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Q99816

- TS101_HUMAN

UniProt

Q99816 - TS101_HUMAN

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Protein
Tumor susceptibility gene 101 protein
Gene
TSG101
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. calcium-dependent protein binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. protein homodimerization activity Source: UniProt
  5. transcription corepressor activity Source: ProtInc
  6. ubiquitin binding Source: UniProt
  7. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. cell cycle arrest Source: Ensembl
  2. cell division Source: UniProtKB-KW
  3. cellular protein modification process Source: InterPro
  4. endosomal transport Source: Reactome
  5. intracellular transport of virus Source: Reactome
  6. keratinocyte differentiation Source: Ensembl
  7. membrane organization Source: Reactome
  8. negative regulation of cell proliferation Source: Ensembl
  9. negative regulation of transcription, DNA-templated Source: Ensembl
  10. protein transport Source: UniProtKB-KW
  11. regulation of cell growth Source: Ensembl
  12. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: UniProtKB
  13. viral budding Source: UniProtKB
  14. viral life cycle Source: Reactome
  15. viral process Source: Reactome
  16. viral protein processing Source: Reactome
  17. virion assembly Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Growth regulation, Host-virus interaction, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_115893. Membrane binding and targetting of GAG proteins.
REACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
REACT_6359. Budding and maturation of HIV virion.

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor susceptibility gene 101 protein
Alternative name(s):
ESCRT-I complex subunit TSG101
Gene namesi
Name:TSG101
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:15971. TSG101.

Subcellular locationi

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.4 Publications

GO - Cellular componenti

  1. ESCRT I complex Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. early endosome Source: UniProtKB
  4. endosome membrane Source: Reactome
  5. extracellular vesicular exosome Source: UniProt
  6. late endosome Source: BHF-UCL
  7. late endosome membrane Source: UniProtKB-SubCell
  8. multivesicular body Source: HGNC
  9. nucleolus Source: HPA
  10. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi43 – 431V → A: Reduces interaction with ubiquitin; inhibits down-regulation of EGFR. 1 Publication
Mutagenesisi45 – 451N → A: Reduces interaction with ubiquitin. No effect on MGRN1-binding. 3 Publications
Mutagenesisi46 – 461D → A: Reduces interaction with ubiquitin. 1 Publication
Mutagenesisi63 – 631Y → A: Reduces interaction with HIV-1 p6; impairs HIV-1 budding. 1 Publication
Mutagenesisi88 – 881F → A: Reduces interaction with ubiquitin; no effect on in interaction with HIV-1 p6. 1 Publication
Mutagenesisi89 – 891V → A: No change in interaction with p6; no effect on HIV-1 budding. 1 Publication
Mutagenesisi95 – 951M → 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. 5 Publications
Mutagenesisi141 – 1411V → A: Reduces interaction with HIV-1 p6. 1 Publication
Mutagenesisi158 – 1625Missing: Abolishes interaction with CEP55 and midbody localization; no effect on interaction with ESCRT-I proteins, PDCD6IP and viral proteins. 1 Publication
Mutagenesisi158 – 1603PPN → AAA: Abolishes interaction with CEP55. 1 Publication
Mutagenesisi368 – 3714RKQF → AAAA: Loss of interaction with VPS28. No effect on interaction with VPS37C. 1 Publication

Organism-specific databases

PharmGKBiPA38068.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 390389Tumor susceptibility gene 101 protein
PRO_0000082606Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiQ99816.
PaxDbiQ99816.
PeptideAtlasiQ99816.
PRIDEiQ99816.

PTM databases

PhosphoSiteiQ99816.

Expressioni

Tissue specificityi

Heart, brain, placenta, lung, liver, skeletal, kidney and pancreas.

Gene expression databases

ArrayExpressiQ99816.
BgeeiQ99816.
CleanExiHS_TSG101.
GenevestigatoriQ99816.

Organism-specific databases

HPAiCAB004283.
HPA006161.

Interactioni

Subunit structurei

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 MGRN1.25 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CD2APQ9Y5K62EBI-346882,EBI-298152
CEP55Q53EZ412EBI-346882,EBI-747776
DAXXQ9UER74EBI-346882,EBI-77321
IQGAP1P469405EBI-346882,EBI-297509
LITAFQ997323EBI-346882,EBI-725647
PTPN23Q9H3S72EBI-346882,EBI-724478
ROCK1Q134644EBI-346882,EBI-876651
VPS28Q9UK413EBI-346882,EBI-727424

Protein-protein interaction databases

BioGridi113102. 106 interactions.
DIPiDIP-31809N.
IntActiQ99816. 74 interactions.
MINTiMINT-234338.
STRINGi9606.ENSP00000251968.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 117
Turni12 – 143
Helixi18 – 3114
Beta strandi35 – 4410
Turni47 – 493
Beta strandi51 – 6212
Beta strandi67 – 759
Turni78 – 825
Beta strandi86 – 894
Beta strandi95 – 973
Beta strandi100 – 1034
Beta strandi107 – 1093
Helixi112 – 1154
Turni119 – 1213
Helixi124 – 13714
Beta strandi140 – 1434
Helixi230 – 29970

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ99816.
SMRiQ99816. Positions 3-143, 228-379.

Miscellaneous databases

EvolutionaryTraceiQ99816.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 145144UEV
Add
BLAST
Domaini322 – 39069SB
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni158 – 1625Interaction with CEP55

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili235 – 31682 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi320 – 3234PTAP motif

Domaini

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.

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG317261.
HOGENOMiHOG000247008.
HOVERGENiHBG057450.
InParanoidiQ99816.
KOiK12183.
OMAiASYMPGM.
PhylomeDBiQ99816.
TreeFamiTF312917.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR017916. Steadiness_box.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR008883. UEV_N.
[Graphical view]
PfamiPF05743. UEV. 1 hit.
PF09454. Vps23_core. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS51312. SB. 1 hit.
PS51322. UEV. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist. Several shorter isoforms are detected in primary breast cancers and other tumors.

Isoform 1 (identifier: Q99816-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAVSESQLKK MVSKYKYRDL TVRETVNVIT LYKDLKPVLD SYVFNDGSSR    50
ELMNLTGTIP VPYRGNTYNI PICLWLLDTY PYNPPICFVK PTSSMTIKTG 100
KHVDANGKIY LPYLHEWKHP QSDLLGLIQV MIVVFGDEPP VFSRPISASY 150
PPYQATGPPN TSYMPGMPGG ISPYPSGYPP NPSGYPGCPY PPGGPYPATT 200
SSQYPSQPPV TTVGPSRDGT ISEDTIRASL ISAVSDKLRW RMKEEMDRAQ 250
AELNALKRTE EDLKKGHQKL EEMVTRLDQE VAEVDKNIEL LKKKDEELSS 300
ALEKMENQSE NNDIDEVIIP TAPLYKQILN LYAEENAIED TIFYLGEALR 350
RGVIDLDVFL KHVRLLSRKQ FQLRALMQKA RKTAGLSDLY 390
Length:390
Mass (Da):43,944
Last modified:August 1, 1998 - v2
Checksum:iADD6912FC22DF162
GO
Isoform 2 (identifier: Q99816-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     15-119: Missing.

Note: Detected in normal as well as cancer tissues.

Show »
Length:285
Mass (Da):31,732
Checksum:i035C70BEC887273D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1671M → I.
Corresponds to variant rs34385327 [ dbSNP | Ensembl ].
VAR_034572

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei15 – 119105Missing in isoform 2.
VSP_004440Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti343 – 3431F → L in AAH02487. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U82130 mRNA. Translation: AAC52083.1.
BC002487 mRNA. Translation: AAH02487.1.
CCDSiCCDS7842.1. [Q99816-1]
RefSeqiNP_006283.1. NM_006292.3. [Q99816-1]
UniGeneiHs.523512.

Genome annotation databases

EnsembliENST00000251968; ENSP00000251968; ENSG00000074319. [Q99816-1]
ENST00000357193; ENSP00000349721; ENSG00000074319. [Q99816-2]
GeneIDi7251.
KEGGihsa:7251.
UCSCiuc001mor.3. human. [Q99816-1]

Polymorphism databases

DMDMi9789790.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U82130 mRNA. Translation: AAC52083.1 .
BC002487 mRNA. Translation: AAH02487.1 .
CCDSi CCDS7842.1. [Q99816-1 ]
RefSeqi NP_006283.1. NM_006292.3. [Q99816-1 ]
UniGenei Hs.523512.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KPP NMR - A 1-145 [» ]
1KPQ NMR - A 1-145 [» ]
1M4P NMR - A 1-145 [» ]
1M4Q NMR - A 1-145 [» ]
1S1Q X-ray 2.00 A/C 1-145 [» ]
2F0R X-ray 2.26 A/B 1-145 [» ]
3IV1 X-ray 2.50 A/B/C/D/E/F/G/H 229-304 [» ]
3OBQ X-ray 1.40 A 2-145 [» ]
3OBS X-ray 1.50 A 2-145 [» ]
3OBU X-ray 1.60 A 2-145 [» ]
3OBX X-ray 1.60 A 2-145 [» ]
3P9G X-ray 1.80 A 2-145 [» ]
3P9H X-ray 1.80 A 2-145 [» ]
4EJE X-ray 2.20 A/B 1-145 [» ]
ProteinModelPortali Q99816.
SMRi Q99816. Positions 3-143, 228-379.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113102. 106 interactions.
DIPi DIP-31809N.
IntActi Q99816. 74 interactions.
MINTi MINT-234338.
STRINGi 9606.ENSP00000251968.

Chemistry

BindingDBi Q99816.
ChEMBLi CHEMBL6157.

PTM databases

PhosphoSitei Q99816.

Polymorphism databases

DMDMi 9789790.

Proteomic databases

MaxQBi Q99816.
PaxDbi Q99816.
PeptideAtlasi Q99816.
PRIDEi Q99816.

Protocols and materials databases

DNASUi 7251.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000251968 ; ENSP00000251968 ; ENSG00000074319 . [Q99816-1 ]
ENST00000357193 ; ENSP00000349721 ; ENSG00000074319 . [Q99816-2 ]
GeneIDi 7251.
KEGGi hsa:7251.
UCSCi uc001mor.3. human. [Q99816-1 ]

Organism-specific databases

CTDi 7251.
GeneCardsi GC11M018501.
HGNCi HGNC:15971. TSG101.
HPAi CAB004283.
HPA006161.
MIMi 601387. gene.
neXtProti NX_Q99816.
PharmGKBi PA38068.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG317261.
HOGENOMi HOG000247008.
HOVERGENi HBG057450.
InParanoidi Q99816.
KOi K12183.
OMAi ASYMPGM.
PhylomeDBi Q99816.
TreeFami TF312917.

Enzyme and pathway databases

Reactomei REACT_115893. Membrane binding and targetting of GAG proteins.
REACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
REACT_6359. Budding and maturation of HIV virion.

Miscellaneous databases

ChiTaRSi TSG101. human.
EvolutionaryTracei Q99816.
GeneWikii TSG101.
GenomeRNAii 7251.
NextBioi 28353.
PROi Q99816.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q99816.
Bgeei Q99816.
CleanExi HS_TSG101.
Genevestigatori Q99816.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR017916. Steadiness_box.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR008883. UEV_N.
[Graphical view ]
Pfami PF05743. UEV. 1 hit.
PF09454. Vps23_core. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS51312. SB. 1 hit.
PS51322. UEV. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: SELF-ASSOCIATION, INTERACTION WITH PDCD6IP; VPS28; SNF8 AND VPS36, MUTAGENESIS OF MET-95.
  12. 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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-145 IN COMPLEX WITH UBIQUITIN.
  39. 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.

Entry informationi

Entry nameiTS101_HUMAN
AccessioniPrimary (citable) accession number: Q99816
Secondary accession number(s): Q9BUM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: September 3, 2014
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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