";
RL EMBO J. 21:2397-2406(2002).
RN [44]
RP STRUCTURE BY NMR OF 1-145.
RX PubMed=12379843; DOI=10.1038/nsb856;
RA Pornillos O., Alam S.L., Davis D.R., Sundquist W.I.;
RT "Structure of the Tsg101 UEV domain in complex with the PTAP motif of the
RT HIV-1 p6 protein.";
RL Nat. Struct. Biol. 9:812-817(2002).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-145 IN COMPLEX WITH UBIQUITIN.
RX PubMed=15053872; DOI=10.1016/s1097-2765(04)00129-7;
RA Sundquist W.I., Schubert H.L., Kelly B.N., Hill G.C., Holton J.M.,
RA Hill C.P.;
RT "Ubiquitin recognition by the human TSG101 protein.";
RL Mol. Cell 13:783-789(2004).
RN [46]
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 1-145.
RX PubMed=16552148; DOI=10.1107/s0907444906005221;
RA Palencia A., Martinez J.C., Mateo P.L., Luque I., Camara-Artigas A.;
RT "Structure of human TSG101 UEV domain.";
RL Acta Crystallogr. D 62:458-464(2006).
RN [47]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 2-145 IN COMPLEX WITH HIV-1 GAG P6
RP PEPTIDE (MICROBIAL INFECTION), FUNCTION, AND SUBUNIT.
RX PubMed=21070952; DOI=10.1016/j.str.2010.08.010;
RA Im Y.J., Kuo L., Ren X., Burgos P.V., Zhao X.Z., Liu F., Burke T.R. Jr.,
RA Bonifacino J.S., Freed E.O., Hurley J.H.;
RT "Crystallographic and functional analysis of the ESCRT-I /HIV-1 Gag PTAP
RT interaction.";
RL Structure 18:1536-1547(2010).
RN [48]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-145 IN COMPLEX WITH HIV-1 GAG P6
RP PEPTIDE (MICROBIAL INFECTION), AND SUBUNIT.
RX PubMed=21643473; DOI=10.1021/ml1002579;
RA Kim S.E., Liu F., Im Y.J., Stephen A.G., Fivash M.J., Waheed A.A.,
RA Freed E.O., Fisher R.J., Hurley J.H., Burke T.R. Jr.;
RT "Elucidation of new binding interactions with the tumor susceptibility gene
RT 101 (Tsg101) protein using modified HIV-1 Gag-p6 derived peptide ligands.";
RL ACS Med. Chem. Lett. 2:337-341(2011).
CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular
CC trafficking process. Binds to ubiquitinated cargo proteins and is
CC required for the sorting of endocytic ubiquitinated cargos into
CC multivesicular bodies (MVBs). Mediates the association between the
CC ESCRT-0 and ESCRT-I complex. Required for completion of cytokinesis;
CC the function requires CEP55. May be involved in cell growth and
CC differentiation. Acts as a negative growth regulator. Involved in the
CC budding of many viruses through an interaction with viral proteins that
CC contain a late-budding motif P-[ST]-A-P. This interaction is essential
CC for viral particle budding of numerous retroviruses. Required for the
CC exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). It may
CC also play a role in the extracellular release of microvesicles that
CC differ from the exosomes (PubMed:22315426).
CC {ECO:0000269|PubMed:11916981, ECO:0000269|PubMed:17556548,
CC ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:21070952,
CC ECO:0000269|PubMed:21757351, ECO:0000269|PubMed:22315426,
CC ECO:0000269|PubMed:22660413}.
CC -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I) which consists of TSG101, VPS28, a VPS37
CC protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1 stoichiometry
CC (PubMed:18005716). Interacts with VPS37A, VPS37B and VPS37C
CC (PubMed:15218037, PubMed:15509564). Interacts with DMAP1
CC (PubMed:10888872). Interacts with ubiquitin (PubMed:11595185).
CC Interacts with stathmin, GMCL and AATF (By similarity). Component of an
CC ESCRT-I complex (endosomal sorting complex required for transport I)
CC which consists of TSG101, VPS28, VPS37A and UBAP1 in a 1:1:1:1
CC stoichiometry (PubMed:21757351). Interacts with HGS; the interaction
CC mediates the association with the ESCRT-0 complex. Interacts with GGA1
CC and GGA3 (PubMed:15143060, PubMed:15039775). Interacts (via UEV domain)
CC with PDCD6IP/AIP1 (PubMed:14505570, PubMed:14519844). Interacts with
CC VPS28, SNF8 and VPS36 (PubMed:14505570). Self-associates
CC (PubMed:14505570, PubMed:14519844). Interacts with MVB12A; the
CC association appears to be mediated by the TSG101-VPS37 binary
CC subcomplex. Interacts with VPS37D. Interacts with LRSAM1. Interacts
CC with CEP55; the interaction is required for cytokinesis but not for
CC viral budding (PubMed:17853893). Interacts with PDCD6
CC (PubMed:18256029). Interacts with LITAF (PubMed:23166352). Interacts
CC with MGRN1 (PubMed:17229889). Interacts with ARRDC1; recruits TSG101 to
CC the plasma membrane (PubMed:21191027, PubMed:22315426). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q6IRE4, ECO:0000269|PubMed:10888872,
CC ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:15039775,
CC ECO:0000269|PubMed:15053872, ECO:0000269|PubMed:15143060,
CC ECO:0000269|PubMed:15218037, ECO:0000269|PubMed:15509564,
CC ECO:0000269|PubMed:15858022, ECO:0000269|PubMed:17229889,
CC ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893,
CC ECO:0000269|PubMed:18005716, ECO:0000269|PubMed:18256029,
CC ECO:0000269|PubMed:19520058, ECO:0000269|PubMed:19703557,
CC ECO:0000269|PubMed:21191027, ECO:0000269|PubMed:21757351,
CC ECO:0000269|PubMed:22315426, ECO:0000269|PubMed:23166352}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 p6.
CC {ECO:0000269|PubMed:11427703, ECO:0000269|PubMed:11595185,
CC ECO:0000269|PubMed:12900394, ECO:0000269|PubMed:21070952,
CC ECO:0000269|PubMed:21643473}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human spumavirus Gag.
CC {ECO:0000269|PubMed:15858022}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 Gag.
CC {ECO:0000269|PubMed:14581525}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Ebola virus VP40.
CC {ECO:0000269|PubMed:12559917}.
CC -!- SUBUNIT: (Microbial infection) Interacts with EIAV p9; the interaction
CC has been shown in vitro. {ECO:0000269|PubMed:14519844}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Lassa virus protein Z.
CC {ECO:0000269|PubMed:16571837}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis E virus protein
CC ORF3. {ECO:0000269|PubMed:21068219}.
CC -!- INTERACTION:
CC Q99816; Q96IF1: AJUBA; NbExp=4; IntAct=EBI-346882, EBI-949782;
CC Q99816; O95429: BAG4; NbExp=3; IntAct=EBI-346882, EBI-2949658;
CC Q99816; Q9ULD4-2: BRPF3; NbExp=3; IntAct=EBI-346882, EBI-23662416;
CC Q99816; Q8TC20-4: CAGE1; NbExp=3; IntAct=EBI-346882, EBI-11522698;
CC Q99816; Q9Y3M2: CBY1; NbExp=3; IntAct=EBI-346882, EBI-947308;
CC Q99816; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-346882, EBI-347573;
CC Q99816; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-346882, EBI-10175300;
CC Q99816; Q9Y5K6: CD2AP; NbExp=2; IntAct=EBI-346882, EBI-298152;
CC Q99816; Q53EZ4: CEP55; NbExp=24; IntAct=EBI-346882, EBI-747776;
