ADP-ribosylation factor GTPase-activating protein GCS1

<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

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

• GTPase activator activity Source: SGD <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
  • "Role for Gcs1p in regulation of Arl1p at trans-Golgi compartments."
    Liu Y.W., Huang C.F., Huang K.B., Lee F.J.
    Mol. Biol. Cell 16:4024-4033(2005) [PubMed] [Europe PMC] [Abstract]
  • "Saccharomyces cerevisiae Gcs1 is an ADP-ribosylation factor GTPase-activating protein."
    Poon P.P., Wang X., Rotman M., Huber I., Cukierman E., Cassel D., Singer R.A., Johnston G.C.
    Proc. Natl. Acad. Sci. U.S.A. 93:10074-10077(1996) [PubMed] [Europe PMC] [Abstract]
• actin binding Source: SGDInferred from direct assayⁱ
  • "GCS1, an Arf guanosine triphosphatase-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro."
    Blader I.J., Cope M.J., Jackson T.R., Profit A.A., Greenwood A.F., Drubin D.G., Prestwich G.D., Theibert A.B.
    Mol. Biol. Cell 10:581-596(1999) [PubMed] [Europe PMC] [Abstract]
• metal ion binding Source: UniProtKB-KW

GO - Biological processⁱ

• Golgi to plasma membrane protein transport Source: SGD <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
  • "Arl1p is involved in transport of the GPI-anchored protein Gas1p from the late Golgi to the plasma membrane."
    Liu Y.W., Lee S.W., Lee F.J.
    J. Cell. Sci. 119:3845-3855(2006) [PubMed] [Europe PMC] [Abstract]
• actin filament reorganization involved in cell cycle Source: SGDInferred from mutant phenotypeⁱ
  • "GCS1, an Arf guanosine triphosphatase-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro."
    Blader I.J., Cope M.J., Jackson T.R., Profit A.A., Greenwood A.F., Drubin D.G., Prestwich G.D., Theibert A.B.
    Mol. Biol. Cell 10:581-596(1999) [PubMed] [Europe PMC] [Abstract]
• endoplasmic reticulum to Golgi vesicle-mediated transport Source: SGDInferred from mutant phenotypeⁱ
  • Ref.4

    "Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function."
    Poon P.P., Cassel D., Spang A., Rotman M., Pick E., Singer R.A., Johnston G.C.
    EMBO J. 18:555-564(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum Source: SGDInferred from direct assayⁱ
  • Ref.4

    "Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function."
    Poon P.P., Cassel D., Spang A., Rotman M., Pick E., Singer R.A., Johnston G.C.
    EMBO J. 18:555-564(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.

<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

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

<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 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

GO - Molecular functionⁱ

• actin binding Source: SGDInferred from direct assayⁱ
  • "GCS1, an Arf guanosine triphosphatase-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro."
    Blader I.J., Cope M.J., Jackson T.R., Profit A.A., Greenwood A.F., Drubin D.G., Prestwich G.D., Theibert A.B.
    Mol. Biol. Cell 10:581-596(1999) [PubMed] [Europe PMC] [Abstract]

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

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_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
MSDWKVDPDT RRRLLQLQKI GANKKCMDCG APNPQWATPK FGAFICLECA 
        60         70         80         90        100
GIHRGLGVHI SFVRSITMDQ FKPEELLRME KGGNEPLTEW FKSHNIDLSL 
       110        120        130        140        150
PQKVKYDNPV AEDYKEKLTC LCEDRVFEER EHLDFDASKL SATSQTAASA 
       160        170        180        190        200
TPGVAQSREG TPLENRRSAT PANSSNGANF QKEKNEAYFA ELGKKNQSRP 
       210        220        230        240        250
DHLPPSQGGK YQGFGSTPAK PPQERSAGSS NTLSLENFQA DPLGTLSRGW 
       260        270        280        290        300
GLFSSAVTKS FEDVNETVIK PHVQQWQSGE LSEETKRAAA QFGQKFQETS 
       310        320        330        340        350
SYGFQAFSNF TKNFNGNAED SSTAGNTTHT EYQKIDNNDK KNEQDEDKWD 

DF                                                     

Natural variant

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

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous 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. Yeast
   Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
3. Yeast chromosome IV
   Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names