Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Actin-like protein ARP9

Gene

ARP9

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

Functioni

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 ARP9 and ARP7 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.8 Publications

GO - Molecular functioni

  • structural molecule activity Source: UniProtKB

GO - Biological processi

  • ATP-dependent chromatin remodeling Source: UniProtKB
  • chromatin organization Source: UniProtKB
  • nucleosome disassembly Source: SGD
  • nucleosome mobilization Source: SGD
  • nucleosome positioning Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • regulation of transcription, DNA-templated Source: UniProtKB
  • transcription elongation from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-32738-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-like protein ARP9
Alternative name(s):
Chromatin structure-remodeling complex protein ARP9
SWI/SNF complex component ARP9
Gene namesi
Name:ARP9
Synonyms:SWP59
Ordered Locus Names:YMR033W
ORF Names:YM9973.07
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR033W.
SGDiS000004636. ARP9.

Subcellular locationi

  • Nucleus 1 Publication

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

GO - Cellular componenti

  • nucleus Source: SGD
  • RSC complex Source: UniProtKB
  • SWI/SNF complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi337 – 3371G → V: Impaired heterodimerization with ARP7; when associated with L-338. 1 Publication
Mutagenesisi338 – 3381G → L: Impaired heterodimerization with ARP7; when associated with V-337. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 467467Actin-like protein ARP9PRO_0000089129Add
BLAST

Proteomic databases

MaxQBiQ05123.

Interactioni

Subunit structurei

Forms a heterodimer with ARP7. Interacts with LDB7 and 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/SWP29.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARP7Q124065EBI-2972,EBI-2962

Protein-protein interaction databases

BioGridi35205. 107 interactions.
DIPiDIP-6709N.
IntActiQ05123. 62 interactions.
MINTiMINT-669840.

Structurei

Secondary structure

1
467
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Beta strandi10 – 145Combined sources
Beta strandi16 – 249Combined sources
Beta strandi27 – 293Combined sources
Beta strandi35 – 395Combined sources
Beta strandi41 – 455Combined sources
Beta strandi51 – 566Combined sources
Helixi58 – 603Combined sources
Beta strandi62 – 654Combined sources
Beta strandi72 – 743Combined sources
Helixi76 – 9823Combined sources
Turni101 – 1066Combined sources
Beta strandi111 – 1155Combined sources
Helixi121 – 13313Combined sources
Beta strandi139 – 1446Combined sources
Helixi145 – 1528Combined sources
Beta strandi157 – 1648Combined sources
Beta strandi169 – 1757Combined sources
Turni181 – 1833Combined sources
Beta strandi185 – 1884Combined sources
Helixi191 – 20111Combined sources
Helixi207 – 2148Combined sources
Helixi224 – 2285Combined sources
Beta strandi229 – 2324Combined sources
Beta strandi251 – 2544Combined sources
Helixi276 – 2783Combined sources
Beta strandi282 – 2854Combined sources
Beta strandi291 – 2944Combined sources
Helixi296 – 2994Combined sources
Helixi303 – 31715Combined sources
Helixi323 – 3297Combined sources
Beta strandi333 – 3375Combined sources
Helixi338 – 3414Combined sources
Helixi345 – 35713Combined sources
Helixi363 – 37210Combined sources
Helixi379 – 3868Combined sources
Beta strandi401 – 4033Combined sources
Helixi417 – 4226Combined sources
Turni425 – 4273Combined sources
Helixi428 – 44013Combined sources
Beta strandi448 – 4503Combined sources
Helixi451 – 4577Combined sources
Helixi458 – 4647Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WEEX-ray3.10A1-467[»]
4I6MX-ray2.80B1-467[»]
ProteinModelPortaliQ05123.
SMRiQ05123. Positions 6-467.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

HOGENOMiHOG000034076.
InParanoidiQ05123.
KOiK11768.
OMAiYFPEWKK.
OrthoDBiEOG092C2C2S.

Family and domain databases

InterProiIPR004000. Actin.
IPR027665. Arp9_fungi.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 3 hits.
PTHR11937:SF231. PTHR11937:SF231. 3 hits.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05123-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPFRQDSIL IIYPRSQTTL VQFGLNEETF TVPELEIPTQ IYRTTRQDGS
60 70 80 90 100
YTYHSTNKDN KAELIKPIQN GEIIDISAFT QFLRLIFVSI LSDRANKNQD
110 120 130 140 150
AFEAELSNIP LLLITHHSWS QSDLEIITQY VFESLEINNL IQLPASLAAT
160 170 180 190 200
YSMISLQNCC IIDVGTHHTD IIPIVDYAQL DHLVSSIPMG GQSINDSLKK
210 220 230 240 250
LLPQWDDDQI ESLKKSPIFE VLSDDAKKLS SFDFGNENED EDEGTLNVAE
260 270 280 290 300
IITSGRDTRE VLEERERGQK VKNVKNSDLE FNTFWDEKGN EIKVGKQRFQ
310 320 330 340 350
GCNNLIKNIS NRVGLTLDNI DDINKAKAVW ENIIIVGGTT SISGFKEALL
360 370 380 390 400
GQLLKDHLII EPEEEKSKRE EEAKSVLPAA TKKKSKFMTN STAFVPTIEY
410 420 430 440 450
VQCPTVIKLA KYPDYFPEWK KSGYSEIIFL GAQIVSKQIF THPKDTFYIT
460
REKYNMKGPA ALWDVQF
Length:467
Mass (Da):53,074
Last modified:November 1, 1997 - v1
Checksum:iEE1AB154A906420E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49213 Genomic DNA. Translation: CAA89149.1.
BK006946 Genomic DNA. Translation: DAA09932.1.
PIRiS53950.
RefSeqiNP_013747.1. NM_001182530.1.

Genome annotation databases

EnsemblFungiiYMR033W; YMR033W; YMR033W.
GeneIDi855049.
KEGGisce:YMR033W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49213 Genomic DNA. Translation: CAA89149.1.
BK006946 Genomic DNA. Translation: DAA09932.1.
PIRiS53950.
RefSeqiNP_013747.1. NM_001182530.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WEEX-ray3.10A1-467[»]
4I6MX-ray2.80B1-467[»]
ProteinModelPortaliQ05123.
SMRiQ05123. Positions 6-467.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35205. 107 interactions.
DIPiDIP-6709N.
IntActiQ05123. 62 interactions.
MINTiMINT-669840.

Proteomic databases

MaxQBiQ05123.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR033W; YMR033W; YMR033W.
GeneIDi855049.
KEGGisce:YMR033W.

Organism-specific databases

EuPathDBiFungiDB:YMR033W.
SGDiS000004636. ARP9.

Phylogenomic databases

HOGENOMiHOG000034076.
InParanoidiQ05123.
KOiK11768.
OMAiYFPEWKK.
OrthoDBiEOG092C2C2S.

Enzyme and pathway databases

BioCyciYEAST:G3O-32738-MONOMER.

Miscellaneous databases

PROiQ05123.

Family and domain databases

InterProiIPR004000. Actin.
IPR027665. Arp9_fungi.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 3 hits.
PTHR11937:SF231. PTHR11937:SF231. 3 hits.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiARP9_YEAST
AccessioniPrimary (citable) accession number: Q05123
Secondary accession number(s): D6VZK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1790 molecules/cell in log phase SD medium.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.