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Q05123

- ARP9_YEAST

UniProt

Q05123 - ARP9_YEAST

Protein

Actin-like protein ARP9

Gene

ARP9

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    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

    1. protein binding Source: UniProtKB
    2. structural molecule activity Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. ATP-dependent chromatin remodeling Source: UniProtKB
    3. chromatin organization Source: UniProtKB
    4. nucleosome disassembly Source: SGD
    5. nucleosome mobilization Source: SGD
    6. nucleosome positioning Source: SGD
    7. positive regulation of transcription from RNA polymerase II promoter Source: SGD
    8. regulation of transcription, DNA-templated Source: UniProtKB
    9. transcription elongation from RNA polymerase II promoter Source: SGD

    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
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYMR033w.
    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

    1. nucleus Source: SGD
    2. RSC complex Source: UniProtKB
    3. SWI/SNF complex Source: UniProtKB

    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.
    PaxDbiQ05123.
    PeptideAtlasiQ05123.

    Expressioni

    Gene expression databases

    GenevestigatoriQ05123.

    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. 108 interactions.
    DIPiDIP-6709N.
    IntActiQ05123. 60 interactions.
    MINTiMINT-669840.
    STRINGi4932.YMR033W.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    eggNOGiCOG5277.
    HOGENOMiHOG000034076.
    KOiK11768.
    OMAiDHEMATE.
    OrthoDBiEOG7JHMF8.

    Family and domain databases

    InterProiIPR004000. Actin-related.
    IPR027665. Arp9_fungi.
    [Graphical view]
    PANTHERiPTHR11937. PTHR11937. 1 hit.
    PTHR11937:SF182. PTHR11937:SF182. 1 hit.
    PfamiPF00022. Actin. 1 hit.
    [Graphical view]
    SMARTiSM00268. ACTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q05123-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPFRQDSIL IIYPRSQTTL VQFGLNEETF TVPELEIPTQ IYRTTRQDGS    50
    YTYHSTNKDN KAELIKPIQN GEIIDISAFT QFLRLIFVSI LSDRANKNQD 100
    AFEAELSNIP LLLITHHSWS QSDLEIITQY VFESLEINNL IQLPASLAAT 150
    YSMISLQNCC IIDVGTHHTD IIPIVDYAQL DHLVSSIPMG GQSINDSLKK 200
    LLPQWDDDQI ESLKKSPIFE VLSDDAKKLS SFDFGNENED EDEGTLNVAE 250
    IITSGRDTRE VLEERERGQK VKNVKNSDLE FNTFWDEKGN EIKVGKQRFQ 300
    GCNNLIKNIS NRVGLTLDNI DDINKAKAVW ENIIIVGGTT SISGFKEALL 350
    GQLLKDHLII EPEEEKSKRE EEAKSVLPAA TKKKSKFMTN STAFVPTIEY 400
    VQCPTVIKLA KYPDYFPEWK KSGYSEIIFL GAQIVSKQIF THPKDTFYIT 450
    REKYNMKGPA ALWDVQF 467
    Length:467
    Mass (Da):53,074
    Last modified:November 1, 1997 - v1
    Checksum:iEE1AB154A906420E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49213 Genomic DNA. Translation: CAA89149.1 .
    BK006946 Genomic DNA. Translation: DAA09932.1 .
    PIRi S53950.
    RefSeqi NP_013747.1. NM_001182530.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3WEE X-ray 3.10 A 1-467 [» ]
    4I6M X-ray 2.80 B 1-467 [» ]
    ProteinModelPortali Q05123.
    SMRi Q05123. Positions 6-467.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35205. 108 interactions.
    DIPi DIP-6709N.
    IntActi Q05123. 60 interactions.
    MINTi MINT-669840.
    STRINGi 4932.YMR033W.

    Proteomic databases

    MaxQBi Q05123.
    PaxDbi Q05123.
    PeptideAtlasi Q05123.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR033W ; YMR033W ; YMR033W .
    GeneIDi 855049.
    KEGGi sce:YMR033W.

    Organism-specific databases

    CYGDi YMR033w.
    SGDi S000004636. ARP9.

    Phylogenomic databases

    eggNOGi COG5277.
    HOGENOMi HOG000034076.
    KOi K11768.
    OMAi DHEMATE.
    OrthoDBi EOG7JHMF8.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32738-MONOMER.

    Miscellaneous databases

    NextBioi 978283.

    Gene expression databases

    Genevestigatori Q05123.

    Family and domain databases

    InterProi IPR004000. Actin-related.
    IPR027665. Arp9_fungi.
    [Graphical view ]
    PANTHERi PTHR11937. PTHR11937. 1 hit.
    PTHR11937:SF182. PTHR11937:SF182. 1 hit.
    Pfami PF00022. Actin. 1 hit.
    [Graphical view ]
    SMARTi SM00268. ACTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. 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 16-37 AND 459-467, FUNCTION, IDENTIFICATION IN THE RSC AND SWI/SNF COMPLEXES.
    4. 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 ARP7 WITHIN THE RSC COMPLEX, MUTAGENESIS OF GLY-337 AND GLY-338.
    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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    14. "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 LDB7 AND NPL6.

    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: October 1, 2014
    This is version 111 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

    External Data

    Dasty 3