Zinc finger protein RFP

<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

• S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC:2.3.2.27

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

• DNA binding Source: UniProtKB-KW
• identical protein binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.17

    "Unique features of TRIM5alpha among closely related human TRIM family members."
    Li X., Gold B., O'hUigin C., Diaz-Griffero F., Song B., Si Z., Li Y., Yuan W., Stremlau M., Mische C., Javanbakht H., Scally M., Winkler C., Dean M., Sodroski J.
    Virology 360:419-433(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
• metal ion binding Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.1

    "Developmentally regulated expression of a human 'finger'-containing gene encoded by the 5' half of the ret transforming gene."
    Takahashi M., Inaguma Y., Hiai H., Hirose F.
    Mol. Cell. Biol. 8:1853-1856(1988) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
• nucleic acid binding Source: ProtIncTraceable author statementⁱ
  • Ref.1

    "Developmentally regulated expression of a human 'finger'-containing gene encoded by the 5' half of the ret transforming gene."
    Takahashi M., Inaguma Y., Hiai H., Hirose F.
    Mol. Cell. Biol. 8:1853-1856(1988) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
• ubiquitin protein ligase activity Source: ReactomeInferred from experimentⁱ
  • "RFP-mediated ubiquitination of PTEN modulates its effect on AKT activation."
    Lee J.T., Shan J., Zhong J., Li M., Zhou B., Zhou A., Parsons R., Gu W.
    Cell Res. 23:552-564(2013) [PubMed] [Europe PMC] [Abstract]
• ubiquitin-protein transferase 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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.20

    "Tripartite motif containing protein 27 negatively regulates CD4 T cells by ubiquitinating and inhibiting the class II PI3K-C2beta."
    Cai X., Srivastava S., Sun Y., Li Z., Wu H., Zuvela-Jelaska L., Li J., Salamon R.S., Backer J.M., Skolnik E.Y.
    Proc. Natl. Acad. Sci. U.S.A. 108:20072-20077(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS UBIQUITIN LIGASE, INTERACTION WITH PIK3C2B.
• zinc ion binding Source: InterPro

GO - Biological processⁱ

• Arp2/3 complex-mediated actin nucleation Source: UniProtKBInferred from direct assayⁱ
  • Ref.21

    "Regulation of WASH-dependent actin polymerization and protein trafficking by ubiquitination."
    Hao Y.H., Doyle J.M., Ramanathan S., Gomez T.S., Jia D., Xu M., Chen Z.J., Billadeau D.D., Rosen M.K., Potts P.R.
    Cell 152:1051-1064(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH MAGEL2, SUBCELLULAR LOCATION.
• innate immune response Source: UniProtKBInferred from direct assayⁱ
  • "TRIM E3 ligases interfere with early and late stages of the retroviral life cycle."
    Uchil P.D., Quinlan B.D., Chan W.T., Luna J.M., Mothes W.
    PLoS Pathog. 4:E16-E16(2008) [PubMed] [Europe PMC] [Abstract]
• interferon-gamma secretion 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.20

    "Tripartite motif containing protein 27 negatively regulates CD4 T cells by ubiquitinating and inhibiting the class II PI3K-C2beta."
    Cai X., Srivastava S., Sun Y., Li Z., Wu H., Zuvela-Jelaska L., Li J., Salamon R.S., Backer J.M., Skolnik E.Y.
    Proc. Natl. Acad. Sci. U.S.A. 108:20072-20077(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS UBIQUITIN LIGASE, INTERACTION WITH PIK3C2B.
• negative regulation of adaptive immune response Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.20

    "Tripartite motif containing protein 27 negatively regulates CD4 T cells by ubiquitinating and inhibiting the class II PI3K-C2beta."
    Cai X., Srivastava S., Sun Y., Li Z., Wu H., Zuvela-Jelaska L., Li J., Salamon R.S., Backer J.M., Skolnik E.Y.
    Proc. Natl. Acad. Sci. U.S.A. 108:20072-20077(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS UBIQUITIN LIGASE, INTERACTION WITH PIK3C2B.
• negative regulation of calcium ion import Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.20

    "Tripartite motif containing protein 27 negatively regulates CD4 T cells by ubiquitinating and inhibiting the class II PI3K-C2beta."
    Cai X., Srivastava S., Sun Y., Li Z., Wu H., Zuvela-Jelaska L., Li J., Salamon R.S., Backer J.M., Skolnik E.Y.
    Proc. Natl. Acad. Sci. U.S.A. 108:20072-20077(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS UBIQUITIN LIGASE, INTERACTION WITH PIK3C2B.
• negative regulation of gene expression, epigenetic Source: MGIInferred from direct assayⁱ
  • Ref.11

    "RET finger protein is a transcriptional repressor and interacts with enhancer of polycomb that has dual transcriptional functions."
    Shimono Y., Murakami H., Hasegawa Y., Takahashi M.
    J. Biol. Chem. 275:39411-39419(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH EPC1, FUNCTION.
• negative regulation of interleukin-2 secretion Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.20

    "Tripartite motif containing protein 27 negatively regulates CD4 T cells by ubiquitinating and inhibiting the class II PI3K-C2beta."
    Cai X., Srivastava S., Sun Y., Li Z., Wu H., Zuvela-Jelaska L., Li J., Salamon R.S., Backer J.M., Skolnik E.Y.
    Proc. Natl. Acad. Sci. U.S.A. 108:20072-20077(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS UBIQUITIN LIGASE, INTERACTION WITH PIK3C2B.
• negative regulation of protein kinase activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.20

    "Tripartite motif containing protein 27 negatively regulates CD4 T cells by ubiquitinating and inhibiting the class II PI3K-C2beta."
    Cai X., Srivastava S., Sun Y., Li Z., Wu H., Zuvela-Jelaska L., Li J., Salamon R.S., Backer J.M., Skolnik E.Y.
    Proc. Natl. Acad. Sci. U.S.A. 108:20072-20077(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS UBIQUITIN LIGASE, INTERACTION WITH PIK3C2B.
• negative regulation of transcription by RNA polymerase II Source: MGIInferred from direct assayⁱ
  • Ref.11

    "RET finger protein is a transcriptional repressor and interacts with enhancer of polycomb that has dual transcriptional functions."
    Shimono Y., Murakami H., Hasegawa Y., Takahashi M.
    J. Biol. Chem. 275:39411-39419(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH EPC1, FUNCTION.
• negative regulation of tumor necrosis factor production Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.20

    "Tripartite motif containing protein 27 negatively regulates CD4 T cells by ubiquitinating and inhibiting the class II PI3K-C2beta."
    Cai X., Srivastava S., Sun Y., Li Z., Wu H., Zuvela-Jelaska L., Li J., Salamon R.S., Backer J.M., Skolnik E.Y.
    Proc. Natl. Acad. Sci. U.S.A. 108:20072-20077(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS UBIQUITIN LIGASE, INTERACTION WITH PIK3C2B.
• negative regulation of viral release from host cell Source: Ensembl
• negative regulation of viral transcription Source: UniProtKBInferred from direct assayⁱ
  • "TRIM E3 ligases interfere with early and late stages of the retroviral life cycle."
    Uchil P.D., Quinlan B.D., Chan W.T., Luna J.M., Mothes W.
    PLoS Pathog. 4:E16-E16(2008) [PubMed] [Europe PMC] [Abstract]
• positive regulation of actin nucleation Source: Ensembl
• positive regulation of DNA-binding transcription factor activity Source: UniProtKBInferred from direct assayⁱ
  • "TRIM protein-mediated regulation of inflammatory and innate immune signaling and its association with antiretroviral activity."
    Uchil P.D., Hinz A., Siegel S., Coenen-Stass A., Pertel T., Luban J., Mothes W.
    J. Virol. 87:257-272(2013) [PubMed] [Europe PMC] [Abstract]
• protein K63-linked ubiquitination Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.21

    "Regulation of WASH-dependent actin polymerization and protein trafficking by ubiquitination."
    Hao Y.H., Doyle J.M., Ramanathan S., Gomez T.S., Jia D., Xu M., Chen Z.J., Billadeau D.D., Rosen M.K., Potts P.R.
    Cell 152:1051-1064(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH MAGEL2, SUBCELLULAR LOCATION.
• retrograde transport, endosome to Golgi Source: UniProtKBInferred from direct assayⁱ
  • Ref.21

