Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q02884

- ELP4_YEAST

UniProt

Q02884 - ELP4_YEAST

Protein

Elongator complex protein 4

Gene

ELP4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. ELP4 is required for the complex integrity and the complex HAT activity but is not required for the association of the complex with nascent RNA transcript. 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.7 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. regulation of transcription from RNA polymerase II promoter Source: SGD
    3. transcription, DNA-templated Source: UniProtKB-KW
    4. tRNA wobble uridine modification Source: SGD

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-34004-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongator complex protein 4
    Alternative name(s):
    Gamma-toxin target 7
    HAT-associated protein 1
    Gene namesi
    Name:ELP4
    Synonyms:HAP1, TOT7
    Ordered Locus Names:YPL101W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    CYGDiYPL101w.
    SGDiS000006022. ELP4.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. Elongator holoenzyme complex Source: SGD
    3. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 456456Elongator complex protein 4PRO_0000235812Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei222 – 2221Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ02884.
    PaxDbiQ02884.

    Expressioni

    Gene expression databases

    GenevestigatoriQ02884.

    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). ELP4 interacts with KTI12.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ELP2P429357EBI-35277,EBI-23459
    ELP6Q0486810EBI-35277,EBI-27653
    IKI1P3887410EBI-35277,EBI-9061
    IKI3Q067069EBI-35277,EBI-9068

    Protein-protein interaction databases

    BioGridi36079. 218 interactions.
    DIPiDIP-6718N.
    IntActiQ02884. 6 interactions.
    MINTiMINT-672307.
    STRINGi4932.YPL101W.

    Structurei

    Secondary structure

    1
    456
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi75 – 773
    Turni79 – 813
    Beta strandi84 – 863
    Helixi91 – 966
    Beta strandi99 – 1035
    Beta strandi107 – 1126
    Helixi119 – 13517
    Beta strandi149 – 1546
    Helixi158 – 1636
    Beta strandi165 – 1673
    Beta strandi241 – 2466
    Turni253 – 2553
    Beta strandi256 – 2594
    Beta strandi261 – 2633
    Helixi265 – 27814
    Turni279 – 2813
    Beta strandi282 – 2887
    Turni289 – 2924
    Turni294 – 2963
    Helixi299 – 3024
    Helixi304 – 32017
    Turni321 – 3244
    Beta strandi325 – 3328
    Helixi333 – 3353
    Helixi338 – 34710
    Beta strandi349 – 3568
    Helixi359 – 36810
    Turni369 – 3713
    Helixi373 – 3753
    Beta strandi379 – 3857
    Helixi389 – 3924
    Beta strandi398 – 4069
    Beta strandi411 – 4155

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4A8JX-ray2.10A/D66-426[»]
    4EJSX-ray2.61A67-438[»]
    ProteinModelPortaliQ02884.
    SMRiQ02884. Positions 67-168, 234-419.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ELP4 family.Curated

    Phylogenomic databases

    eggNOGiNOG250551.
    HOGENOMiHOG000175573.
    KOiK11375.
    OMAiWRYGLNK.
    OrthoDBiEOG7WDNCM.

    Family and domain databases

    InterProiIPR008728. Elongator_complex_protein_4.
    [Graphical view]
    PfamiPF05625. PAXNEB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q02884-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFRKRGEIL NDRGSGLRGP LLRGPPRTSS TPLRTGNRRA PGNVPLSDTT    50
    ARLKKLNIAD ESKTKMGLDS SHVGVRPSPA TSQPTTSTGS ADLDSILGHM 100
    GLPLGNSVLV EEQSTTEFHS ILGKLFAAQG IVHNRISDSS ADKTRNGDTH 150
    VIVLSLNQMF AKELPGIYKG SRKQMKKNLI SEEESKVTVQ NLNETQRSTP 200
    SRYKDLKIAW KYKLADEKRL GSPDRDDIQQ NSEYKDYNHQ FDITTRLMPA 250
    PIASELTFIA PTQPVSTILS QIEQTIKRND KKLIRIVIPS LLHPAMYPPK 300
    MFESSEIIGL MHGVRSLVKK YYERVVLFAS ISIDIITPPL LVLLRNMFDS 350
    VINLEPFNQE MTEFLERVYK SQPGKIQHGL VHILKLPVFT DRGEMRVLKS 400
    EWAFKNGRKK FEIEQWGIPV DDAEGSAASE QSHSHSHSDE ISHNIPAKKT 450
    KISLDY 456
    Length:456
    Mass (Da):51,156
    Last modified:November 1, 1996 - v1
    Checksum:i276F0D1538EAA8FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U43281 Genomic DNA. Translation: AAB68198.1.
    BK006949 Genomic DNA. Translation: DAA11331.1.
    PIRiS61965.
    RefSeqiNP_015224.1. NM_001183915.1.

    Genome annotation databases

    EnsemblFungiiYPL101W; YPL101W; YPL101W.
    GeneIDi856002.
    KEGGisce:YPL101W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U43281 Genomic DNA. Translation: AAB68198.1 .
    BK006949 Genomic DNA. Translation: DAA11331.1 .
    PIRi S61965.
    RefSeqi NP_015224.1. NM_001183915.1.

    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 A/D 66-426 [» ]
    4EJS X-ray 2.61 A 67-438 [» ]
    ProteinModelPortali Q02884.
    SMRi Q02884. Positions 67-168, 234-419.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36079. 218 interactions.
    DIPi DIP-6718N.
    IntActi Q02884. 6 interactions.
    MINTi MINT-672307.
    STRINGi 4932.YPL101W.

    Proteomic databases

    MaxQBi Q02884.
    PaxDbi Q02884.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPL101W ; YPL101W ; YPL101W .
    GeneIDi 856002.
    KEGGi sce:YPL101W.

    Organism-specific databases

    CYGDi YPL101w.
    SGDi S000006022. ELP4.

    Phylogenomic databases

    eggNOGi NOG250551.
    HOGENOMi HOG000175573.
    KOi K11375.
    OMAi WRYGLNK.
    OrthoDBi EOG7WDNCM.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-34004-MONOMER.

    Miscellaneous databases

    NextBioi 980875.
    PROi Q02884.

    Gene expression databases

    Genevestigatori Q02884.

    Family and domain databases

    InterProi IPR008728. Elongator_complex_protein_4.
    [Graphical view ]
    Pfami PF05625. PAXNEB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "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.
    4. "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.
    5. "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.
    6. "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.
    7. "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.
    8. "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.
    9. "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.
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. "Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-elongator."
      Petrakis T.G., Wittschieben B.O., Svejstrup J.Q.
      J. Biol. Chem. 279:32087-32092(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Physical and functional interaction between Elongator and the chromatin-associated Kti12 protein."
      Petrakis T.G., Soegaard T.M.M., Erdjument-Bromage H., Tempst P., Svejstrup J.Q.
      J. Biol. Chem. 280:19454-19460(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KTI12.
    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.
    15. "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-222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.

    Entry informationi

    Entry nameiELP4_YEAST
    AccessioniPrimary (citable) accession number: Q02884
    Secondary accession number(s): D6W3R5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2006
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 106 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 358 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 XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

    External Data

    Dasty 3