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Q9R085 (UBP15_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. 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 carboxyl-terminal hydrolase of 109 kDa
Ubiquitin thioesterase 15
Ubiquitin-specific-processing protease 15
Gene names
Name:Usp15
Synonyms:ubp109
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length952 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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). Ref.1

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. Nucleus Ref.1.

Tissue specificity

Highly expressed in testis and spleen, and at lower level in other tissues. Ref.1

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_0000420490

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
Q9R085 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6BE7449FD93CF658

FASTA952109,255
        10         20         30         40         50         60 
MAEGGAADLD TQRSDIATLL KTSLRKGDTW YLVDSRWFKQ WKKYVGFDSW DKYQMGDQNV 

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

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

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

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

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

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

       430        440        450        460        470        480 
ECAKISVTFD PFCYLTLPLP MKKERSLEVY LVRMDPLAKP MQYKVIVPKI GNILDLCTAL 

       490        500        510        520        530        540 
SALSGVPADK MIVTDIYNHR FHRIFAMDEN LSSIMERDDI YVFEININRT EDTEHVVIPV 

       550        560        570        580        590        600 
CLREKFRHSS YTHHTGSSLF GQPFLMAVPR NNTEDKLYNL LLLRMCRYVK MSTETEETDG 

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

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

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

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

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

       910        920        930        940        950 
YQRQDTFSGT GFFPLDRETK GASAATGVPL ESDEDSNDND NDLENENCMH TN 

« Hide

References

« Hide 'large scale' references
[1]"Tissue-specificity, functional characterization and subcellular localization of a rat ubiquitin-specific processing protease, UBP109, whose mRNA expression is developmentally regulated."
Park K.C., Choi E.J., Min S.W., Chung S.S., Kim H., Suzuki T., Tanaka K., Chung C.H.
Biochem. J. 349:443-453(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Skeletal muscle.
[2]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF106657 mRNA. Translation: AAF14188.1.
RefSeqNP_660185.1. NM_145184.1.
UniGeneRn.161933.

3D structure databases

ProteinModelPortalQ9R085.
SMRQ9R085. Positions 1-120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000034485.

Protein family/group databases

MEROPSC19.022.

PTM databases

PhosphoSiteQ9R085.

Proteomic databases

PRIDEQ9R085.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID171329.
KEGGrno:171329.

Organism-specific databases

CTD9958.
RGD628795. Usp15.

Phylogenomic databases

eggNOGCOG5560.
HOGENOMHOG000264375.
HOVERGENHBG000864.
KOK11835.
OrthoDBEOG77Q4VW.
PhylomeDBQ9R085.

Gene expression databases

GenevestigatorQ9R085.

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.
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.
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

NextBio35574809.

Entry information

Entry nameUBP15_RAT
AccessionPrimary (citable) accession number: Q9R085
Secondary accession number(s): E9PSP9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 83 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