Ubiquitin carboxyl-terminal hydrolase 14 - Oryctolagus cuniculus (Rabbit)

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P40826 (UBP14_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 96. 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 14
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 14
Ubiquitin thioesterase 14
Ubiquitin-specific-processing protease 14

Gene names

Name:	USP14
Synonyms:	TGT

Organism

Oryctolagus cuniculus (Rabbit) [Reference proteome]

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Indispensable for synaptic development and function at neuromuscular junctions (NMJs) 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	Homodimer Potential. Associates with the 26S proteasome. Interacts with FANCC, CXCR4 and ERN1 By similarity.
Subcellular location	Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity.
Sequence similarities	Belongs to the peptidase C19 family. USP14/UBP6 subfamily. Contains 1 ubiquitin-like domain.
Caution	Was originally (Ref.1) thought to be a guanine tRNA-ribosyltransferase.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cell membrane Cytoplasm Membrane Proteasome
Molecular function	Hydrolase Protease Thiol protease
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of chemotaxis Inferred from electronic annotation. Source: Compara regulation of proteasomal protein catabolic process Inferred from electronic annotation. Source: Compara synaptic transmission Inferred from electronic annotation. Source: Compara ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cell surface Inferred from electronic annotation. Source: Compara cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome complex Inferred from electronic annotation. Source: UniProtKB-KW synapse Inferred from electronic annotation. Source: Compara
Molecular_function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW endopeptidase inhibitor activity Inferred from electronic annotation. Source: Compara ubiquitin thiolesterase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 493

493

Ubiquitin carboxyl-terminal hydrolase 14

PRO_0000080639

Regions

Domain

4 – 80

Ubiquitin-like

Sites

Active site

114

Nucleophile By similarity

Active site

434

Proton acceptor By similarity

Amino acid modifications

Modified residue

136

Phosphotyrosine By similarity

Modified residue

143

Phosphoserine By similarity

Modified residue

222

Phosphoserine By similarity

Modified residue

448

N6-acetyllysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P40826 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 598553BF435E6495
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FASTA

493

55,922

        10         20         30         40         50         60 
MPLYSVTVKW GKEKFGGVEL NTDEPPMVFK AQLFALTGVQ PARQRVMVKG GTLKDDDWGN 

        70         80         90        100        110        120 
IKIKNGMTIL MMGSADALPE EPSAKTVFVE DMTEEQLASA MELPCGLTNL GNTCYMNATV 

       130        140        150        160        170        180 
QCIRSVPELK DALKRYAGAL RASGEMASAQ YITAALRDLF DSMDKTSSSI PPIILLQFLH 

       190        200        210        220        230        240 
MAFPQFAEKG EQGQYLQQDA NECWIQMMRV LQQKLEAIED DSVKETDSSA AAVAPSKKKS 

       250        260        270        280        290        300 
LIDQFFGVEF ETTMKCTESE EEEVTKGKEN QLQLSCFINQ EVKYLFTGLK LRLQEEITKQ 

       310        320        330        340        350        360 
SPTLQRNALY IKSSKISRLP AYLTIQMVRF FYKEKESVNA KVLKDVKFPL MLDVYELCTP 

       370        380        390        400        410        420 
ELQEKMVSFR SKFKDIEDKK VNQQPNASDK KSSPQKEVRY EPFSFADDIG SNNCGYYDLQ 

       430        440        450        460        470        480 
AVLTHQGRSS SSGHYVSWVK RKHDEWIKFD DDKVSIVTPE DILRLSGGGD WHIAYVLLYG 

       490 
PRRVEIMEEE NEQ

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References

[1]

"Cloning and characterization of cDNA encoding the rabbit tRNA-guanine transglycosylase 60-kilodalton subunit."
Deshpande K.L., Seubert P.H., Tillman D.M., Farkas W.R., Katze J.R.
Arch. Biochem. Biophys. 326:1-7(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: New Zealand white.
Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L37420 mRNA. Translation: AAA96133.1.
PIR	S68430.
RefSeq	NP_001075726.1. NM_001082257.1.
UniGene	Ocu.2060.
3D structure databases
ProteinModelPortal	P40826.
SMR	P40826. Positions 6-86, 98-482.
ModBase	Search...
Protein-protein interaction databases
STRING	9986.ENSOCUP00000015687.
Protein family/group databases
MEROPS	C19.015.
Proteomic databases
PRIDE	P40826.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSOCUT00000029186; ENSOCUP00000015687; ENSOCUG00000011595.
GeneID	100009078.
Organism-specific databases
CTD	9097.
Phylogenomic databases
eggNOG	NOG286607.
GeneTree	ENSGT00390000009615.
HOGENOM	HOG000202292.
HOVERGEN	HBG054185.
OMA	YGPRRIE.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR000626. Ubiquitin. IPR019954. Ubiquitin_CS. IPR019955. Ubiquitin_supergroup. [Graphical view]
Pfam	PF00443. UCH. 1 hit. [Graphical view]
SMART	SM00213. UBQ. 1 hit. [Graphical view]
PROSITE	PS00299. UBIQUITIN_1. 1 hit. PS50053. UBIQUITIN_2. 1 hit. PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBP14_RABIT

Accession

Primary (citable) accession number: P40826

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 96 of the entry and version 3 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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents