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P60010 (ACT_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin
Gene names
Name:ACT1
Synonyms:ABY1, END7
Ordered Locus Names:YFL039C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

Subunit structure

Component of the INO80 complex. Component of the SWR1 complex. Component of the NuA4 complex.

Subcellular location

Cytoplasmcytoskeleton.

Sequence similarities

Belongs to the actin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from direct assay PubMed 16135807. Source: SGD

actomyosin contractile ring contraction

Inferred from direct assay PubMed 9732290. Source: SGD

ascospore wall assembly

Inferred from direct assay PubMed 17118118. Source: SGD

budding cell isotropic bud growth

Traceable author statement PubMed 10652251. Source: SGD

cellular response to oxidative stress

Inferred from genetic interaction PubMed 17287397. Source: SGD

chronological cell aging

Inferred from mutant phenotype PubMed 15024029. Source: SGD

endocytosis

Inferred from mutant phenotype PubMed 8590801. Source: SGD

establishment of cell polarity

Inferred from genetic interaction PubMed 9864365. Source: SGD

establishment of mitotic spindle orientation

Traceable author statement PubMed 10652251. Source: SGD

exocytosis

Traceable author statement PubMed 10652251. Source: SGD

fungal-type cell wall organization

Traceable author statement PubMed 10652251. Source: SGD

histone acetylation

Inferred from direct assay PubMed 10911987. Source: SGD

mitochondrion inheritance

Traceable author statement PubMed 10652251. Source: SGD

protein secretion

Inferred from mutant phenotype PubMed 10793147. Source: SGD

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 10911987. Source: SGD

vacuole inheritance

Inferred from mutant phenotype PubMed 8978821. Source: SGD

vesicle transport along actin filament

Traceable author statement PubMed 10652251. Source: SGD

   Cellular_componentIno80 complex

Inferred from physical interaction PubMed 10952318PubMed 24034245. Source: SGD

NuA4 histone acetyltransferase complex

Inferred from direct assay PubMed 10911987. Source: SGD

Swr1 complex

Inferred from direct assay PubMed 14645854PubMed 14690608PubMed 16299513. Source: SGD

actin cortical patch

Inferred from direct assay PubMed 3967297PubMed 6365930PubMed 8163554. Source: SGD

actin filament

Inferred from direct assay PubMed 6217414. Source: SGD

actin filament bundle

Inferred from direct assay PubMed 3967297PubMed 6365930PubMed 8163554. Source: SGD

cellular bud neck contractile ring

Inferred from direct assay PubMed 3967297PubMed 8163554. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of cytoskeleton

Inferred from direct assay PubMed 6217414. Source: SGD

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Actin
PRO_0000089051

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9 Ref.14

Natural variations

Natural variant1431Y → F in strain: CBS 1907.

Experimental info

Sequence conflict1781I → L in CAA24598. Ref.2
Sequence conflict3081G → S in CAA24598. Ref.2

Secondary structure

................................................................................. 375
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60010 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 87AC19B0B0BC9E71

FASTA37541,690
        10         20         30         40         50         60 
MDSEVAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGIMVGMGQK DSYVGDEAQS 

        70         80         90        100        110        120 
KRGILTLRYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPM NPKSNREKMT 

       130        140        150        160        170        180 
QIMFETFNVP AFYVSIQAVL SLYSSGRTTG IVLDSGDGVT HVVPIYAGFS LPHAILRIDL 

       190        200        210        220        230        240 
AGRDLTDYLM KILSERGYSF STTAEREIVR DIKEKLCYVA LDFEQEMQTA AQSSSIEKSY 

       250        260        270        280        290        300 
ELPDGQVITI GNERFRAPEA LFHPSVLGLE SAGIDQTTYN SIMKCDVDVR KELYGNIVMS 

       310        320        330        340        350        360 
GGTTMFPGIA ERMQKEITAL APSSMKVKII APPERKYSVW IGGSILASLT TFQQMWISKQ 

       370 
EYDESGPSIV HHKCF 

« Hide

References

« Hide 'large scale' references
[1]"Structure of a split yeast gene: complete nucleotide sequence of the actin gene in Saccharomyces cerevisiae."
Gallwitz D., Sures I.
Proc. Natl. Acad. Sci. U.S.A. 77:2546-2550(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Isolation and sequence of the gene for actin in Saccharomyces cerevisiae."
Ng R., Abelson J.
Proc. Natl. Acad. Sci. U.S.A. 77:3912-3916(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Lariat structures are in vivo intermediates in yeast pre-mRNA splicing."
Domdey H., Apostol B., Lin R.J., Newman A., Brody E., Abelson J.
Cell 39:611-621(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-58.
[4]"Molecular cloning of the actin gene from yeast Saccharomyces cerevisiae."
Gallwitz D., Seidel R.
Nucleic Acids Res. 8:1043-1059(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-57.
[5]"The nucleotide sequences of the actin genes from Saccharomyces carlsbergensis and Saccharomyces cerevisiae are identical except for their introns."
Nellen W., Donath C., Moos M., Gallwitz D.
J. Mol. Appl. Genet. 1:239-244(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Carlsbergensis.
[6]"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae."
Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T.
Nat. Genet. 10:261-268(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[7]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[8]"Partial sequence analysis of the actin gene and its potential for studying the phylogeny of Candida species and their teleomorphs."
Daniel H.-M., Sorrell T.C., Meyer W.
Int. J. Syst. Evol. Microbiol. 51:1593-1606(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-358.
Strain: ATCC 18824 / CBS 1171 / DSM 70449 / IFO 10217 / NRRL Y-12632 and CBS 1907.
[9]"Unusual metabolism of the yeast actin amino terminus."
Cook R.K., Sheff D.R., Rubenstein P.A.
J. Biol. Chem. 266:16825-16833(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT MET-1, PROTEIN SEQUENCE OF N-TERMINUS.
[10]"Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae."
Norbeck J., Blomberg A.
FEMS Microbiol. Lett. 137:1-8(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-25.
Strain: ATCC 38531 / Y41.
[11]"Site-directed mutagenesis of the yeast actin gene: a test for actin function in vivo."
Johannes F.-Z., Gallwitz D.
EMBO J. 10:3951-3958(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[12]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01288 Genomic DNA. Translation: CAA24597.1.
V01289 Genomic DNA. Translation: CAA24598.1. Sequence problems.
V01290 Genomic DNA. Translation: CAA24599.1.
L00026 Genomic DNA. Translation: AAA34391.1.
D50617 Genomic DNA. Translation: BAA21512.1.
AJ389075 Genomic DNA. Translation: CAC00716.1.
AJ389076 Genomic DNA. Translation: CAC00717.1.
BK006940 Genomic DNA. Translation: DAA12401.1.
PIRATBY. A03005.
JS0702.
RefSeqNP_116614.1. NM_001179927.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YAGX-ray1.90A1-375[»]
1YVNX-ray2.10A1-375[»]
ProteinModelPortalP60010.
SMRP60010. Positions 4-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31107. 694 interactions.
DIPDIP-310N.
IntActP60010. 140 interactions.
MINTMINT-374866.

2D gel databases

SWISS-2DPAGEP60010.

Proteomic databases

PaxDbP60010.
PeptideAtlasP60010.
PRIDEP60010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYFL039C; YFL039C; YFL039C.
GeneID850504.
KEGGsce:YFL039C.

Organism-specific databases

CYGDYFL039c.
SGDS000001855. ACT1.

Phylogenomic databases

eggNOGCOG5277.
GeneTreeENSGT00710000106384.
HOGENOMHOG000233340.
KOK05692.
OMANGIADRM.
OrthoDBEOG75B8FT.

Enzyme and pathway databases

BioCycYEAST:G3O-30423-MONOMER.

Gene expression databases

GenevestigatorP60010.

Family and domain databases

InterProIPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERPTHR11937. PTHR11937. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
PRINTSPR00190. ACTIN.
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP60010.
NextBio966206.

Entry information

Entry nameACT_YEAST
AccessionPrimary (citable) accession number: P60010
Secondary accession number(s): D6VTJ1 expand/collapse secondary AC list , P02579, Q9P3X6, Q9P3X7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VI

Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references