Protein farnesyltransferase subunit beta

<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

• (2E,6E)-farnesyl diphosphate

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  + L-cysteinyl-[protein]

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  • Search chemical reactions in Rhea for this molecule.

  = diphosphate

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  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  + S-(2E,6E)-farnesyl-L-cysteinyl-[protein]

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  • Search chemical reactions in Rhea for this molecule.

  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.3

    "Structure-guided development of selective RabGGTase inhibitors."
    Bon R.S., Guo Z., Stigter E.A., Wetzel S., Menninger S., Wolf A., Choidas A., Alexandrov K., Blankenfeldt W., Goody R.S., Waldmann H.
    Angew. Chem. Int. Ed. Engl. 50:4957-4961(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-427 IN COMPLEX WITH FNTA AND ZINC IONS, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
  EC:2.5.1.58
  • Search proteins in UniProtKB for this EC number.
  • See the description of this EC number in ENZYME.
  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.3

    "Structure-guided development of selective RabGGTase inhibitors."
    Bon R.S., Guo Z., Stigter E.A., Wetzel S., Menninger S., Wolf A., Choidas A., Alexandrov K., Blankenfeldt W., Goody R.S., Waldmann H.
    Angew. Chem. Int. Ed. Engl. 50:4957-4961(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-427 IN COMPLEX WITH FNTA AND ZINC IONS, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
  Source: Rhea

  • Search for this reaction in UniProtKB.
  • See the description of this reaction in Rhea.

  . Show »« Hide
  (2E,6E)-farnesyl diphosphate

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

  +

  L-cysteinyl-[protein]

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  • Search chemical reactions in Rhea for this molecule.

  

  L-cysteine residue

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  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

  =

  diphosphate

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

  +

  S-(2E,6E)-farnesyl-L-cysteinyl-[protein]

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  

  S-(2E,6E)-farnesyl-L-cysteine residue

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactorⁱ

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

• drug binding Source: Ensembl
• farnesyltranstransferase activity Source: MGI <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
  • "Protein farnesyltransferase in embryogenesis, adult homeostasis, and tumor development."
    Mijimolle N., Velasco J., Dubus P., Guerra C., Weinbaum C.A., Casey P.J., Campuzano V., Barbacid M.
    Cancer Cell 7:313-324(2005) [PubMed] [Europe PMC] [Abstract]
• isoprenoid binding Source: Ensembl
• peptide binding Source: Ensembl
• protein farnesyltransferase activity Source: UniProtKB
• zinc ion binding Source: UniProtKB

GO - Biological processⁱ

• negative regulation of cell population proliferation Source: MGIInferred from mutant phenotypeⁱ
  • "Protein farnesyltransferase in embryogenesis, adult homeostasis, and tumor development."
    Mijimolle N., Velasco J., Dubus P., Guerra C., Weinbaum C.A., Casey P.J., Campuzano V., Barbacid M.
    Cancer Cell 7:313-324(2005) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cell cycle Source: MGI
• positive regulation of cell population proliferation Source: MGIInferred from mutant phenotypeⁱ
  • "Protein farnesyltransferase in embryogenesis, adult homeostasis, and tumor development."
    Mijimolle N., Velasco J., Dubus P., Guerra C., Weinbaum C.A., Casey P.J., Campuzano V., Barbacid M.
    Cancer Cell 7:313-324(2005) [PubMed] [Europe PMC] [Abstract]
• positive regulation of fibroblast proliferation Source: MGIInferred from mutant phenotypeⁱ
  • "Protein farnesyltransferase in embryogenesis, adult homeostasis, and tumor development."
    Mijimolle N., Velasco J., Dubus P., Guerra C., Weinbaum C.A., Casey P.J., Campuzano V., Barbacid M.
    Cancer Cell 7:313-324(2005) [PubMed] [Europe PMC] [Abstract]
• positive regulation of nitric-oxide synthase biosynthetic process Source: MGI
• protein farnesylation Source: UniProtKB
• protein prenylation 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%2Dgo%2Devidence%2Dcodes#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]
• regulation of fibroblast proliferation Source: MGIInferred from mutant phenotypeⁱ
  • "Targeting isoprenylcysteine methylation ameliorates disease in a mouse model of progeria."
    Ibrahim M.X., Sayin V.I., Akula M.K., Liu M., Fong L.G., Young S.G., Bergo M.O.
    Science 340:1330-1333(2013) [PubMed] [Europe PMC] [Abstract]
• response to cytokine Source: MGI
• response to inorganic substance Source: MGI
• response to organic cyclic compound Source: MGI
• wound healing Source: MGIInferred from mutant phenotypeⁱ
  • "Protein farnesyltransferase in embryogenesis, adult homeostasis, and tumor development."
    Mijimolle N., Velasco J., Dubus P., Guerra C., Weinbaum C.A., Casey P.J., Campuzano V., Barbacid M.
    Cancer Cell 7:313-324(2005) [PubMed] [Europe PMC] [Abstract]

<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

<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

<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

Chemistry 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

Amino acid modifications

Keywords - PTMⁱ

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

Gene expression 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

Protein-protein interaction databases

Chemistry 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 information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

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>Sequence (1+)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 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MASSSSFTYY CPPSSSPVWS EPLYSLRPEH VRERLQDDSV ETVTSIEQAK 
        60         70         80         90        100
VEEKIQEVFS SYKFNHLVPR LILQREKHFH YLKRGLRQLT DAYECLDASR 
       110        120        130        140        150
PWLCYWILHS LELLDEPIPQ IVATDVCQFL ELCQSPDGGF GGGPGQYPHL 
       160        170        180        190        200
APTYAAVNAL CIIGTEEAYN VINREKLLQY LYSLKQPDGS FLMHVGGEVD 
       210        220        230        240        250
VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG GVPGMEAHGG 
       260        270        280        290        300
YTFCGLAALV ILKKERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY 
       310        320        330        340        350
SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL 
       360        370        380        390        400
LDKPGKSRDF YHTCYCLSGL SIAQHFGSGA MLHDMVMGVP ENVLQPTHPV 
       410        420        430 
YNIGPEKVIQ ATTHFLQKPV PGFEECEDEV TSDPATD               

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

• 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

PTM databases

Proteomic 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. MGD cross-references
   Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
2. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
3. SIMILARITY comments
   Index of protein domains and families