CC Q99816; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-346882, EBI-11522539;
CC Q99816; Q96RK0: CIC; NbExp=2; IntAct=EBI-346882, EBI-945857;
CC Q99816; Q9UER7: DAXX; NbExp=4; IntAct=EBI-346882, EBI-77321;
CC Q99816; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-346882, EBI-1752811;
CC Q99816; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-346882, EBI-10175124;
CC Q99816; Q9NZ52: GGA3; NbExp=2; IntAct=EBI-346882, EBI-447404;
CC Q99816; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-346882, EBI-712073;
CC Q99816; Q96CS2: HAUS1; NbExp=6; IntAct=EBI-346882, EBI-2514791;
CC Q99816; O14964: HGS; NbExp=5; IntAct=EBI-346882, EBI-740220;
CC Q99816; Q96JZ2: HSH2D; NbExp=4; IntAct=EBI-346882, EBI-3919324;
CC Q99816; Q0VD86: INCA1; NbExp=3; IntAct=EBI-346882, EBI-6509505;
CC Q99816; P46940: IQGAP1; NbExp=5; IntAct=EBI-346882, EBI-297509;
CC Q99816; Q86T90: KIAA1328; NbExp=3; IntAct=EBI-346882, EBI-3437878;
CC Q99816; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-346882, EBI-2125614;
CC Q99816; A1A4E9: KRT13; NbExp=3; IntAct=EBI-346882, EBI-10171552;
CC Q99816; P08779: KRT16; NbExp=3; IntAct=EBI-346882, EBI-356410;
CC Q99816; P05783: KRT18; NbExp=4; IntAct=EBI-346882, EBI-297888;
CC Q99816; Q15323: KRT31; NbExp=6; IntAct=EBI-346882, EBI-948001;
CC Q99816; O76011: KRT34; NbExp=5; IntAct=EBI-346882, EBI-1047093;
CC Q99816; Q92764: KRT35; NbExp=3; IntAct=EBI-346882, EBI-1058674;
CC Q99816; O95678: KRT75; NbExp=3; IntAct=EBI-346882, EBI-2949715;
CC Q99816; P80188: LCN2; NbExp=3; IntAct=EBI-346882, EBI-11911016;
CC Q99816; Q96PV6: LENG8; NbExp=3; IntAct=EBI-346882, EBI-739546;
CC Q99816; Q99732: LITAF; NbExp=3; IntAct=EBI-346882, EBI-725647;
CC Q99816; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-346882, EBI-739832;
CC Q99816; Q6UWE0: LRSAM1; NbExp=8; IntAct=EBI-346882, EBI-720984;
CC Q99816; Q14676: MDC1; NbExp=5; IntAct=EBI-346882, EBI-495644;
CC Q99816; O60291: MGRN1; NbExp=5; IntAct=EBI-346882, EBI-2129851;
CC Q99816; Q8WU39: MZB1; NbExp=3; IntAct=EBI-346882, EBI-7212043;
CC Q99816; Q9NR12: PDLIM7; NbExp=10; IntAct=EBI-346882, EBI-350517;
CC Q99816; Q96KN3: PKNOX2; NbExp=4; IntAct=EBI-346882, EBI-2692890;
CC Q99816; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-346882, EBI-1105153;
CC Q99816; Q9H3S7: PTPN23; NbExp=2; IntAct=EBI-346882, EBI-724478;
CC Q99816; Q13464: ROCK1; NbExp=4; IntAct=EBI-346882, EBI-876651;
CC Q99816; Q6ZMJ2-2: SCARA5; NbExp=3; IntAct=EBI-346882, EBI-12823227;
CC Q99816; O95295: SNAPIN; NbExp=3; IntAct=EBI-346882, EBI-296723;
CC Q99816; Q8N0S2: SYCE1; NbExp=6; IntAct=EBI-346882, EBI-6872807;
CC Q99816; Q86VP1: TAX1BP1; NbExp=6; IntAct=EBI-346882, EBI-529518;
CC Q99816; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-346882, EBI-1105213;
CC Q99816; Q15025: TNIP1; NbExp=3; IntAct=EBI-346882, EBI-357849;
CC Q99816; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-346882, EBI-2130429;
CC Q99816; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-346882, EBI-11059915;
CC Q99816; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-346882, EBI-739895;
CC Q99816; Q9UK41: VPS28; NbExp=10; IntAct=EBI-346882, EBI-727424;
CC Q99816; Q9UK41-2: VPS28; NbExp=6; IntAct=EBI-346882, EBI-12146727;
CC Q99816; Q8NEZ2: VPS37A; NbExp=6; IntAct=EBI-346882, EBI-2850578;
CC Q99816; Q8NEZ2-2: VPS37A; NbExp=5; IntAct=EBI-346882, EBI-10270911;
CC Q99816; Q9H9H4: VPS37B; NbExp=3; IntAct=EBI-346882, EBI-4400866;
CC Q99816; A5D8V6: VPS37C; NbExp=6; IntAct=EBI-346882, EBI-2559305;
CC Q99816; P49750: YLPM1; NbExp=2; IntAct=EBI-346882, EBI-712871;
CC Q99816; O95229: ZWINT; NbExp=3; IntAct=EBI-346882, EBI-1001132;
CC Q99816; Q99LI8: Hgs; Xeno; NbExp=3; IntAct=EBI-346882, EBI-2119135;
CC Q99816-1; O14964: HGS; NbExp=2; IntAct=EBI-15891993, EBI-740220;
CC Q99816-1; PRO_0000038598 [P04591]: gag; Xeno; NbExp=3; IntAct=EBI-15891993, EBI-10634977;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17853893}. Early
CC endosome membrane {ECO:0000269|PubMed:23166352}; Peripheral membrane
CC protein {ECO:0000305|PubMed:23166352}; Cytoplasmic side
CC {ECO:0000305|PubMed:23166352}. Late endosome membrane
CC {ECO:0000269|PubMed:11916981, ECO:0000269|PubMed:17229889}; Peripheral
CC membrane protein. Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:17853893}. Midbody, Midbody ring
CC {ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893}. Nucleus
CC {ECO:0000269|PubMed:17229889}. Note=Mainly cytoplasmic. Membrane-
CC associated when active and soluble when inactive. Nuclear localization
CC is cell cycle-dependent. Interaction with CEP55 is required for
CC localization to the midbody during cytokinesis.
CC {ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist. Several shorter isoforms
CC are detected in primary breast cancers and other tumors.;
CC Name=1;
CC IsoId=Q99816-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99816-2; Sequence=VSP_004440;
CC -!- TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal,
CC kidney and pancreas.
CC -!- DOMAIN: The UEV domain is required for the interaction of the complex
CC with ubiquitin. It also mediates the interaction with PTAP/PSAP motifs
CC of HIV-1 P6 protein and human spumaretrovirus Gag protein.
CC -!- DOMAIN: The coiled coil domain may interact with stathmin.
CC -!- DOMAIN: The UEV domain binds ubiquitin and P-[ST]-A-P peptide motif
CC independently.
CC -!- PTM: Monoubiquitinated at multiple sites by LRSAM1 and by MGRN1.
CC Ubiquitination inactivates it, possibly by regulating its shuttling
CC between an active membrane-bound protein and an inactive soluble form.
CC Ubiquitination by MGRN1 requires the presence of UBE2D1.
CC {ECO:0000269|PubMed:15256501, ECO:0000269|PubMed:17229889,
CC ECO:0000269|PubMed:19703557}.
CC -!- MISCELLANEOUS: [Isoform 2]: Detected in normal as well as cancer
CC tissues. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UEV
CC subfamily. {ECO:0000305}.
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DR EMBL; U82130; AAC52083.1; -; mRNA.
DR EMBL; BC002487; AAH02487.1; -; mRNA.
DR CCDS; CCDS7842.1; -. [Q99816-1]
DR RefSeq; NP_006283.1; NM_006292.3. [Q99816-1]
DR PDB; 1KPP; NMR; -; A=1-145.
DR PDB; 1KPQ; NMR; -; A=1-145.
DR PDB; 1M4P; NMR; -; A=1-145.
DR PDB; 1M4Q; NMR; -; A=1-145.
DR PDB; 1S1Q; X-ray; 2.00 A; A/C=1-145.
DR PDB; 2F0R; X-ray; 2.26 A; A/B=1-145.
DR PDB; 3IV1; X-ray; 2.50 A; A/B/C/D/E/F/G/H=229-304.
DR PDB; 3OBQ; X-ray; 1.40 A; A=2-145.
DR PDB; 3OBS; X-ray; 1.50 A; A=2-145.
DR PDB; 3OBU; X-ray; 1.60 A; A=2-145.
DR PDB; 3OBX; X-ray; 1.60 A; A=2-145.
DR PDB; 3P9G; X-ray; 1.80 A; A=2-145.
DR PDB; 3P9H; X-ray; 1.80 A; A=2-145.
