Ubiquitin carboxyl-terminal hydrolase 15

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Q2HJE4 (UBP15_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 58. 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 15
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 15
Ubiquitin thioesterase 15
Ubiquitin-specific-processing protease 15

Gene names

Name:

USP15

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	952 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes. According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal. Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP 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	Identified in a complex with the COP9 signalosome complex (CSN). Interacts with SMAD1, SMAD2 and SMAD3; the interaction is direct. Forms a complex with SMURF2 and SMAD7. Interacts with TGFBR1 By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Post-translational modification	Phosphorylated. Phosphorylation protects against ubiquitination and subsequent degradation by the proteasome By similarity. Ubiquitinated, leading to degradation by the proteasome By similarity.
Sequence similarities	Belongs to the peptidase C19 family. Contains 1 DUSP domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Molecular function	Hydrolase Protease Thiol protease
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	BMP signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB monoubiquitinated protein deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB pathway-restricted SMAD protein phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB transforming growth factor beta receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
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 ubiquitin-specific protease activity 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

Initiator methionine

Removed By similarity

Chain

2 – 952

951

Ubiquitin carboxyl-terminal hydrolase 15

PRO_0000420489

Regions

Domain

7 – 118

112

DUSP

Sites

Active site

269

Nucleophile By similarity

Active site

862

Proton acceptor By similarity

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

932

Phosphoserine By similarity

Modified residue

936

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q2HJE4 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: A4151AAE16BE8B53
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FASTA

952

109,442

        10         20         30         40         50         60 
MAEGGAADLD IQRSDIATLL KTSLRKGDTW YLVDSRWFKQ WKKYVGFDSW DKYQMGDQNV 

        70         80         90        100        110        120 
YPGPIDNSGL LRDGDAQSLK EHLIDELDYI LLPTEGWNKL VSWYTLMEGQ EPIARKVVEQ 

       130        140        150        160        170        180 
GMFVKHCKVE VYLTELKLCE NGNMNNVVTR RFSKADTIDT IEKEIRKIFN IPDEKETRLW 

       190        200        210        220        230        240 
NKYMSNTFEP LNKPDSTIQD AGLYQGQVLV IEQKNEDGTW PRGPSTPNVK NSNYCLPSYT 

       250        260        270        280        290        300 
AYKNYDYSEP GRNNEQPGLC GLSNLGNTCF MNSAFQCLSN TPPLTEYFLN DKYQEELNFD 

       310        320        330        340        350        360 
NPLGMRGEIA KSYAELIKQM WSGKYSYVTP RAFKTQVGRF APQFSGYQQQ DCQELLAFLL 

       370        380        390        400        410        420 
DGLHEDLNRI RKKPYIQLKD ADGRPDKVVA EEAWENHLKR NDSIIVDIFH GLFKSTLVCP 

       430        440        450        460        470        480 
ECAKISVTFD PFCYLTLPLP MKKERTLEVY LVRMDPLTKP MQYKVVVPKI GNILDLCTAL 

       490        500        510        520        530        540 
SLLSGVPADK MIVTDIYNHR FHRIFAMDEN LSSIMERDDI YVFEININRT EDTEHVIIPV 

       550        560        570        580        590        600 
CLREKFRHSS YTHHTGSSLF GQPFLMAVPR NNTEDKLYNL LLVRMCRYVK ISTDTEDTEG 

       610        620        630        640        650        660 
SLHCCKDQNI NGNGPNGIHE EGSPSEMETD EPDDESSQDQ ELPSENENSQ SEDSVGGDND 

       670        680        690        700        710        720 
SENGLCTEET CRGQLTGHKK RLFTFQFNNL GNTDINYIKD DTRHIRFDDR QLRLDERSFL 

       730        740        750        760        770        780 
ALDWDPDLKK RYFDENAAED FEKHESVEYK PPKKPFVKLK DCIELFTTKE KLGAEDPWYC 

       790        800        810        820        830        840 
PNCKEHQQAT KKLDLWSLPP VLVVHLKRFS YSRYMRDKLD TLVDFPINDL DMSEFLINPN 

       850        860        870        880        890        900 
AGPCRYNLIA VSNHYGGMGG GHYTAFAKNK DDGKWYYFDD SSVSTASEDQ IVSKAAYVLF 

       910        920        930        940        950 
YQRQDTFSGT GFFPLDRETK GASAATGIPL ESDEDSNDND NDIENENCMH TN

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References

[1]	"The genome sequence of taurine cattle: a window to ruminant biology and evolution." The bovine genome sequencing and analysis consortium Science 324:522-528(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hereford.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Uterus.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DAAA02013374 Genomic DNA. No translation available. DAAA02013375 Genomic DNA. No translation available. DAAA02013376 Genomic DNA. No translation available. DAAA02013377 Genomic DNA. No translation available. DAAA02013378 Genomic DNA. No translation available. BC105521 mRNA. Translation: AAI05522.1.
IPI	IPI00697254.
RefSeq	NP_001039895.1. NM_001046430.2. XP_003586138.1. XM_003586090.1.
UniGene	Bt.29017.
3D structure databases
ProteinModelPortal	Q2HJE4.
SMR	Q2HJE4. Positions 1-120.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000037402.
Protein family/group databases
MEROPS	C19.022.
Proteomic databases
PRIDE	Q2HJE4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000037574; ENSBTAP00000037402; ENSBTAG00000010428.
GeneID	538284.
KEGG	bta:538284.
Organism-specific databases
CTD	9958.
Phylogenomic databases
eggNOG	COG5560.
GeneTree	ENSGT00670000097750.
HOGENOM	HOG000264375.
HOVERGEN	HBG000864.
InParanoid	Q2HJE4.
KO	K11835.
OMA	RMDPLAK.
OrthoDB	EOG4DNF3R.
Enzyme and pathway databases
BioCyc	CATTLE:538284-MONOMER.
Family and domain databases
InterPro	IPR006615. Pept_C19_DUSP. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b. [Graphical view]
Pfam	PF06337. DUSP. 1 hit. PF00443. UCH. 1 hit. [Graphical view]
SMART	SM00695. DUSP. 1 hit. [Graphical view]
SUPFAM	SSF55205. RNA3'_cycl/enolpyr_transf_A/B. 1 hit.
PROSITE	PS51283. DUSP. 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
NextBio	20877322.

Entry information

Entry name

UBP15_BOVIN

Accession

Primary (citable) accession number: Q2HJE4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2012
Last sequence update:	March 21, 2006
Last modified:	May 29, 2013
This is version 58 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

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

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents