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P38874

- ELP5_YEAST

UniProt

P38874 - ELP5_YEAST

Protein

Elongator complex protein 5

Gene

IKI1

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 116 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Acts as component of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (RNAPII) holoenzyme and is involved in transcriptional elongation. Association with elongating RNAPII requires a hyperphosphorylated state of the RNAPII C-terminal domain (CTD). Elongator binds to both naked and nucleosomal DNA, can acetylate both core and nucleosomal histones, and is involved in chromatin remodeling. It acetylates histones H3, preferentially at 'Lys-14', and H4, preferentially at 'Lys-8'. It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin). May also be involved in sensitiviy to Pichia inositovora toxin. May be involved in tRNA modification. IKI1 is required for an early step in synthesis of 5-methoxycarbonylmethyl (mcm5) and 5-carbamoylmethyl (ncm5) groups present on uridines at the wobble position in tRNA.6 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. regulation of transcription, DNA-templated Source: UniProtKB-KW
    3. transcription, DNA-templated Source: UniProtKB-KW
    4. tRNA modification Source: SGD

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31217-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongator complex protein 5
    Alternative name(s):
    Gamma-toxin target 5
    HAT-associated protein 2
    Protein IKI1
    Gene namesi
    Name:IKI1
    Synonyms:ELP5, HAP2, TOT5
    Ordered Locus Names:YHR187W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VIII

    Organism-specific databases

    CYGDiYHR187w.
    SGDiS000001230. IKI1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. Elongator holoenzyme complex Source: SGD
    3. nucleoplasm Source: Reactome
    4. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 309309Elongator complex protein 5PRO_0000084178Add
    BLAST

    Proteomic databases

    MaxQBiP38874.
    PaxDbiP38874.

    Expressioni

    Gene expression databases

    GenevestigatoriP38874.

    Interactioni

    Subunit structurei

    Component of the RNA polymerase II elongator complex, which consists of IKI3, ELP2, ELP3, ELP4, IKI1 and ELP6. ELP4, IKI1 and ELP6 form a distinct subcomplex (HAP).3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ELP2P429356EBI-9061,EBI-23459
    ELP3Q029086EBI-9061,EBI-33957
    ELP4Q0288410EBI-9061,EBI-35277
    ELP6Q048686EBI-9061,EBI-27653
    IKI3Q067068EBI-9061,EBI-9068

    Protein-protein interaction databases

    BioGridi36621. 118 interactions.
    DIPiDIP-1967N.
    IntActiP38874. 9 interactions.
    MINTiMINT-385467.
    STRINGi4932.YHR187W.

    Structurei

    Secondary structure

    1
    309
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 169
    Beta strandi23 – 308
    Helixi36 – 4813
    Beta strandi55 – 617
    Beta strandi70 – 745
    Helixi80 – 8910
    Beta strandi102 – 1076
    Helixi109 – 1113
    Helixi114 – 1163
    Helixi117 – 1248
    Beta strandi129 – 1368
    Turni151 – 1533
    Helixi157 – 1648
    Beta strandi166 – 1738
    Helixi181 – 1899
    Beta strandi200 – 20910
    Beta strandi215 – 2239
    Turni224 – 2274
    Beta strandi228 – 2314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4A8JX-ray2.10B/E1-270[»]
    4EJSX-ray2.61B1-238[»]
    ProteinModelPortaliP38874.
    SMRiP38874. Positions 7-234.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ELP5 family.Curated

    Phylogenomic databases

    eggNOGiNOG72129.
    HOGENOMiHOG000248152.
    KOiK11376.
    OMAiTNIIYLS.
    OrthoDBiEOG7XWQ03.

    Family and domain databases

    InterProiIPR019519. Elp5.
    [Graphical view]
    PfamiPF10483. Elong_Iki1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38874-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASSSHNPVI LLKRILSLTE SSPFILCLDS IAQTSYKLIQ EFVHQSKSKG    50
    NEYPIVYISF ETVNKPSYCT QFIDATQMDF VHLVKQIISY LPAATATQAK 100
    KHMVIIDSLN YISTEYITRF LSEIASPHCT MVATYHKDIK DENRTVIPDW 150
    NNNYPDKLTL LQFMATTIVD IDVVLTGTLD TEEVSELLNE FRIPRGLNND 200
    IFQLRLVNKR KSGRSLEYDF IVNSNTHEYE LLSTTKQEEE SSSNGLETPE 250
    MLQGLTTFNL GTSNKQKLAK DQVALPFLEA QSFGQGGAIV YEYEKDDDYD 300
    EEDPYEDPF 309
    Length:309
    Mass (Da):35,220
    Last modified:February 1, 1995 - v1
    Checksum:iDFD93D7BA583E2F5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D83267 Genomic DNA. Translation: BAA20087.1.
    U00030 Genomic DNA. Translation: AAB68362.1.
    BK006934 Genomic DNA. Translation: DAA06879.1.
    PIRiS46684.
    RefSeqiNP_012057.3. NM_001179318.3.

    Genome annotation databases

    EnsemblFungiiYHR187W; YHR187W; YHR187W.
    GeneIDi856594.
    KEGGisce:YHR187W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D83267 Genomic DNA. Translation: BAA20087.1 .
    U00030 Genomic DNA. Translation: AAB68362.1 .
    BK006934 Genomic DNA. Translation: DAA06879.1 .
    PIRi S46684.
    RefSeqi NP_012057.3. NM_001179318.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4A8J X-ray 2.10 B/E 1-270 [» ]
    4EJS X-ray 2.61 B 1-238 [» ]
    ProteinModelPortali P38874.
    SMRi P38874. Positions 7-234.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36621. 118 interactions.
    DIPi DIP-1967N.
    IntActi P38874. 9 interactions.
    MINTi MINT-385467.
    STRINGi 4932.YHR187W.

    Proteomic databases

    MaxQBi P38874.
    PaxDbi P38874.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YHR187W ; YHR187W ; YHR187W .
    GeneIDi 856594.
    KEGGi sce:YHR187W.

    Organism-specific databases

    CYGDi YHR187w.
    SGDi S000001230. IKI1.

    Phylogenomic databases

    eggNOGi NOG72129.
    HOGENOMi HOG000248152.
    KOi K11376.
    OMAi TNIIYLS.
    OrthoDBi EOG7XWQ03.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31217-MONOMER.

    Miscellaneous databases

    NextBioi 982478.
    PROi P38874.

    Gene expression databases

    Genevestigatori P38874.

    Family and domain databases

    InterProi IPR019519. Elp5.
    [Graphical view ]
    Pfami PF10483. Elong_Iki1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of IKI1 and IKI3 genes conferring pGKL killer sensitivity on Saccharomyces cerevisiae."
      Yajima H., Tokunaga M., Nakayama-Murayama A., Hishinuma F.
      Biosci. Biotechnol. Biochem. 61:704-709(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation."
      Otero G., Fellows J., Li Y., de Bizemont T., Dirac A.M., Gustafsson C.M., Erdjument-Bromage H., Tempst P., Svejstrup J.Q.
      Mol. Cell 3:109-118(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX IN TRANSCRIPTIONAL REGULATION, SUBCELLULAR LOCATION.
    5. "Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin."
      Frohloff F., Fichtner L., Jablonowski D., Breunig K.D., Schaffrath R.
      EMBO J. 20:1993-2003(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX IN ZYMOCIN SENSITIVITY.
    6. "RNA polymerase II elongator holoenzyme is composed of two discrete subcomplexes."
      Winkler G.S., Petrakis T.G., Ethelberg S., Tokunaga M., Erdjument-Bromage H., Tempst P., Svejstrup J.Q.
      J. Biol. Chem. 276:32743-32749(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR COMPLEX.
    7. "A multiprotein complex that interacts with RNA polymerase II elongator."
      Li Y., Takagi Y., Jiang Y., Tokunaga M., Erdjument-Bromage H., Tempst P., Kornberg R.D.
      J. Biol. Chem. 276:29628-29631(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "Characterization of a six-subunit holo-elongator complex required for the regulated expression of a group of genes in Saccharomyces cerevisiae."
      Krogan N.J., Greenblatt J.F.
      Mol. Cell. Biol. 21:8203-8212(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR COMPLEX, FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX IN TRANSCRIPTIONAL REGULATION.
    9. "Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo."
      Winkler G.S., Kristjuhan A., Erdjument-Bromage H., Tempst P., Svejstrup J.Q.
      Proc. Natl. Acad. Sci. U.S.A. 99:3517-3522(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX IN HISTONE ACETYLATION.
    10. "Structural and functional analysis of the killer element pPin1-3 from Pichia inositovora."
      Klassen R., Meinhardt F.
      Mol. Genet. Genomics 270:190-199(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX IN PICHIA INOSITOVORA TOXIN SENSITIVITY.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    13. "Elp1p, the yeast homolog of the FD disease syndrome protein, negatively regulates exocytosis independently of transcriptional elongation."
      Rahl P.B., Chen C.Z., Collins R.N.
      Mol. Cell 17:841-853(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "An early step in wobble uridine tRNA modification requires the Elongator complex."
      Huang B., Johansson M.J.O., Bystroem A.S.
      RNA 11:424-436(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRNA MODIFICATION.

    Entry informationi

    Entry nameiELP5_YEAST
    AccessioniPrimary (citable) accession number: P38874
    Secondary accession number(s): D3DLD5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 116 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 3870 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 VIII
      Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

    External Data

    Dasty 3