Ubiquitin carboxyl-terminal hydrolase 33 - Pongo abelii (Sumatran orangutan)

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Q5REG5 (UBP33_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 50. 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 33
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 33
Ubiquitin thioesterase 33
Ubiquitin-specific-processing protease 33

Gene names

Name:

USP33

Organism

Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	914 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Deubiquitinating enzyme involved in various processes such as cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. 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 By similarity.
Subcellular location	Cytoplasm › perinuclear region 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.

Ontologies

Keywords
Biological process	Endocytosis Ubl conjugation pathway
Cellular component	Cytoplasm
Domain	Repeat Zinc-finger
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	axon guidance Inferred from sequence or structural similarity. Source: UniProtKB cell migration 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 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_component	perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cysteine-type endopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin thiolesterase 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 914

914

Ubiquitin carboxyl-terminal hydrolase 33

PRO_0000390425

Regions

Domain

685 – 778

DUSP 1

Domain

786 – 893

108

DUSP 2

Zinc finger

28 – 92

UBP-type

Sites

Active site

163

Nucleophile By similarity

Active site

641

Proton acceptor By similarity

Amino acid modifications

Modified residue

407

Phosphoserine By similarity

Experimental info

Sequence conflict

Q → H in CAH92249. Ref.1

Sequence conflict

I → V in CAH92249. Ref.1

Sequence conflict

305

S → R in CAH92249. Ref.1

Sequence conflict

787

E → K in CAH92249. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q5REG5 [UniParc].

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

FASTA

914

103,637

        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

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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.
RefSeq	NP_001124855.1. NM_001131383.1.
UniGene	Pab.19411.
3D structure databases
ProteinModelPortal	Q5REG5.
SMR	Q5REG5. Positions 5-99.
ModBase	Search...
Protein family/group databases
MEROPS	C19.037.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100171716.
KEGG	pon:100171716.
Organism-specific databases
CTD	23032.
Phylogenomic databases
HOGENOM	HOG000286031.
HOVERGEN	HBG054196.
InParanoid	Q5REG5.
KO	K11848.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR006615. Pept_C19_DUSP. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR013083. Znf_RING/FYVE/PHD. IPR001607. Znf_UBP. [Graphical view]
Pfam	PF06337. DUSP. 1 hit. PF00443. UCH. 1 hit. PF02148. zf-UBP. 1 hit. [Graphical view]
SMART	SM00695. DUSP. 2 hits. [Graphical view]
PROSITE	PS51283. DUSP. 2 hits. PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. PS50271. ZF_UBP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBP33_PONAB

Accession

Primary (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 3, 2013
This is version 50 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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents