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B3LGK1 (UBP4_YEAS1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 4

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 4
Ubiquitin thioesterase 4
Ubiquitin-specific-processing protease 4
Vacuole biogenesis protein SSV7
Gene names
Name:DOA4
Synonyms:DOS1, MUT4, NPI2, SSV7, UBP4
ORF Names:SCRG_00446
OrganismSaccharomyces cerevisiae (strain RM11-1a) (Baker's yeast) [Complete proteome]
Taxonomic identifier285006 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length926 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Ubiquitin thioesterase that acts at the late endosome/prevacuolar compartment to recover ubiquitin from ubiquitinated membrane proteins en route to the vacuole. Removes also ubiquitin from soluble proteins targeted to proteasomes. Is essential to maintain a normal level of free ubiquitin. Involved in the ammonium-induced down-regulation of the GAP1 permease and the UME3 destruction in response to oxidative stress. Has a role in the RAD9 checkpoint response to TOP1 poisons. Required for promoting coordination of DNA replication and avoids DNA overreplication By similarity.

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).

Enzyme regulation

RFU1 is an inhibitor of deubiquitination activity By similarity.

Subunit structure

Interacts with BRO1, RFU1 and VPS32. Associates with the 26S proteasome By similarity.

Subcellular location

Cytoplasm By similarity. Late endosome membrane; Peripheral membrane protein By similarity. Note: Recruited to the late endosome by BRO1 By similarity.

Domain

Residues 1-208 are essential for the localization to the late endosome and constitute a late endosome localization (LEL) domain By similarity.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 rhodanese domain.

Contains 1 USP domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Endosome
Membrane
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentlate endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 926926Ubiquitin carboxyl-terminal hydrolase 4
PRO_0000376822

Regions

Domain205 – 328124Rhodanese
Domain562 – 923362USP
Compositional bias128 – 1347Poly-Asn
Compositional bias386 – 3927Poly-Gln

Sites

Active site5711Nucleophile By similarity
Active site8801Proton acceptor By similarity

Amino acid modifications

Modified residue4431Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B3LGK1 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: BE75CFBAE9C1A9F6

FASTA926105,188
        10         20         30         40         50         60 
MEQNIISTIR DECIRHRSKY LTIAQLTAIA EAKINEFIIT GKAKDQDLSS LLDKCIDILS 

        70         80         90        100        110        120 
IYKKNSKDIK NIISCKNKGA MISSNSVMII QLNYVYYKVI HIIVTTNIPH LSEFAKIKLH 

       130        140        150        160        170        180 
KSTSDEGNGN NNNNEFQLMN IYNTLLETLL KDENIAKIKS FIKSSIKQTK LNHEQEECNL 

       190        200        210        220        230        240 
MRTGSYITSN QLNSLISSSA NSASSQMEIL LIDIRSRLEF NKSHIDTKNI ICLEPISFKM 

       250        260        270        280        290        300 
SYSDHDLEKK SLITSPNSEI KMFQSRNLFK FIILYTDANE YNVKQQSVLL DILVNHSFEK 

       310        320        330        340        350        360 
PISDDFTKIF ILESGFPGWL KSNYGRQVSS SFPSNNNIKD DSVYINGNTS GLSLQHLPKM 

       370        380        390        400        410        420 
SPSIRHSMDD SMKEMLVAPT PLNHLQQQQQ QQSDNDHVLK RSSSFKKLFS NYTSPNPKNS 

       430        440        450        460        470        480 
NSNLYSISSL SISSSPSPLP LHSPDPVKGN SLPINYPETP HLWKNSETDF MTNQREQLNH 

       490        500        510        520        530        540 
NSFAHVAPIN TKAITSPSRT ATPKLQRFPQ TISMNLNMNS NGHSSATSTI QPSCLSLSNN 

       550        560        570        580        590        600 
DSLDHTDVTP TSSHNYDLDF AVGLENLGNS CYMNCIIQCI LGTHELTQIF LDDSYAKHIN 

       610        620        630        640        650        660 
INSKLGSKGI LAKYFARLVH MMYKEQVDGS KKIPISPIKF KLACGSVNSL FKTASQQDCQ 

       670        680        690        700        710        720 
EFCQFLLDGL HEDLNQCGSN PPLKELSQEA EARREKLSLR IASSIEWERF LTTDFSVIVD 

       730        740        750        760        770        780 
LFQGQYASRL KCKVCSHTST TYQPFTVLSI PIPKKNSRNN ITIEDCFREF TKCENLEVDE 

       790        800        810        820        830        840 
QWLCPHCEKR QPSTKQLTIT RLPRNLIVHL KRFDNLLNKN NDFVIYPFLL DLTPFWANDF 

       850        860        870        880        890        900 
DGVFPPGVND DELPIRGQIP PFKYELYGVA CHFGTLYGGH YTAYVKKGLK KGWLYFDDTK 

       910        920 
YKPVKNKADA INSNAYVLFY HRVYGV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH408043 Genomic DNA. Translation: EDV08230.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OrthoDBEOG7R2BSX.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR001763. Rhodanese-like_dom.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00581. Rhodanese. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUBP4_YEAS1
AccessionPrimary (citable) accession number: B3LGK1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: September 2, 2008
Last modified: April 16, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries