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Q12406 (ARP7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. 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-related protein 7
Alternative name(s):
Actin-like protein ARP7
Chromatin structure-remodeling complex protein ARP7
SWI/SNF complex component ARP7
Gene names
Name:ARP7
Synonyms:SWP61
Ordered Locus Names:YPR034W
ORF Names:YP9367.14
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is involved in transcriptional regulation. Heterodimer of ARP7 and ARP9 functions with HMG box proteins to facilitate proper chromatin architecture. Heterodimer formation is necessary for assembly into RSC complex. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. Ref.3 Ref.4 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12

Subunit structure

Forms a heterodimer with ARP9. Interacts with NPL6. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin. Component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29. Ref.3 Ref.12 Ref.15

Subcellular location

Nucleus. Note: Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1. Ref.12

Miscellaneous

Present with 1360 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the actin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARP9Q051235EBI-2962,EBI-2972

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 477477Actin-related protein 7
PRO_0000089122

Experimental info

Mutagenesis191A → P: Impaired heterodimerization with ARP9. Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. Ref.3 Ref.11
Mutagenesis331S → F: Impaired heterodimerization with ARP9. Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. Ref.3 Ref.11
Mutagenesis3961G → V: Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. Ref.3
Mutagenesis4111E → K: Impaired heterodimerization with ARP9. Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. Ref.3 Ref.11

Secondary structure

...................................................................... 477
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12406 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8E105921576FA213

FASTA47753,810
        10         20         30         40         50         60 
MTLNRKCVVI HNGSHRTVAG FSNVELPQCI IPSSYIKRTD EGGEAEFIFG TYNMIDAAAE 

        70         80         90        100        110        120 
KRNGDEVYTL VDSQGLPYNW DALEMQWRYL YDTQLKVSPE ELPLVITMPA TNGKPDMAIL 

       130        140        150        160        170        180 
ERYYELAFDK LNVPVFQIVI EPLAIALSMG KSSAFVIDIG ASGCNVTPII DGIVVKNAVV 

       190        200        210        220        230        240 
RSKFGGDFLD FQVHERLAPL IKEENDMENM ADEQKRSTDV WYEASTWIQQ FKSTMLQVSE 

       250        260        270        280        290        300 
KDLFELERYY KEQADIYAKQ QEQLKQMDQQ LQYTALTGSP NNPLVQKKNF LFKPLNKTLT 

       310        320        330        340        350        360 
LDLKECYQFA EYLFKPQLIS DKFSPEDGLG PLMAKSVKKA GASINSMKAN TSTNPNGLGT 

       370        380        390        400        410        420 
SHINTNVGDN NSTASSSNIS PEQVYSLLLT NVIITGSTSL IEGMEQRIIK ELSIRFPQYK 

