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Q99816 (TS101_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor susceptibility gene 101 protein
Alternative name(s):
ESCRT-I complex subunit TSG101
Gene names
Name:TSG101
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.10 Ref.26 Ref.28 Ref.34 Ref.40

Subunit structure

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 stoechiometry. Interacts with VPS37A, VPS37B and VPS37C. Interacts with ubiquitin, stathmin, GMCL, DMAP1 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 stoechiometry. Interacts with HGS; the interaction mediates the association with the ESCRT-0 complex. Interacts with GGA1 and GGA3. Interacts (via UEV domain) with PDCD6IP/AIP1. Interacts with VPS28, SNF8 and VPS36. Self-associates. 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. Interacts with PDCD6. Interacts with HIV-1 p6. Interacts with human spumavirus Gag. Interacts with HTLV-1 Gag. Interacts with Ebola virus VP40. Interacts with EIAV p9; the interaction has been shown in vitro. Interacts with MGRN1. Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.31 Ref.32 Ref.34 Ref.36 Ref.40 Ref.41

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein. Nucleus. Late endosome membrane; Peripheral membrane protein. Note: Mainly cytoplasmic. Membrane-associated when active and soluble when inactive. Depending on the stage of the cell cycle, detected in the nucleus. Colocalized with CEP55 in the midbody during cytokinesis. Ref.10 Ref.26 Ref.27 Ref.28

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.

The coiled coil domain may interact with stathmin.

The UEV domain binds ubiquitin and P-[ST]-A-P peptide motif independently.

Post-translational modification

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.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family. UEV subfamily.

Contains 1 SB (steadiness box) domain.

Contains 1 UEV (ubiquitin E2 variant) domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Growth regulation
Host-virus interaction
Protein transport
Transport
   Cellular componentCytoplasm
Endosome
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMAcetylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle arrest

Inferred from electronic annotation. Source: Ensembl

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

cellular protein modification process

Inferred from electronic annotation. Source: InterPro

endosomal transport

Traceable author statement. Source: Reactome

intracellular transport of virus

Traceable author statement. Source: Reactome

keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

membrane organization

Traceable author statement. Source: Reactome

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway

Inferred from mutant phenotype Ref.34. Source: UniProtKB

viral budding

Inferred from sequence or structural similarity. Source: UniProtKB

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral protein processing

Traceable author statement. Source: Reactome

virion assembly

Traceable author statement. Source: Reactome

   Cellular_componentESCRT I complex

Inferred from direct assay Ref.34. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 18077552. Source: UniProtKB

early endosome

Inferred from direct assay Ref.27. Source: UniProtKB

endosome membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 15326289PubMed 19056867PubMed 23376485. Source: UniProt

late endosome

Inferred from mutant phenotype PubMed 15126635. Source: BHF-UCL

late endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

multivesicular body

Traceable author statement PubMed 15611048. Source: HGNC

nucleolus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Traceable author statement Ref.7. Source: ProtInc

calcium-dependent protein binding

Inferred from physical interaction Ref.31. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18077552Ref.29. Source: UniProtKB

transcription corepressor activity

Traceable author statement Ref.7. Source: ProtInc

ubiquitin binding

Inferred from direct assay PubMed 20654576. Source: UniProt

ubiquitin protein ligase binding

Inferred from physical interaction Ref.27. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist. Several shorter isoforms are detected in primary breast cancers and other tumors.
Isoform 1 (identifier: Q99816-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q99816-2)

The sequence of this isoform differs from the canonical sequence as follows:
     15-119: Missing.
Note: Detected in normal as well as cancer tissues.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.30
Chain2 – 390389Tumor susceptibility gene 101 protein
PRO_0000082606

Regions

Domain2 – 145144UEV
Domain322 – 39069SB
Region158 – 1625Interaction with CEP55
Coiled coil235 – 31682 Potential
Motif320 – 3234PTAP motif

Amino acid modifications

Modified residue21N-acetylalanine Ref.30 Ref.35

Natural variations

Alternative sequence15 – 119105Missing in isoform 2.
VSP_004440
Natural variant1671M → I.
Corresponds to variant rs34385327 [ dbSNP | Ensembl ].
VAR_034572

Experimental info

Mutagenesis431V → A: Reduces interaction with ubiquitin; inhibits down-regulation of EGFR. Ref.36
Mutagenesis451N → A: Reduces interaction with ubiquitin. No effect on MGRN1-binding. Ref.15 Ref.27 Ref.36
Mutagenesis461D → A: Reduces interaction with ubiquitin. Ref.36
Mutagenesis631Y → A: Reduces interaction with HIV-1 p6; impairs HIV-1 budding. Ref.36
Mutagenesis881F → A: Reduces interaction with ubiquitin; no effect on in interaction with HIV-1 p6. Ref.36
Mutagenesis891V → A: No change in interaction with p6; no effect on HIV-1 budding. Ref.36
Mutagenesis951M → 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. Ref.11 Ref.15 Ref.19 Ref.27 Ref.36
Mutagenesis1411V → A: Reduces interaction with HIV-1 p6. Ref.36
Mutagenesis158 – 1625Missing: Abolishes interaction with CEP55 and midbody localization; no effect on interaction with ESCRT-I proteins, PDCD6IP and viral proteins. Ref.28
Mutagenesis158 – 1603PPN → AAA: Abolishes interaction with CEP55. Ref.26
Mutagenesis368 – 3714RKQF → AAAA: Loss of interaction with VPS28. No effect on interaction with VPS37C. Ref.22
Sequence conflict3431F → L in AAH02487. Ref.3

Secondary structure

.................................. 390
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1998. Version 2.
Checksum: ADD6912FC22DF162

FASTA39043,944
        10         20         30         40         50         60 
MAVSESQLKK MVSKYKYRDL TVRETVNVIT LYKDLKPVLD SYVFNDGSSR ELMNLTGTIP 

        70         80         90        100        110        120 
VPYRGNTYNI PICLWLLDTY PYNPPICFVK PTSSMTIKTG KHVDANGKIY LPYLHEWKHP 

       130        140        150        160        170        180 
QSDLLGLIQV MIVVFGDEPP VFSRPISASY PPYQATGPPN TSYMPGMPGG ISPYPSGYPP 

       190        200        210        220        230        240 
NPSGYPGCPY PPGGPYPATT SSQYPSQPPV TTVGPSRDGT ISEDTIRASL ISAVSDKLRW 

       250        260        270        280        290        300 
RMKEEMDRAQ AELNALKRTE EDLKKGHQKL EEMVTRLDQE VAEVDKNIEL LKKKDEELSS 

       310        320        330        340        350        360 
ALEKMENQSE NNDIDEVIIP TAPLYKQILN LYAEENAIED TIFYLGEALR RGVIDLDVFL 

       370        380        390 
KHVRLLSRKQ FQLRALMQKA RKTAGLSDLY 

« Hide

Isoform 2 [UniParc].

Checksum: 035C70BEC887273D
Show »

FASTA28531,732

References

« Hide 'large scale' references
[1]"The TSG101 tumor susceptibility gene is located in chromosome 11 band p15 and is mutated in human breast cancer."
Li L., Li X., Francke U., Cohen S.N.
Cell 88:143-154(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]Erratum
Li L., Francke U., Cohen S.N.
Cell 93:661-661(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: RETRACTION.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Eye.
[4]"Aberrant splicing of the TSG101 and FHIT genes occurs frequently in multiple malignancies and in normal tissues and mimics alterations previously described in tumours."
Gayther S.A., Barski P., Batley S.J., Li L., de Foy K.A., Cohen S.N., Ponder B.A., Caldas C.
Oncogene 15:2119-2126(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 2).
[5]"Aberrant splicing but not mutations of TSG101 in human breast cancer."
Lee M.P., Feinberg A.P.
Cancer Res. 57:3131-3134(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[6]"Genomic architecture and transcriptional activation of the mouse and human tumor susceptibility gene TSG101: common types of shorter transcripts are true alternative splice variants."
Wagner K.-U., Dierisseau P., Rucker E.B. III, Robinson G.W., Hennighausen L.
Oncogene 17:2761-2770(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[7]"DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci."
Rountree M.R., Bachman K.E., Baylin S.B.
Nat. Genet. 25:269-277(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DMAP1.
[8]"Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding."
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.
Cell 107:55-65(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 P6 AND UBIQUITIN.
[9]"Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag)."
VerPlank L., Bouamr F., LaGrassa T.J., Agresta B., Kikonyogo A., Leis J., Carter C.A.
Proc. Natl. Acad. Sci. U.S.A. 98:7724-7729(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 P6.
[10]"Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates."
Bishop N., Horman A., Woodman P.
J. Cell Biol. 157:91-101(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"The protein network of HIV budding."
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.
Cell 114:701-713(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SELF-ASSOCIATION, INTERACTION WITH PDCD6IP; VPS28; SNF8 AND VPS36, MUTAGENESIS OF MET-95.
[12]"HIV Gag mimics the Tsg101-recruiting activity of the human Hrs protein."
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.
J. Cell Biol. 162:425-434(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 GAG AND HGS, SELF-ASSOCIATION.
[13]"Ebola virus matrix protein VP40 interaction with human cellular factors Tsg101 and Nedd4."
Timmins J., Schoehn G., Ricard-Blum S., Scianimanico S., Vernet T., Ruigrok R.W., Weissenhorn W.
J. Mol. Biol. 326:493-502(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EBOLA VIRUS VP40.
[14]"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."
Bouamr F., Melillo J.A., Wang M.Q., Nagashima K., de Los Santos M., Rein A., Goff S.P.
J. Virol. 77:11882-11895(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTLV-1 GAG.
[15]"TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation."
Lu Q., Hope L.W., Brasch M., Reinhard C., Cohen S.N.
Proc. Natl. Acad. Sci. U.S.A. 100:7626-7631(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASN-45 AND MET-95.
[16]"Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins."
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SELF-ASSOCIATION, INTERACTION WITH PDCD6IP AND EIAV P9.
[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]"Tal, a Tsg101-specific E3 ubiquitin ligase, regulates receptor endocytosis and retrovirus budding."
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.
Genes Dev. 18:1737-1752(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY LRSAM1.
[19]"The human endosomal sorting complex required for transport (ESCRT-I) and its role in HIV-1 budding."
Stuchell M.D., Garrus J.E., Mueller B., Stray K.M., Ghaffarian S., McKinnon R., Kraeusslich H.-G., Morham S.G., Sundquist W.I.
J. Biol. Chem. 279:36059-36071(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VPS37A AND VPS37B, MUTAGENESIS OF MET-95.
[20]"The trihelical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites."
Mattera R., Puertollano R., Smith W.J., Bonifacino J.S.
J. Biol. Chem. 279:31409-31418(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GGA1.
[21]"Interactions of GGA3 with the ubiquitin sorting machinery."
Puertollano R., Bonifacino J.S.
Nat. Cell Biol. 6:244-251(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GGA3.
[22]"Identification of human VPS37C, a component of endosomal sorting complex required for transport-I important for viral budding."
Eastman S.W., Martin-Serrano J., Chung W., Zang T., Bieniasz P.D.
J. Biol. Chem. 280:628-636(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VPS37C, MUTAGENESIS OF 368-ARG--PHE-371.
[23]"Identification of domains in gag important for prototypic foamy virus egress."
Patton G.S., Morris S.A., Chung W., Bieniasz P.D., McClure M.O.
J. Virol. 79:6392-6399(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN SPUMARETROVIRUS GAG.
[24]"Cellular factors required for Lassa virus budding."
Urata S., Noda T., Kawaoka Y., Yokosawa H., Yasuda J.
J. Virol. 80:4191-4195(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LASSA VIRUS RING FINGER PROTEIN Z.
[25]"Identification of human MVB12 proteins as ESCRT-I subunits that function in HIV budding."
Morita E., Sandrin V., Alam S.L., Eckert D.M., Gygi S.P., Sundquist W.I.
Cell Host Microbe 2:41-53(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VPS28; VPS37A; VPS37B; VPS37C; VPS37D; MVB12A AND MVB12B, RECONSTITUTION OF THE ESCRT-I COMPLEX.
[26]"Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis."
Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I.
EMBO J. 26:4215-4227(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH CEP55; CD2AP; IQGAP1 AND ROCK1, MUTAGENESIS OF 158-PRO--ASN-160.
[27]"Spongiform neurodegeneration-associated E3 ligase Mahogunin ubiquitylates TSG101 and regulates endosomal trafficking."
Kim B.Y., Olzmann J.A., Barsh G.S., Chin L.S., Li L.
Mol. Biol. Cell 18:1129-1142(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MGRN1, UBIQUITINATION BY MGRN1, SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-45 AND MET-95.
[28]"Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery."
Carlton J.G., Martin-Serrano J.
Science 316:1908-1912(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, MUTAGENESIS OF 158-PRO--SER-162.
[29]"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."
Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T., Maki M.
J. Biol. Chem. 283:9623-9632(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDCD6.
[30]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[31]"Penta-EF-hand protein ALG-2 functions as a Ca2+-dependent adaptor that bridges Alix and TSG101."
Okumura M., Ichioka F., Kobayashi R., Suzuki H., Yoshida H., Shibata H., Maki M.
Biochem. Biophys. Res. Commun. 386:237-241(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDCD6IP.
[32]"Abnormal regulation of TSG101 in mice with spongiform neurodegeneration."
Jiao J., Sun K., Walker W.P., Bagher P., Cota C.D., Gunn T.M.
Biochim. Biophys. Acta 1792:1027-1035(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MGRN1, UBIQUITINATION BY MGRN1.
[33]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"UBAP1 is a component of an endosome-specific ESCRT-I complex that is essential for MVB sorting."
Stefani F., Zhang L., Taylor S., Donovan J., Rollinson S., Doyotte A., Brownhill K., Bennion J., Pickering-Brown S., Woodman P.
Curr. Biol. 21:1245-1250(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, IDENTIFICATION IN AN ESCRT-I COMPLEX WITH UBAP1.
[35]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Structure and functional interactions of the Tsg101 UEV domain."
Pornillos O.W., Alam S.L., Rich R.L., Myszka D.G., Davis D.R., Sundquist W.I.
EMBO J. 21:2397-2406(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-145, INTERACTION WITH HIV-1 P6 AND UBIQUITIN, MUTAGENESIS OF VAL-43; ASN-45; ASP-46; TYR-63; PHE-88; VAL-89; MET-95 AND VAL-141.
[37]"Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein."
Pornillos O., Alam S.L., Davis D.R., Sundquist W.I.
Nat. Struct. Biol. 9:812-817(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-145.
[38]"Ubiquitin recognition by the human TSG101 protein."
Sundquist W.I., Schubert H.L., Kelly B.N., Hill G.C., Holton J.M., Hill C.P.
Mol. Cell 13:783-789(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-145 IN COMPLEX WITH UBIQUITIN.
[39]"Structure of human TSG101 UEV domain."
Palencia A., Martinez J.C., Mateo P.L., Luque I., Camara-Artigas A.
Acta Crystallogr. D 62:458-464(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 1-145.
[40]"Crystallographic and functional analysis of the ESCRT-I /HIV-1 Gag PTAP interaction."
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.
Structure 18:1536-1547(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 2-145 IN COMPLEX WITH HIV-1 GAG P6 PEPTIDE, FUNCTION, SUBUNIT.
[41]"Elucidation of new binding interactions with the tumor susceptibility gene 101 (Tsg101) protein using modified HIV-1 Gag-p6 derived peptide ligands."
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.
ACS Med. Chem. Lett. 2:337-341(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-145 IN COMPLEX WITH HIV-1 GAG P6 PEPTIDE, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U82130 mRNA. Translation: AAC52083.1.
BC002487 mRNA. Translation: AAH02487.1.
CCDSCCDS7842.1. [Q99816-1]
RefSeqNP_006283.1. NM_006292.3. [Q99816-1]
UniGeneHs.523512.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KPPNMR-A1-145[»]
1KPQNMR-A1-145[»]
1M4PNMR-A1-145[»]
1M4QNMR-A1-145[»]
1S1QX-ray2.00A/C1-145[»]
2F0RX-ray2.26A/B1-145[»]
3IV1X-ray2.50A/B/C/D/E/F/G/H229-304[»]
3OBQX-ray1.40A2-145[»]
3OBSX-ray1.50A2-145[»]
3OBUX-ray1.60A2-145[»]
3OBXX-ray1.60A2-145[»]
3P9GX-ray1.80A2-145[»]
3P9HX-ray1.80A2-145[»]
4EJEX-ray2.20A/B1-145[»]
ProteinModelPortalQ99816.
SMRQ99816. Positions 3-143, 228-379.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113102. 105 interactions.
DIPDIP-31809N.
IntActQ99816. 74 interactions.
MINTMINT-234338.
STRING9606.ENSP00000251968.

Chemistry

BindingDBQ99816.
ChEMBLCHEMBL6157.

PTM databases

PhosphoSiteQ99816.

Polymorphism databases

DMDM9789790.

Proteomic databases

MaxQBQ99816.
PaxDbQ99816.
PeptideAtlasQ99816.
PRIDEQ99816.

Protocols and materials databases

DNASU7251.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000251968; ENSP00000251968; ENSG00000074319. [Q99816-1]
ENST00000357193; ENSP00000349721; ENSG00000074319. [Q99816-2]
GeneID7251.
KEGGhsa:7251.
UCSCuc001mor.3. human. [Q99816-1]

Organism-specific databases

CTD7251.
GeneCardsGC11M018501.
HGNCHGNC:15971. TSG101.
HPACAB004283.
HPA006161.
MIM601387. gene.
neXtProtNX_Q99816.
PharmGKBPA38068.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG317261.
HOGENOMHOG000247008.
HOVERGENHBG057450.
InParanoidQ99816.
KOK12183.
OMAASYMPGM.
PhylomeDBQ99816.
TreeFamTF312917.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ99816.
BgeeQ99816.
CleanExHS_TSG101.
GenevestigatorQ99816.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR017916. Steadiness_box.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR008883. UEV_N.
[Graphical view]
PfamPF05743. UEV. 1 hit.
PF09454. Vps23_core. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS51312. SB. 1 hit.
PS51322. UEV. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTSG101. human.
EvolutionaryTraceQ99816.
GeneWikiTSG101.
GenomeRNAi7251.
NextBio28353.
PROQ99816.
SOURCESearch...

Entry information

Entry nameTS101_HUMAN
AccessionPrimary (citable) accession number: Q99816
Secondary accession number(s): Q9BUM5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM