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Q9Y4E8

- UBP15_HUMAN

UniProt

Q9Y4E8 - UBP15_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 15

Gene

USP15

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 3 (12 Feb 2003)
      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 (PubMed:21947082). 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 (PubMed:22344298). 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. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway.7 Publications

    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).4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei298 – 2981Nucleophile
    Active sitei891 – 8911Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: UniProtKB
    2. identical protein binding Source: IntAct
    3. SMAD binding Source: UniProtKB
    4. transforming growth factor beta receptor binding Source: UniProtKB
    5. ubiquitin-specific protease activity Source: UniProtKB
    6. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. BMP signaling pathway Source: UniProtKB
    2. monoubiquitinated protein deubiquitination Source: UniProtKB
    3. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
    4. pathway-restricted SMAD protein phosphorylation Source: UniProtKB
    5. protein deubiquitination Source: UniProtKB
    6. transforming growth factor beta receptor signaling pathway Source: UniProtKB
    7. 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_120727. 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 thioesterase 15
    Ubiquitin-specific-processing protease 15
    Unph-2
    Unph4
    Gene namesi
    Name:USP15
    Synonyms:KIAA0529
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:12613. 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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi298 – 2981C → A: Loss of enzyme activity. 3 Publications
    Mutagenesisi812 – 8121C → A: Loss of activity towards polyubiquitin. 2 Publications

    Organism-specific databases

    PharmGKBiPA37239.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 981980Ubiquitin carboxyl-terminal hydrolase 15PRO_0000080641Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei229 – 2291Phosphoserine6 Publications
    Modified residuei242 – 2421Phosphoserine2 Publications
    Modified residuei961 – 9611Phosphoserine3 Publications
    Modified residuei965 – 9651Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated. Phosphorylation protects against ubiquitination and subsequent degradation by the proteasome.6 Publications
    Ubiquitinated, leading to degradation by the proteasome.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y4E8.
    PaxDbiQ9Y4E8.
    PRIDEiQ9Y4E8.

    PTM databases

    PhosphoSiteiQ9Y4E8.

    Expressioni

    Tissue specificityi

    Expressed in skeletal muscle, kidney, heart, placenta, liver, thymus, lung, and ovary, with little or no expression in other tissues.

    Gene expression databases

    ArrayExpressiQ9Y4E8.
    BgeeiQ9Y4E8.
    CleanExiHS_USP15.
    GenevestigatoriQ9Y4E8.

    Organism-specific databases

    HPAiHPA006237.

    Interactioni

    Subunit structurei

    A homodimer structure has been reported; however it is unclear whether the protein form a homodimer in vivo (PubMed:22001210). 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. Interacts with human papillomavirus type 16 protein E6.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-1043104,EBI-1043104

    Protein-protein interaction databases

    BioGridi115283. 115 interactions.
    DIPiDIP-50239N.
    IntActiQ9Y4E8. 35 interactions.
    MINTiMINT-4542165.
    STRINGi9606.ENSP00000258123.

    Structurei

    Secondary structure

    1
    981
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63
    Helixi9 – 1911
    Beta strandi29 – 346
    Helixi35 – 4511
    Turni46 – 483
    Turni53 – 564
    Helixi58 – 603
    Helixi68 – 703
    Beta strandi73 – 764
    Turni86 – 883
    Beta strandi89 – 935
    Helixi94 – 10411
    Beta strandi114 – 1207
    Beta strandi127 – 1293
    Beta strandi134 – 1407
    Beta strandi143 – 15210
    Helixi158 – 16811
    Beta strandi173 – 1753
    Beta strandi177 – 1848
    Beta strandi187 – 1904
    Helixi198 – 2014
    Beta strandi208 – 2136

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W6VNMR-A1-120[»]
    3LMNX-ray2.15A/B1-133[»]
    3PPAX-ray2.35A6-223[»]
    3PV1X-ray2.60A/B1-223[»]
    3T9LX-ray1.50A1-222[»]
    4A3OX-ray2.20A/B4-223[»]
    4A3PX-ray1.40A6-223[»]
    ProteinModelPortaliQ9Y4E8.
    SMRiQ9Y4E8. Positions 6-222, 285-470, 786-934.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y4E8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 118112DUSPPROSITE-ProRule annotationAdd
    BLAST
    Domaini289 – 933645USPAdd
    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.
    InParanoidiQ9Y4E8.
    KOiK11835.
    OMAiRYVKTCT.
    OrthoDBiEOG77Q4VW.
    PhylomeDBiQ9Y4E8.
    TreeFamiTF106276.

    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]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y4E8-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAEGGAADLD TQRSDIATLL KTSLRKGDTW YLVDSRWFKQ WKKYVGFDSW    50
    DKYQMGDQNV YPGPIDNSGL LKDGDAQSLK EHLIDELDYI LLPTEGWNKL 100
    VSWYTLMEGQ EPIARKVVEQ GMFVKHCKVE VYLTELKLCE NGNMNNVVTR 150
    RFSKADTIDT IEKEIRKIFS IPDEKETRLW NKYMSNTFEP LNKPDSTIQD 200
    AGLYQGQVLV IEQKNEDGTW PRGPSTPKSP GASNFSTLPK ISPSSLSNNY 250
    NNMNNRNVKN SNYCLPSYTA YKNYDYSEPG RNNEQPGLCG LSNLGNTCFM 300
    NSAIQCLSNT PPLTEYFLND KYQEELNFDN PLGMRGEIAK SYAELIKQMW 350
    SGKFSYVTPR AFKTQVGRFA PQFSGYQQQD CQELLAFLLD GLHEDLNRIR 400
    KKPYIQLKDA DGRPDKVVAE EAWENHLKRN DSIIVDIFHG LFKSTLVCPE 450
    CAKISVTFDP FCYLTLPLPM KKERTLEVYL VRMDPLTKPM QYKVVVPKIG 500
    NILDLCTALS ALSGIPADKM IVTDIYNHRF HRIFAMDENL SSIMERDDIY 550
    VFEININRTE DTEHVIIPVC LREKFRHSSY THHTGSSLFG QPFLMAVPRN 600
    NTEDKLYNLL LLRMCRYVKI STETEETEGS LHCCKDQNIN GNGPNGIHEE 650
    GSPSEMETDE PDDESSQDQE LPSENENSQS EDSVGGDNDS ENGLCTEDTC 700
    KGQLTGHKKR LFTFQFNNLG NTDINYIKDD TRHIRFDDRQ LRLDERSFLA 750
    LDWDPDLKKR YFDENAAEDF EKHESVEYKP PKKPFVKLKD CIELFTTKEK 800
    LGAEDPWYCP NCKEHQQATK KLDLWSLPPV LVVHLKRFSY SRYMRDKLDT 850
    LVDFPINDLD MSEFLINPNA GPCRYNLIAV SNHYGGMGGG HYTAFAKNKD 900
    DGKWYYFDDS SVSTASEDQI VSKAAYVLFY QRQDTFSGTG FFPLDRETKG 950
    ASAATGIPLE SDEDSNDNDN DIENENCMHT N 981
    Length:981
    Mass (Da):112,419
    Last modified:February 12, 2003 - v3
    Checksum:iE81FEB9DE57F7089
    GO
    Isoform 2 (identifier: Q9Y4E8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         228-256: Missing.

    Show »
    Length:952
    Mass (Da):109,297
    Checksum:i852ED3768FB5725A
    GO
    Isoform 3 (identifier: Q9Y4E8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         217-256: DGTWPRGPSTPKSPGASNFSTLPKISPSSLSNNYNNMNNR → QKNEDGTWPRGPSTP

    Show »
    Length:956
    Mass (Da):109,796
    Checksum:iF9F83D3886404B11
    GO
    Isoform 4 (identifier: Q9Y4E8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         229-235: SPGASNF → KPLEQSC
         236-981: Missing.

    Show »
    Length:235
    Mass (Da):27,094
    Checksum:iF69B0D2783E2A443
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti559 – 5591T → A in AAG28973. 1 PublicationCurated
    Sequence conflicti747 – 7471S → F in AAI25124. (PubMed:15489334)Curated
    Sequence conflicti968 – 9681N → H in AAG28973. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei217 – 25640DGTWP…NMNNR → QKNEDGTWPRGPSTP in isoform 3. 1 PublicationVSP_005260Add
    BLAST
    Alternative sequencei228 – 25629Missing in isoform 2. 3 PublicationsVSP_005261Add
    BLAST
    Alternative sequencei229 – 2357SPGASNF → KPLEQSC in isoform 4. 2 PublicationsVSP_045165
    Alternative sequencei236 – 981746Missing in isoform 4. 2 PublicationsVSP_045166Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF106069 mRNA. Translation: AAD52099.1.
    AB011101 mRNA. Translation: BAA25455.2.
    AF153604 mRNA. Translation: AAD41086.1.
    AK023703 mRNA. Translation: BAB14648.1.
    AK292337 mRNA. Translation: BAF85026.1.
    AC048342 Genomic DNA. No translation available.
    AC079035 Genomic DNA. No translation available.
    AC117370 Genomic DNA. No translation available.
    BC020688 mRNA. Translation: AAH20688.1.
    BC063454 mRNA. Translation: AAH63454.1.
    BC125123 mRNA. Translation: AAI25124.1.
    AF013990 mRNA. Translation: AAG28973.1.
    CCDSiCCDS58250.1. [Q9Y4E8-4]
    CCDS58251.1. [Q9Y4E8-1]
    CCDS8963.1. [Q9Y4E8-2]
    RefSeqiNP_001239007.1. NM_001252078.1. [Q9Y4E8-1]
    NP_001239008.1. NM_001252079.1. [Q9Y4E8-4]
    NP_006304.1. NM_006313.2. [Q9Y4E8-2]
    UniGeneiHs.434951.

    Genome annotation databases

    EnsembliENST00000280377; ENSP00000280377; ENSG00000135655. [Q9Y4E8-1]
    ENST00000312635; ENSP00000309240; ENSG00000135655. [Q9Y4E8-4]
    ENST00000353364; ENSP00000258123; ENSG00000135655. [Q9Y4E8-2]
    GeneIDi9958.
    KEGGihsa:9958.
    UCSCiuc001sra.3. human.
    uc001srb.2. human. [Q9Y4E8-2]
    uc001src.2. human. [Q9Y4E8-1]

    Polymorphism databases

    DMDMi28381406.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF106069 mRNA. Translation: AAD52099.1 .
    AB011101 mRNA. Translation: BAA25455.2 .
    AF153604 mRNA. Translation: AAD41086.1 .
    AK023703 mRNA. Translation: BAB14648.1 .
    AK292337 mRNA. Translation: BAF85026.1 .
    AC048342 Genomic DNA. No translation available.
    AC079035 Genomic DNA. No translation available.
    AC117370 Genomic DNA. No translation available.
    BC020688 mRNA. Translation: AAH20688.1 .
    BC063454 mRNA. Translation: AAH63454.1 .
    BC125123 mRNA. Translation: AAI25124.1 .
    AF013990 mRNA. Translation: AAG28973.1 .
    CCDSi CCDS58250.1. [Q9Y4E8-4 ]
    CCDS58251.1. [Q9Y4E8-1 ]
    CCDS8963.1. [Q9Y4E8-2 ]
    RefSeqi NP_001239007.1. NM_001252078.1. [Q9Y4E8-1 ]
    NP_001239008.1. NM_001252079.1. [Q9Y4E8-4 ]
    NP_006304.1. NM_006313.2. [Q9Y4E8-2 ]
    UniGenei Hs.434951.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1W6V NMR - A 1-120 [» ]
    3LMN X-ray 2.15 A/B 1-133 [» ]
    3PPA X-ray 2.35 A 6-223 [» ]
    3PV1 X-ray 2.60 A/B 1-223 [» ]
    3T9L X-ray 1.50 A 1-222 [» ]
    4A3O X-ray 2.20 A/B 4-223 [» ]
    4A3P X-ray 1.40 A 6-223 [» ]
    ProteinModelPortali Q9Y4E8.
    SMRi Q9Y4E8. Positions 6-222, 285-470, 786-934.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115283. 115 interactions.
    DIPi DIP-50239N.
    IntActi Q9Y4E8. 35 interactions.
    MINTi MINT-4542165.
    STRINGi 9606.ENSP00000258123.

    Protein family/group databases

    MEROPSi C19.022.

    PTM databases

    PhosphoSitei Q9Y4E8.

    Polymorphism databases

    DMDMi 28381406.

    Proteomic databases

    MaxQBi Q9Y4E8.
    PaxDbi Q9Y4E8.
    PRIDEi Q9Y4E8.

    Protocols and materials databases

    DNASUi 9958.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000280377 ; ENSP00000280377 ; ENSG00000135655 . [Q9Y4E8-1 ]
    ENST00000312635 ; ENSP00000309240 ; ENSG00000135655 . [Q9Y4E8-4 ]
    ENST00000353364 ; ENSP00000258123 ; ENSG00000135655 . [Q9Y4E8-2 ]
    GeneIDi 9958.
    KEGGi hsa:9958.
    UCSCi uc001sra.3. human.
    uc001srb.2. human. [Q9Y4E8-2 ]
    uc001src.2. human. [Q9Y4E8-1 ]

    Organism-specific databases

    CTDi 9958.
    GeneCardsi GC12P062706.
    H-InvDB HIX0010773.
    HGNCi HGNC:12613. USP15.
    HPAi HPA006237.
    MIMi 604731. gene.
    neXtProti NX_Q9Y4E8.
    PharmGKBi PA37239.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5560.
    HOGENOMi HOG000264375.
    HOVERGENi HBG000864.
    InParanoidi Q9Y4E8.
    KOi K11835.
    OMAi RYVKTCT.
    OrthoDBi EOG77Q4VW.
    PhylomeDBi Q9Y4E8.
    TreeFami TF106276.

    Enzyme and pathway databases

    Reactomei REACT_120727. Downregulation of TGF-beta receptor signaling.

    Miscellaneous databases

    ChiTaRSi USP15. human.
    EvolutionaryTracei Q9Y4E8.
    GeneWikii USP15.
    GenomeRNAii 9958.
    NextBioi 37576.
    PROi Q9Y4E8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y4E8.
    Bgeei Q9Y4E8.
    CleanExi HS_USP15.
    Genevestigatori Q9Y4E8.

    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. "Identification and characterization of a new human deubiquitinating enzyme Unph4."
      Kim K.I., Nagase T., Chung C.H.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Brain.
    2. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "A catalogue of genes in the human dermal papilla cells as identified by expressed sequence tags."
      Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Chung H.J., Sohn M.Y., Hwang S.Y., Im S.U., Jung E.J., Lee J.H., Kim J.C.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Hair follicle dermal papilla.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Placenta.
    6. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
      Tissue: Brain and Lung.
    8. Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-21; 475-482 AND 924-932, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Mammary carcinoma.
    9. "Cloning and identification of human Unph-2."
      Kimura Y., Saya H., Nakao M.
      Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-981 (ISOFORM 3).
      Tissue: Fetal brain.
    10. "Identification, functional characterization, and chromosomal localization of USP15, a novel human ubiquitin-specific protease related to the UNP oncoprotein, and a systematic nomenclature for human ubiquitin-specific proteases."
      Baker R.T., Wang X.-W., Woollatt E., White J.A., Sutherland G.R.
      Genomics 59:264-274(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION (ISOFORM 2), CATALYTIC ACTIVITY.
    11. "Isolation and characterization of the mouse ubiquitin-specific protease Usp15."
      Angelats C., Wang X.-W., Jermiin L.S., Copeland N.G., Jenkins N.A., Baker R.T.
      Mamm. Genome 14:31-46(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
    12. "The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1."
      Hetfeld B.K., Helfrich A., Kapelari B., Scheel H., Hofmann K., Guterman A., Glickman M., Schade R., Kloetzel P.M., Dubiel W.
      Curr. Biol. 15:1217-1221(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-812, IDENTIFICATION IN A COMPLEX WITH THE COP9 SIGNALOSOME, PHOSPHORYLATION, UBIQUITINATION.
    13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "CSN controls NF-kappaB by deubiquitinylation of IkappaBalpha."
      Schweitzer K., Bozko P.M., Dubiel W., Naumann M.
      EMBO J. 26:1532-1541(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229; SER-961 AND SER-965, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "COP9 signalosome interacts ATP-dependently with p97/valosin-containing protein (VCP) and controls the ubiquitination status of proteins bound to p97/VCP."
      Cayli S., Klug J., Chapiro J., Frohlich S., Krasteva G., Orel L., Meinhardt A.
      J. Biol. Chem. 284:34944-34953(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "The COP9 signalosome mediates beta-catenin degradation by deneddylation and blocks adenomatous polyposis coli destruction via USP15."
      Huang X., Langelotz C., Hetfeld-Pechoc B.K., Schwenk W., Dubiel W.
      J. Mol. Biol. 391:691-702(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-812.
    19. "The ubiquitin-specific peptidase USP15 regulates human papillomavirus type 16 E6 protein stability."
      Vos R.M., Altreuter J., White E.A., Howley P.M.
      J. Virol. 83:8885-8892(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-298, INTERACTION WITH HUMAN PAPILLOMAVIRUS TYPE 16 PROTEIN E6.
    20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229; SER-242; SER-961 AND SER-965, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH SMAD1; SMAD2 AND SMAD3, MUTAGENESIS OF CYS-298.
    24. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "USP15 stabilizes TGF-beta receptor I and promotes oncogenesis through the activation of TGF-beta signaling in glioblastoma."
      Eichhorn P.J., Rodon L., Gonzalez-Junca A., Dirac A., Gili M., Martinez-Saez E., Aura C., Barba I., Peg V., Prat A., Cuartas I., Jimenez J., Garcia-Dorado D., Sahuquillo J., Bernards R., Baselga J., Seoane J.
      Nat. Med. 18:429-435(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TGFBR1 AND SMAD7, MUTAGENESIS OF CYS-298.
    27. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Solution structure of the human ubiquitin-specific protease 15 DUSP domain."
      de Jong R.N., Ab E., Diercks T., Truffault V., Danieels M., Kaptein R., Folkers G.E.
      J. Biol. Chem. 281:5026-5031(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-120.
    29. "Structure of the USP15 N-terminal domains: a beta-hairpin mediates close association between the DUSP and UBL domains."
      Harper S., Besong T.M., Emsley J., Scott D.J., Dreveny I.
      Biochemistry 50:7995-8004(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-222.
    30. "Structural variability of the ubiquitin specific protease DUSP-UBL double domains."
      Elliott P.R., Liu H., Pastok M.W., Grossmann G.J., Rigden D.J., Clague M.J., Urbe S., Barsukov I.L.
      FEBS Lett. 585:3385-3390(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-223.
    31. "Crystal structure of the human ubiquitin-specific protease 15 DUSP domain."
      Structural genomics consortium (SGC)
      Submitted (APR-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-133.

    Entry informationi

    Entry nameiUBP15_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y4E8
    Secondary accession number(s): Q08AL5
    , Q9H8G9, Q9HCA6, Q9UNP0, Q9Y5B5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: February 12, 2003
    Last modified: October 1, 2014
    This is version 144 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3