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Q9R085

- UBP15_RAT

UniProt

Q9R085 - UBP15_RAT

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Protein

Ubiquitin carboxyl-terminal hydrolase 15

Gene
Usp15, ubp109
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei269 – 2691Nucleophile By similarity
Active sitei862 – 8621Proton acceptor By similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. ubiquitin-specific protease activity Source: RGD
  3. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

  1. BMP signaling pathway Source: UniProtKB
  2. monoubiquitinated protein deubiquitination Source: UniProtKB
  3. pathway-restricted SMAD protein phosphorylation Source: UniProtKB
  4. protein deubiquitination Source: UniProtKB
  5. transforming growth factor beta receptor signaling pathway Source: UniProtKB
  6. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_194641. Downregulation of TGF-beta receptor signaling.

Protein family/group databases

MEROPSiC19.022.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Usp15
Synonyms:ubp109
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi628795. Usp15.

Subcellular locationi

Cytoplasm. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 952951Ubiquitin carboxyl-terminal hydrolase 15PRO_0000420490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei932 – 9321Phosphoserine By similarity
Modified residuei936 – 9361Phosphoserine By similarity

Post-translational modificationi

Phosphorylated. Phosphorylation protects against ubiquitination and subsequent degradation by the proteasome By similarity.
Ubiquitinated, leading to degradation by the proteasome By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ9R085.

PTM databases

PhosphoSiteiQ9R085.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriQ9R085.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000034485.

Structurei

3D structure databases

ProteinModelPortaliQ9R085.
SMRiQ9R085. Positions 1-120.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 118112DUSPAdd
BLAST
Domaini260 – 904645USPAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.
Contains 1 DUSP domain.
Contains 1 USP domain.

Phylogenomic databases

eggNOGiCOG5560.
HOGENOMiHOG000264375.
HOVERGENiHBG000864.
KOiK11835.
OrthoDBiEOG77Q4VW.
PhylomeDBiQ9R085.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. 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]
PfamiPF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTiSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMiSSF143791. SSF143791. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF55205. SSF55205. 1 hit.
PROSITEiPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R085-1 [UniParc]FASTAAdd to Basket

« Hide

MAEGGAADLD TQRSDIATLL KTSLRKGDTW YLVDSRWFKQ WKKYVGFDSW    50
DKYQMGDQNV YPGPIDNSGL LKDGDAQSLK EHLIDELDYI LLPTEGWNKL 100
VSWYTLMEGQ EPIARKVVEQ GMFVKHCKVE VYLTELKLCE NGNMNNVVTR 150
RFSKADTIDT IEKEIRKIFN IPDEKEARLW NKYMSNTFEP LNKPDSTIQD 200
AGLYQGQVLV IEQKNEDGTW PRGPSAPNVK NSNYCLPSYT AYKNYDYSEP 250
GRNNEQPGLC GLSNLGNTCF MNSAIQCLSN TPPLTEYFLN DKYQEELNFD 300
NPLGMRGEIA KSYAELIKQM WSGKFSYVTP RAFKTQVGRF APQFSGYQQQ 350
DCQELLAFLL DGLHEDLNRI RKKPYIQLKD ADGRPDKVVA EEAWENHLKR 400
NDSIIVDIFH GLFKSTLVCP ECAKISVTFD PFCYLTLPLP MKKERSLEVY 450
LVRMDPLAKP MQYKVIVPKI GNILDLCTAL SALSGVPADK MIVTDIYNHR 500
FHRIFAMDEN LSSIMERDDI YVFEININRT EDTEHVVIPV CLREKFRHSS 550
YTHHTGSSLF GQPFLMAVPR NNTEDKLYNL LLLRMCRYVK MSTETEETDG 600
PLRCCEDQNI NGNGPNGIHE EGSPSEMETD EPDDESSQDQ ELPSENENSQ 650
SEDSVGGDND SENGLCTEET CKGRLTGHKK RLFTFQFNNL GNTDINYIKD 700
DTRHIRFDDR QLRLDERSFL ALDWDPDLKK RYFDENAAED FEKHESVEYK 750
PPKRPFVKLK DCIELFTTKE KLGAEDPWYC PNCKEHQQAT KKLDLWSLPP 800
VLVVHLKRFS YSRYMRDKLD TLVDFPISDL DMSEFLINPN AGPCRYNLIA 850
VSNHYGGMGG GHYTAFAKNK DDGKWYYFDD SSVSSASEDQ IVSKAAYVLF 900
YQRQDTFSGT GFFPLDRETK GASAATGVPL ESDEDSNDND NDLENENCMH 950
TN 952
Length:952
Mass (Da):109,255
Last modified:May 1, 2000 - v1
Checksum:i6BE7449FD93CF658
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF106657 mRNA. Translation: AAF14188.1.
RefSeqiNP_660185.1. NM_145184.1.
UniGeneiRn.161933.

Genome annotation databases

GeneIDi171329.
KEGGirno:171329.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF106657 mRNA. Translation: AAF14188.1 .
RefSeqi NP_660185.1. NM_145184.1.
UniGenei Rn.161933.

3D structure databases

ProteinModelPortali Q9R085.
SMRi Q9R085. Positions 1-120.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000034485.

Protein family/group databases

MEROPSi C19.022.

PTM databases

PhosphoSitei Q9R085.

Proteomic databases

PRIDEi Q9R085.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 171329.
KEGGi rno:171329.

Organism-specific databases

CTDi 9958.
RGDi 628795. Usp15.

Phylogenomic databases

eggNOGi COG5560.
HOGENOMi HOG000264375.
HOVERGENi HBG000864.
KOi K11835.
OrthoDBi EOG77Q4VW.
PhylomeDBi Q9R085.

Enzyme and pathway databases

Reactomei REACT_194641. Downregulation of TGF-beta receptor signaling.

Miscellaneous databases

NextBioi 35574809.

Gene expression databases

Genevestigatori Q9R085.

Family and domain databases

Gene3Di 3.30.2230.10. 1 hit.
InterProi IPR006615. 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 ]
Pfami PF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view ]
SMARTi SM00695. DUSP. 1 hit.
[Graphical view ]
SUPFAMi SSF143791. SSF143791. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF55205. SSF55205. 1 hit.
PROSITEi PS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiUBP15_RAT
AccessioniPrimary (citable) accession number: Q9R085
Secondary accession number(s): E9PSP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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