Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5REG5 (UBP33_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 57. 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 33

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 33
Ubiquitin thioesterase 33
Ubiquitin-specific-processing protease 33
Gene names
Name:USP33
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length914 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains 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 VHL, leading to its ubiquitination and subsequent degradation. Interacts with ARRB1, ARRB2, ADRB2, DIO2 and ROBO1. Interacts with SELENBP1; in a selenium-dependent manner. Interacts with CCP110 By similarity.

Subcellular location

Cytoplasmperinuclear region By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Note: Associates with centrosomes predominantly in S and G2 phases but less in G1 phase By similarity.

Domain

The UBP-type zinc finger binds 3 zinc ions. However, it does not bind ubiquitin, probably because the conserved Arg in position 55 is replaced by a Glu residue By similarity.

Post-translational modification

Ubiquitinated via a VHL-dependent pathway for proteasomal degradation By similarity.

Sequence similarities

Belongs to the peptidase C19 family. USP20/USP33 subfamily.

Contains 2 DUSP domains.

Contains 1 UBP-type zinc finger.

Contains 1 USP domain.

Ontologies

Keywords
   Biological processEndocytosis
Ubl conjugation pathway
   Cellular componentCytoplasm
Cytoskeleton
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

centrosome duplication

Inferred from sequence or structural similarity. Source: UniProtKB

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

protein K48-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein K63-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of G-protein coupled receptor protein signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcentrosome

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type endopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin thiolesterase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 914914Ubiquitin carboxyl-terminal hydrolase 33
PRO_0000390425

Regions

Domain154 – 683530USP
Domain685 – 77894DUSP 1
Domain786 – 893108DUSP 2
Zinc finger28 – 9265UBP-type

Sites

Active site1631Nucleophile By similarity
Active site6411Proton acceptor By similarity

Amino acid modifications

Modified residue4071Phosphoserine By similarity

Experimental info

Sequence conflict271Q → H in CAH92249. Ref.1
Sequence conflict631I → V in CAH92249. Ref.1
Sequence conflict3051S → R in CAH92249. Ref.1
Sequence conflict7871E → K in CAH92249. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5REG5 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: DD772E64F42C0829

FASTA914103,637
        10         20         30         40         50         60 
MSAFRNHCPH LDSVGEITKE DLIQKSQGTC QDCKVRGPNL WACLENRCSY VGCGESQVDH 

        70         80         90        100        110        120 
STIHSQETKH YLTVNLTTLR VWCYACSKEV FLDRKLGTQP SLPHVRQPHQ IQENSVQDFK 

       130        140        150        160        170        180 
IPSNTTLKTP LVAVFDDLDI EVDEEDELRA RGLTGLKNIG NTCYMNAALQ ALSNCPPLTQ 

       190        200        210        220        230        240 
FFLDCGGLAR TDKKPAICKS YLKLMTELWH KSRPGSVVPT NLFQGIKTVN PTFRGYSQQD 

       250        260        270        280        290        300 
AQEFLRCLMD LLHEELKEQV MEVEDPQTIT TEETMEEDKS QSDVDFQSCE SCSNSDKAEN 

       310        320        330        340        350        360 
ENGSSCFSED NNETTMLIQD DENNSEMSKD WQKEKMCNKI NKVNSEGELD KDRDSISETV 

       370        380        390        400        410        420 
DLNNQETVKV QIHSRASEYI TDVHSNDLST PQILPSNESI NPRLSASPPK SGNLWPGLAP 

       430        440        450        460        470        480 
PHKKAQSASP KRKKQHKKYR SVISDIFDGT IISSVQCLTC DRVSVTLETF QDLSLPIPGK 

       490        500        510        520        530        540 
EDLAKLHSSS HPTSIVKAGS CGEAYAPQGW IAFFMEYVKR FVVSCVPSWF WGPVVTLQDC 

       550        560        570        580        590        600 
LAAFFARDEL KGDNMYSCEK CKKLRNGVKF CKVQKFPEIL CIHLKRFRHE LMFSTKISTH 

       610        620        630        640        650        660 
VSFPLEGLDL QPFLAKDSPA QIVTYDLLSV ICHHGTASSG HYIAYCRNNL NNLWYEFDDQ 

       670        680        690        700        710        720 
SVTEVSESTV QNAEAYVLFY RKSSEEAQKE RRRISNLLNI MEPSLLQFYI SRQWLNKFKT 

       730        740        750        760        770        780 
FAEPGPISNN DFLCIHGGVP PRKAGYIEDL VLMLPQNIWD NLYSRYGGGP AVNHLYICHT 

       790        800        810        820        830        840 
CQIEAEEIEK KKKNRRKTEL EIFIRLNRAF QKEDSPATFY CISMQWFREW ESFVKGKDGD 

       850        860        870        880        890        900 
PPGPIDNTKI AVTKCGSVML RQGADSGQIS EETWNFLQSI YGGGPEVILR PPVVHVDPDI 

       910 
LQAEEKIEVE TRSL 

« Hide

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR857564 mRNA. Translation: CAH89842.1.
CR860104 mRNA. Translation: CAH92249.1.
RefSeqNP_001124855.1. NM_001131383.1.

3D structure databases

ProteinModelPortalQ5REG5.
SMRQ5REG5. Positions 5-99.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC19.037.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100171716.
KEGGpon:100171716.

Organism-specific databases

CTD23032.

Phylogenomic databases

HOGENOMHOG000286031.
HOVERGENHBG054196.
InParanoidQ5REG5.
KOK11848.

Family and domain databases

Gene3D3.30.2230.10. 2 hits.
3.30.40.10. 1 hit.
InterProIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamPF06337. DUSP. 1 hit.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
SMARTSM00695. DUSP. 2 hits.
[Graphical view]
SUPFAMSSF143791. SSF143791. 2 hits.
PROSITEPS51283. DUSP. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUBP33_PONAB
AccessionPrimary (citable) accession number: Q5REG5
Secondary accession number(s): Q5R7L1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 57 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