P40818 (UBP8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 8
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 8
Ubiquitin isopeptidase Y
Short name=hUBPy
Ubiquitin thioesterase 8
Ubiquitin-specific-processing protease 8

Gene names

Name:	USP8
Synonyms:	KIAA0055, UBPY

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	1118 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. Ref.4 Ref.5 Ref.7 Ref.8
Catalytic activity	Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Subunit structure	Forms a ternary complex with RNF128 and OTUB1. Interacts (via C-terminal UCH catalytic domain) with OTUB1 isoform 1. Interacts with STAM2 (via SH3 domain). Interacts with DNAJB3, EGFR, EPS15, RASGRF1, RNF41, YWHAE, YWHAG and YWHAZ By similarity. Interacts with NBR1, RASGRF1, RNF41 and IST1. Associates with the ESCRT-0 complex and with microtubules By similarity. Interacts with BIRC6/bruce and KIF23/MKLP1. Ref.7 Ref.8 Ref.10 Ref.11
Subcellular location	Cytoplasm. Nucleus By similarity. Endosome membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein Ref.5 Ref.7 Ref.10.
Induction	Upon growth stimulation in starved human fibroblasts. Decreases in response to growth arrest induced by cell-cell contact. Ref.4
Domain	The MIT domain is required for endosomal localization, CHMP1B-binding, maintenance of ESCRT-0 stability and EGFR degradation. Ref.7 The rhodanese domain is sufficent for RNF41-binding By similarity. Ref.7
Post-translational modification	Phosphorylation of Ser-718 is essential for interaction with YWHAE and for cytosol localization By similarity. Undergoes dephosphorylation at Ser-718 in the M phase By similarity. Tyrosine-phosphorylated in its N-terminal half in an EGFR-dependent manner By similarity. Ubiquitinated. Inactive form is mostly monoubiquitinated, but polyubiquitination happens too. Ubiquitination is increased in EGF-stimulated cells. Ubiquitination of active form is undetectable, suggesting a possibility that USP8 deubiquitinates itself, thereby regulating its own function By similarity.
Sequence similarities	Belongs to the peptidase C19 family. Contains 1 MIT domain. Contains 1 rhodanese domain.
Sequence caution	The sequence AAH38801.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH51345.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	Cell cycle Ubl conjugation pathway
Cellular component	Cell membrane Cytoplasm Endosome Membrane Nucleus
Coding sequence diversity	Polymorphism
Domain	SH3-binding
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Ras protein signal transduction Inferred from electronic annotation. Source: Compara cell proliferation Traceable author statement Ref.4. Source: ProtInc cytokinesis after mitosis Inferred from mutant phenotype PubMed 18388320. Source: MGI endosome organization Inferred from mutant phenotype Ref.5. Source: UniProtKB protein K48-linked deubiquitination Inferred from direct assay Ref.5. Source: UniProtKB protein K63-linked deubiquitination Inferred from direct assay Ref.5. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Inferred from direct assay Ref.5. Source: UniProtKB early endosome Inferred from direct assay Ref.5. Source: UniProtKB endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to plasma membrane Inferred from direct assay Ref.5. Source: UniProtKB midbody Inferred from direct assay PubMed 18388320. Source: MGI nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cysteine-type endopeptidase activity Traceable author statement PubMed 9827704. Source: ProtInc ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro ubiquitin-specific protease activity Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CHMP1A	Q9HD42	2	EBI-1050865,EBI-1057156
CHMP1B	Q7LBR1	4	EBI-1050865,EBI-2118090

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1118

1118

Ubiquitin carboxyl-terminal hydrolase 8

PRO_0000080627

Regions

Domain

33 – 116

84

MIT

Domain

195 – 313

119

Rhodanese

Motif

405 – 413

9

SH3-binding By similarity

Sites

Active site

786

1

Nucleophile By similarity

Active site

1067

1

Proton acceptor By similarity

Amino acid modifications

Modified residue

160

1

Phosphoserine Ref.13

Modified residue

452

1

Phosphoserine Ref.9

Modified residue

577

1

Phosphothreonine Ref.15

Modified residue

718

1

Phosphoserine Ref.9 Ref.13 Ref.15

Modified residue

719

1

Phosphoserine Ref.9

Modified residue

945

1

Phosphothreonine By similarity

Natural variations

Natural variant

443

1

D → G.
Corresponds to variant rs3743044 [ dbSNP | Ensembl ].

VAR_017796

Natural variant

739

1

T → A.
Corresponds to variant rs11638390 [ dbSNP | Ensembl ].

VAR_051525

Natural variant

827

1

A → G.
Corresponds to variant rs1056577 [ dbSNP | Ensembl ].

VAR_017797

Experimental info

Mutagenesis

786

1

C → S: Impairs deubiquitination activity and leads to endosome membrane accumulation. Ref.5

Sequence conflict

526

1

E → G in CAD97662. Ref.2

Sequence conflict

717

1

Y → H in CAD97662. Ref.2

Sequence conflict

945

1

T → A in CAD97662. Ref.2

Secondary structure

1

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1118

Helix Strand Turn

Details...

Helix

17 – 21

5

Helix

22 – 24

3

Helix

28 – 30

3

Helix

33 – 52

20

Helix

56 – 73

18

Helix

77 – 81

5

Helix

83 – 90

8

Helix

92 – 138

47

Beta strand

181 – 183

3

Helix

185 – 193

9

Beta strand

195 – 197

3

Beta strand

199 – 203

5

Helix

207 – 212

6

Beta strand

219 – 221

3

Helix

223 – 225

3

Helix

232 – 237

6

Helix

241 – 248

8

Turn

249 – 252

4

Beta strand

253 – 259

7

Helix

265 – 267

3

Helix

273 – 282

10

Beta strand

295 – 297

3

Helix

300 – 307

8

Helix

309 – 311

3

Helix

763 – 765

3

Beta strand

782 – 784

3

Helix

786 – 796

11

Helix

799 – 806

8

Turn

807 – 809

3

Helix

810 – 813

4

Helix

825 – 839

15

Beta strand

842 – 845

4

Helix

848 – 857

10

Helix

859 – 861

3

Beta strand

862 – 865

4

Helix

869 – 884

16

Helix

903 – 917

15

Helix

921 – 926

6

Beta strand

928 – 936

9

Turn

937 – 939

3

Beta strand

942 – 954

13

Beta strand

959 – 963

5

Helix

964 – 971

8

Beta strand

975 – 977

3

Helix

979 – 981

3

Beta strand

983 – 985

3

Turn

986 – 989

4

Beta strand

990 – 992

3

Beta strand

994 – 1002

9

Beta strand

1005 – 1011

7

Beta strand

1014 – 1016

3

Beta strand

1018 – 1023

6

Beta strand

1027 – 1029

3

Helix

1038 – 1040

3

Beta strand

1051 – 1061

11

Turn

1063 – 1065

3

Beta strand

1067 – 1074

8

Turn

1075 – 1078

4

Beta strand

1079 – 1084

6

Beta strand

1087 – 1090

4

Helix

1093 – 1095

3

Beta strand

1101 – 1107

7

Sequences

	Sequence		Length	Mass (Da)
	P40818 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 8B884B7A842F9A9A	FASTA	1,118	127,523
	10 20 30 40 50 60 MPAVASVPKE LYLSSSLKDL NKKTEVKPEK ISTKSYVHSA LKIFKTAEEC RLDRDEERAY 70 80 90 100 110 120 VLYMKYVTVY NLIKKRPDFK QQQDYFHSIL GPGNIKKAVE EAERLSESLK LRYEEAEVRK 130 140 150 160 170 180 KLEEKDRQEE AQRLQQKRQE TGREDGGTLA KGSLENVLDS KDKTQKSNGE KNEKCETKEK 190 200 210 220 230 240 GAITAKELYT MMTDKNISLI IMDARRMQDY QDSCILHSLS VPEEAISPGV TASWIEAHLP 250 260 270 280 290 300 DDSKDTWKKR GNVEYVVLLD WFSSAKDLQI GTTLRSLKDA LFKWESKTVL RNEPLVLEGG 310 320 330 340 350 360 YENWLLCYPQ YTTNAKVTPP PRRQNEEVSI SLDFTYPSLE ESIPSKPAAQ TPPASIEVDE 370 380 390 400 410 420 NIELISGQNE RMGPLNISTP VEPVAASKSD VSPIIQPVPS IKNVPQIDRT KKPAVKLPEE 430 440 450 460 470 480 HRIKSESTNH EQQSPQSGKV IPDRSTKPVV FSPTLMLTDE EKARIHAETA LLMEKNKQEK 490 500 510 520 530 540 ELRERQQEEQ KEKLRKEEQE QKAKKKQEAE ENEITEKQQK AKEEMEKKES EQAKKEDKET 550 560 570 580 590 600 SAKRGKEITG VKRQSKSEHE TSDAKKSVED RGKRCPTPEI QKKSTGDVPH TSVTGDSGSG 610 620 630 640 650 660 KPFKIKGQPE SGILRTGTFR EDTDDTERNK AQREPLTRAR SEEMGRIVPG LPSGWAKFLD 670 680 690 700 710 720 PITGTFRYYH SPTNTVHMYP PEMAPSSAPP STPPTHKAKP QIPAERDREP SKLKRSYSSP 730 740 750 760 770 780 DITQAIQEEE KRKPTVTPTV NRENKPTCYP KAEISRLSAS QIRNLNPVFG GSGPALTGLR 790 800 810 820 830 840 NLGNTCYMNS ILQCLCNAPH LADYFNRNCY QDDINRSNLL GHKGEVAEEF GIIMKALWTG 850 860 870 880 890 900 QYRYISPKDF KITIGKINDQ FAGYSQQDSQ ELLLFLMDGL HEDLNKADNR KRYKEENNDH 910 920 930 940 950 960 LDDFKAAEHA WQKHKQLNES IIVALFQGQF KSTVQCLTCH KKSRTFEAFM YLSLPLASTS 970 980 990 1000 1010 1020 KCTLQDCLRL FSKEEKLTDN NRFYCSHCRA RRDSLKKIEI WKLPPVLLVH LKRFSYDGRW 1030 1040 1050 1060 1070 1080 KQKLQTSVDF PLENLDLSQY VIGPKNNLKK YNLFSVSNHY GGLDGGHYTA YCKNAARQRW 1090 1100 1110 FKFDDHEVSD ISVSSVKSSA AYILFYTSLG PRVTDVAT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1." Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S. DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[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]. Tissue: Lung and Lymph.
[4]	"UBPY: a growth-regulated human ubiquitin isopeptidase." Naviglio S., Mattecucci C., Matoskova B., Nagase T., Nomura N., Di Fiore P.P., Draetta G.F. EMBO J. 17:3241-3250(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[5]	"The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation." Row P.E., Prior I.A., McCullough J., Clague M.J., Urbe S. J. Biol. Chem. 281:12618-12624(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-786.
[6]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[7]	"The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation." Row P.E., Liu H., Hayes S., Welchman R., Charalabous P., Hofmann K., Clague M.J., Sanderson C.M., Urbe S. J. Biol. Chem. 282:30929-30937(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN, INTERACTION WITH CHMP1A; CHMP1B AND CHMP7, FUNCTION, SUBCELLULAR LOCATION.
[8]	"Final stages of cytokinesis and midbody ring formation are controlled by BRUCE." Pohl C., Jentsch S. Cell 132:832-845(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH BIRC6/BRUCE AND KIF23/MKLP1.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452; SER-718 AND SER-719, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover." Waters S., Marchbank K., Solomon E., Whitehouse C., Gautel M. FEBS Lett. 583:1846-1852(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NBR1, SUBCELLULAR LOCATION.
[11]	"Essential role of hIST1 in cytokinesis." Agromayor M., Carlton J.G., Phelan J.P., Matthews D.R., Carlin L.M., Ameer-Beg S., Bowers K., Martin-Serrano J. Mol. Biol. Cell 20:1374-1387(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IST1.
[12]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[13]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-718, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-577 AND SER-718, MASS SPECTROMETRY.
[16]	"Solution structure of the rhodanese-like domain in human ubiquitin specific protease 8 (UBP8)." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 174-317.
[17]	"Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8)." Avvakumov G.V., Walker J.R., Xue S., Finerty P.J. Jr., Mackenzie F., Newman E.M., Dhe-Paganon S. J. Biol. Chem. 281:38061-38070(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-318 IN COMPLEX WITH RNF41.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D29956 mRNA. Translation: BAA06225.2.
BX537420 mRNA. Translation: CAD97662.1.
BC038801 mRNA. Translation: AAH38801.1. Sequence problems.
BC051345 mRNA. Translation: AAH51345.1. Sequence problems.
BC110590 mRNA. Translation: AAI10591.1.

IPI

IPI00030915.

RefSeq

NP_001122082.1. NM_001128610.1.
NP_001122083.1. NM_001128611.1.
NP_005145.3. NM_005154.3.

UniGene

Hs.443731.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WHB	NMR	-	A	176-317	[»]
2A9U	X-ray	2.10	A/B	1-142	[»]
2GFO	X-ray	2.00	A	734-1110	[»]
2GWF	X-ray	2.30	A/C/E	181-318	[»]
3N3K	X-ray	2.60	A	734-1110	[»]

ProteinModelPortal

P40818.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-40365N.

IntAct

P40818. 8 interactions.

MINT

MINT-244406.

STRING

9606.ENSP00000302239.

Protein family/group databases

MEROPS

C19.011.

PTM databases

PhosphoSite

P40818.

Polymorphism databases

DMDM

731046.

Proteomic databases

PaxDb

P40818.

PeptideAtlas

P40818.

PRIDE

P40818.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000307179; ENSP00000302239; ENSG00000138592.
ENST00000396444; ENSP00000379721; ENSG00000138592.
ENST00000433963; ENSP00000405537; ENSG00000138592.

GeneID

9101.

KEGG

hsa:9101.

UCSC

uc001zyl.4. human.

Organism-specific databases

CTD

9101.

GeneCards

GC15P050716.

H-InvDB

HIX0172812.

HGNC

HGNC:12631. USP8.

HPA

HPA004869.

MIM

603158. gene.

neXtProt

NX_P40818.

PharmGKB

PA37256.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5533.

HOGENOM

HOG000231497.

HOVERGEN

HBG012631.

InParanoid

P40818.

KO

K11839.

OMA

KINDQFA.

OrthoDB

EOG4XKV6B.

PhylomeDB

P40818.

Enzyme and pathway databases

BRENDA

3.1.2.15. 2681.

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P40818.

Bgee

P40818.

CleanEx

HS_USP8.

Genevestigator

P40818.

GermOnline

ENSG00000138592. Homo sapiens.

Family and domain databases

Gene3D

3.40.250.10. 1 hit.

InterPro

IPR015063. DUF1873.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
IPR001763. Rhodanese-like_dom.
[Graphical view]

Pfam

PF08969. DUF1873. 1 hit.
PF00581. Rhodanese. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]

SMART

SM00450. RHOD. 1 hit.
[Graphical view]

SUPFAM

SSF52821. Rhodanese-like. 1 hit.

PROSITE

PS50206. RHODANESE_3. 1 hit.
PS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

USP8. human.

EvolutionaryTrace

P40818.

GenomeRNAi

9101.

NextBio

34117.

SOURCE

Search...

Entry information

Entry name

UBP8_HUMAN

Accession

Primary (citable) accession number: P40818
Secondary accession number(s): Q2TB31 , Q7Z3U2, Q86VA0, Q8IWI7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 141 of the entry and version 1 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.