       430        440        450        460        470 
LTTFANQVMM DRKIQGWLGA LTMANLPSWS LGKWYSKEDY ETLKRDRKQS QATNATN 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Two actin-related proteins are shared functional components of the chromatin-remodeling complexes RSC and SWI/SNF."
Cairns B.R., Erdjument-Bromage H., Tempst P., Winston F., Kornberg R.D.
Mol. Cell 2:639-651(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 184-196; 217-232 AND 289-297, FUNCTION, IDENTIFICATION IN THE RSC AND SWI/SNF COMPLEXES, MUTAGENESIS OF ALA-19; SER-33; GLY-396 AND GLU-411.
[4]"RSC, an essential, abundant chromatin-remodeling complex."
Cairns B.R., Lorch Y., Li Y., Zhang M., Lacomis L., Erdjument-Bromage H., Tempst P., Du J., Laurent B.C., Kornberg R.D.
Cell 87:1249-1260(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE RSC COMPLEX, COMPOSITION OF THE RSC COMPLEX.
[5]"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.
[6]"Histone octamer transfer by a chromatin-remodeling complex."
Lorch Y., Zhang M., Kornberg R.D.
Cell 96:389-392(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE RSC COMPLEX.
[7]"Transcriptional repression of the yeast CHA1 gene requires the chromatin-remodeling complex RSC."
Moreira J.M.A., Holmberg S.
EMBO J. 18:2836-2844(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE RSC COMPLEX.
[8]"Two functionally distinct forms of the RSC nucleosome-remodeling complex, containing essential AT hook, BAH, and bromodomains."
Cairns B.R., Schlichter A., Erdjument-Bromage H., Tempst P., Kornberg R.D., Winston F.
Mol. Cell 4:715-723(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPOSITION OF THE RSC COMPLEX.
[9]"Chromatin remodeling by RSC involves ATP-dependent DNA translocation."
Saha A., Wittmeyer J., Cairns B.R.
Genes Dev. 16:2120-2134(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE RSC COMPLEX.
[10]"Yeast RSC function is required for organization of the cellular cytoskeleton via an alternative PKC1 pathway."
Chai B., Hsu J.-M., Du J., Laurent B.C.
Genetics 161:575-584(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE RSC COMPLEX.
[11]"The nuclear actin-related proteins Arp7 and Arp9: a dimeric module that cooperates with architectural proteins for chromatin remodeling."
Szerlong H., Saha A., Cairns B.R.
EMBO J. 22:3175-3187(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, HETERODIMERIC COMPLEX FORMATION WITH ARP9 WITHIN THE RSC COMPLEX, MUTAGENESIS OF ALA-19; SER-33 AND GLU-411.
[12]"The yeast RSC chromatin-remodeling complex is required for kinetochore function in chromosome segregation."
Hsu J.-M., Huang J., Meluh P.B., Laurent B.C.
Mol. Cell. Biol. 23:3202-3215(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE RSC COMPLEX, SUBCELLULAR LOCATION, INTERACTION OF THE RSC COMPLEX WITH HISTONES.
[13]"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].
[14]"Structural analysis of the yeast SWI/SNF chromatin remodeling complex."
Smith C.L., Horowitz-Scherer R., Flanagan J.F., Woodcock C.L., Peterson C.L.
Nat. Struct. Biol. 10:141-145(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF THE SWI/SNF COMPLEX, ELECTRON MICROSCOPY OF THE SWI/SNF COMPLEX.
[15]"The RSC chromatin remodeling complex bears an essential fungal-specific protein module with broad functional roles."
Wilson B., Erdjument-Bromage H., Tempst P., Cairns B.R.
Genetics 172:795-809(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NPL6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z71255 Genomic DNA. Translation: CAA94984.1.
Z49274 Genomic DNA. Translation: CAA89288.1.
BK006949 Genomic DNA. Translation: DAA11460.1.
PIRS54508.
RefSeqNP_015359.1. NM_001184131.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3WEEX-ray3.10B1-477[»]
4I6MX-ray2.80A1-477[»]
ProteinModelPortalQ12406.
SMRQ12406. Positions 2-466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36212. 57 interactions.
DIPDIP-6351N.
IntActQ12406. 55 interactions.
MINTMINT-686249.
STRING4932.YPR034W.

Proteomic databases

PaxDbQ12406.
PeptideAtlasQ12406.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPR034W; YPR034W; YPR034W.
GeneID856146.
KEGGsce:YPR034W.

Organism-specific databases

CYGDYPR034w.
SGDS000006238. ARP7.

Phylogenomic databases

eggNOGCOG5277.
HOGENOMHOG000034072.
KOK11767.
OMAGMEQRII.
OrthoDBEOG7X6M98.

Enzyme and pathway databases

BioCycYEAST:G3O-34193-MONOMER.

Gene expression databases

GenevestigatorQ12406.

Family and domain databases

InterProIPR004000. Actin-related.
[Graphical view]
PANTHERPTHR11937. PTHR11937. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio981268.

Entry information

Entry nameARP7_YEAST
AccessionPrimary (citable) accession number: Q12406
Secondary accession number(s): D6W444
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 118 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 XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: 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