DR PDB; 4EJE; X-ray; 2.20 A; A/B=1-145.
DR PDB; 4YC1; X-ray; 2.00 A; A/B/C=1-145.
DR PDB; 4ZNY; X-ray; 2.40 A; A=4-145.
DR PDB; 5VKG; NMR; -; A=2-145.
DR PDB; 6UD0; NMR; -; C=1-145.
DR PDB; 6VME; X-ray; 2.19 A; B/F/G/H/I/J=308-388.
DR PDB; 7NLC; X-ray; 1.40 A; A=1-145.
DR PDBsum; 1KPP; -.
DR PDBsum; 1KPQ; -.
DR PDBsum; 1M4P; -.
DR PDBsum; 1M4Q; -.
DR PDBsum; 1S1Q; -.
DR PDBsum; 2F0R; -.
DR PDBsum; 3IV1; -.
DR PDBsum; 3OBQ; -.
DR PDBsum; 3OBS; -.
DR PDBsum; 3OBU; -.
DR PDBsum; 3OBX; -.
DR PDBsum; 3P9G; -.
DR PDBsum; 3P9H; -.
DR PDBsum; 4EJE; -.
DR PDBsum; 4YC1; -.
DR PDBsum; 4ZNY; -.
DR PDBsum; 5VKG; -.
DR PDBsum; 6UD0; -.
DR PDBsum; 6VME; -.
DR PDBsum; 7NLC; -.
DR AlphaFoldDB; Q99816; -.
DR SMR; Q99816; -.
DR BioGRID; 113102; 256.
DR ComplexPortal; CPX-2505; ESCRT-I complex, VPS37B-MVB12A variant.
DR ComplexPortal; CPX-7146; ESCRT-I complex, VPS37A-MVB12B variant.
DR ComplexPortal; CPX-7147; ESCRT-I complex, VPS37C-MVB12A variant.
DR ComplexPortal; CPX-7148; ESCRT-I complex, VPS37D-MVB12A variant.
DR ComplexPortal; CPX-7162; ESCRT-I complex, VPS37A-MVB12A variant.
DR ComplexPortal; CPX-7164; ESCRT-I complex, VPS37B-MVB12B variant.
DR ComplexPortal; CPX-7166; ESCRT-I complex, VPS37C-MVB12B variant.
DR ComplexPortal; CPX-7167; ESCRT-I complex, VPS37D-MVB12B variant.
DR ComplexPortal; CPX-7181; ESCRT-I complex, VPS37A-UBAP1 variant.
DR ComplexPortal; CPX-7201; ESCRT-I complex, VPS37B-UBAP1 variant.
DR ComplexPortal; CPX-7202; ESCRT-I complex, VPS37C-UBAP1 variant.
DR ComplexPortal; CPX-7203; ESCRT-I complex, VPS37D-UBAP1 variant.
DR CORUM; Q99816; -.
DR DIP; DIP-31809N; -.
DR ELM; Q99816; -.
DR IntAct; Q99816; 259.
DR MINT; Q99816; -.
DR STRING; 9606.ENSP00000251968; -.
DR BindingDB; Q99816; -.
DR ChEMBL; CHEMBL6157; -.
DR MoonDB; Q99816; Curated.
DR GlyGen; Q99816; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99816; -.
DR PhosphoSitePlus; Q99816; -.
DR BioMuta; TSG101; -.
DR DMDM; 9789790; -.
DR EPD; Q99816; -.
DR jPOST; Q99816; -.
DR MassIVE; Q99816; -.
DR MaxQB; Q99816; -.
DR PaxDb; Q99816; -.
DR PeptideAtlas; Q99816; -.
DR PRIDE; Q99816; -.
DR ProteomicsDB; 78490; -. [Q99816-1]
DR ProteomicsDB; 78491; -. [Q99816-2]
DR Antibodypedia; 1752; 490 antibodies from 40 providers.
DR DNASU; 7251; -.
DR Ensembl; ENST00000251968.4; ENSP00000251968.3; ENSG00000074319.13. [Q99816-1]
DR GeneID; 7251; -.
DR KEGG; hsa:7251; -.
DR MANE-Select; ENST00000251968.4; ENSP00000251968.3; NM_006292.4; NP_006283.1.
DR UCSC; uc001mor.4; human. [Q99816-1]
DR CTD; 7251; -.
DR DisGeNET; 7251; -.
DR GeneCards; TSG101; -.
DR HGNC; HGNC:15971; TSG101.
DR HPA; ENSG00000074319; Low tissue specificity.
DR MIM; 601387; gene.
DR neXtProt; NX_Q99816; -.
DR OpenTargets; ENSG00000074319; -.
DR PharmGKB; PA38068; -.
DR VEuPathDB; HostDB:ENSG00000074319; -.
DR eggNOG; KOG2391; Eukaryota.
DR GeneTree; ENSGT00940000153903; -.
DR HOGENOM; CLU_017548_1_1_1; -.
DR InParanoid; Q99816; -.
DR OMA; YMNFPQP; -.
DR OrthoDB; 1435538at2759; -.
DR PhylomeDB; Q99816; -.
DR TreeFam; TF312917; -.
DR PathwayCommons; Q99816; -.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins.
DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR SignaLink; Q99816; -.
DR BioGRID-ORCS; 7251; 746 hits in 1096 CRISPR screens.
DR ChiTaRS; TSG101; human.
DR EvolutionaryTrace; Q99816; -.
DR GeneWiki; TSG101; -.
DR GenomeRNAi; 7251; -.
DR Pharos; Q99816; Tbio.
DR PRO; PR:Q99816; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q99816; protein.
DR Bgee; ENSG00000074319; Expressed in oocyte and 208 other tissues.
DR ExpressionAtlas; Q99816; baseline and differential.
DR Genevisible; Q99816; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IMP:BHF-UCL.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005771; C:multivesicular body; TAS:HGNC-UCL.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0046790; F:virion binding; IDA:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; TAS:ParkinsonsUK-UCL.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:1990182; P:exosomal secretion; IEA:Ensembl.
DR GO; GO:0006858; P:extracellular transport; IMP:UniProtKB.
DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
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:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB.
DR GO; GO:2000397; P:positive regulation of ubiquitin-dependent endocytosis; IEA:Ensembl.
DR GO; GO:1903774; P:positive regulation of viral budding via host ESCRT complex; IMP:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
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:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
DR GO; GO:1903551; P:regulation of extracellular exosome assembly; IMP:UniProtKB.
DR GO; GO:0043405; P:regulation of MAP kinase activity; IMP:UniProtKB.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:HGNC-UCL.
DR GO; GO:0046755; P:viral budding; IMP:UniProtKB.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; TAS:ParkinsonsUK-UCL.
DR GO; GO:0019076; P:viral release from host cell; IMP:UniProtKB.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR037202; ESCRT_assembly_dom.
DR InterPro; IPR017916; SB_dom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR008883; UEV_N.
DR Pfam; PF05743; UEV; 1.
DR Pfam; PF09454; Vps23_core; 1.
DR SUPFAM; SSF140111; SSF140111; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS51312; SB; 1.
DR PROSITE; PS51322; UEV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Cytoskeleton; Endosome; Growth regulation;
KW Host-virus interaction; Membrane; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..390
FT /note="Tumor susceptibility gene 101 protein"
FT /id="PRO_0000082606"
FT DOMAIN 2..145
FT /note="UEV"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00652"
FT DOMAIN 322..390
FT /note="SB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00644"
FT REGION 158..162
FT /note="Interaction with CEP55"
FT REGION 198..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 235..316
FT /evidence="ECO:0000255"
FT MOTIF 320..323
FT /note="PTAP motif"
FT COMPBIAS 199..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 15..119
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004440"
FT VARIANT 167
FT /note="M -> I (in dbSNP:rs34385327)"
FT /id="VAR_034572"
FT MUTAGEN 43
FT /note="V->A: Reduces interaction with ubiquitin; inhibits
FT down-regulation of EGFR."
FT /evidence="ECO:0000269|PubMed:12006492"
FT MUTAGEN 45
FT /note="N->A: Reduces interaction with ubiquitin. No effect
FT on MGRN1-binding."
FT /evidence="ECO:0000269|PubMed:12006492,
FT ECO:0000269|PubMed:12802020, ECO:0000269|PubMed:17229889"
FT MUTAGEN 46
FT /note="D->A: Reduces interaction with ubiquitin."
FT /evidence="ECO:0000269|PubMed:12006492"
FT MUTAGEN 63
FT /note="Y->A: Reduces interaction with HIV-1 p6; impairs
FT HIV-1 budding."
FT /evidence="ECO:0000269|PubMed:12006492"
FT MUTAGEN 88
FT /note="F->A: Reduces interaction with ubiquitin; no effect
FT on in interaction with HIV-1 p6."
FT /evidence="ECO:0000269|PubMed:12006492"
FT MUTAGEN 89
FT /note="V->A: No change in interaction with p6; no effect on
FT HIV-1 budding."
FT /evidence="ECO:0000269|PubMed:12006492"
FT MUTAGEN 95
FT /note="M->A: Reduces interaction with VPS37B and HIV-1 p6;
FT abolishes interaction with PDCD6IP; impairs HIV-1 budding;
FT inhibits down-regulation of EGFR. Abolishes MGRN1-binding.
FT Loss of interaction with ARRDC1."
FT /evidence="ECO:0000269|PubMed:12006492,
FT ECO:0000269|PubMed:12802020, ECO:0000269|PubMed:14505570,
FT ECO:0000269|PubMed:15218037, ECO:0000269|PubMed:17229889,
FT ECO:0000269|PubMed:22315426"
FT MUTAGEN 141
FT /note="V->A: Reduces interaction with HIV-1 p6."
FT /evidence="ECO:0000269|PubMed:12006492"
FT MUTAGEN 158..162
FT /note="Missing: Abolishes interaction with CEP55 and
FT midbody localization; no effect on interaction with ESCRT-I
FT proteins, PDCD6IP and viral proteins."
FT /evidence="ECO:0000269|PubMed:17556548"
FT MUTAGEN 158..160
FT /note="PPN->AAA: Abolishes interaction with CEP55."
FT /evidence="ECO:0000269|PubMed:17853893"
FT MUTAGEN 368..371
FT /note="RKQF->AAAA: Loss of interaction with VPS28. No
FT effect on interaction with VPS37C."
FT /evidence="ECO:0000269|PubMed:15509564"
FT CONFLICT 343
FT /note="F -> L (in Ref. 3; AAH02487)"
FT /evidence="ECO:0000305"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:3OBQ"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:3OBQ"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:3OBQ"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:3OBQ"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:3P9G"
FT STRAND 51..62
FT /evidence="ECO:0007829|PDB:3OBQ"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:3OBQ"
FT TURN 78..82
FT /evidence="ECO:0007829|PDB:3OBQ"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:3OBQ"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3OBQ"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1S1Q"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1KPP"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:3OBQ"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:3OBQ"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:3OBQ"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:3OBQ"
FT HELIX 230..299
FT /evidence="ECO:0007829|PDB:3IV1"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:6VME"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:6VME"
FT HELIX 323..350
FT /evidence="ECO:0007829|PDB:6VME"
FT HELIX 356..383
FT /evidence="ECO:0007829|PDB:6VME"
SQ SEQUENCE 390 AA; 43944 MW; ADD6912FC22DF162 CRC64;
MAVSESQLKK MVSKYKYRDL TVRETVNVIT LYKDLKPVLD SYVFNDGSSR ELMNLTGTIP
VPYRGNTYNI PICLWLLDTY PYNPPICFVK PTSSMTIKTG KHVDANGKIY LPYLHEWKHP
QSDLLGLIQV MIVVFGDEPP VFSRPISASY PPYQATGPPN TSYMPGMPGG ISPYPSGYPP
NPSGYPGCPY PPGGPYPATT SSQYPSQPPV TTVGPSRDGT ISEDTIRASL ISAVSDKLRW
RMKEEMDRAQ AELNALKRTE EDLKKGHQKL EEMVTRLDQE VAEVDKNIEL LKKKDEELSS
ALEKMENQSE NNDIDEVIIP TAPLYKQILN LYAEENAIED TIFYLGEALR RGVIDLDVFL
KHVRLLSRKQ FQLRALMQKA RKTAGLSDLY
