Ubiquitin carboxyl-terminal hydrolase 4

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B2GUZ1 (UBP4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 31. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	961 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of protein ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein localization to cell surface Inferred from sequence or structural similarity. Source: UniProtKB regulation of protein stability Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-specific protease activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 961

961

Ubiquitin carboxyl-terminal hydrolase 4

PRO_0000396806

Regions

Domain

11 – 122

112

DUSP

Domain

142 – 226

Ubiquitin-like 1

Domain

483 – 571

Ubiquitin-like 2

Region

405 – 407

Necessary for interaction with RBL2 By similarity

Region

459 – 463

Necessary for interaction with RB1 and RBL2 By similarity

Motif

133 – 141

Nuclear export signal By similarity

Motif

765 – 770

Nuclear localization signal By similarity

Sites

Active site

311

By similarity

Active site

879

By similarity

Metal binding

461

Zinc By similarity

Metal binding

464

Zinc By similarity

Metal binding

797

Zinc By similarity

Metal binding

800

Zinc By similarity

Amino acid modifications

Modified residue

679

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

B2GUZ1 [UniParc].

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

961

108,373

        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' referencesShow '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.
IPI	IPI00914176.
RefSeq	NP_001128484.1. NM_001135012.1.
UniGene	Rn.92126.
3D structure databases
ProteinModelPortal	B2GUZ1.
SMR	B2GUZ1. Positions 1-124.
ModBase	Search...
PTM databases
PhosphoSite	B2GUZ1.
Proteomic databases
PRIDE	B2GUZ1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000073725; ENSRNOP00000066449; ENSRNOG00000046486.
GeneID	290864.
KEGG	rno:290864.
Organism-specific databases
CTD	7375.
RGD	1587387. Usp4.
Phylogenomic databases
GeneTree	ENSGT00670000097750.
HOVERGEN	HBG000864.
KO	K11835.
Gene expression databases
Genevestigator	B2GUZ1.
Family and domain databases
InterPro	IPR006615. Pept_C19_DUSP. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF06337. DUSP. 1 hit. PF00443. UCH. 1 hit. [Graphical view]
SMART	SM00695. DUSP. 1 hit. [Graphical view]
PROSITE	PS51283. DUSP. 1 hit. PS00299. UBIQUITIN_1. False negative. PS50053. UBIQUITIN_2. False negative. PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	631779.

Entry information

Entry name

UBP4_RAT

Accession

Primary (citable) accession number: B2GUZ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 10, 2010
Last sequence update:	June 10, 2008
Last modified:	April 3, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents