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Reviewed, UniProtKB/Swiss-Prot P40818 (UBP8_HUMAN)

Last modified November 25, 2008. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Ubiquitin carboxyl-terminal hydrolase 8
    EC=3.1.2.15
Alternative name(s):
    Ubiquitin thioesterase 8
    Ubiquitin-specific-processing protease 8
    Deubiquitinating enzyme 8
      Short name=hUBPy
Gene names
Name: USP8
Synonyms: KIAA0055, UBPY
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length1118 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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. Involved in cell proliferation. Probably regulates the stability of STAM2 and RASGRF1. 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 STAM2.

Catalytic activity

Ubiquitin C-terminal thioester + H(2)O = ubiquitin + a thiol.

Subunit structure

Forms a ternary complex with RNF128 and OTUB1. Interacts with the SH3 domain of STAM2. Interacts with RASGRF1 and RNF41.

Induction

Upon growth stimulation in starved human fibroblasts. Decreases in response to growth arrest induced by cell-cell contact.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 rhodanese domain.

Sequence caution

The sequence AAH38801.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

The sequence AAH51345.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

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Ontologies

Keywords

   Biological processUbl conjugation pathway
   Coding sequence diversityPolymorphism
   DomainSH3-binding
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processcell proliferation Ref.4

Traceable author statement. Source: ProtInc

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleus

Inferred from direct assay. Source: HPA

   Molecular functionSH3 domain binding

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-type endopeptidase activity

Traceable author statement. Source: ProtInc

ubiquitin thiolesterase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

YWHABP319461EBI-1050865,EBI-359815
YWHAQP273481EBI-1050865,EBI-359854
YWHAZP631041EBI-1050865,EBI-347088

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11181118Ubiquitin carboxyl-terminal hydrolase 8
PRO_0000080627

Regions

Domain195 – 313119Rhodanese
Motif405 – 4139SH3-binding By similarity

Sites

Active site7861 By similarity
Active site10591 By similarity
Active site10671 By similarity

Amino acid modifications

Modified residue4341Phosphoserine
Modified residue4521Phosphoserine
Modified residue7181Phosphoserine
Modified residue7191Phosphoserine

Natural variations

Natural variant4431D → G: dbSNP rs3743044.
VAR_017796
Natural variant8271A → G: dbSNP rs1056577.
VAR_017797

Experimental info

Sequence conflict5261E → G in CAD97662. Ref.2
Sequence conflict7171Y → H in CAD97662. Ref.2
Sequence conflict9451T → A in CAD97662. Ref.2

Secondary structure

1 ................................................................................................................. 1118
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P40818-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 8B884B7A842F9A9A

FASTA1,118127,523
        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