Ubiquitin carboxyl-terminal hydrolase 17

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Miscellaneous

Caution

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>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).3 Publications

  Manual assertion based on experiment inⁱ

  • Ref.1

    "DUB-3, a cytokine-inducible deubiquitinating enzyme that blocks proliferation."
    Burrows J.F., McGrattan M.J., Rascle A., Humbert M., Baek K.-H., Johnston J.A.
    J. Biol. Chem. 279:13993-14000(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY CYTOKINES, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-89.
  • Ref.8

    "The ubiquitin-specific protease 17 is involved in virus-triggered type I IFN signaling."
    Chen R., Zhang L., Zhong B., Tan B., Liu Y., Shu H.B.
    Cell Res. 20:802-811(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY, FUNCTION IN CELLULAR ANTIVIRAL RESPONSE.
  • Ref.10

    "Ubiquitin hydrolase Dub3 promotes oncogenic transformation by stabilizing Cdc25A."
    Pereg Y., Liu B.Y., O'Rourke K.M., Sagolla M., Dey A., Komuves L., French D.M., Dixit V.M.
    Nat. Cell Biol. 12:400-406(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY, FUNCTION IN CELL PROLIFERATION.

  EC:3.4.19.12

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• cysteine-type endopeptidase activity Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• thiol-dependent ubiquitin-specific protease activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.10

    "Ubiquitin hydrolase Dub3 promotes oncogenic transformation by stabilizing Cdc25A."
    Pereg Y., Liu B.Y., O'Rourke K.M., Sagolla M., Dey A., Komuves L., French D.M., Dixit V.M.
    Nat. Cell Biol. 12:400-406(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY, FUNCTION IN CELL PROLIFERATION.
  • Ref.11

    "Lys-63-specific deubiquitination of SDS3 by USP17 regulates HDAC activity."
    Ramakrishna S., Suresh B., Lee E.J., Lee H.J., Ahn W.S., Baek K.H.
    J. Biol. Chem. 286:10505-10514(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH SUDS3, SUBCELLULAR LOCATION.
• thiol-dependent ubiquitinyl hydrolase activity Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.10

    "Ubiquitin hydrolase Dub3 promotes oncogenic transformation by stabilizing Cdc25A."
    Pereg Y., Liu B.Y., O'Rourke K.M., Sagolla M., Dey A., Komuves L., French D.M., Dixit V.M.
    Nat. Cell Biol. 12:400-406(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY, FUNCTION IN CELL PROLIFERATION.

GO - Biological processⁱ

• apoptotic process Source: UniProtKB-KW
• CAAX-box protein processing Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.5

    "USP17 regulates Ras activation and cell proliferation by blocking RCE1 activity."
    Burrows J.F., Kelvin A.A., McFarlane C., Burden R.E., McGrattan M.J., De la Vega M., Govender U., Quinn D.J., Dib K., Gadina M., Scott C.J., Johnston J.A.
    J. Biol. Chem. 284:9587-9595(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN CELL PROLIFERATION, SUBCELLULAR LOCATION.
• mitotic cell cycle checkpoint Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.10

    "Ubiquitin hydrolase Dub3 promotes oncogenic transformation by stabilizing Cdc25A."
    Pereg Y., Liu B.Y., O'Rourke K.M., Sagolla M., Dey A., Komuves L., French D.M., Dixit V.M.
    Nat. Cell Biol. 12:400-406(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY, FUNCTION IN CELL PROLIFERATION.
• negative regulation of GTPase activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "USP17 regulates Ras activation and cell proliferation by blocking RCE1 activity."
    Burrows J.F., Kelvin A.A., McFarlane C., Burden R.E., McGrattan M.J., De la Vega M., Govender U., Quinn D.J., Dib K., Gadina M., Scott C.J., Johnston J.A.
    J. Biol. Chem. 284:9587-9595(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN CELL PROLIFERATION, SUBCELLULAR LOCATION.
• negative regulation of histone deacetylation Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.11

    "Lys-63-specific deubiquitination of SDS3 by USP17 regulates HDAC activity."
    Ramakrishna S., Suresh B., Lee E.J., Lee H.J., Ahn W.S., Baek K.H.
    J. Biol. Chem. 286:10505-10514(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH SUDS3, SUBCELLULAR LOCATION.
• negative regulation of protein processing Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.5

    "USP17 regulates Ras activation and cell proliferation by blocking RCE1 activity."
    Burrows J.F., Kelvin A.A., McFarlane C., Burden R.E., McGrattan M.J., De la Vega M., Govender U., Quinn D.J., Dib K., Gadina M., Scott C.J., Johnston J.A.
    J. Biol. Chem. 284:9587-9595(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN CELL PROLIFERATION, SUBCELLULAR LOCATION.
• negative regulation of protein targeting to membrane Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.5

    "USP17 regulates Ras activation and cell proliferation by blocking RCE1 activity."
    Burrows J.F., Kelvin A.A., McFarlane C., Burden R.E., McGrattan M.J., De la Vega M., Govender U., Quinn D.J., Dib K., Gadina M., Scott C.J., Johnston J.A.
    J. Biol. Chem. 284:9587-9595(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN CELL PROLIFERATION, SUBCELLULAR LOCATION.
• positive regulation of GTPase activity Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.12

    "The deubiquitinating enzyme USP17 is essential for GTPase subcellular localization and cell motility."
    de la Vega M., Kelvin A.A., Dunican D.J., McFarlane C., Burrows J.F., Jaworski J., Stevenson N.J., Dib K., Rappoport J.Z., Scott C.J., Long A., Johnston J.A.
    Nat. Commun. 2:259-259(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN CELL MIGRATION, INDUCTION BY CHEMOKINE.
• positive regulation of MDA-5 signaling pathway Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.8

    "The ubiquitin-specific protease 17 is involved in virus-triggered type I IFN signaling."
    Chen R., Zhang L., Zhong B., Tan B., Liu Y., Shu H.B.
    Cell Res. 20:802-811(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY, FUNCTION IN CELLULAR ANTIVIRAL RESPONSE.
• positive regulation of RIG-I signaling pathway Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.8

    "The ubiquitin-specific protease 17 is involved in virus-triggered type I IFN signaling."
    Chen R., Zhang L., Zhong B., Tan B., Liu Y., Shu H.B.
    Cell Res. 20:802-811(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY, FUNCTION IN CELLULAR ANTIVIRAL RESPONSE.
• protein deubiquitination Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "Ubiquitin hydrolase Dub3 promotes oncogenic transformation by stabilizing Cdc25A."
    Pereg Y., Liu B.Y., O'Rourke K.M., Sagolla M., Dey A., Komuves L., French D.M., Dixit V.M.
    Nat. Cell Biol. 12:400-406(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY, FUNCTION IN CELL PROLIFERATION.
• protein K48-linked deubiquitination Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.5

    "USP17 regulates Ras activation and cell proliferation by blocking RCE1 activity."
    Burrows J.F., Kelvin A.A., McFarlane C., Burden R.E., McGrattan M.J., De la Vega M., Govender U., Quinn D.J., Dib K., Gadina M., Scott C.J., Johnston J.A.
    J. Biol. Chem. 284:9587-9595(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN CELL PROLIFERATION, SUBCELLULAR LOCATION.
  • Ref.8

    "The ubiquitin-specific protease 17 is involved in virus-triggered type I IFN signaling."
    Chen R., Zhang L., Zhong B., Tan B., Liu Y., Shu H.B.
    Cell Res. 20:802-811(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY, FUNCTION IN CELLULAR ANTIVIRAL RESPONSE.
• protein K63-linked deubiquitination Source: UniProtKBInferred from direct assayⁱ
  • Ref.11

    "Lys-63-specific deubiquitination of SDS3 by USP17 regulates HDAC activity."
    Ramakrishna S., Suresh B., Lee E.J., Lee H.J., Ahn W.S., Baek K.H.
    J. Biol. Chem. 286:10505-10514(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH SUDS3, SUBCELLULAR LOCATION.
• regulation of apoptotic process Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.11

    "Lys-63-specific deubiquitination of SDS3 by USP17 regulates HDAC activity."
    Ramakrishna S., Suresh B., Lee E.J., Lee H.J., Ahn W.S., Baek K.H.
    J. Biol. Chem. 286:10505-10514(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH SUDS3, SUBCELLULAR LOCATION.
• regulation of cell migration Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.12

    "The deubiquitinating enzyme USP17 is essential for GTPase subcellular localization and cell motility."
    de la Vega M., Kelvin A.A., Dunican D.J., McFarlane C., Burrows J.F., Jaworski J., Stevenson N.J., Dib K., Rappoport J.Z., Scott C.J., Long A., Johnston J.A.
    Nat. Commun. 2:259-259(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN CELL MIGRATION, INDUCTION BY CHEMOKINE.
• regulation of cell population proliferation Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.5

    "USP17 regulates Ras activation and cell proliferation by blocking RCE1 activity."
    Burrows J.F., Kelvin A.A., McFarlane C., Burden R.E., McGrattan M.J., De la Vega M., Govender U., Quinn D.J., Dib K., Gadina M., Scott C.J., Johnston J.A.
    J. Biol. Chem. 284:9587-9595(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN CELL PROLIFERATION, SUBCELLULAR LOCATION.
• regulation of defense response to virus by host Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.8

    "The ubiquitin-specific protease 17 is involved in virus-triggered type I IFN signaling."
    Chen R., Zhang L., Zhong B., Tan B., Liu Y., Shu H.B.
    Cell Res. 20:802-811(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY, FUNCTION IN CELLULAR ANTIVIRAL RESPONSE.
• regulation of ruffle assembly Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.12

    "The deubiquitinating enzyme USP17 is essential for GTPase subcellular localization and cell motility."
    de la Vega M., Kelvin A.A., Dunican D.J., McFarlane C., Burrows J.F., Jaworski J., Stevenson N.J., Dib K., Rappoport J.Z., Scott C.J., Long A., Johnston J.A.
    Nat. Commun. 2:259-259(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN CELL MIGRATION, INDUCTION BY CHEMOKINE.
• ubiquitin-dependent protein catabolic process Source: InterPro

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MEDDSLYLGG EWQFNHFSKL TSSRPDAAFA EIQRTSLPEK SPLSSEARVD 
        60         70         80         90        100
LCDDLAPVAR QLAPRKKLPL SSRRPAAVGA GLQNMGNTCY ENASLQCLTY 
       110        120        130        140        150
TPPLANYMLS REHSQTCQRP KCCMLCTMQA HITWALHSPG HVIQPSQALA 
       160        170        180        190        200
AGFHRGKQED AHEFLMFTVD AMKKACLPGH KQVDHHSKDT TLIHQIFGGC 
       210        220        230        240        250
WRSQIKCLHC HGISDTFDPY LDIALDIQAA QSVKQALEQL VKPEELNGEN 
       260        270        280        290        300
AYHCGLCLQR APASKTLTLH TSAKVLILVL KRFSDVTGNK LAKNVQYPEC 
       310        320        330        340        350
LDMQPYMSQQ NTGPLVYVLY AVLVHAGWSC HDGHYFSYVK AQEGQWYKMD 
       360        370        380        390        400
DAKVTACSIT SVLSQQAYVL FYIQKSEWER HSESVSRGRE PRALGAEDTD 
       410        420        430        440        450
RRATQGELKR DHPCLQAPEL DERLVERATQ ESTLDHWKFP QEQNKTKPEF 
       460        470        480        490        500
NVRKVEGTLP PNVLVIHQSK YKCGMKNHHP EQQSSLLNLS STTRTDQESV 
       510        520        530
NTGTLASLQG RTRRSKGKNK HSKRALLVCQ                       

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. SIMILARITY comments
   Index of protein domains and families
2. Human chromosome 8
   Human chromosome 8: entries, gene names and cross-references to MIM
3. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations
4. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
5. Peptidase families
   Classification of peptidase families and list of entries
6. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot