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Q5RCD3 (UBP4_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. 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
Gene names
Name:USP4
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length963 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 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).

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.

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 – 963963Ubiquitin carboxyl-terminal hydrolase 4
PRO_0000301667

Regions

Domain11 – 122112DUSP
Domain142 – 22685Ubiquitin-like 1
Domain302 – 923622USP
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
Motif767 – 7726Nuclear localization signal By similarity

Sites

Active site3111Nucleophile By similarity
Active site8811Proton acceptor By similarity
Metal binding4611Zinc By similarity
Metal binding4641Zinc By similarity
Metal binding7991Zinc By similarity
Metal binding8021Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RCD3 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 818FB26F04B5AD2D

FASTA963108,318
        10         20         30         40         50         60 
MAEGGGCRER PDAETQKSEL GALMRTTLQR GAQWYLIDSR WFKQWKKYVG FGSWDMYNVG 

        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 
ARLWNKYMSN TYEQLSKLDN TVQDAGLYLG QVLVIEPQNE DGTWPRQTLQ SKSSTAPSRN 

       250        260        270        280        290        300 
FTTSPKSSAS PYSSVSDSLI ANGDSTSTCG MHSSGVSRGG SGFSASYNCQ EPPSSHIQPG 

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

       370        380        390        400        410        420 
QMWSGRDAHV APRMFKTQVG RFAPQFSGYQ QQDSQELLAF LLDGLHEDLN RVKKKPYLEL 

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

       490        500        510        520        530        540 
LPLKKDRVME VFLVPADPHC RPTQYRVTVP LMGAVSDLCE ALSRLSGIAA ENMVVADVYN 

       550        560        570        580        590        600 
HRFHKIFQMD EGLNHIMPRD DIFVYEVCST SVDGSECVTL PVYFRERKSR PSSTSSASAL 

       610        620        630        640        650        660 
YGQPLLLSVP KHKLTLESLY QAVCDRISRY VKQPLPDEFG SSPLEPGACN GSRNSCEGED 

       670        680        690        700        710        720 
EEEMEHQEEG KEQLSETEGS GEDEPGSDPS ETTQKKIKGQ PCPKRLFTFS LVNSYGTADI 

       730        740        750        760        770        780 
NSLAADGKLL KLNSRSTLAM DWDSETRSLY YDEQESEAYE KHVSMLQPQK KKKTTVALRD 

       790        800        810        820        830        840 
CIELFTTMET LGEHDPWYCP NCKKHQQATK KSDLWSLPKI LVVHLKRFSY NRYWRDKLDT 

       850        860        870        880        890        900 
VVEFPIRGLN MSEFVCNLSA RPYVYDLIAV SNHYGAMGVG HYTAYAKNKL NGKWYYFDDS 

       910        920        930        940        950        960 
NVSLASEDQI VTKAAYVLFY QRRDDEFYKT PSLSSSGSSD GGTRPSSSQQ GLGDDEACSM 


DTN 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR858339 mRNA. Translation: CAH90574.1.
RefSeqNP_001125307.1. NM_001131835.1.
UniGenePab.8716.

3D structure databases

ProteinModelPortalQ5RCD3.
SMRQ5RCD3. Positions 1-124.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5RCD3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100172206.
KEGGpon:100172206.

Organism-specific databases

CTD7375.

Phylogenomic databases

HOVERGENHBG000864.
InParanoidQ5RCD3.
KOK11835.

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:SF34. PTHR24006:SF34. 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...

Entry information

Entry nameUBP4_PONAB
AccessionPrimary (citable) accession number: Q5RCD3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 55 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