Ubiquitin thioesterase ZRANB1

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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).1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.8

    "OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
    Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
    Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY.

  EC:3.4.19.12

Sites

Regions

<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

• K63-linked polyubiquitin modification-dependent protein binding Source: BHF-UCL <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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.6

    "Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains."
    Tran H., Hamada F., Schwarz-Romond T., Bienz M.
    Genes Dev. 22:528-542(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH APC, DOMAIN, MUTAGENESIS OF CYS-10; 14-THR-TYR-15; CYS-90; 94-THR-TYR-95; CYS-155; 159-THR-TYR-160 AND CYS-443.
• metal ion binding Source: UniProtKB-KW
• thiol-dependent ubiquitin-specific protease activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
    Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
    Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY.
• 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%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.6

    "Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains."
    Tran H., Hamada F., Schwarz-Romond T., Bienz M.
    Genes Dev. 22:528-542(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH APC, DOMAIN, MUTAGENESIS OF CYS-10; 14-THR-TYR-15; CYS-90; 94-THR-TYR-95; CYS-155; 159-THR-TYR-160 AND CYS-443.

GO - Biological processⁱ

• cell migration Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.7

    "Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
    Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
    BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• cytoskeleton organization Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.7

    "Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
    Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
    BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• positive regulation of Wnt signaling pathway Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.6

    "Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains."
    Tran H., Hamada F., Schwarz-Romond T., Bienz M.
    Genes Dev. 22:528-542(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH APC, DOMAIN, MUTAGENESIS OF CYS-10; 14-THR-TYR-15; CYS-90; 94-THR-TYR-95; CYS-155; 159-THR-TYR-160 AND CYS-443.
• protein deubiquitination Source: Reactome
• protein deubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCLInferred from mutant phenotypeⁱ
  • Ref.6

    "Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains."
    Tran H., Hamada F., Schwarz-Romond T., Bienz M.
    Genes Dev. 22:528-542(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH APC, DOMAIN, MUTAGENESIS OF CYS-10; 14-THR-TYR-15; CYS-90; 94-THR-TYR-95; CYS-155; 159-THR-TYR-160 AND CYS-443.
• protein K29-linked deubiquitination Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
    Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
    Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY.
• protein K33-linked deubiquitination Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
    Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
    Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  • "K33-linked polyubiquitination of coronin 7 by Cul3-KLHL20 ubiquitin E3 ligase regulates protein trafficking."
    Yuan W.C., Lee Y.R., Lin S.Y., Chang L.Y., Tan Y.P., Hung C.C., Kuo J.C., Liu C.H., Lin M.Y., Xu M., Chen Z.J., Chen R.H.
    Mol. Cell 54:586-600(2014) [PubMed] [Europe PMC] [Abstract]
• protein K63-linked deubiquitination Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
    Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
    Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY.
• regulation of cell morphogenesis Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.7

    "Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
    Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
    BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• Wnt signaling pathway Source: UniProtKB-KW

<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

Miscellaneous 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

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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• K63-linked polyubiquitin modification-dependent protein binding Source: BHF-UCLInferred from direct assayⁱ
  • Ref.6

    "Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains."
    Tran H., Hamada F., Schwarz-Romond T., Bienz M.
    Genes Dev. 22:528-542(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH APC, DOMAIN, MUTAGENESIS OF CYS-10; 14-THR-TYR-15; CYS-90; 94-THR-TYR-95; CYS-155; 159-THR-TYR-160 AND CYS-443.

Protein-protein interaction databases

Miscellaneous 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

Secondary structure

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 general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

<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

Zinc finger

Keywords - Domainⁱ

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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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
MSERGIKWAC EYCTYENWPS AIKCTMCRAQ RPSGTIITED PFKSGSSDVG 
        60         70         80         90        100
RDWDPSSTEG GSSPLICPDS SARPRVKSSY SMENANKWSC HMCTYLNWPR 
       110        120        130        140        150
AIRCTQCLSQ RRTRSPTESP QSSGSGSRPV AFSVDPCEEY NDRNKLNTRT 
       160        170        180        190        200
QHWTCSVCTY ENWAKAKRCV VCDHPRPNNI EAIELAETEE ASSIINEQDR 
       210        220        230        240        250
ARWRGSCSSG NSQRRSPPAT KRDSEVKMDF QRIELAGAVG SKEELEVDFK 
       260        270        280        290        300
KLKQIKNRMK KTDWLFLNAC VGVVEGDLAA IEAYKSSGGD IARQLTADEV 
       310        320        330        340        350
RLLNRPSAFD VGYTLVHLAI RFQRQDMLAI LLTEVSQQAA KCIPAMVCPE 
       360        370        380        390        400
LTEQIRREIA ASLHQRKGDF ACYFLTDLVT FTLPADIEDL PPTVQEKLFD 
       410        420        430        440        450
EVLDRDVQKE LEEESPIINW SLELATRLDS RLYALWNRTA GDCLLDSVLQ 
       460        470        480        490        500
ATWGIYDKDS VLRKALHDSL HDCSHWFYTR WKDWESWYSQ SFGLHFSLRE 
       510        520        530        540        550
EQWQEDWAFI LSLASQPGAS LEQTHIFVLA HILRRPIIVY GVKYYKSFRG 
       560        570        580        590        600
ETLGYTRFQG VYLPLLWEQS FCWKSPIALG YTRGHFSALV AMENDGYGNR 
       610        620        630        640        650
GAGANLNTDD DVTITFLPLV DSERKLLHVH FLSAQELGNE EQQEKLLREW 
       660        670        680        690        700
LDCCVTEGGV LVAMQKSSRR RNHPLVTQMV EKWLDRYRQI RPCTSLSDGE 

EDEDDEDE                                               

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Experimental Info

Sequence databases

Genome annotation databases

<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

• 100% Identity
• 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

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. Peptidase families
   Classification of peptidase families and list of entries
2. SIMILARITY comments
   Index of protein domains and families
3. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
4. Human chromosome 10
   Human chromosome 10: entries, gene names and cross-references to MIM
5. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references