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Q28CN3 (UBP33_XENTR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 53. 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
ORF Names:TEgg041n23.1
OrganismXenopus tropicalis (Western clawed frog) (Silurana tropicalis) [Reference proteome]
Taxonomic identifier8364 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana

Protein attributes

Sequence length892 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). 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).

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.

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
   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 – 892892Ubiquitin carboxyl-terminal hydrolase 33
PRO_0000390427

Regions

Domain148 – 665518USP
Domain667 – 76094DUSP 1
Domain768 – 871104DUSP 2
Zinc finger28 – 9265UBP-type

Sites

Active site1571Nucleophile By similarity
Active site6231Proton acceptor By similarity

Experimental info

Sequence conflict3201S → I in CAJ82183. Ref.1
Sequence conflict6711K → I in AAI71081. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q28CN3 [UniParc].

Last modified May 29, 2013. Version 2.
Checksum: 8605699C7AB5B8AC

FASTA892100,733
        10         20         30         40         50         60 
MSSLVCDCPH LESVGEVTKE ELIKKSHGSC QDCRVRGPNL WACLENGCSY VGCGESHVDH 

        70         80         90        100        110        120 
STLHSQDTKH CLTVNLTTLR VWCYTCSKEV FLDRKLSTQP TSAKLQDSHT QESKMSSSLT 

       130        140        150        160        170        180 
LKIPAAVVSE NLDIELEEED ELKTRGLTGL KNIGNTCYMN AALQALSNCP PLTHYFLDCG 

       190        200        210        220        230        240 
GLARTDKKPA LCKSYQKLMS DIWHKNRPGF VIPTNLFQGI KSVNPTFRGY SQQDAQEFLR 

       250        260        270        280        290        300 
CLMDVLHEEL KEQIVEVEED AQTGIVEENL DEDKSQSDND FHSCDSGSSS DHAESESRKL 

       310        320        330        340        350        360 
SEELTESTML IHEDQKDVES CKTWQKEKKF SNNLNQNHFL QDFEKNIQST IEESECLKQE 

       370        380        390        400        410        420 
TVKVQIQSKA ADFTAEVNMN DLPTSQTPLL NEGATTHLSS SPPKPGAVWT GHKKVPGLCP 

       430        440        450        460        470        480 
AKKRKQKKYH SVIADIFDGT IVSSVQCLTC DRVSVTLETF QDLSLPIPGK EDLAKLHSSS 

       490        500        510        520        530        540 
HQSSLVKAGS CGEAYAPQGW IAFFLEYFKS WFWGPTVTLQ DCLAAFFARD ELKGDNMYSC 

       550        560        570        580        590        600 
EKCKKLRNGV KFCKVQKFPE ILCIHLKRFR HELMFSTKIG THVSFPLEGL DLQPFLAKDS 

       610        620        630        640        650        660 
PSQIVTYDLL SVICHHGTAS SGHYIAYCRN NLNNLWYEFD DQSVTEVSEA TVQNAEAYVL 

       670        680        690        700        710        720 
FYRKASEEAQ KERRRVSCLL NIMEPSLLQF YISRQWLNKF KTFAEPGPIS NNDFLCIHGG 

       730        740        750        760        770        780 
VPPRKASFIE DLVVMLPQNI WDYLYSRYGG GPAVNHLYVC YTCQTEMEKI EKRRKMELET 

       790        800        810        820        830        840 
FIRLNKAFQE EESPAVIYCI SMQWFREWEG FVKSKDSDPP GPIDNTKIAA AKCGHITLRQ 

       850        860        870        880        890 
GADSGQISEE TWLFLQSIYG GGPEITLRQN VTLAESEGGH AEEKIDVETR NI 

« Hide

References

[1]Sanger Xenopus tropicalis EST/cDNA project
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Egg.
[2]"The genome of the Western clawed frog Xenopus tropicalis."
Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R., Gerhard D.S. expand/collapse author list , Goodstein D., Graves T., Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., Rokhsar D.S.
Science 328:633-636(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]NIH - Xenopus Gene Collection (XGC) project
Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Neurula.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR926290 mRNA. Translation: CAJ82183.1.
AAMC01095352 Genomic DNA. No translation available.
AAMC01095353 Genomic DNA. No translation available.
BC171081 mRNA. Translation: AAI71081.1.
RefSeqNP_001016228.1. NM_001016228.2.
UniGeneStr.42260.

3D structure databases

ProteinModelPortalQ28CN3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING8364.ENSXETP00000028749.

Protein family/group databases

MEROPSC19.037.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID548982.
KEGGxtr:548982.

Organism-specific databases

CTD23032.
XenbaseXB-GENE-1016674. usp33.

Phylogenomic databases

eggNOGCOG5560.
HOGENOMHOG000286031.
HOVERGENHBG054196.
KOK11848.
OrthoDBEOG7CRTP2.
TreeFamTF352179.

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. 2 hits.
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_XENTR
AccessionPrimary (citable) accession number: Q28CN3
Secondary accession number(s): B7ZU27, F7EIJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: May 29, 2013
Last modified: April 16, 2014
This is version 53 of the entry and version 2 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