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Q02908

- ELP3_YEAST

UniProt

Q02908 - ELP3_YEAST

Protein

Elongator complex protein 3

Gene

ELP3

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 113 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Acts as catalytic subunit of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (Pol II) 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. ELP3 is required for the complex integrity and for the association of the complex with nascent RNA transcript. Independently, ELP3 may be involved in polarized exocytosis. 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.9 Publications

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].

    Cofactori

    Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi108 – 1081Iron-sulfur (4Fe-4S-S-AdoMet)Curated
    Metal bindingi118 – 1181Iron-sulfur (4Fe-4S-S-AdoMet)Curated
    Metal bindingi121 – 1211Iron-sulfur (4Fe-4S-S-AdoMet)Curated

    GO - Molecular functioni

    1. histone acetyltransferase activity Source: SGD
    2. iron-sulfur cluster binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. histone acetylation Source: GOC
    2. protein transport Source: UniProtKB-KW
    3. regulation of transcription from RNA polymerase II promoter Source: SGD
    4. transcription, DNA-templated Source: UniProtKB-KW
    5. tRNA wobble uridine modification Source: SGD

    Keywords - Molecular functioni

    Acyltransferase, Chromatin regulator, Transferase

    Keywords - Biological processi

    Protein transport, Transcription, Transcription regulation, Transport

    Keywords - Ligandi

    Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33992-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongator complex protein 3 (EC:2.3.1.48)
    Alternative name(s):
    Gamma-toxin target 3
    Gene namesi
    Name:ELP3
    Synonyms:HPA1, TOT3
    Ordered Locus Names:YPL086C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    CYGDiYPL086c.
    SGDiS000006007. ELP3.

    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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi108 – 1081C → S: Eliminates iron contents; when associated with S-118 and S-121. 1 Publication
    Mutagenesisi118 – 1181C → S: Eliminates iron contents; when associated with S-108 and S-121. 1 Publication
    Mutagenesisi121 – 1211C → S: Eliminates iron contents; when associated with S-108 and S-118. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 557557Elongator complex protein 3PRO_0000235811Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki453 – 453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ02908.
    PaxDbiQ02908.
    PeptideAtlasiQ02908.

    Expressioni

    Gene expression databases

    GenevestigatoriQ02908.

    Interactioni

    Subunit structurei

    Component of the RNA polymerase II elongator complex, which consists of IKI3, ELP2, ELP3, ELP4, IKI1 and ELP6. IKI3, ELP2, and ELP3 form the Elongator core complex. ELP3 interacts with KTI12.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IKI1P388746EBI-33957,EBI-9061

    Protein-protein interaction databases

    BioGridi36095. 306 interactions.
    DIPiDIP-2385N.
    IntActiQ02908. 16 interactions.
    MINTiMINT-645857.
    STRINGi4932.YPL086C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ02908.
    SMRiQ02908. Positions 501-550.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini405 – 557153N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ELP3 family.Curated
    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1243.
    GeneTreeiENSGT00390000013141.
    HOGENOMiHOG000227514.
    KOiK07739.
    OMAiGYKVVSH.
    OrthoDBiEOG7Z95VX.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    3.80.30.20. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR006638. Elp3/MiaB/NifB.
    IPR000182. GNAT_dom.
    IPR005910. Hist_AcTrfase_ELP3.
    IPR007197. rSAM.
    IPR023404. rSAM_horseshoe.
    [Graphical view]
    PfamiPF00583. Acetyltransf_1. 1 hit.
    PF04055. Radical_SAM. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
    SMARTiSM00729. Elp3. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    TIGRFAMsiTIGR01211. ELP3. 1 hit.
    PROSITEiPS51186. GNAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q02908-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARHGKGPKT NKKKLAPEKE RFIQCCADIT LELTDSLTSG TTREINLNGL    50
    ITKYSKKYKL KQQPRLTDII NSIPDQYKKY LLPKLKAKPV RTASGIAVVA 100
    VMCKPHRCPH IAYTGNICVY CPGGPDSDFE YSTQSYTGYE PTSMRAIRAR 150
    YDPYEQARGR VEQLKQLGHS IDKVEYVLMG GTFMSLPKEY REDFIVKLHN 200
    ALSGFNGNDI DEAILYSQQS LTKCVGITIE TRPDYCTQTH LDDMLKYGCT 250
    RLEIGVQSLY EDVARDTNRG HTVRSVCETF AVSKDAGYKV VSHMMPDLPN 300
    VGMERDIEQF KEYFENPDFR TDGLKIYPTL VIRGTGLYEL WKTGRYKSYS 350
    ANALVDLVAR ILALVPPWTR IYRVQRDIPM PLVTSGVDNG NLRELALARM 400
    KDLGTTCRDV RTREVGIQEV HHKVQPDQVE LIRRDYYANG GWETFLSYED 450
    PKKDILIGLL RLRKASKKYT YRKEFTSQRT SIVRELHVYG SVVPLHSRDP 500
    RKFQHQGFGT LLMEEAERIA KEEHGSEKIS VISGVGVRNY YGKLGYELDG 550
    PYMSKRI 557
    Length:557
    Mass (Da):63,657
    Last modified:November 1, 1996 - v1
    Checksum:i64EF8B42D3C3102E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U43281 Genomic DNA. Translation: AAB68213.1.
    BK006949 Genomic DNA. Translation: DAA11347.1.
    PIRiS61980.
    RefSeqiNP_015239.1. NM_001183900.1.

    Genome annotation databases

    EnsemblFungiiYPL086C; YPL086C; YPL086C.
    GeneIDi856019.
    KEGGisce:YPL086C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U43281 Genomic DNA. Translation: AAB68213.1 .
    BK006949 Genomic DNA. Translation: DAA11347.1 .
    PIRi S61980.
    RefSeqi NP_015239.1. NM_001183900.1.

    3D structure databases

    ProteinModelPortali Q02908.
    SMRi Q02908. Positions 501-550.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36095. 306 interactions.
    DIPi DIP-2385N.
    IntActi Q02908. 16 interactions.
    MINTi MINT-645857.
    STRINGi 4932.YPL086C.

    Proteomic databases

    MaxQBi Q02908.
    PaxDbi Q02908.
    PeptideAtlasi Q02908.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPL086C ; YPL086C ; YPL086C .
    GeneIDi 856019.
    KEGGi sce:YPL086C.

    Organism-specific databases

    CYGDi YPL086c.
    SGDi S000006007. ELP3.

    Phylogenomic databases

    eggNOGi COG1243.
    GeneTreei ENSGT00390000013141.
    HOGENOMi HOG000227514.
    KOi K07739.
    OMAi GYKVVSH.
    OrthoDBi EOG7Z95VX.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33992-MONOMER.

    Miscellaneous databases

    NextBioi 980923.
    PROi Q02908.

    Gene expression databases

    Genevestigatori Q02908.

    Family and domain databases

    Gene3Di 3.40.630.30. 1 hit.
    3.80.30.20. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR006638. Elp3/MiaB/NifB.
    IPR000182. GNAT_dom.
    IPR005910. Hist_AcTrfase_ELP3.
    IPR007197. rSAM.
    IPR023404. rSAM_horseshoe.
    [Graphical view ]
    Pfami PF00583. Acetyltransf_1. 1 hit.
    PF04055. Radical_SAM. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
    SMARTi SM00729. Elp3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55729. SSF55729. 1 hit.
    TIGRFAMsi TIGR01211. ELP3. 1 hit.
    PROSITEi PS51186. GNAT. 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. "A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme."
      Wittschieben B.O., Otero G., de Bizemont T., Fellows J., Erdjument-Bromage H., Ohba R., Li Y., Allis C.D., Tempst P., Svejstrup J.Q.
      Mol. Cell 4:123-128(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR COMPLEX.
    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. "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: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-453.
      Strain: SUB592.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    13. "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.
    14. "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.
    15. "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: FUNCTION IN EXOCYTOSIS REGULATION, SUBCELLULAR LOCATION.
    16. "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.
    17. "The Elongator subunit Elp3 contains a Fe4S4 cluster and binds S-adenosylmethionine."
      Paraskevopoulou C., Fairhurst S.A., Lowe D.J., Brick P., Onesti S.
      Mol. Microbiol. 59:795-806(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: S-ADENOSYLMETHIONINE-BINDING, MUTAGENESIS OF CYS-108; CYS-118 AND CYS-121.

    Entry informationi

    Entry nameiELP3_YEAST
    AccessioniPrimary (citable) accession number: Q02908
    Secondary accession number(s): D6W3T1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2006
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 113 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 4760 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

    External Data

    Dasty 3