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Tumor susceptibility gene 101 protein (ESCRT-I complex subunit TSG101)

 TS101_HUMAN             Reviewed;         390 AA.
Q99816; Q9BUM5;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 2.
28-MAR-2018, entry version 201.
RecName: Full=Tumor susceptibility gene 101 protein;
AltName: Full=ESCRT-I complex subunit TSG101;
Name=TSG101;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=9019400; DOI=10.1016/S0092-8674(00)81866-8;
Li L., Li X., Francke U., Cohen S.N.;
"The TSG101 tumor susceptibility gene is located in chromosome 11 band
p15 and is mutated in human breast cancer.";
Cell 88:143-154(1997).
[2]
ERRATUM, AND RETRACTION.
PubMed=9867424; DOI=10.1016/S0092-8674(00)89342-3;
Li L., Francke U., Cohen S.N.;
Cell 93:661-661(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
ALTERNATIVE SPLICING (ISOFORM 2).
PubMed=9366528; DOI=10.1038/sj.onc.1201591;
Gayther S.A., Barski P., Batley S.J., Li L., de Foy K.A., Cohen S.N.,
Ponder B.A., Caldas C.;
"Aberrant splicing of the TSG101 and FHIT genes occurs frequently in
multiple malignancies and in normal tissues and mimics alterations
previously described in tumours.";
Oncogene 15:2119-2126(1997).
[5]
ALTERNATIVE SPLICING.
PubMed=9242438;
Lee M.P., Feinberg A.P.;
"Aberrant splicing but not mutations of TSG101 in human breast
cancer.";
Cancer Res. 57:3131-3134(1997).
[6]
ALTERNATIVE SPLICING.
PubMed=9840940; DOI=10.1038/sj.onc.1202529;
Wagner K.-U., Dierisseau P., Rucker E.B. III, Robinson G.W.,
Hennighausen L.;
"Genomic architecture and transcriptional activation of the mouse and
human tumor susceptibility gene TSG101: common types of shorter
transcripts are true alternative splice variants.";
Oncogene 17:2761-2770(1998).
[7]
INTERACTION WITH DMAP1.
PubMed=10888872; DOI=10.1038/77023;
Rountree M.R., Bachman K.E., Baylin S.B.;
"DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at
replication foci.";
Nat. Genet. 25:269-277(2000).
[8]
INTERACTION WITH HIV-1 P6 AND UBIQUITIN.
PubMed=11595185; DOI=10.1016/S0092-8674(01)00506-2;
Garrus J.E., von Schwedler U.K., Pornillos O.W., Morham S.G.,
Zavitz K.H., Wang H.E., Wettstein D.A., Stray K.M., Cote M.,
Rich R.L., Myszka D.G., Sundquist W.I.;
"Tsg101 and the vacuolar protein sorting pathway are essential for
HIV-1 budding.";
Cell 107:55-65(2001).
[9]
INTERACTION WITH HIV-1 P6.
PubMed=11427703; DOI=10.1073/pnas.131059198;
VerPlank L., Bouamr F., LaGrassa T.J., Agresta B., Kikonyogo A.,
Leis J., Carter C.A.;
"Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the
L domain in HIV type 1 Pr55(Gag).";
Proc. Natl. Acad. Sci. U.S.A. 98:7724-7729(2001).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11916981; DOI=10.1083/jcb.200112080;
Bishop N., Horman A., Woodman P.;
"Mammalian class E vps proteins recognize ubiquitin and act in the
removal of endosomal protein-ubiquitin conjugates.";
J. Cell Biol. 157:91-101(2002).
[11]
SELF-ASSOCIATION, INTERACTION WITH PDCD6IP; VPS28; SNF8 AND VPS36, AND
MUTAGENESIS OF MET-95.
PubMed=14505570; DOI=10.1016/S0092-8674(03)00714-1;
von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y.,
Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A.,
Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.;
"The protein network of HIV budding.";
Cell 114:701-713(2003).
[12]
INTERACTION WITH HIV-1 GAG AND HGS, AND SELF-ASSOCIATION.
PubMed=12900394; DOI=10.1083/jcb.200302138;
Pornillos O., Higginson D.S., Stray K.M., Fisher R.D., Garrus J.E.,
Payne M., He G.P., Wang H.E., Morham S.G., Sundquist W.I.;
"HIV Gag mimics the Tsg101-recruiting activity of the human Hrs
protein.";
J. Cell Biol. 162:425-434(2003).
[13]
INTERACTION WITH EBOLA VIRUS VP40.
PubMed=12559917; DOI=10.1016/S0022-2836(02)01406-7;
Timmins J., Schoehn G., Ricard-Blum S., Scianimanico S., Vernet T.,
Ruigrok R.W., Weissenhorn W.;
"Ebola virus matrix protein VP40 interaction with human cellular
factors Tsg101 and Nedd4.";
J. Mol. Biol. 326:493-502(2003).
[14]
INTERACTION WITH HTLV-1 GAG.
PubMed=14581525; DOI=10.1128/JVI.77.22.11882-11895.2003;
Bouamr F., Melillo J.A., Wang M.Q., Nagashima K., de Los Santos M.,
Rein A., Goff S.P.;
"PPPYVEPTAP motif is the late domain of human T-cell leukemia virus
type 1 Gag and mediates its functional interaction with cellular
proteins Nedd4 and Tsg101.";
J. Virol. 77:11882-11895(2003).
[15]
MUTAGENESIS OF ASN-45 AND MET-95.
PubMed=12802020; DOI=10.1073/pnas.0932599100;
Lu Q., Hope L.W., Brasch M., Reinhard C., Cohen S.N.;
"TSG101 interaction with HRS mediates endosomal trafficking and
receptor down-regulation.";
Proc. Natl. Acad. Sci. U.S.A. 100:7626-7631(2003).
[16]
SELF-ASSOCIATION, AND INTERACTION WITH PDCD6IP AND EIAV P9.
PubMed=14519844; DOI=10.1073/pnas.2133846100;
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
"Divergent retroviral late-budding domains recruit vacuolar protein
sorting factors by using alternative adaptor proteins.";
Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
[17]
ERRATUM.
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
[18]
UBIQUITINATION BY LRSAM1.
PubMed=15256501; DOI=10.1101/gad.294904;
Amit I., Yakir L., Katz M., Zwang Y., Marmor M.D., Citri A.,
Shtiegman K., Alroy I., Tuvia S., Reiss Y., Roubini E., Cohen M.,
Wides R., Bacharach E., Schubert U., Yarden Y.;
"Tal, a Tsg101-specific E3 ubiquitin ligase, regulates receptor
endocytosis and retrovirus budding.";
Genes Dev. 18:1737-1752(2004).
[19]
INTERACTION WITH VPS37A AND VPS37B, AND MUTAGENESIS OF MET-95.
PubMed=15218037; DOI=10.1074/jbc.M405226200;
Stuchell M.D., Garrus J.E., Mueller B., Stray K.M., Ghaffarian S.,
McKinnon R., Kraeusslich H.-G., Morham S.G., Sundquist W.I.;
"The human endosomal sorting complex required for transport (ESCRT-I)
and its role in HIV-1 budding.";
J. Biol. Chem. 279:36059-36071(2004).
[20]
INTERACTION WITH GGA1.
PubMed=15143060; DOI=10.1074/jbc.M402183200;
Mattera R., Puertollano R., Smith W.J., Bonifacino J.S.;
"The trihelical bundle subdomain of the GGA proteins interacts with
multiple partners through overlapping but distinct sites.";
J. Biol. Chem. 279:31409-31418(2004).
[21]
INTERACTION WITH GGA3.
PubMed=15039775; DOI=10.1038/ncb1106;
Puertollano R., Bonifacino J.S.;
"Interactions of GGA3 with the ubiquitin sorting machinery.";
Nat. Cell Biol. 6:244-251(2004).
[22]
INTERACTION WITH VPS37C, AND MUTAGENESIS OF 368-ARG--PHE-371.
PubMed=15509564; DOI=10.1074/jbc.M410384200;
Eastman S.W., Martin-Serrano J., Chung W., Zang T., Bieniasz P.D.;
"Identification of human VPS37C, a component of endosomal sorting
complex required for transport-I important for viral budding.";
J. Biol. Chem. 280:628-636(2005).
[23]
INTERACTION WITH HUMAN SPUMARETROVIRUS GAG.
PubMed=15858022; DOI=10.1128/JVI.79.10.6392-6399.2005;
Patton G.S., Morris S.A., Chung W., Bieniasz P.D., McClure M.O.;
"Identification of domains in gag important for prototypic foamy virus
egress.";
J. Virol. 79:6392-6399(2005).
[24]
INTERACTION WITH LASSA VIRUS RING FINGER PROTEIN Z.
PubMed=16571837; DOI=10.1128/JVI.80.8.4191-4195.2006;
Urata S., Noda T., Kawaoka Y., Yokosawa H., Yasuda J.;
"Cellular factors required for Lassa virus budding.";
J. Virol. 80:4191-4195(2006).
[25]
INTERACTION WITH VPS28; VPS37A; VPS37B; VPS37C; VPS37D; MVB12A AND
MVB12B, AND RECONSTITUTION OF THE ESCRT-I COMPLEX.
PubMed=18005716; DOI=10.1016/j.chom.2007.06.003;
Morita E., Sandrin V., Alam S.L., Eckert D.M., Gygi S.P.,
Sundquist W.I.;
"Identification of human MVB12 proteins as ESCRT-I subunits that
function in HIV budding.";
Cell Host Microbe 2:41-53(2007).
[26]
FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH CEP55;
CD2AP; IQGAP1 AND ROCK1, AND MUTAGENESIS OF 158-PRO--ASN-160.
PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P.,
Rodesch C.K., Sundquist W.I.;
"Human ESCRT and ALIX proteins interact with proteins of the midbody
and function in cytokinesis.";
EMBO J. 26:4215-4227(2007).
[27]
INTERACTION WITH MGRN1, UBIQUITINATION BY MGRN1, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF ASN-45 AND MET-95.
PubMed=17229889; DOI=10.1091/mbc.E06-09-0787;
Kim B.Y., Olzmann J.A., Barsh G.S., Chin L.S., Li L.;
"Spongiform neurodegeneration-associated E3 ligase Mahogunin
ubiquitylates TSG101 and regulates endosomal trafficking.";
Mol. Biol. Cell 18:1129-1142(2007).
[28]
FUNCTION IN CYTOKINESIS, FUNCTION IN HIV-1 BUDDING, SUBCELLULAR
LOCATION, SELF-ASSOCIATION, INTERACTION WITH CEP55; HSG; VPS28;
VPS37A; VPS37B; VPS37C; VPS37D; PDCD6IP; LRSAM1; HIV-1 GAG AND EBOLA
VIRUS VP40, AND MUTAGENESIS OF 158-PRO--SER-162.
PubMed=17556548; DOI=10.1126/science.1143422;
Carlton J.G., Martin-Serrano J.;
"Parallels between cytokinesis and retroviral budding: a role for the
ESCRT machinery.";
Science 316:1908-1912(2007).
[29]
INTERACTION WITH PDCD6.
PubMed=18256029; DOI=10.1074/jbc.M800717200;
Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T.,
Maki M.;
"Identification of Alix-type and non-Alix-type ALG-2-binding sites in
human phospholipid scramblase 3: differential binding to an
alternatively spliced isoform and amino acid-substituted mutants.";
J. Biol. Chem. 283:9623-9632(2008).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[31]
INTERACTION WITH PDCD6IP.
PubMed=19520058; DOI=10.1016/j.bbrc.2009.06.015;
Okumura M., Ichioka F., Kobayashi R., Suzuki H., Yoshida H.,
Shibata H., Maki M.;
"Penta-EF-hand protein ALG-2 functions as a Ca2+-dependent adaptor
that bridges Alix and TSG101.";
Biochem. Biophys. Res. Commun. 386:237-241(2009).
[32]
INTERACTION WITH MGRN1, AND UBIQUITINATION BY MGRN1.
PubMed=19703557; DOI=10.1016/j.bbadis.2009.08.009;
Jiao J., Sun K., Walker W.P., Bagher P., Cota C.D., Gunn T.M.;
"Abnormal regulation of TSG101 in mice with spongiform
neurodegeneration.";
Biochim. Biophys. Acta 1792:1027-1035(2009).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[34]
FUNCTION, SUBUNIT, AND IDENTIFICATION IN AN ESCRT-I COMPLEX WITH
UBAP1.
PubMed=21757351; DOI=10.1016/j.cub.2011.06.028;
Stefani F., Zhang L., Taylor S., Donovan J., Rollinson S., Doyotte A.,
Brownhill K., Bennion J., Pickering-Brown S., Woodman P.;
"UBAP1 is a component of an endosome-specific ESCRT-I complex that is
essential for MVB sorting.";
Curr. Biol. 21:1245-1250(2011).
[35]
INTERACTION WITH ARRDC1.
PubMed=21191027; DOI=10.1128/JVI.02045-10;
Rauch S., Martin-Serrano J.;
"Multiple interactions between the ESCRT machinery and arrestin-
related proteins: implications for PPXY-dependent budding.";
J. Virol. 85:3546-3556(2011).
[36]
INTERACTION WITH LITAF, AND SUBCELLULAR LOCATION.
PubMed=23166352; DOI=10.1083/jcb.201204137;
Lee S.M., Chin L.S., Li L.;
"Charcot-Marie-Tooth disease-linked protein SIMPLE functions with the
ESCRT machinery in endosomal trafficking.";
J. Cell Biol. 199:799-816(2012).
[37]
FUNCTION.
PubMed=22660413; DOI=10.1038/ncb2502;
Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G.,
Geeraerts A., Ivarsson Y., Depoortere F., Coomans C., Vermeiren E.,
Zimmermann P., David G.;
"Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.";
Nat. Cell Biol. 14:677-685(2012).
[38]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[39]
FUNCTION, INTERACTION WITH ARRDC1, AND MUTAGENESIS OF MET-95.
PubMed=22315426; DOI=10.1073/pnas.1200448109;
Nabhan J.F., Hu R., Oh R.S., Cohen S.N., Lu Q.;
"Formation and release of arrestin domain-containing protein 1-
mediated microvesicles (ARMMs) at plasma membrane by recruitment of
TSG101 protein.";
Proc. Natl. Acad. Sci. U.S.A. 109:4146-4151(2012).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[41]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[42]
STRUCTURE BY NMR OF 1-145, INTERACTION WITH HIV-1 P6 AND UBIQUITIN,
AND MUTAGENESIS OF VAL-43; ASN-45; ASP-46; TYR-63; PHE-88; VAL-89;
MET-95 AND VAL-141.
PubMed=12006492; DOI=10.1093/emboj/21.10.2397;
Pornillos O.W., Alam S.L., Rich R.L., Myszka D.G., Davis D.R.,
Sundquist W.I.;
"Structure and functional interactions of the Tsg101 UEV domain.";
EMBO J. 21:2397-2406(2002).
[43]
STRUCTURE BY NMR OF 1-145.
PubMed=12379843; DOI=10.1038/nsb856;
Pornillos O., Alam S.L., Davis D.R., Sundquist W.I.;
"Structure of the Tsg101 UEV domain in complex with the PTAP motif of
the HIV-1 p6 protein.";
Nat. Struct. Biol. 9:812-817(2002).
[44]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-145 IN COMPLEX WITH
UBIQUITIN.
PubMed=15053872; DOI=10.1016/S1097-2765(04)00129-7;
Sundquist W.I., Schubert H.L., Kelly B.N., Hill G.C., Holton J.M.,
Hill C.P.;
"Ubiquitin recognition by the human TSG101 protein.";
Mol. Cell 13:783-789(2004).
[45]
X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 1-145.
PubMed=16552148; DOI=10.1107/S0907444906005221;
Palencia A., Martinez J.C., Mateo P.L., Luque I., Camara-Artigas A.;
"Structure of human TSG101 UEV domain.";
Acta Crystallogr. D 62:458-464(2006).
[46]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 2-145 IN COMPLEX WITH HIV-1
GAG P6 PEPTIDE, FUNCTION, AND SUBUNIT.
PubMed=21070952; DOI=10.1016/j.str.2010.08.010;
Im Y.J., Kuo L., Ren X., Burgos P.V., Zhao X.Z., Liu F.,
Burke T.R. Jr., Bonifacino J.S., Freed E.O., Hurley J.H.;
"Crystallographic and functional analysis of the ESCRT-I /HIV-1 Gag
PTAP interaction.";
Structure 18:1536-1547(2010).
[47]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-145 IN COMPLEX WITH HIV-1
GAG P6 PEPTIDE, AND SUBUNIT.
PubMed=21643473; DOI=10.1021/ml1002579;
Kim S.E., Liu F., Im Y.J., Stephen A.G., Fivash M.J., Waheed A.A.,
Freed E.O., Fisher R.J., Hurley J.H., Burke T.R. Jr.;
"Elucidation of new binding interactions with the tumor susceptibility
gene 101 (Tsg101) protein using modified HIV-1 Gag-p6 derived peptide
ligands.";
ACS Med. Chem. Lett. 2:337-341(2011).
-!- FUNCTION: Component of the ESCRT-I complex, a regulator of
vesicular trafficking process. Binds to ubiquitinated cargo
proteins and is required for the sorting of endocytic
ubiquitinated cargos into multivesicular bodies (MVBs). Mediates
the association between the ESCRT-0 and ESCRT-I complex. Required
for completion of cytokinesis; the function requires CEP55. May be
involved in cell growth and differentiation. Acts as a negative
growth regulator. Involved in the budding of many viruses through
an interaction with viral proteins that contain a late-budding
motif P-[ST]-A-P. This interaction is essential for viral particle
budding of numerous retroviruses. Required for the exosomal
release of SDCBP, CD63 and syndecan (PubMed:22660413). It may also
play a role in the extracellular release of microvesicles that
differ from the exosomes (PubMed:22315426).
{ECO:0000269|PubMed:11916981, ECO:0000269|PubMed:17556548,
ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:21070952,
ECO:0000269|PubMed:21757351, ECO:0000269|PubMed:22315426,
ECO:0000269|PubMed:22660413}.
-!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting
complex required for transport I) which consists of TSG101, VPS28,
a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1
stoichiometry (PubMed:18005716). Interacts with VPS37A, VPS37B and
VPS37C (PubMed:15218037, PubMed:15509564). Interacts with DMAP1
(PubMed:10888872). Interacts with ubiquitin (PubMed:11595185).
Interacts with stathmin, GMCL and AATF (By similarity). Component
of an ESCRT-I complex (endosomal sorting complex required for
transport I) which consists of TSG101, VPS28, VPS37A and UBAP1 in
a 1:1:1:1 stoichiometry (PubMed:21757351). Interacts with HGS; the
interaction mediates the association with the ESCRT-0 complex.
Interacts with GGA1 and GGA3 (PubMed:15143060, PubMed:15039775).
Interacts (via UEV domain) with PDCD6IP/AIP1 (PubMed:14505570,
PubMed:14519844). Interacts with VPS28, SNF8 and VPS36
(PubMed:14505570). Self-associates (PubMed:14505570,
PubMed:14519844). Interacts with MVB12A; the association appears
to be mediated by the TSG101-VPS37 binary subcomplex. Interacts
with VPS37D. Interacts with LRSAM1. Interacts with CEP55; the
interaction is required for cytokinesis but not for viral budding
(PubMed:17853893). Interacts with PDCD6 (PubMed:18256029).
Interacts with LITAF (PubMed:23166352). Interacts with HIV-1 p6
(PubMed:11595185, PubMed:11427703, PubMed:12006492,
PubMed:21070952, PubMed:21643473). Interacts with human spumavirus
Gag (PubMed:15858022). Interacts with HTLV-1 Gag
(PubMed:14581525). Interacts with Ebola virus VP40
(PubMed:12559917). Interacts with EIAV p9; the interaction has
been shown in vitro (PubMed:14519844). Interacts with MGRN1
(PubMed:17229889). Interacts with ARRDC1; recruits TSG101 to the
plasma membrane (PubMed:21191027, PubMed:22315426). {ECO:0000250,
ECO:0000250|UniProtKB:Q6IRE4, ECO:0000269|PubMed:10888872,
ECO:0000269|PubMed:11427703, ECO:0000269|PubMed:11595185,
ECO:0000269|PubMed:12006492, ECO:0000269|PubMed:12559917,
ECO:0000269|PubMed:12900394, ECO:0000269|PubMed:14505570,
ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:14581525,
ECO:0000269|PubMed:15039775, ECO:0000269|PubMed:15053872,
ECO:0000269|PubMed:15143060, ECO:0000269|PubMed:15218037,
ECO:0000269|PubMed:15509564, ECO:0000269|PubMed:15858022,
ECO:0000269|PubMed:16571837, ECO:0000269|PubMed:17229889,
ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893,
ECO:0000269|PubMed:18005716, ECO:0000269|PubMed:18256029,
ECO:0000269|PubMed:19520058, ECO:0000269|PubMed:19703557,
ECO:0000269|PubMed:21070952, ECO:0000269|PubMed:21191027,
ECO:0000269|PubMed:21643473, ECO:0000269|PubMed:21757351,
ECO:0000269|PubMed:22315426, ECO:0000269|PubMed:23166352}.
-!- INTERACTION:
O95429:BAG4; NbExp=4; IntAct=EBI-346882, EBI-2949658;
Q9Y5K6:CD2AP; NbExp=2; IntAct=EBI-346882, EBI-298152;
Q53EZ4:CEP55; NbExp=23; IntAct=EBI-346882, EBI-747776;
Q96MT8-3:CEP63; NbExp=4; IntAct=EBI-346882, EBI-11522539;
Q9UER7:DAXX; NbExp=4; IntAct=EBI-346882, EBI-77321;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-346882, EBI-10175124;
P04591:gag (xeno); NbExp=3; IntAct=EBI-15891993, EBI-10634977;
Q96CS2:HAUS1; NbExp=5; IntAct=EBI-346882, EBI-2514791;
O14964:HGS; NbExp=4; IntAct=EBI-346882, EBI-740220;
Q99LI8:Hgs (xeno); NbExp=5; IntAct=EBI-346882, EBI-2119135;
P46940:IQGAP1; NbExp=5; IntAct=EBI-346882, EBI-297509;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-346882, EBI-2125614;
A1A4E9:KRT13; NbExp=3; IntAct=EBI-346882, EBI-10171552;
P05783:KRT18; NbExp=3; IntAct=EBI-346882, EBI-297888;
Q15323:KRT31; NbExp=5; IntAct=EBI-346882, EBI-948001;
Q99732:LITAF; NbExp=3; IntAct=EBI-346882, EBI-725647;
Q8TBB1:LNX1; NbExp=4; IntAct=EBI-346882, EBI-739832;
Q6UWE0:LRSAM1; NbExp=9; IntAct=EBI-346882, EBI-720984;
O60291:MGRN1; NbExp=4; IntAct=EBI-346882, EBI-2129851;
Q9NR12:PDLIM7; NbExp=5; IntAct=EBI-346882, EBI-350517;
Q9H3S7:PTPN23; NbExp=2; IntAct=EBI-346882, EBI-724478;
Q13464:ROCK1; NbExp=4; IntAct=EBI-346882, EBI-876651;
Q8N0S2:SYCE1; NbExp=5; IntAct=EBI-346882, EBI-6872807;
Q86VP1:TAX1BP1; NbExp=7; IntAct=EBI-346882, EBI-529518;
Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-346882, EBI-739895;
Q9UK41:VPS28; NbExp=9; IntAct=EBI-346882, EBI-727424;
Q8NEZ2:VPS37A; NbExp=5; IntAct=EBI-346882, EBI-2850578;
Q8NEZ2-2:VPS37A; NbExp=5; IntAct=EBI-346882, EBI-10270911;
A5D8V6:VPS37C; NbExp=7; IntAct=EBI-346882, EBI-2559305;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17853893}.
Early endosome membrane {ECO:0000269|PubMed:23166352}; Peripheral
membrane protein {ECO:0000305|PubMed:23166352}; Cytoplasmic side
{ECO:0000305|PubMed:23166352}. Late endosome membrane
{ECO:0000269|PubMed:11916981, ECO:0000269|PubMed:17229889};
Peripheral membrane protein. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:17853893}.
Midbody, Midbody ring {ECO:0000269|PubMed:17556548,
ECO:0000269|PubMed:17853893}. Nucleus
{ECO:0000269|PubMed:17229889}. Note=Mainly cytoplasmic. Membrane-
associated when active and soluble when inactive. Nuclear
localization is cell cycle-dependent. Interaction with CEP55 is
required for localization to the midbody during cytokinesis.
{ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist. Several shorter
isoforms are detected in primary breast cancers and other
tumors.;
Name=1;
IsoId=Q99816-1; Sequence=Displayed;
Name=2;
IsoId=Q99816-2; Sequence=VSP_004440;
Note=Detected in normal as well as cancer tissues.;
-!- TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal,
kidney and pancreas.
-!- DOMAIN: The UEV domain is required for the interaction of the
complex with ubiquitin. It also mediates the interaction with
PTAP/PSAP motifs of HIV-1 P6 protein and human spumaretrovirus Gag
protein.
-!- DOMAIN: The coiled coil domain may interact with stathmin.
-!- DOMAIN: The UEV domain binds ubiquitin and P-[ST]-A-P peptide
motif independently.
-!- PTM: Monoubiquitinated at multiple sites by LRSAM1 and by MGRN1.
Ubiquitination inactivates it, possibly by regulating its
shuttling between an active membrane-bound protein and an inactive
soluble form. Ubiquitination by MGRN1 requires the presence of
UBE2D1. {ECO:0000269|PubMed:15256501, ECO:0000269|PubMed:17229889,
ECO:0000269|PubMed:19703557}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
UEV subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U82130; AAC52083.1; -; mRNA.
EMBL; BC002487; AAH02487.1; -; mRNA.
CCDS; CCDS7842.1; -. [Q99816-1]
RefSeq; NP_006283.1; NM_006292.3. [Q99816-1]
UniGene; Hs.523512; -.
PDB; 1KPP; NMR; -; A=1-145.
PDB; 1KPQ; NMR; -; A=1-145.
PDB; 1M4P; NMR; -; A=1-145.
PDB; 1M4Q; NMR; -; A=1-145.
PDB; 1S1Q; X-ray; 2.00 A; A/C=1-145.
PDB; 2F0R; X-ray; 2.26 A; A/B=1-145.
PDB; 3IV1; X-ray; 2.50 A; A/B/C/D/E/F/G/H=229-304.
PDB; 3OBQ; X-ray; 1.40 A; A=2-145.
PDB; 3OBS; X-ray; 1.50 A; A=2-145.
PDB; 3OBU; X-ray; 1.60 A; A=2-145.
PDB; 3OBX; X-ray; 1.60 A; A=2-145.
PDB; 3P9G; X-ray; 1.80 A; A=2-145.
PDB; 3P9H; X-ray; 1.80 A; A=2-145.
PDB; 4EJE; X-ray; 2.20 A; A/B=1-145.
PDB; 4YC1; X-ray; 2.00 A; A/B/C=1-145.
PDB; 4ZNY; X-ray; 2.40 A; A=4-145.
PDB; 5VKG; NMR; -; A=2-145.
PDBsum; 1KPP; -.
PDBsum; 1KPQ; -.
PDBsum; 1M4P; -.
PDBsum; 1M4Q; -.
PDBsum; 1S1Q; -.
PDBsum; 2F0R; -.
PDBsum; 3IV1; -.
PDBsum; 3OBQ; -.
PDBsum; 3OBS; -.
PDBsum; 3OBU; -.
PDBsum; 3OBX; -.
PDBsum; 3P9G; -.
PDBsum; 3P9H; -.
PDBsum; 4EJE; -.
PDBsum; 4YC1; -.
PDBsum; 4ZNY; -.
PDBsum; 5VKG; -.
ProteinModelPortal; Q99816; -.
SMR; Q99816; -.
BioGrid; 113102; 174.
CORUM; Q99816; -.
DIP; DIP-31809N; -.
ELM; Q99816; -.
IntAct; Q99816; 133.
MINT; Q99816; -.
STRING; 9606.ENSP00000251968; -.
BindingDB; Q99816; -.
ChEMBL; CHEMBL6157; -.
iPTMnet; Q99816; -.
PhosphoSitePlus; Q99816; -.
BioMuta; TSG101; -.
DMDM; 9789790; -.
EPD; Q99816; -.
MaxQB; Q99816; -.
PaxDb; Q99816; -.
PeptideAtlas; Q99816; -.
PRIDE; Q99816; -.
DNASU; 7251; -.
Ensembl; ENST00000251968; ENSP00000251968; ENSG00000074319. [Q99816-1]
GeneID; 7251; -.
KEGG; hsa:7251; -.
UCSC; uc001mor.4; human. [Q99816-1]
CTD; 7251; -.
DisGeNET; 7251; -.
EuPathDB; HostDB:ENSG00000074319.12; -.
GeneCards; TSG101; -.
HGNC; HGNC:15971; TSG101.
HPA; CAB004283; -.
HPA; HPA006161; -.
MalaCards; TSG101; -.
MIM; 601387; gene.
neXtProt; NX_Q99816; -.
OpenTargets; ENSG00000074319; -.
PharmGKB; PA38068; -.
eggNOG; KOG2391; Eukaryota.
eggNOG; ENOG410XT2Q; LUCA.
GeneTree; ENSGT00530000064004; -.
HOGENOM; HOG000247008; -.
HOVERGEN; HBG057450; -.
InParanoid; Q99816; -.
KO; K12183; -.
OMA; DHNGKVY; -.
OrthoDB; EOG091G0HRA; -.
PhylomeDB; Q99816; -.
TreeFam; TF312917; -.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins.
Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
ChiTaRS; TSG101; human.
EvolutionaryTrace; Q99816; -.
GeneWiki; TSG101; -.
GenomeRNAi; 7251; -.
PRO; PR:Q99816; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000074319; -.
CleanEx; HS_TSG101; -.
ExpressionAtlas; Q99816; baseline and differential.
Genevisible; Q99816; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0005770; C:late endosome; IMP:BHF-UCL.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005771; C:multivesicular body; TAS:HGNC.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0046790; F:virion binding; IDA:UniProtKB.
GO; GO:0097352; P:autophagosome maturation; TAS:ParkinsonsUK-UCL.
GO; GO:0007050; P:cell cycle arrest; IEA:Ensembl.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0016197; P:endosomal transport; TAS:Reactome.
GO; GO:0008333; P:endosome to lysosome transport; IEA:Ensembl.
GO; GO:1990182; P:exosomal secretion; IEA:Ensembl.
GO; GO:0006858; P:extracellular transport; IMP:UniProtKB.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0036258; P:multivesicular body assembly; TAS:ParkinsonsUK-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; IMP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB.
GO; GO:2000397; P:positive regulation of ubiquitin-dependent endocytosis; IEA:Ensembl.
GO; GO:1903774; P:positive regulation of viral budding via host ESCRT complex; IMP:UniProtKB.
GO; GO:0048524; P:positive regulation of viral process; IMP:UniProtKB.
GO; GO:1902188; P:positive regulation of viral release from host cell; IMP:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
GO; GO:1903551; P:regulation of extracellular exosome assembly; IMP:UniProtKB.
GO; GO:0043405; P:regulation of MAP kinase activity; IMP:UniProtKB.
GO; GO:1903772; P:regulation of viral budding via host ESCRT complex; IMP:UniProtKB.
GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:HGNC.
GO; GO:0046755; P:viral budding; IMP:BHF-UCL.
GO; GO:0039702; P:viral budding via host ESCRT complex; TAS:ParkinsonsUK-UCL.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR037202; ESCRT_assembly_dom.
InterPro; IPR017916; SB_dom.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
InterPro; IPR008883; UEV_N.
