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B2GUZ1 (UBP4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Gene names
Name:Usp4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length961 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolase that deubiquitinates target proteins such as the receptor ADORA2A, PDPK1 and TRIM21. Deubiquitination of ADORA2A increases the amount of functional receptor at the cell surface. Plays a role in the regulation of quality control in the ER. Ref.3

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

Interacts with RB1 (both dephosphorylated and hypophosphorylated forms). Interacts with ADORA2A (via cytoplasmic C-terminus); the interaction is direct. Interacts with RB1, RBL1 and RBL2 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Shuttles between the nucleus and cytoplasm. Exported to the cytoplasm in a CRM1-dependent manner and recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The relative amounts found in the nucleus and cytoplasm vary according to the cell type By similarity.

Tissue specificity

Expressed in hippocampus and striatum (at protein level). Ref.3

Domain

The Ubiquitin-like domain 2 inserts into the catalytic domain and competes with the ubiquitin substrate, partially inhibiting DUB activity By similarity.

Post-translational modification

Monoubiquitinated by TRIM21. Ubiquitination does not lead to its proteasomal degradation. Autodeubiquitinated By similarity.

Sequence similarities

Belongs to the peptidase C19 family. USP4 subfamily.

Contains 1 DUSP domain.

Contains 2 ubiquitin-like domains.

Contains 1 USP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 961961Ubiquitin carboxyl-terminal hydrolase 4
PRO_0000396806

Regions

Domain11 – 122112DUSP
Domain142 – 22685Ubiquitin-like 1
Domain302 – 921620USP
Domain483 – 57189Ubiquitin-like 2
Region405 – 4073Necessary for interaction with RBL2 By similarity
Region459 – 4635Necessary for interaction with RB1 and RBL2 By similarity
Motif133 – 1419Nuclear export signal By similarity
Motif765 – 7706Nuclear localization signal By similarity

Sites

Active site3111 By similarity
Active site8791 By similarity
Metal binding4611Zinc By similarity
Metal binding4641Zinc By similarity
Metal binding7971Zinc By similarity
Metal binding8001Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
B2GUZ1 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: D6DD975327451B9F

FASTA961108,373
        10         20         30         40         50         60 
MAEGRGTHER PDVETQKTEL GALMGTTLQR GAQWYLIDSR WFKQWKKYVG FDSWDMYNVG 

        70         80         90        100        110        120 
EHNLFPGPID NSGLFSDPES QTLKEHLIDE LDYVLVPTEA WNKLLNWYGC VEGQQPIVRK 

       130        140        150        160        170        180 
VVEHGLFVKH CKVEVYLLEL KLCENSDPTN VLSCHFSKAD TIATIEKEMR KLFNIPAERE 

       190        200        210        220        230        240 
TRLWNKYMSN TYEQLSKLDN TIQDAGLYQG QVLVIEPQNE DGTWPRQTLQ SKSSTAPSRN 

       250        260        270        280        290        300 
FTTSSKPSAS PYSSMSASLI ANGDSTNSSG MHNSGVSRGG AGFSASYNCQ EPPSPHIQPG 

       310        320        330        340        350        360 
LCGLGNLGNT CFMNSALQCL SNTGPLTEYF LKDEYEAEIN RDNPLGMKGE IAEAYAELIK 

       370        380        390        400        410        420 
QMWSGRDTHV APRMFKTQVG RFAPQFSGYQ QQDSQELLAF ILDGLHEDLN RVKKKPYLEP 

       430        440        450        460        470        480 
KDANGRPDAV VAKEAWENHR LRNDSVIVDT FHGLFKSTLV CPECAKVSVT FDPFCYLTLP 

       490        500        510        520        530        540 
LPLKKDRIME VFLVPADPHC RPIQYRVTVP LMGAISDLCE ALSKLSGIAA ENMVVTDVYN 

       550        560        570        580        590        600 
HRFHKIFQMD EGLSHITPRD DIFVYEICTT PMDGSEYITL PVYFREKKSR PSSTSSGAVL 

       610        620        630        640        650        660 
YGQPLLVSVP KHRLTLESLY QAVCERISRY IKQPLPEEFL SSPLEPGACN GSRGSYEGDE 

       670        680        690        700        710        720 
EEMDHQEEGK EQLSEVEESG EDSQGGDPTE TTQKAKGPPR HKRLFTFSLV NSCGTADINS 

       730        740        750        760        770        780 
LATDGKLLKL NSRSTLAIDW DSETRSLYFD EQESEACEKH TSMSQPQKKK KAAIALRECI 

       790        800        810        820        830        840 
ELFTTMETLG EHDPWYCPTC KKHQQATKKF DLWSLPKILV VHLKRFSYNR YWRDKLDTVV 

       850        860        870        880        890        900 
EFPVRALNMS EFVCDRAARP YVYDLIAVSN HYGAMGVGHY TAYAKNRLNG KWYYFDDSSV 

       910        920        930        940        950        960 
SLASEDQIVT KAAYVLFYQR RDDECPSTSS PVSFPGSDGG AKLSSSQQDL GEEEAYTMDT 


N 

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References

« Hide 'large scale' references
[1]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"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.
[3]"The ubiquitin-specific protease Usp4 regulates the cell surface level of the A2A receptor."
Milojevic T., Reiterer V., Stefan E., Korkhov V.M., Dorostkar M.M., Ducza E., Ogris E., Boehm S., Freissmuth M., Nanoff C.
Mol. Pharmacol. 69:1083-1094(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC166460 mRNA. Translation: AAI66460.1.
CH473954 Genomic DNA. Translation: EDL77177.1.
RefSeqNP_001128484.1. NM_001135012.1.
XP_006243773.1. XM_006243711.1.
UniGeneRn.92126.

3D structure databases

ProteinModelPortalB2GUZ1.
SMRB2GUZ1. Positions 1-124.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid253348. 1 interaction.

PTM databases

PhosphoSiteB2GUZ1.

Proteomic databases

PRIDEB2GUZ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000073725; ENSRNOP00000066449; ENSRNOG00000046486.
GeneID290864.
KEGGrno:290864.

Organism-specific databases

CTD7375.
RGD1587387. Usp4.

Phylogenomic databases

GeneTreeENSGT00670000097750.
HOVERGENHBG000864.
KOK11835.
OMAVEFPTRG.
OrthoDBEOG77Q4VW.
PhylomeDBB2GUZ1.

Gene expression databases

GenevestigatorB2GUZ1.

Family and domain databases

Gene3D3.30.2230.10. 1 hit.
InterProIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028135. Ub_USP-typ.
IPR028889. UCH/PAN2.
IPR028134. USP.
[Graphical view]
PANTHERPTHR24006:SF360. PTHR24006:SF360. 1 hit.
PfamPF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMSSF143791. SSF143791. 1 hit.
PROSITEPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio631779.

Entry information

Entry nameUBP4_RAT
AccessionPrimary (citable) accession number: B2GUZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: June 10, 2008
Last modified: June 11, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries