[1]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
DOI=10.1016/S0092-8674(00)81866-8; PubMed=9019400 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[2]
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ERRATUM, AND RETRACTION.
DOI=10.1016/S0092-8674(00)89342-3; PubMed=9867424 [NCBI, ExPASy, EBI, Israel, Japan]
Li L.,
Francke U.,
Cohen S.N.;
Cell 93:661-661(1998).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[4]
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ALTERNATIVE SPLICING (ISOFORM 2).
DOI=10.1038/sj.onc.1201591; PubMed=9366528 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[5]
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ALTERNATIVE SPLICING.
PubMed=9242438 [NCBI, ExPASy, EBI, Israel, Japan]
Lee M.P.,
Feinberg A.P.;
"Aberrant splicing but not mutations of TSG101 in human breast cancer.";
Cancer Res. 57:3131-3134(1997).
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[6]
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ALTERNATIVE SPLICING.
DOI=10.1038/sj.onc.1202529; PubMed=9840940 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[7]
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INTERACTION WITH DMAP1.
DOI=10.1038/77023; PubMed=10888872 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[8]
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INTERACTION WITH HIV-1 P6.
DOI=10.1016/S0092-8674(01)00506-2; PubMed=11595185 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[9]
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INTERACTION WITH HIV-1 P6.
DOI=10.1073/pnas.131059198; PubMed=11427703 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[10]
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INTERACTION WITH PDCD6IP.
DOI=10.1016/S0092-8674(03)00714-1; PubMed=14505570 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[11]
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INTERACTION WITH EBOLAVIRUS VP40.
DOI=10.1016/S0022-2836(02)01406-7; PubMed=12559917 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[12]
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INTERACTION WITH HTLV-1 GAG.
DOI=10.1128/JVI.77.22.11882-11895.2003; PubMed=14581525 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[13]
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UBIQUITINATION BY LRSAM1.
DOI=10.1101/gad.294904; PubMed=15256501 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[14]
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INTERACTION WITH VPS37A AND VPS37B.
DOI=10.1074/jbc.M405226200; PubMed=15218037 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[15]
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INTERACTION WITH GGA1.
DOI=10.1074/jbc.M402183200; PubMed=15143060 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[16]
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INTERACTION WITH GGA3.
DOI=10.1038/ncb1106; PubMed=15039775 [NCBI, ExPASy, EBI, Israel, Japan]
Puertollano R.,
Bonifacino J.S.;
"Interactions of GGA3 with the ubiquitin sorting machinery.";
Nat. Cell Biol. 6:244-251(2004).
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[17]
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INTERACTION WITH VPS37C, AND MUTAGENESIS OF 368-ARG--PHE-371.
DOI=10.1074/jbc.M410384200; PubMed=15509564 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[18]
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INTERACTION WITH HUMAN SPUMARETROVIRUS GAG.
DOI=10.1128/JVI.79.10.6392-6399.2005; PubMed=15858022 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[19]
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INTERACTION WITH LASSA VIRUS RING FINGER PROTEIN Z.
DOI=10.1128/JVI.80.8.4191-4195.2006; PubMed=16571837 [NCBI, ExPASy, EBI, Israel, Japan]
Urata S.,
Noda T.,
Kawaoka Y.,
Yokosawa H.,
Yasuda J.;
"Cellular factors required for Lassa virus budding.";
J. Virol. 80:4191-4195(2006).
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[20]
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STRUCTURE BY NMR OF 1-145.
DOI=10.1093/emboj/21.10.2397; PubMed=12006492 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[21]
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STRUCTURE BY NMR OF 1-145.
DOI=10.1038/nsb856; PubMed=12379843 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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- FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation. Acts as a negative growth regulator. Involved in the budding of many viruses.
- SUBUNIT: Component of ESCRT-I, endosomal sorting complex required for transport I, which consists of VPS28, VPS37, and TSG101. Interacts with VPS37A, VPS37B and VPS37C. Interacts with ubiquitin, stathmin, GMCL, DMAP1, HGS and AATF (By similarity). Interacts with GGA1 and GGA3. Interacts with PDCD6IP/AIP1. Interacts with viral proteins that contain a late-budding motif P-[ST]-A-P. This interaction is essential for viral particle budding of numerous retroviruses like HIV-1 p6, human spumavirus Gag, HTLV-1 Gag, as well as of Ebolavirus VP40.
- INTERACTION:
Q9UER7:DAXX; NbExp=1; IntAct=EBI-346882, EBI-77321;
Q9NPF5:DMAP1; NbExp=1; IntAct=EBI-346882, EBI-399105;
P08631:HCK; NbExp=1; IntAct=EBI-346882, EBI-346340;
Q8WUM4:PDCD6IP; NbExp=1; IntAct=EBI-346882, EBI-310624;
- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Nucleus. Note=Mainly cytoplasmic. Membrane-associated when active and soluble when inactive. Depending on the stage of the cell cycle, detected in the nucleus.
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist. Several shorter isoforms are detected in primary breast cancers and other tumors.
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| Name | 2 |
| Isoform ID | Q99816-2 |
| Note: Detected in normal as well as cancer tissues. |
| Features which should be applied to build the isoform sequence: VSP_004440. |
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- 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.
- PTM: Monoubiquitinated at multiple sites by LRSAM1. Ubiquitination inactivates it, possibly by regulating its shuttling between an active membrane-bound protein and an inactive soluble form.
- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UEV subfamily.
- SIMILARITY: Contains 1 SB (steadiness box) domain.
- SIMILARITY: Contains 1 UEV (ubiquitin E2 variant) domain.
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