Actin

<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>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

• ATP binding Source: WormBase <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

    "The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism."
    Vorobiev S., Strokopytov B., Drubin D.G., Frieden C., Ono S., Condeelis J., Rubenstein P.A., Almo S.C.
    Proc. Natl. Acad. Sci. U.S.A. 100:5760-5765(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
• identical protein binding Source: IntAct <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
  • "High-quality binary protein interaction map of the yeast interactome network."
    Yu H., Braun P., Yildirim M.A., Lemmens I., Venkatesan K., Sahalie J., Hirozane-Kishikawa T., Gebreab F., Li N., Simonis N., Hao T., Rual J.F., Dricot A., Vazquez A., Murray R.R., Simon C., Tardivo L., Tam S.

    , Svrzikapa N., Fan C., de Smet A.S., Motyl A., Hudson M.E., Park J., Xin X., Cusick M.E., Moore T., Boone C., Snyder M., Roth F.P., Barabasi A.L., Tavernier J., Hill D.E., Vidal M.
    Science 322:104-110(2008) [PubMed] [Europe PMC] [Abstract]
  • "Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin."
    Kudryashov D.S., Durer Z.A., Ytterberg A.J., Sawaya M.R., Pashkov I., Prochazkova K., Yeates T.O., Loo R.R., Loo J.A., Satchell K.J., Reisler E.
    Proc. Natl. Acad. Sci. U.S.A. 105:18537-18542(2008) [PubMed] [Europe PMC] [Abstract]
  • "Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness."
    Kang H., Bradley M.J., McCullough B.R., Pierre A., Grintsevich E.E., Reisler E., De La Cruz E.M.
    Proc. Natl. Acad. Sci. U.S.A. 109:16923-16927(2012) [PubMed] [Europe PMC] [Abstract]
  • "Defining protein interactions with yeast actin in vivo."
    Amberg D.C., Basart E., Botstein D.
    Nat. Struct. Biol. 2:28-35(1995) [PubMed] [Europe PMC] [Abstract]
• structural constituent of cytoskeleton Source: SGDInferred from direct assayⁱ
  • "Actin from Saccharomyces cerevisiae."
    Greer C., Schekman R.
    Mol. Cell. Biol. 2:1270-1278(1982) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• ascospore wall assembly Source: SGDInferred from direct assayⁱ
  • "Dynamic organization of the actin cytoskeleton during meiosis and spore formation in budding yeast."
    Taxis C., Maeder C., Reber S., Rathfelder N., Miura K., Greger K., Stelzer E.H., Knop M.
    Traffic 7:1628-1642(2006) [PubMed] [Europe PMC] [Abstract]
• cellular response to oxidative stress Source: SGD <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Conserved actin cysteine residues are oxidative stress sensors that can regulate cell death in yeast."
    Farah M.E., Amberg D.C.
    Mol. Biol. Cell 18:1359-1365(2007) [PubMed] [Europe PMC] [Abstract]
• chronological cell aging 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%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "A role for the actin cytoskeleton in cell death and aging in yeast."
    Gourlay C.W., Carpp L.N., Timpson P., Winder S.J., Ayscough K.R.
    J. Cell Biol. 164:803-809(2004) [PubMed] [Europe PMC] [Abstract]
• DNA repair Source: SGDInferred from direct assayⁱ
  • "Regulation of NuA4 histone acetyltransferase activity in transcription and DNA repair by phosphorylation of histone H4."
    Utley R.T., Lacoste N., Jobin-Robitaille O., Allard S., Cote J.
    Mol. Cell. Biol. 25:8179-8190(2005) [PubMed] [Europe PMC] [Abstract]
• endocytosis Source: SGDInferred from mutant phenotypeⁱ
  • "end5, end6, and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae."
    Munn A.L., Stevenson B.J., Geli M.I., Riezman H.
    Mol. Biol. Cell 6:1721-1742(1995) [PubMed] [Europe PMC] [Abstract]
• establishment of cell polarity Source: SGDInferred from genetic interactionⁱ
  • "Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast."
    Pruyne D.W., Schott D.H., Bretscher A.
    J. Cell Biol. 143:1931-1945(1998) [PubMed] [Europe PMC] [Abstract]
• histone acetylation Source: SGDInferred from direct assayⁱ
  • "Multiple links between the NuA4 histone acetyltransferase complex and epigenetic control of transcription."
    Galarneau L., Nourani A., Boudreault A.A., Zhang Y., Heliot L., Allard S., Savard J., Lane W.S., Stillman D.J., Cote J.
    Mol. Cell 5:927-937(2000) [PubMed] [Europe PMC] [Abstract]
• mitotic actomyosin contractile ring contraction Source: SGDInferred from mutant phenotypeⁱ
  • "Involvement of an actomyosin contractile ring in Saccharomyces cerevisiae cytokinesis."
    Bi E., Maddox P., Lew D.J., Salmon E.D., McMillan J.N., Yeh E., Pringle J.R.
    J. Cell Biol. 142:1301-1312(1998) [PubMed] [Europe PMC] [Abstract]
• protein secretion Source: SGDInferred from mutant phenotypeⁱ
  • "Role of actin and Myo2p in polarized secretion and growth of Saccharomyces cerevisiae."
    Karpova T.S., Reck-Peterson S.L., Elkind N.B., Mooseker M.S., Novick P.J., Cooper J.A.
    Mol. Biol. Cell 11:1727-1737(2000) [PubMed] [Europe PMC] [Abstract]
• vacuole inheritance Source: SGDInferred from mutant phenotypeⁱ
  • "Actin and myosin function in directed vacuole movement during cell division in Saccharomyces cerevisiae."
    Hill K.L., Catlett N.L., Weisman L.S.
    J. Cell Biol. 135:1535-1549(1996) [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

