Geranylgeranyl transferase type-1 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

• geranylgeranyl diphosphate

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  • See the description of this molecule in ChEBI.

  + L-cysteinyl-[protein]

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  = diphosphate

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  + S-geranylgeranyl-L-cysteinyl-[protein]

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  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.2

    "Structure of mammalian protein geranylgeranyltransferase type-I."
    Taylor J.S., Reid T.S., Terry K.L., Casey P.J., Beese L.S.
    EMBO J. 22:5963-5974(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS; SUBSTRATE PEPTIDE AND ISPRENOID ANALOG, SUBUNIT, COFACTOR, FUNCTION, CATALYTIC ACTIVITY.
  EC:2.5.1.59
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  • See the description of this EC number in ENZYME.
  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.2

    "Structure of mammalian protein geranylgeranyltransferase type-I."
    Taylor J.S., Reid T.S., Terry K.L., Casey P.J., Beese L.S.
    EMBO J. 22:5963-5974(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS; SUBSTRATE PEPTIDE AND ISPRENOID ANALOG, SUBUNIT, COFACTOR, FUNCTION, CATALYTIC ACTIVITY.
  Source: Rhea

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

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  geranylgeranyl diphosphate

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  • See the description of this molecule in ChEBI.

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  +

  L-cysteinyl-[protein]

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  L-cysteine residue

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  zoom

  =

  diphosphate

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  • See the description of this molecule in ChEBI.

  zoom

  +

  S-geranylgeranyl-L-cysteinyl-[protein]

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  S-geranylgeranyl-L-cysteine residue

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  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

• Zn²⁺
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  • See the description of this molecule in ChEBI.
  3 Publications

  Manual assertion based on experiment inⁱ

  • Ref.2

    "Structure of mammalian protein geranylgeranyltransferase type-I."
    Taylor J.S., Reid T.S., Terry K.L., Casey P.J., Beese L.S.
    EMBO J. 22:5963-5974(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS; SUBSTRATE PEPTIDE AND ISPRENOID ANALOG, SUBUNIT, COFACTOR, FUNCTION, CATALYTIC ACTIVITY.
  • Ref.3

    "Crystallographic analysis reveals that anticancer clinical candidate L-778,123 inhibits protein farnesyltransferase and geranylgeranyltransferase-I by different binding modes."
    Reid T.S., Long S.B., Beese L.S.
    Biochemistry 43:9000-9008(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS AND INHIBITOR, SUBUNIT, COFACTOR.
  • Ref.4

    "Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity."
    Reid T.S., Terry K.L., Casey P.J., Beese L.S.
    J. Mol. Biol. 343:417-433(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS AND SUBSTRATES, SUBUNIT, COFACTOR.
  Note: Binds 1 zinc ion per subunit.3 Publications

  Manual assertion based on experiment inⁱ

  • Ref.2

    "Structure of mammalian protein geranylgeranyltransferase type-I."
    Taylor J.S., Reid T.S., Terry K.L., Casey P.J., Beese L.S.
    EMBO J. 22:5963-5974(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS; SUBSTRATE PEPTIDE AND ISPRENOID ANALOG, SUBUNIT, COFACTOR, FUNCTION, CATALYTIC ACTIVITY.
  • Ref.3

    "Crystallographic analysis reveals that anticancer clinical candidate L-778,123 inhibits protein farnesyltransferase and geranylgeranyltransferase-I by different binding modes."
    Reid T.S., Long S.B., Beese L.S.
    Biochemistry 43:9000-9008(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS AND INHIBITOR, SUBUNIT, COFACTOR.
  • Ref.4

    "Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity."
    Reid T.S., Terry K.L., Casey P.J., Beese L.S.
    J. Mol. Biol. 343:417-433(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS AND SUBSTRATES, SUBUNIT, COFACTOR.
• Mg²⁺
  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.
  By similarity

  <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toⁱ

  • UniProtKB:P18898 (PGTB1_YEAST)

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

• CAAX-protein geranylgeranyltransferase 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.2

    "Structure of mammalian protein geranylgeranyltransferase type-I."
    Taylor J.S., Reid T.S., Terry K.L., Casey P.J., Beese L.S.
    EMBO J. 22:5963-5974(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS; SUBSTRATE PEPTIDE AND ISPRENOID ANALOG, SUBUNIT, COFACTOR, FUNCTION, CATALYTIC ACTIVITY.
• protein geranylgeranyltransferase activity Source: UniProtKB
• zinc ion binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.2

    "Structure of mammalian protein geranylgeranyltransferase type-I."
    Taylor J.S., Reid T.S., Terry K.L., Casey P.J., Beese L.S.
    EMBO J. 22:5963-5974(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS; SUBSTRATE PEPTIDE AND ISPRENOID ANALOG, SUBUNIT, COFACTOR, FUNCTION, CATALYTIC ACTIVITY.

GO - Biological processⁱ

• negative regulation of nitric-oxide synthase biosynthetic process Source: RGD <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
  • "Inhibition of protein geranylgeranylation causes a superinduction of nitric-oxide synthase-2 by interleukin-1beta in vascular smooth muscle cells."
    Finder J.D., Litz J.L., Blaskovich M.A., McGuire T.F., Qian Y., Hamilton A.D., Davies P., Sebti S.M.
    J Biol Chem 272:13484-13488(1997) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cell cycle Source: RGDInferred from mutant phenotypeⁱ
  • "Combination of the novel farnesyltransferase inhibitor RPR130401 and the geranylgeranyltransferase-1 inhibitor GGTI-298 disrupts MAP kinase activation and G(1)-S transition in Ki-Ras-overexpressing transformed adrenocortical cells."
    Mazet J.L., Padieu M., Osman H., Maume G., Mailliet P., Dereu N., Hamilton A.D., Lavelle F., Sebti S.M., Maume B.F.
    FEBS Lett 460:235-240(1999) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cell population proliferation Source: RGDInferred from mutant phenotypeⁱ
  • "Combination of the novel farnesyltransferase inhibitor RPR130401 and the geranylgeranyltransferase-1 inhibitor GGTI-298 disrupts MAP kinase activation and G(1)-S transition in Ki-Ras-overexpressing transformed adrenocortical cells."
    Mazet J.L., Padieu M., Osman H., Maume G., Mailliet P., Dereu N., Hamilton A.D., Lavelle F., Sebti S.M., Maume B.F.
    FEBS Lett 460:235-240(1999) [PubMed] [Europe PMC] [Abstract]
• protein geranylgeranylation Source: UniProtKBInferred from direct assayⁱ
  • Ref.2

    "Structure of mammalian protein geranylgeranyltransferase type-I."
    Taylor J.S., Reid T.S., Terry K.L., Casey P.J., Beese L.S.
    EMBO J. 22:5963-5974(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS; SUBSTRATE PEPTIDE AND ISPRENOID ANALOG, SUBUNIT, COFACTOR, FUNCTION, CATALYTIC ACTIVITY.
• 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 Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• response to cytokine Source: RGDInferred from mutant phenotypeⁱ
  • "Inhibition of protein geranylgeranylation causes a superinduction of nitric-oxide synthase-2 by interleukin-1beta in vascular smooth muscle cells."
    Finder J.D., Litz J.L., Blaskovich M.A., McGuire T.F., Qian Y., Hamilton A.D., Davies P., Sebti S.M.
    J Biol Chem 272:13484-13488(1997) [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

<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

• UniProt annotation
• GO - Cellular component

<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

Proteomic 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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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

Protein-protein interaction databases

Chemistry 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

Miscellaneous 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>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
MAATEDDRLA GSGEGERLDF LRDRHVRFFQ RCLQVLPERY SSLETSRLTI 
        60         70         80         90        100
AFFALSGLDM LDSLDVVNKD DIIEWIYSLQ VLPTEDRSNL DRCGFRGSSY 
       110        120        130        140        150
LGIPFNPSKN PGTAHPYDSG HIAMTYTGLS CLIILGDDLS RVDKEACLAG 
       160        170        180        190        200
LRALQLEDGS FCAVPEGSEN DMRFVYCASC ICYMLNNWSG MDMKKAISYI 
       210        220        230        240        250
RRSMSYDNGL AQGAGLESHG GSTFCGIASL CLMGKLEEVF SEKELNRIKR 
       260        270        280        290        300
WCIMRQQNGY HGRPNKPVDT CYSFWVGATL KLLKIFQYTN FEKNRNYILS 
       310        320        330        340        350
TQDRLVGGFA KWPDSHPDAL HAYFGICGLS LMEESGICKV HPALNVSTRT 
       360        370 
SERLRDLHQS WKTKDSKQCS DNVHISS                          

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

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic 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. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families