Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q12386 (ARP8_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 123. 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-like protein ARP8
Gene names
Name:ARP8
Ordered Locus Names:YOR141C
ORF Names:YOR3348C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length881 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin remodeling complex. Exhibits low basal ATPase activity, and unable to polymerize. Strongly prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex. Ref.10

Subunit structure

Component of the chromatin-remodeling INO80 complex, at least composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3, IES4, IES6, ACT1, IES2, IES5 and INO80. Exists as monomers and dimers, but the dimer is most probably the biologically relevant form required for stable interactions with histones that exploits the twofold symmetry of the nucleosome core By similarity. Ref.5 Ref.10

Subcellular location

Nucleus. Cytoplasmcytoskeleton.

Miscellaneous

Present with 1010 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the actin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACTA1P681352EBI-2967,EBI-367540From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 881881Actin-like protein ARP8
PRO_0000089128

Regions

Nucleotide binding502 – 5054ATP By similarity
Compositional bias22 – 276Poly-Asp

Amino acid modifications

Modified residue651Phosphoserine Ref.7 Ref.8 Ref.9
Modified residue701Phosphoserine Ref.8

Secondary structure

....................................................................................................... 881
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12386 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8174851B6B077A19

FASTA881100,209
        10         20         30         40         50         60 
MSQEEAESSI IYEEPIDIPL EDDDDEDELE EENSVPLSSQ ADQENAENES DDSVDNVVGS 

        70         80         90        100        110        120 
ETPRSVTGLS VDPRDVADEE DEDEEGEDED EDEDDNDVDN EDENDNDNAN ENENELGSSR 

       130        140        150        160        170        180 
DKRAPPAVQT SKRYKKYPKL DPAKAPPGKK VPLHLLEKRR LGRIKAAEEF AKTLKKIGIE 

       190        200        210        220        230        240 
KVETTTLPAT GLFQPLMLIN QKNYSSDYLK KDDQIFALRD RKFLRNNNTS QISSTNTPDV 

       250        260        270        280        290        300 
IDLKSLPHSE ASAAPLNDEI DLNDPTATIV IHPGSNSIKI GFPKDDHPVV VPNCVAVPKK 

       310        320        330        340        350        360 
WLDLENSEHV ENVCLQREQS EEFNNIKSEM EKNFRERMRY YKRKVPGNAH EQVVSFNENS 

       370        380        390        400        410        420 
KPEIISEKND PSPIEWIFDD SKLYYGSDAL RCVDEKFVIR KPFRGGSFNV KSPYYKSLAE 

       430        440        450        460        470        480 
LISDVTKLLE HALNSETLNV KPTKFNQYKV VLVIPDIFKK SHVETFIRVL LTELQFQAVA 

       490        500        510        520        530        540 
IIQESLATCY GAGISTSTCV VNIGAAETRI ACVDEGTVLE HSAITLDYGG DDITRLFALF 

       550        560        570        580        590        600 
LLQSDFPLQD WKIDSKHGWL LAERLKKNFT TFQDADVAVQ LYNFMNRSPN QPTEKYEFKL 

       610        620        630        640        650        660 
FDEVMLAPLA LFFPQIFKLI RTSSHKNSSL EFQLPESRDL FTNELNDWNS LSQFESKEGN 

       670        680        690        700        710        720 
LYCDLNDDLK ILNRILDAHN IIDQLQDKPE NYGNTLKENF APLEKAIVQS IANASITADV 

       730        740        750        760        770        780 
TRMNSFYSNI LIVGGSSKIP ALDFILTDRI NIWRPSLLSS ASFPQFYKKL TKEIKDLEGH 

       790        800        810        820        830        840 
YVNAPDKTED ENKQILQAQI KEKIVEELEE QHQNIEHQNG NEHIFPVSII PPPRDMNPAL 

       850        860        870        880 
IIWKGASVLA QIKLVEELFI TNSDWDVHGS RILQYKCIFT Y 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequencing and analysis of 130 kb from yeast chromosome XV."
Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C., Schwager C., Paces V., Sander C., Ansorge W.
Yeast 13:655-672(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Who's who among the Saccharomyces cerevisiae actin-related proteins? A classification and nomenclature proposal for a large family."
Poch O., Winsor B.
Yeast 13:1053-1058(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE NAME.
[5]"Involvement of actin-related proteins in ATP-dependent chromatin remodeling."
Shen X., Ranallo R., Choi E., Wu C.
Mol. Cell 12:147-155(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[8]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Interactions between the nucleosome histone core and Arp8 in the INO80 chromatin remodeling complex."
Saravanan M., Wuerges J., Bose D., McCormack E.A., Cook N.J., Zhang X., Wigley D.B.
Proc. Natl. Acad. Sci. U.S.A. 109:20883-20888(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 248-881, ELECTRON MICROSCOPY, FUNCTION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X94335 Genomic DNA. Translation: CAA64058.1.
Z75049 Genomic DNA. Translation: CAA99341.1.
BK006948 Genomic DNA. Translation: DAA10913.1.
PIRS67026.
RefSeqNP_014784.1. NM_001183560.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4AM6X-ray2.70A/B248-881[»]
4AM7X-ray3.25A/B248-881[»]
ProteinModelPortalQ12386.
SMRQ12386. Positions 259-881.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34535. 468 interactions.
DIPDIP-6706N.
IntActQ12386. 30 interactions.
MINTMINT-659970.
STRING4932.YOR141C.

Proteomic databases

MaxQBQ12386.
PaxDbQ12386.
PeptideAtlasQ12386.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR141C; YOR141C; YOR141C.
GeneID854309.
KEGGsce:YOR141C.

Organism-specific databases

CYGDYOR141c.
SGDS000005667. ARP8.

Phylogenomic databases

eggNOGCOG5277.
GeneTreeENSGT00390000001763.
HOGENOMHOG000246531.
KOK11673.
OMATFQDADI.
OrthoDBEOG71RXT9.

Enzyme and pathway databases

BioCycYEAST:G3O-33662-MONOMER.

Gene expression databases

GenevestigatorQ12386.

Family and domain databases

InterProIPR004000. Actin-related.
IPR027668. Arp8/plant_Arp9.
[Graphical view]
PANTHERPTHR11937. PTHR11937. 1 hit.
PTHR11937:SF13. PTHR11937:SF13. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio976325.
PROQ12386.

Entry information

Entry nameARP8_YEAST
AccessionPrimary (citable) accession number: Q12386
Secondary accession number(s): D6W2J7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 123 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 XV

Yeast (Saccharomyces cerevisiae) chromosome XV: 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