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P60010

- ACT_YEAST

UniProt

P60010 - ACT_YEAST

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Protein

Actin

Gene

ACT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. structural constituent of cytoskeleton Source: SGD

GO - Biological processi

  1. actomyosin contractile ring contraction Source: SGD
  2. ascospore wall assembly Source: SGD
  3. budding cell isotropic bud growth Source: SGD
  4. cellular response to oxidative stress Source: SGD
  5. chronological cell aging Source: SGD
  6. DNA repair Source: SGD
  7. endocytosis Source: SGD
  8. establishment of cell polarity Source: SGD
  9. establishment of mitotic spindle orientation Source: SGD
  10. exocytosis Source: SGD
  11. fungal-type cell wall organization Source: SGD
  12. histone acetylation Source: SGD
  13. mitochondrion inheritance Source: SGD
  14. protein secretion Source: SGD
  15. vacuole inheritance Source: SGD
  16. vesicle transport along actin filament Source: SGD
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30423-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin
Gene namesi
Name:ACT1
Synonyms:ABY1, END7
Ordered Locus Names:YFL039C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VI

Organism-specific databases

CYGDiYFL039c.
SGDiS000001855. ACT1.

Subcellular locationi

GO - Cellular componenti

  1. actin cortical patch Source: SGD
  2. actin filament Source: SGD
  3. actin filament bundle Source: SGD
  4. cellular bud neck contractile ring Source: SGD
  5. Ino80 complex Source: SGD
  6. NuA4 histone acetyltransferase complex Source: SGD
  7. Swr1 complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375ActinPRO_0000089051Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP60010.
PaxDbiP60010.
PeptideAtlasiP60010.
PRIDEiP60010.

2D gel databases

SWISS-2DPAGEP60010.

Expressioni

Gene expression databases

GenevestigatoriP60010.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
groLP0A6F55EBI-2169,EBI-543750From a different organism.
HSP82P028292EBI-2169,EBI-8659
SRV2P175555EBI-2169,EBI-4024
SWR1Q0547112EBI-2169,EBI-22102
TCP1P126123EBI-2169,EBI-19045

Protein-protein interaction databases

BioGridi31107. 699 interactions.
DIPiDIP-310N.
IntActiP60010. 142 interactions.
MINTiMINT-374866.

Structurei

Secondary structure

1
375
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Beta strandi14 – 218Combined sources
Beta strandi28 – 325Combined sources
Beta strandi35 – 406Combined sources
Turni45 – 473Combined sources
Helixi56 – 605Combined sources
Helixi62 – 643Combined sources
Beta strandi65 – 684Combined sources
Beta strandi70 – 723Combined sources
Beta strandi75 – 773Combined sources
Helixi79 – 9113Combined sources
Turni92 – 943Combined sources
Helixi98 – 1003Combined sources
Beta strandi103 – 1075Combined sources
Helixi113 – 12513Combined sources
Beta strandi130 – 1367Combined sources
Helixi137 – 1448Combined sources
Beta strandi148 – 1558Combined sources
Beta strandi160 – 1667Combined sources
Helixi172 – 1743Combined sources
Beta strandi176 – 1794Combined sources
Helixi182 – 19413Combined sources
Turni195 – 1973Combined sources
Helixi203 – 21614Combined sources
Helixi223 – 2286Combined sources
Turni229 – 2313Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi238 – 2414Combined sources
Beta strandi247 – 2504Combined sources
Helixi253 – 2564Combined sources
Helixi258 – 2614Combined sources
Helixi264 – 2674Combined sources
Helixi274 – 28310Combined sources
Helixi287 – 2948Combined sources
Beta strandi297 – 3015Combined sources
Helixi302 – 3043Combined sources
Helixi309 – 32012Combined sources
Turni333 – 3364Combined sources
Helixi338 – 34811Combined sources
Helixi350 – 3545Combined sources
Beta strandi356 – 3583Combined sources
Helixi359 – 3657Combined sources
Helixi367 – 3693Combined sources
Helixi370 – 3734Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YAGX-ray1.90A1-375[»]
1YVNX-ray2.10A1-375[»]
ProteinModelPortaliP60010.
SMRiP60010. Positions 4-375.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60010.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiCOG5277.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
InParanoidiP60010.
KOiK05692.
OMAiSIVHLKC.
OrthoDBiEOG75B8FT.

Family and domain databases

InterProiIPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P60010-1 [UniParc]FASTAAdd to Basket

« Hide

        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
Length:375
Mass (Da):41,690
Last modified:July 21, 1986 - v1
Checksum:i87AC19B0B0BC9E71
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti178 – 1781I → L in CAA24598. (PubMed:7001447)Curated
Sequence conflicti308 – 3081G → S in CAA24598. (PubMed:7001447)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti143 – 1431Y → F in strain: CBS 1907.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA03005. ATBY.
JS0702.
RefSeqiNP_116614.1. NM_001179927.1.

Genome annotation databases

EnsemblFungiiYFL039C; YFL039C; YFL039C.
GeneIDi850504.
KEGGisce:YFL039C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A03005. ATBY.
JS0702.
RefSeqi NP_116614.1. NM_001179927.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YAG X-ray 1.90 A 1-375 [» ]
1YVN X-ray 2.10 A 1-375 [» ]
ProteinModelPortali P60010.
SMRi P60010. Positions 4-375.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31107. 699 interactions.
DIPi DIP-310N.
IntActi P60010. 142 interactions.
MINTi MINT-374866.

2D gel databases

SWISS-2DPAGE P60010.

Proteomic databases

MaxQBi P60010.
PaxDbi P60010.
PeptideAtlasi P60010.
PRIDEi P60010.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YFL039C ; YFL039C ; YFL039C .
GeneIDi 850504.
KEGGi sce:YFL039C.

Organism-specific databases

CYGDi YFL039c.
SGDi S000001855. ACT1.

Phylogenomic databases

eggNOGi COG5277.
GeneTreei ENSGT00760000118957.
HOGENOMi HOG000233340.
InParanoidi P60010.
KOi K05692.
OMAi SIVHLKC.
OrthoDBi EOG75B8FT.

Enzyme and pathway databases

BioCyci YEAST:G3O-30423-MONOMER.

Miscellaneous databases

EvolutionaryTracei P60010.
NextBioi 966206.

Gene expression databases

Genevestigatori P60010.

Family and domain databases

InterProi IPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view ]
PANTHERi PTHR11937. PTHR11937. 1 hit.
Pfami PF00022. Actin. 1 hit.
[Graphical view ]
PRINTSi PR00190. ACTIN.
SMARTi SM00268. ACTIN. 1 hit.
[Graphical view ]
PROSITEi PS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  7. 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. 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).

Entry informationi

Entry nameiACT_YEAST
AccessioniPrimary (citable) accession number: P60010
Secondary accession number(s): D6VTJ1
, P02579, Q9P3X6, Q9P3X7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3