Q99816 (TS101_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tumor susceptibility gene 101 protein

Alternative name(s):
ESCRT-I complex subunit TSG101

Gene names

Name:

TSG101

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Protein existence	Evidence 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
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. 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.30 Ref.31 Ref.33
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 process	Cell cycle Cell division Growth regulation Host-virus interaction Protein transport Transport
Cellular component	Cytoplasm Endosome Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle arrest Inferred from electronic annotation. Source: Compara cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular membrane organization Traceable author statement. Source: Reactome cellular protein modification process Inferred from electronic annotation. Source: InterPro egress of virus within host cell Traceable author statement. Source: Reactome endosomal transport Traceable author statement. Source: Reactome keratinocyte differentiation Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara non-lytic virus budding Inferred from sequence or structural similarity. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell growth Inferred from electronic annotation. Source: Compara ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Inferred from direct assay PubMed 15611048. Source: HGNC
Cellular_component	early endosome Inferred from direct assay Ref.27. Source: UniProtKB endosome membrane Traceable author statement. Source: Reactome 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_function	DNA binding Traceable author statement Ref.7. Source: ProtInc transcription corepressor activity Traceable author statement Ref.7. Source: ProtInc ubiquitin binding Traceable author statement PubMed 15611048. Source: HGNC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DAXX	Q9UER7	4	EBI-346882,EBI-77321
LITAF	Q99732	3	EBI-346882,EBI-725647
VPS28	Q9UK41	3	EBI-346882,EBI-727424

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 390

390

Tumor susceptibility gene 101 protein

PRO_0000082606

Regions

Domain

2 – 145

144

UEV

Domain

322 – 390

69

SB

Region

158 – 162

5

Interaction with CEP55

Coiled coil

235 – 316

82

Potential

Motif

320 – 323

4

PTAP motif

Natural variations

Alternative sequence

15 – 119

105

Missing in isoform 2.

VSP_004440

Natural variant

167

1

M → I.
Corresponds to variant rs34385327 [ dbSNP | Ensembl ].

VAR_034572

Experimental info

Mutagenesis

43

1

V → A: Reduces interaction with ubiquitin; inhibits down-regulation of EGFR. Ref.33

Mutagenesis

45

1

N → A: Reduces interaction with ubiquitin. No effect on MGRN1-binding. Ref.15 Ref.27 Ref.33

Mutagenesis

46

1

D → A: Reduces interaction with ubiquitin. Ref.33

Mutagenesis

63

1

Y → A: Reduces interaction with HIV-1 p6; impairs HIV-1 budding. Ref.33

Mutagenesis

88

1

F → A: Reduces interaction with ubiquitin; no effect on in interaction with HIV-1 p6. Ref.33

Mutagenesis

89

1

V → A: No change in interaction with p6; no effect on HIV-1 budding. Ref.33

Mutagenesis

95

1

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. Ref.11 Ref.15 Ref.19 Ref.27 Ref.33

Mutagenesis

141

1

V → A: Reduces interaction with HIV-1 p6. Ref.33

Mutagenesis

158 – 162

5

Missing: Abolishes interaction with CEP55 and midbody localization; no effect on interaction with ESCRT-I proteins, PDCD6IP and viral proteins. Ref.28

Mutagenesis

158 – 160

3

PPN → AAA: Abolishes interaction with CEP55. Ref.26

Mutagenesis

368 – 371

4

RKQF → AAAA: Loss of interaction with VPS28. No effect on interaction with VPS37C. Ref.22

Sequence conflict

343

1

F → L in AAH02487. Ref.3

Secondary structure

1

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390

Helix Strand Turn

Details...

Helix

5 – 11

7

Turn

12 – 14

3

Helix

18 – 31

14

Beta strand

35 – 42

8

Turn

47 – 49

3

Beta strand

51 – 62

12

Beta strand

67 – 75

9

Turn

78 – 82

5

Beta strand

86 – 89

4

Beta strand

95 – 97

3

Beta strand

100 – 103

4

Beta strand

107 – 109

3

Helix

112 – 115

4

Turn

119 – 121

3

Helix

124 – 137

14

Beta strand

140 – 143

4

Helix

230 – 299

70

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 1, 1998. Version 2. Checksum: ADD6912FC22DF162	FASTA	390	43,944
	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
	Isoform 2 [UniParc]. Checksum: 035C70BEC887273D	FASTA	285	31,732
	10 20 30 40 50 60 MAVSESQLKK MVSKPQSDLL GLIQVMIVVF GDEPPVFSRP ISASYPPYQA TGPPNTSYMP 70 80 90 100 110 120 GMPGGISPYP SGYPPNPSGY PGCPYPPGGP YPATTSSQYP SQPPVTTVGP SRDGTISEDT 130 140 150 160 170 180 IRASLISAVS DKLRWRMKEE MDRAQAELNA LKRTEEDLKK GHQKLEEMVT RLDQEVAEVD 190 200 210 220 230 240 KNIELLKKKD EELSSALEKM ENQSENNDID EVIIPTAPLY KQILNLYAEE NAIEDTIFYL 250 260 270 280 GEALRRGVID LDVFLKHVRL LSRKQFQLRA LMQKARKTAG LSDLY

References

	« Hide 'large scale' referencesShow '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]	"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.
[31]	"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.
[32]	"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].
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U82130 mRNA. Translation: AAC52083.1.
BC002487 mRNA. Translation: AAH02487.1.

IPI

IPI00018434.
IPI00219826.

RefSeq

NP_006283.1. NM_006292.3.

UniGene

Hs.523512.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q99816.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31809N.

IntAct

Q99816. 65 interactions.

MINT

MINT-234338.

STRING

9606.ENSP00000251968.

PTM databases

PhosphoSite

Q99816.

Polymorphism databases

DMDM

9789790.

Proteomic databases

PaxDb

Q99816.

PeptideAtlas

Q99816.

PRIDE

Q99816.

Protocols and materials databases

DNASU

7251.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000251968; ENSP00000251968; ENSG00000074319.
ENST00000357193; ENSP00000349721; ENSG00000074319.

GeneID

7251.

KEGG

hsa:7251.

UCSC

uc001mor.3. human.

Organism-specific databases

CTD

7251.

GeneCards

GC11M018501.

HGNC

HGNC:15971. TSG101.

HPA

CAB004283.
HPA006161.

MIM

601387. gene.

neXtProt

NX_Q99816.

PharmGKB

PA38068.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG317261.

HOGENOM

HOG000247008.

HOVERGEN

HBG057450.

InParanoid

Q99816.

KO

K12183.

OMA

MPGMPAV.

OrthoDB

EOG476K0B.

PhylomeDB

Q99816.

Enzyme and pathway databases

Reactome

REACT_11123. Membrane Trafficking.
REACT_116125. Disease.

Gene expression databases

ArrayExpress

Q99816.

Bgee

Q99816.

CleanEx

HS_TSG101.

Genevestigator

Q99816.

GermOnline

ENSG00000074319. Homo sapiens.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR017916. Steadiness_box.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR008883. UEV_N.
[Graphical view]

Pfam

PF05743. UEV. 1 hit.
PF09454. Vps23_core. 1 hit.
[Graphical view]

SUPFAM

SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS51312. SB. 1 hit.
PS00183. UBIQUITIN_CONJUGAT_1. False negative.
PS50127. UBIQUITIN_CONJUGAT_2. False negative.
PS51322. UEV. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q99816.

ChEMBL

CHEMBL6157.

ChiTaRS

TSG101. human.

EvolutionaryTrace

Q99816.

GenomeRNAi

7251.

NextBio

28353.

SOURCE

Search...

Entry information

Entry name

TS101_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 149 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.