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

<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

Sites

Keywords - PTMⁱ

Proteomic databases

2D gel 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

<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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "High-quality binary protein interaction map of the yeast interactome network."
    Yu H., Braun P., Yildirim M.A., Lemmens I., Venkatesan K., Sahalie J., Hirozane-Kishikawa T., Gebreab F., Li N., Simonis N., Hao T., Rual J.F., Dricot A., Vazquez A., Murray R.R., Simon C., Tardivo L., Tam S.

    , Svrzikapa N., Fan C., de Smet A.S., Motyl A., Hudson M.E., Park J., Xin X., Cusick M.E., Moore T., Boone C., Snyder M., Roth F.P., Barabasi A.L., Tavernier J., Hill D.E., Vidal M.
    Science 322:104-110(2008) [PubMed] [Europe PMC] [Abstract]
  • "Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin."
    Kudryashov D.S., Durer Z.A., Ytterberg A.J., Sawaya M.R., Pashkov I., Prochazkova K., Yeates T.O., Loo R.R., Loo J.A., Satchell K.J., Reisler E.
    Proc. Natl. Acad. Sci. U.S.A. 105:18537-18542(2008) [PubMed] [Europe PMC] [Abstract]
  • "Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness."
    Kang H., Bradley M.J., McCullough B.R., Pierre A., Grintsevich E.E., Reisler E., De La Cruz E.M.
    Proc. Natl. Acad. Sci. U.S.A. 109:16923-16927(2012) [PubMed] [Europe PMC] [Abstract]
  • "Defining protein interactions with yeast actin in vivo."
    Amberg D.C., Basart E., Botstein D.
    Nat. Struct. Biol. 2:28-35(1995) [PubMed] [Europe PMC] [Abstract]

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

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

<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

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
MDSEVAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGIMVGMGQK 
        60         70         80         90        100
DSYVGDEAQS KRGILTLRYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE 
       110        120        130        140        150
HPVLLTEAPM NPKSNREKMT QIMFETFNVP AFYVSIQAVL SLYSSGRTTG 
       160        170        180        190        200
IVLDSGDGVT HVVPIYAGFS LPHAILRIDL AGRDLTDYLM KILSERGYSF 
       210        220        230        240        250
STTAEREIVR DIKEKLCYVA LDFEQEMQTA AQSSSIEKSY ELPDGQVITI 
       260        270        280        290        300
GNERFRAPEA LFHPSVLGLE SAGIDQTTYN SIMKCDVDVR KELYGNIVMS 
       310        320        330        340        350
GGTTMFPGIA ERMQKEITAL APSSMKVKII APPERKYSVW IGGSILASLT 
       360        370 
TFQQMWISKQ EYDESGPSIV HHKCF                            

Experimental Info

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

Chemistry databases

Protein family/group databases

PTM databases

2D gel databases

Proteomic 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. SIMILARITY comments
   Index of protein domains and families
3. Yeast chromosome VI
   Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names
4. Yeast
   Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD