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A5PMR2 (UBP33_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. 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:ch211-284g18.1
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length897 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 – 897897Ubiquitin carboxyl-terminal hydrolase 33
PRO_0000390426

Regions

Domain156 – 670515USP
Domain672 – 76594DUSP 1
Domain773 – 876104DUSP 2
Zinc finger29 – 9365UBP-type

Sites

Active site1651Nucleophile By similarity
Active site6281Proton acceptor By similarity

Experimental info

Sequence conflict2071I → V in AAH66557. Ref.2
Sequence conflict2171A → S in AAH66557. Ref.2
Sequence conflict7321A → T in AAH66557. Ref.2

Sequences

Sequence LengthMass (Da)Tools
A5PMR2 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 19103583F04B4315

FASTA897100,655
        10         20         30         40         50         60 
MSGVSSNDCP HLECVGEITK EELIQKSHGQ CQDCKVGGPN LWACLENGCS YVGCGESHAD 

        70         80         90        100        110        120 
HSTVHSQETR HNLTVNLTTL RVWCYACTKE VFLERKLGPH KQLPNAAKAV SPVQTPCQDL 

       130        140        150        160        170        180 
NTPGSPTSLR VPSAGTCDDL DMETEEEDEL RTRGLTGLKN IGNTCYMNAA LQALSNCPPL 

       190        200        210        220        230        240 
TQFFLECGGL VKTDKKPALC KSYQKLITDL WHKNRNAYVV PTNLFQGIKA VNPMFRGYSQ 

       250        260        270        280        290        300 
QDSQEFLRCL MDQLHEELKE LIPEPEDPNQ AVAMDDSPDE DNHSQSDDFQ SCESCGSSDR 

       310        320        330        340        350        360 
ADNEGPRVPE DINEAEMLMP EQNQNNRDWQ KEKNLINNLY RAGSHGDLDK DVDTTSDSRP 

       370        380        390        400        410        420 
IISSQGAIKA QGRTSDSEIQ VSSTVRPQSP TGNEGITSRL SSSPPKSSAW PNLSSTHKKV 

       430        440        450        460        470        480 
PMFTPTKTKR QRKYHSIISE VFDGTIVSSV QCLTCDRVSV TLENFQDISL PIPGKEDLAK 

       490        500        510        520        530        540 
LHSSSHQTAL VKAGSCGEAY APQGWIAFVM EYIKSWFWGP VVTLQDCLAA FFARDELKGD 

       550        560        570        580        590        600 
NMYSCEKCKK LRNGVKFCKV QSLPEILCIH LKRFRHELMF STKIGTHVSF PLEGLEMQPF 

       610        620        630        640        650        660 
LAKDSSALTT TYDLLSVICH HGTASSGHYI AYCRNELNQL WYEFDDQSVT EVSESCVQNA 

       670        680        690        700        710        720 
EAYVLFYKKS NDETQKERRK VTSLFNMMEP SLLQFYVSRQ WLNKFKTFAE PGPISNHDFL 

       730        740        750        760        770        780 
CAHGGIPPNK AAYIDDLVLM IPQNVWDHLY SRYGGGPAVN HLYVCHTCQN EIEKLEKRRK 

       790        800        810        820        830        840 
NELDMFVRLN KAFQEEESPV VIYCISMQWF REWESFVKGK DIDPPGPIDN SKIAVNKNGH 

       850        860        870        880        890 
ITLKPGADSG QISEETWNFL HNIHGGGPVV TVRPSVSHQE SETSQSEEKI EVETRTV 

« Hide

References

[1]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX649634 Genomic DNA. Translation: CAN88027.1.
BC066557 mRNA. Translation: AAH66557.1.
RefSeqNP_998392.1. NM_213227.1.
UniGeneDr.32515.

3D structure databases

ProteinModelPortalA5PMR2.
SMRA5PMR2. Positions 7-98.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC19.037.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000018114; ENSDARP00000014516; ENSDARG00000016163.
GeneID406508.
KEGGdre:406508.

Organism-specific databases

CTD23032.
ZFINZDB-GENE-040426-2323. usp33.

Phylogenomic databases

eggNOGCOG5560.
GeneTreeENSGT00750000117701.
HOGENOMHOG000286031.
HOVERGENHBG054196.
KOK11848.
OMALPSNEGV.
OrthoDBEOG7CRTP2.
PhylomeDBA5PMR2.
TreeFamTF352179.

Gene expression databases

BgeeA5PMR2.

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...

Other

NextBio20818084.
PROA5PMR2.

Entry information

Entry nameUBP33_DANRE
AccessionPrimary (citable) accession number: A5PMR2
Secondary accession number(s): Q6NYK6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: July 10, 2007
Last modified: April 16, 2014
This is version 51 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