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Q12386

- ARP8_YEAST

UniProt

Q12386 - ARP8_YEAST

Protein

Actin-like protein ARP8

Gene

ARP8

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 124 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi502 – 5054ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. mRNA binding Source: SGD
    3. protein binding Source: IntAct

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: SGD
    2. chromatin remodeling Source: SGD
    3. DNA duplex unwinding Source: GOC
    4. double-strand break repair Source: SGD
    5. mitotic recombination Source: SGD
    6. regulation of transcription, DNA-templated Source: UniProtKB-KW
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33662-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin-like protein ARP8
    Gene namesi
    Name:ARP8
    Ordered Locus Names:YOR141C
    ORF Names:YOR3348C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOR141c.
    SGDiS000005667. ARP8.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. cytoskeleton Source: UniProtKB-SubCell
    3. Ino80 complex Source: SGD
    4. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 881881Actin-like protein ARP8PRO_0000089128Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei65 – 651Phosphoserine3 Publications
    Modified residuei70 – 701Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ12386.
    PaxDbiQ12386.
    PeptideAtlasiQ12386.

    Expressioni

    Gene expression databases

    GenevestigatoriQ12386.

    Interactioni

    Subunit structurei

    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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACTA1P681352EBI-2967,EBI-367540From a different organism.

    Protein-protein interaction databases

    BioGridi34535. 468 interactions.
    DIPiDIP-6706N.
    IntActiQ12386. 30 interactions.
    MINTiMINT-659970.
    STRINGi4932.YOR141C.

    Structurei

    Secondary structure

    1
    881
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi265 – 2673
    Beta strandi268 – 2725
    Beta strandi275 – 2817
    Beta strandi285 – 2873
    Beta strandi289 – 2935
    Beta strandi295 – 2984
    Helixi299 – 3013
    Beta strandi305 – 3073
    Helixi321 – 34121
    Helixi352 – 3543
    Beta strandi357 – 3604
    Beta strandi367 – 3704
    Helixi386 – 3905
    Turni394 – 3963
    Beta strandi397 – 4004
    Beta strandi402 – 4043
    Helixi418 – 43316
    Beta strandi434 – 4374
    Helixi442 – 4476
    Beta strandi449 – 4546
    Helixi460 – 47213
    Beta strandi477 – 4837
    Helixi484 – 4918
    Beta strandi498 – 5036
    Beta strandi508 – 5147
    Helixi520 – 5223
    Beta strandi524 – 5274
    Helixi530 – 54314
    Helixi556 – 56914
    Helixi574 – 5763
    Beta strandi579 – 5868
    Beta strandi589 – 5913
    Beta strandi593 – 60210
    Helixi603 – 6097
    Helixi610 – 6123
    Helixi615 – 6195
    Helixi628 – 6314
    Turni640 – 6423
    Helixi651 – 6577
    Helixi662 – 6643
    Helixi668 – 68619
    Helixi703 – 71614
    Helixi720 – 7223
    Helixi723 – 7275
    Beta strandi730 – 7345
    Helixi735 – 7384
    Helixi742 – 75312
    Turni757 – 7593
    Helixi763 – 77816
    Beta strandi786 – 7883
    Turni793 – 7975
    Helixi798 – 81720
    Helixi838 – 8403
    Helixi841 – 8499
    Helixi853 – 8586
    Helixi862 – 8687
    Helixi869 – 8746

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AM6X-ray2.70A/B248-881[»]
    4AM7X-ray3.25A/B248-881[»]
    ProteinModelPortaliQ12386.
    SMRiQ12386. Positions 259-881.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi22 – 276Poly-Asp

    Sequence similaritiesi

    Belongs to the actin family.Curated

    Phylogenomic databases

    eggNOGiCOG5277.
    GeneTreeiENSGT00390000001763.
    HOGENOMiHOG000246531.
    KOiK11673.
    OMAiTFQDADI.
    OrthoDBiEOG71RXT9.

    Family and domain databases

    InterProiIPR004000. Actin-related.
    IPR027668. Arp8/plant_Arp9.
    [Graphical view]
    PANTHERiPTHR11937. PTHR11937. 1 hit.
    PTHR11937:SF13. PTHR11937:SF13. 1 hit.
    PfamiPF00022. Actin. 1 hit.
    [Graphical view]
    SMARTiSM00268. ACTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q12386-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQEEAESSI IYEEPIDIPL EDDDDEDELE EENSVPLSSQ ADQENAENES    50
    DDSVDNVVGS ETPRSVTGLS VDPRDVADEE DEDEEGEDED EDEDDNDVDN 100
    EDENDNDNAN ENENELGSSR DKRAPPAVQT SKRYKKYPKL DPAKAPPGKK 150
    VPLHLLEKRR LGRIKAAEEF AKTLKKIGIE KVETTTLPAT GLFQPLMLIN 200
    QKNYSSDYLK KDDQIFALRD RKFLRNNNTS QISSTNTPDV IDLKSLPHSE 250
    ASAAPLNDEI DLNDPTATIV IHPGSNSIKI GFPKDDHPVV VPNCVAVPKK 300
    WLDLENSEHV ENVCLQREQS EEFNNIKSEM EKNFRERMRY YKRKVPGNAH 350
    EQVVSFNENS KPEIISEKND PSPIEWIFDD SKLYYGSDAL RCVDEKFVIR 400
    KPFRGGSFNV KSPYYKSLAE LISDVTKLLE HALNSETLNV KPTKFNQYKV 450
    VLVIPDIFKK SHVETFIRVL LTELQFQAVA IIQESLATCY GAGISTSTCV 500
    VNIGAAETRI ACVDEGTVLE HSAITLDYGG DDITRLFALF LLQSDFPLQD 550
    WKIDSKHGWL LAERLKKNFT TFQDADVAVQ LYNFMNRSPN QPTEKYEFKL 600
    FDEVMLAPLA LFFPQIFKLI RTSSHKNSSL EFQLPESRDL FTNELNDWNS 650
    LSQFESKEGN LYCDLNDDLK ILNRILDAHN IIDQLQDKPE NYGNTLKENF 700
    APLEKAIVQS IANASITADV TRMNSFYSNI LIVGGSSKIP ALDFILTDRI 750
    NIWRPSLLSS ASFPQFYKKL TKEIKDLEGH YVNAPDKTED ENKQILQAQI 800
    KEKIVEELEE QHQNIEHQNG NEHIFPVSII PPPRDMNPAL IIWKGASVLA 850
    QIKLVEELFI TNSDWDVHGS RILQYKCIFT Y 881
    Length:881
    Mass (Da):100,209
    Last modified:November 1, 1996 - v1
    Checksum:i8174851B6B077A19
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94335 Genomic DNA. Translation: CAA64058.1.
    Z75049 Genomic DNA. Translation: CAA99341.1.
    BK006948 Genomic DNA. Translation: DAA10913.1.
    PIRiS67026.
    RefSeqiNP_014784.1. NM_001183560.1.

    Genome annotation databases

    EnsemblFungiiYOR141C; YOR141C; YOR141C.
    GeneIDi854309.
    KEGGisce:YOR141C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94335 Genomic DNA. Translation: CAA64058.1 .
    Z75049 Genomic DNA. Translation: CAA99341.1 .
    BK006948 Genomic DNA. Translation: DAA10913.1 .
    PIRi S67026.
    RefSeqi NP_014784.1. NM_001183560.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4AM6 X-ray 2.70 A/B 248-881 [» ]
    4AM7 X-ray 3.25 A/B 248-881 [» ]
    ProteinModelPortali Q12386.
    SMRi Q12386. Positions 259-881.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34535. 468 interactions.
    DIPi DIP-6706N.
    IntActi Q12386. 30 interactions.
    MINTi MINT-659970.
    STRINGi 4932.YOR141C.

    Proteomic databases

    MaxQBi Q12386.
    PaxDbi Q12386.
    PeptideAtlasi Q12386.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR141C ; YOR141C ; YOR141C .
    GeneIDi 854309.
    KEGGi sce:YOR141C.

    Organism-specific databases

    CYGDi YOR141c.
    SGDi S000005667. ARP8.

    Phylogenomic databases

    eggNOGi COG5277.
    GeneTreei ENSGT00390000001763.
    HOGENOMi HOG000246531.
    KOi K11673.
    OMAi TFQDADI.
    OrthoDBi EOG71RXT9.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33662-MONOMER.

    Miscellaneous databases

    NextBioi 976325.
    PROi Q12386.

    Gene expression databases

    Genevestigatori Q12386.

    Family and domain databases

    InterProi IPR004000. Actin-related.
    IPR027668. Arp8/plant_Arp9.
    [Graphical view ]
    PANTHERi PTHR11937. PTHR11937. 1 hit.
    PTHR11937:SF13. PTHR11937:SF13. 1 hit.
    Pfami PF00022. Actin. 1 hit.
    [Graphical view ]
    SMARTi SM00268. ACTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiARP8_YEAST
    AccessioniPrimary (citable) accession number: Q12386
    Secondary accession number(s): D6W2J7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 124 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 1010 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, 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 XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3