P60010D6VTJ1P02579Q9P3X6Q9P3X7ACT_YEASTActin3.6.4.-ACT1ABY1END7YFL039CSaccharomyces cerevisiae (strain ATCC 204508 / S288c)Baker's yeastEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomycesStructure of a split yeast gene: complete nucleotide sequence of the actin gene in Saccharomyces cerevisiae.NUCLEOTIDE SEQUENCE [GENOMIC DNA]Isolation and sequence of the gene for actin in Saccharomyces cerevisiae.NUCLEOTIDE SEQUENCE [GENOMIC DNA]Lariat structures are in vivo intermediates in yeast pre-mRNA splicing.NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-58Molecular cloning of the actin gene from yeast Saccharomyces cerevisiae.NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-57The nucleotide sequences of the actin genes from Saccharomyces carlsbergensis and Saccharomyces cerevisiae are identical except for their introns.NUCLEOTIDE SEQUENCE [GENOMIC DNA]Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae.NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The reference genome sequence of Saccharomyces cerevisiae: Then and now.GENOME REANNOTATIONPartial sequence analysis of the actin gene and its potential for studying the phylogeny of Candida species and their teleomorphs.NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-358Unusual metabolism of the yeast actin amino terminus.ACETYLATION AT MET-1PROTEIN SEQUENCE OF N-TERMINUSProtein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae.PROTEIN SEQUENCE OF 19-25Site-directed mutagenesis of the yeast actin gene: a test for actin function in vivo.MUTAGENESISYIH1 is an actin-binding protein that inhibits protein kinase GCN2 and impairs general amino acid control when overexpressed.INTERACTION WITH YIH1A multidimensional chromatography technology for in-depth phosphoproteome analysis.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Gcn1 and actin binding to Yih1: implications for activation of the eIF2 kinase GCN2.INTERACTION WITH YIH1A highly conserved 3-methylhistidine modification is absent in yeast actin.IDENTIFICATION BY MASS SPECTROMETRYLACK OF METHYLATION AT HIS-73N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Sites of ubiquitin attachment in Saccharomyces cerevisiae.UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-191IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Direct Interaction of Chivosazole F with Actin Elicits Cell Responses Similar to Latrunculin A but Distinct from Chondramide.SUBUNITMUTAGENESIS OF ARG-183 AND ARG-335The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism.X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)CATALYTIC ACTIVITYActins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.ATP + H2O = ADP + H(+) + phosphatePolymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix (Probable). Treatments with Lantrunculin A, the microbial peptide Chondramide or the microbial metabolite Chivazole F inhibit actin polymerization (PubMed:28796488). Each actin can bind to 4 others. Interacts with YIH1 (via C-terminus); this interaction occurs in a GCN1-independent manner (PubMed:15126500, PubMed:21239490). Component of the INO80 complex. Component of the SWR1 complex. Component of the NuA4 complex.P60010P60010false6P60010P46680false3P60010Q03048false3P60010Q06440false3P60010P02829false2P60010Q12446false4P60010P07274false4P60010P39743false4P60010P32599false4P60010P17555false7P60010P12612false3P60010P0A6F5true5CytoplasmCytoskeletonBelongs to the actin family.3D-structureAcetylationATP-bindingCytoplasmCytoskeletonDirect protein sequencingHydrolaseIsopeptide bondNucleotide-bindingReference proteomeUbl conjugationYFRKRKILGSMDSEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQSKRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMTQIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDLAGRDLTDYLMKILSERGYSFSTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSYELPDGQVITIGNERFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMSGGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQQMWISKQEYDESGPSIVHHKCF
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