Pfam; PF05743; UEV; 1.
Pfam; PF09454; Vps23_core; 1.
SUPFAM; SSF140111; SSF140111; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS51312; SB; 1.
PROSITE; PS51322; UEV; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Cell division; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Endosome; Growth regulation; Host-virus interaction;
Membrane; Nucleus; Phosphoprotein; Polymorphism; Protein transport;
Reference proteome; Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
CHAIN 2 390 Tumor susceptibility gene 101 protein.
/FTId=PRO_0000082606.
DOMAIN 2 145 UEV. {ECO:0000255|PROSITE-
ProRule:PRU00652}.
DOMAIN 322 390 SB. {ECO:0000255|PROSITE-
ProRule:PRU00644}.
REGION 158 162 Interaction with CEP55.
COILED 235 316 {ECO:0000255}.
MOTIF 320 323 PTAP motif.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 220 220 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 15 119 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_004440.
VARIANT 167 167 M -> I (in dbSNP:rs34385327).
/FTId=VAR_034572.
MUTAGEN 43 43 V->A: Reduces interaction with ubiquitin;
inhibits down-regulation of EGFR.
{ECO:0000269|PubMed:12006492}.
MUTAGEN 45 45 N->A: Reduces interaction with ubiquitin.
No effect on MGRN1-binding.
{ECO:0000269|PubMed:12006492,
ECO:0000269|PubMed:12802020,
ECO:0000269|PubMed:17229889}.
MUTAGEN 46 46 D->A: Reduces interaction with ubiquitin.
{ECO:0000269|PubMed:12006492}.
MUTAGEN 63 63 Y->A: Reduces interaction with HIV-1 p6;
impairs HIV-1 budding.
{ECO:0000269|PubMed:12006492}.
MUTAGEN 88 88 F->A: Reduces interaction with ubiquitin;
no effect on in interaction with HIV-1
p6. {ECO:0000269|PubMed:12006492}.
MUTAGEN 89 89 V->A: No change in interaction with p6;
no effect on HIV-1 budding.
{ECO:0000269|PubMed:12006492}.
MUTAGEN 95 95 M->A: Reduces interaction with VPS37B and
HIV-1 p6; abolishes interaction with
PDCD6IP; impairs HIV-1 budding; inhibits
down-regulation of EGFR. Abolishes MGRN1-
binding. Loss of interaction with ARRDC1.
{ECO:0000269|PubMed:12006492,
ECO:0000269|PubMed:12802020,
ECO:0000269|PubMed:14505570,
ECO:0000269|PubMed:15218037,
ECO:0000269|PubMed:17229889,
ECO:0000269|PubMed:22315426}.
MUTAGEN 141 141 V->A: Reduces interaction with HIV-1 p6.
{ECO:0000269|PubMed:12006492}.
MUTAGEN 158 162 Missing: Abolishes interaction with CEP55
and midbody localization; no effect on
interaction with ESCRT-I proteins,
PDCD6IP and viral proteins.
{ECO:0000269|PubMed:17556548}.
MUTAGEN 158 160 PPN->AAA: Abolishes interaction with
CEP55. {ECO:0000269|PubMed:17853893}.
MUTAGEN 368 371 RKQF->AAAA: Loss of interaction with
VPS28. No effect on interaction with
VPS37C. {ECO:0000269|PubMed:15509564}.
CONFLICT 343 343 F -> L (in Ref. 3; AAH02487).
{ECO:0000305}.
HELIX 5 11 {ECO:0000244|PDB:3OBQ}.
TURN 12 14 {ECO:0000244|PDB:3OBQ}.
HELIX 18 31 {ECO:0000244|PDB:3OBQ}.
STRAND 35 42 {ECO:0000244|PDB:3OBQ}.
TURN 47 49 {ECO:0000244|PDB:3P9G}.
STRAND 51 62 {ECO:0000244|PDB:3OBQ}.
STRAND 67 75 {ECO:0000244|PDB:3OBQ}.
TURN 78 82 {ECO:0000244|PDB:3OBQ}.
STRAND 86 89 {ECO:0000244|PDB:3OBQ}.
STRAND 95 97 {ECO:0000244|PDB:3OBQ}.
STRAND 100 103 {ECO:0000244|PDB:1S1Q}.
STRAND 107 109 {ECO:0000244|PDB:1KPP}.
HELIX 112 115 {ECO:0000244|PDB:3OBQ}.
TURN 119 121 {ECO:0000244|PDB:3OBQ}.
HELIX 124 137 {ECO:0000244|PDB:3OBQ}.
STRAND 140 143 {ECO:0000244|PDB:3OBQ}.
HELIX 230 299 {ECO:0000244|PDB:3IV1}.
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


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