Ubiquitin carboxyl-terminal hydrolase 14

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Reviewed, UniProtKB/Swiss-Prot P54578 (UBP14_HUMAN)

Last modified June 16, 2009. Version 91. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 14
    EC=3.1.2.15
Alternative name(s):
    Ubiquitin thioesterase 14
    Ubiquitin-specific-processing protease 14
    Deubiquitinating enzyme 14

Gene names

Name:	USP14
Synonyms:	TGT

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	Ubiquitin C-terminal thioester + H₂O = ubiquitin + a thiol.
Subunit structure	Homodimer Potential.
Sequence similarities	Belongs to the peptidase C19 family. Contains 1 ubiquitin-like domain.
Caution	Was originally (Ref.1) thought to be a queuine tRNA-ribosyltransferase.

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Ontologies

Keywords
Biological process	Ubl conjugation pathway
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay. Source: HPA
Molecular function	cysteine-type endopeptidase activity Traceable author statement. Source: ProtInc tRNA guanylyltransferase activity Traceable author statement. Source: ProtInc ubiquitin thiolesterase activity Inferred from electronic annotation. Source: EC ubiquitin-specific protease activity Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 494

493

Ubiquitin carboxyl-terminal hydrolase 14

PRO_0000080636

Regions

Domain

4 – 80

Ubiquitin-like

Sites

Active site

114

Active site

426

Active site

435

Amino acid modifications

Modified residue

136

Phosphotyrosine Ref.4

Modified residue

143

Phosphoserine By similarity

Modified residue

222

Phosphoserine By similarity

Secondary structure

494

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P54578-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E6D4679A86E9DF00
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FASTA

494

56,069

        10         20         30         40         50         60 
MPLYSVTVKW GKEKFEGVEL NTDEPPMVFK AQLFALTGVQ PARQKVMVKG GTLKDDDWGN 

        70         80         90        100        110        120 
IKIKNGMTLL 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 DSVKETDSSS ASAATPSKKK 

       250        260        270        280        290        300 
SLIDQFFGVE FETTMKCTES EEEEVTKGKE NQLQLSCFIN QEVKYLFTGL KLRLQEEITK 

       310        320        330        340        350        360 
QSPTLQRNAL YIKSSKISRL PAYLTIQMVR FFYKEKESVN AKVLKDVKFP LMLDMYELCT 

       370        380        390        400        410        420 
PELQEKMVSF RSKFKDLEDK KVNQQPNTSD KKSSPQKEVK YEPFSFADDI GSNNCGYYDL 

       430        440        450        460        470        480 
QAVLTHQGRS SSSGHYVSWV KRKQDEWIKF DDDKVSIVTP EDILRLSGGG DWHIAYVLLY 

       490 
GPRRVEIMEE ESEQ

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"tRNA-guanine transglycosylase cDNA from human placenta." Deshpande K.L., Katze J.R. Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[4]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-136, MASS SPECTROMETRY.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]	"Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14." Hu M., Li P., Song L., Jeffrey P.D., Chenova T.A., Wilkinson K.D., Cohen R.E., Shi Y. EMBO J. 24:3747-3756(2005) [PubMed: 16211010] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 91-494.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

U30888 mRNA. Translation: AAB60365.1.
BT007183 mRNA. Translation: AAP35847.1.
BC003556 mRNA. Translation: AAH03556.1.

IPI

IPI00219913.

PIR

G01932.

RefSeq

NP_001032411.1.
NP_005142.1.

UniGene

Hs.464416
Hs.707058

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AYN	X-ray	3.20	A/B/C	91-494	[»]
2AYO	X-ray	3.50	A	91-494	[»]

SMR

P54578. Positions 6-86.

ModBase

Search...

Protein-protein interaction databases

IntAct

P54578. 2 interactions.

Protein family/group databases

MEROPS

C19.015.

PTM databases

PhosphoSite

P54578.

2-D gel databases

OGP

P54578.

Proteomic databases

PeptideAtlas

P54578.

PRIDE

P54578.

Genome annotation databases

Ensembl

ENSG00000101557. Homo sapiens. [Contig view]

GeneID

9097.

KEGG

hsa:9097.

Organism-specific databases

GeneCards

GC18P000148.

HGNC

HGNC:12612. USP14.

HPA

HPA001308.

MIM

607274. gene.

PharmGKB

PA27523.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P54578.

HOVERGEN

P54578.

Enzyme and pathway databases

BRENDA

3.1.2.15. 247.

Gene expression databases

ArrayExpress

P54578.

Bgee

P54578.

CleanEx

HS_USP14.

GermOnline

ENSG00000101557. Homo sapiens.

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...

Other Resources

NextBio

34093.

SOURCE

Search...

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Entry information

Entry name

UBP14_HUMAN

Accession

Primary (citable) accession number: P54578
Secondary accession number(s): Q53XY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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