    "Regulation of WASH-dependent actin polymerization and protein trafficking by ubiquitination."
    Hao Y.H., Doyle J.M., Ramanathan S., Gomez T.S., Jia D., Xu M., Chen Z.J., Billadeau D.D., Rosen M.K., Potts P.R.
    Cell 152:1051-1064(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH MAGEL2, SUBCELLULAR LOCATION.
• spermatogenesis Source: ProtIncTraceable author statementⁱ
  • Ref.1

    "Developmentally regulated expression of a human 'finger'-containing gene encoded by the 5' half of the ret transforming gene."
    Takahashi M., Inaguma Y., Hiai H., Hirose F.
    Mol. Cell. Biol. 8:1853-1856(1988) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).

<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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseaseⁱ

Sites

Keywords - Diseaseⁱ

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

• identical protein binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.17

    "Unique features of TRIM5alpha among closely related human TRIM family members."
    Li X., Gold B., O'hUigin C., Diaz-Griffero F., Song B., Si Z., Li Y., Yuan W., Stremlau M., Mische C., Javanbakht H., Scally M., Winkler C., Dean M., Sodroski J.
    Virology 360:419-433(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBUNIT, SUBCELLULAR LOCATION.

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

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

Coiled coil

<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>Sequences (2+)ⁱ

<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.

This entry has 2 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MASGSVAECL QQETTCPVCL QYFAEPMMLD CGHNICCACL ARCWGTAETN 
        60         70         80         90        100
VSCPQCRETF PQRHMRPNRH LANVTQLVKQ LRTERPSGPG GEMGVCEKHR 
       110        120        130        140        150
EPLKLYCEED QMPICVVCDR SREHRGHSVL PLEEAVEGFK EQIQNQLDHL 
       160        170        180        190        200
KRVKDLKKRR RAQGEQARAE LLSLTQMERE KIVWEFEQLY HSLKEHEYRL 
       210        220        230        240        250
LARLEELDLA IYNSINGAIT QFSCNISHLS SLIAQLEEKQ QQPTRELLQD 
       260        270        280        290        300
IGDTLSRAER IRIPEPWITP PDLQEKIHIF AQKCLFLTES LKQFTEKMQS 
       310        320        330        340        350
DMEKIQELRE AQLYSVDVTL DPDTAYPSLI LSDNLRQVRY SYLQQDLPDN 
       360        370        380        390        400
PERFNLFPCV LGSPCFIAGR HYWEVEVGDK AKWTIGVCED SVCRKGGVTS 
       410        420        430        440        450
APQNGFWAVS LWYGKEYWAL TSPMTALPLR TPLQRVGIFL DYDAGEVSFY 
       460        470        480        490        500
NVTERCHTFT FSHATFCGPV RPYFSLSYSG GKSAAPLIIC PMSGIDGFSG 
       510 
HVGNHGHSME TSP                                         

        10         20         30         40         50
MASGSVAECL QQETTCPVCL QYFAEPMMLD CGHNICCACL ARCWGTAETN 
        60         70         80         90        100
VSCPQCRETF PQRHMRPNRH LANVTQLVKQ LRTERPSGPG GEMGVCEKHR 
       110        120        130        140        150
EPLKLYCEED QMPICVVCDR SREHRGHSVL PLEEAVEGFK EQIQNQLDHL 
       160        170        180        190        200
KRVKDLKKRR RAQGEQARAE LLSLTQMERE KIVWEFEQLY HSLKEHEYRL 
       210        220        230        240        250
LARLEELDLA IYNSINGAIT QFSCNISHLS SLIAQLEEKQ QQPTRELLQD 
       260        270        280        290        300
IGDTLSRAER IRIPEPWITP PDLQEKIHIF AQKCLFLTES LKQFTEKMQS 
       310        320        330        340        350
DMEKIQELRE AQLYSVDVTL DPDTAYPSLI LSDNLRQVRY SYLQQDLPDN 

PERSPSTT                                               

Experimental Info

Alternative sequence

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

• 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. SIMILARITY comments
   Index of protein domains and families
2. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
3. Human chromosome 6
   Human chromosome 6: entries, gene names and cross-references to MIM