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Q2HJE4 (UBP15_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 67. 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 15

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 15
Ubiquitin thioesterase 15
Ubiquitin-specific-processing protease 15
Gene names
Name:USP15
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length952 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Contains 1 USP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 952951Ubiquitin carboxyl-terminal hydrolase 15
PRO_0000420489

Regions

Domain7 – 118112DUSP
Domain260 – 904645USP

Sites

Active site2691Nucleophile By similarity
Active site8621Proton acceptor By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue9321Phosphoserine By similarity
Modified residue9361Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2HJE4 [UniParc].

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

FASTA952109,442
        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 

« Hide

References

[1]"A whole-genome assembly of the domestic cow, Bos taurus."
Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.
Genome Biol. 10:R42.01-R42.10(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.
RefSeqNP_001039895.1. NM_001046430.2.
UniGeneBt.29017.

3D structure databases

ProteinModelPortalQ2HJE4.
SMRQ2HJE4. Positions 1-120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000037402.

Protein family/group databases

MEROPSC19.022.

Proteomic databases

PRIDEQ2HJE4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000037574; ENSBTAP00000037402; ENSBTAG00000010428.
GeneID538284.
KEGGbta:538284.

Organism-specific databases

CTD9958.

Phylogenomic databases

eggNOGCOG5560.
GeneTreeENSGT00670000097750.
HOGENOMHOG000264375.
HOVERGENHBG000864.
InParanoidQ2HJE4.
KOK11835.
OMARYVKTCT.
OrthoDBEOG77Q4VW.
TreeFamTF106276.

Family and domain databases

Gene3D3.30.2230.10. 1 hit.
InterProIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR028135. Ub_USP-typ.
IPR029071. Ubiquitin-rel_dom.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMSSF143791. SSF143791. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF55205. SSF55205. 1 hit.
PROSITEPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20877322.

Entry information

Entry nameUBP15_BOVIN
AccessionPrimary (citable) accession number: Q2HJE4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: March 21, 2006
Last modified: June 11, 2014
This is version 67 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