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Q9R085

- UBP15_RAT

UniProt

Q9R085 - UBP15_RAT

Protein

Ubiquitin carboxyl-terminal hydrolase 15

Gene

Usp15

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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.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 – 2691NucleophilePROSITE-ProRule annotation
    Active sitei862 – 8621Proton acceptorPROSITE-ProRule annotation

    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

    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 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei932 – 9321PhosphoserineBy similarity
    Modified residuei936 – 9361PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated. Phosphorylation protects against ubiquitination and subsequent degradation by the proteasome By similarity.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.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000034485.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R085.
    SMRiQ9R085. Positions 1-120.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 118112DUSPPROSITE-ProRule annotationAdd
    BLAST
    Domaini260 – 904645USPAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Curated
    Contains 1 DUSP domain.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    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

    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: October 1, 2014
    This is version 86 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