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P42935

- ELP2_YEAST

UniProt

P42935 - ELP2_YEAST

Protein

Elongator complex protein 2

Gene

ELP2

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 130 (01 Oct 2014)
      Sequence version 1 (01 Nov 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. ELP2 is dispensable for the complex integrity and, in vitro, is not required for complex HAT activity. It is not required for the association of the complex with nascent RNA transcript. Independently, ELP2 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.8 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. protein transport Source: UniProtKB-KW
    2. protein urmylation Source: SGD
    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 - Biological processi

    Protein transport, Transcription, Transcription regulation, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30885-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongator complex protein 2
    Alternative name(s):
    Gamma-toxin target 2
    Gene namesi
    Name:ELP2
    Synonyms:TOT2
    Ordered Locus Names:YGR200C
    ORF Names:G7725
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR200c.
    SGDiS000003432. ELP2.

    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 – 788788Elongator complex protein 2PRO_0000051474Add
    BLAST

    Proteomic databases

    MaxQBiP42935.
    PaxDbiP42935.
    PeptideAtlasiP42935.

    Expressioni

    Gene expression databases

    GenevestigatoriP42935.

    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. In the complex, ELP2 interacts with IKI3.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ELP4Q028847EBI-23459,EBI-35277
    IKI1P388746EBI-23459,EBI-9061

    Protein-protein interaction databases

    BioGridi33453. 287 interactions.
    DIPiDIP-2386N.
    IntActiP42935. 15 interactions.
    MINTiMINT-613845.
    STRINGi4932.YGR200C.

    Structurei

    3D structure databases

    ProteinModelPortaliP42935.
    SMRiP42935. Positions 27-311, 386-414, 647-737.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati57 – 8731WD 1Add
    BLAST
    Repeati101 – 13030WD 2Add
    BLAST
    Repeati141 – 18141WD 3Add
    BLAST
    Repeati200 – 23435WD 4Add
    BLAST
    Repeati279 – 30931WD 5Add
    BLAST
    Repeati383 – 41331WD 6Add
    BLAST
    Repeati438 – 46629WD 7Add
    BLAST
    Repeati604 – 63431WD 8Add
    BLAST
    Repeati651 – 68333WD 9Add
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat ELP2 family.Curated
    Contains 9 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    GeneTreeiENSGT00390000000916.
    HOGENOMiHOG000200623.
    KOiK11374.
    OMAiDQVPEIN.
    OrthoDBiEOG7TQV9M.

    Family and domain databases

    Gene3Di2.130.10.10. 3 hits.
    InterProiIPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF00400. WD40. 8 hits.
    [Graphical view]
    SMARTiSM00320. WD40. 11 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 4 hits.
    PROSITEiPS50082. WD_REPEATS_2. 6 hits.
    PS50294. WD_REPEATS_REGION. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P42935-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVECITPEAI FIGANKQTQV SDIHKVKKIV AFGAGKTIAL WDPIEPNNKG    50
    VYATLKGHEA EVTCVRFVPD SDFMVSASED HHVKIWKFTD YSHLQCIQTI 100
    QHYSKTIVAL SALPSLISVG CADGTISIWR QNIQNDEFGL AHEFTIKKGF 150
    FYPLCLSLSK VEEKKYLLAI GGTNVNVFIA SFILSDSGIE KCRVVAELEG 200
    HEDWVKSLAF RHQETPGDYL LCSGSQDRYI RLWRIRINDL IDDSEEDSKK 250
    LTLLSNKQYK FQIDDELRVG INFEALIMGH DDWISSLQWH ESRLQLLAAT 300
    ADTSLMVWEP DETSGIWVCS LRLGEMSSKG ASTATGSSGG FWSCLWFTHE 350
    RMDFFLTNGK TGSWRMWATK DNIICDQRLG ISGATKDVTD IAWSPSGEYL 400
    LATSLDQTTR LFAPWIYDAS GRKREIATWH EFSRPQIHGY DMICVETVTD 450
    TRFVSGGDEK ILRSFDLPKG VAGMLQKFVG IQFEEKSEMP DSATVPVLGL 500
    SNKAGEDDAN EDDEEEEGGN KETPDITDPL SLLECPPMED QLQRHLLWPE 550
    VEKLYGHGFE ITCLDISPDQ KLIASACRSN NVQNAVIRIF STENWLEIKP 600
    ALPFHSLTIT RLKFSKDGKF LLSVCRDRKW ALWERNMEDN TFELRFKNEK 650
    PHTRIIWDAD WAPLEFGNVF VTASRDKTVK VWRHQKEPAD DYVLEASIKH 700
    TKAVTAISIH DSMIREKILI SVGLENGEIY LYSYTLGKFE LITQLNEDIT 750
    PADKITRLRW SHLKRNGKLF LGVGSSDLST RIYSLAYE 788
    Length:788
    Mass (Da):89,411
    Last modified:November 1, 1995 - v1
    Checksum:i5371908FE2E6EC0D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti579 – 5791S → P in AAS56426. (PubMed:17322287)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49133 Genomic DNA. Translation: CAA88993.1.
    Z72985 Genomic DNA. Translation: CAA97227.1.
    AY558100 Genomic DNA. Translation: AAS56426.1.
    BK006941 Genomic DNA. Translation: DAA08293.1.
    PIRiS53923.
    RefSeqiNP_011716.3. NM_001181329.3.

    Genome annotation databases

    EnsemblFungiiYGR200C; YGR200C; YGR200C.
    GeneIDi853114.
    KEGGisce:YGR200C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49133 Genomic DNA. Translation: CAA88993.1 .
    Z72985 Genomic DNA. Translation: CAA97227.1 .
    AY558100 Genomic DNA. Translation: AAS56426.1 .
    BK006941 Genomic DNA. Translation: DAA08293.1 .
    PIRi S53923.
    RefSeqi NP_011716.3. NM_001181329.3.

    3D structure databases

    ProteinModelPortali P42935.
    SMRi P42935. Positions 27-311, 386-414, 647-737.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33453. 287 interactions.
    DIPi DIP-2386N.
    IntActi P42935. 15 interactions.
    MINTi MINT-613845.
    STRINGi 4932.YGR200C.

    Proteomic databases

    MaxQBi P42935.
    PaxDbi P42935.
    PeptideAtlasi P42935.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR200C ; YGR200C ; YGR200C .
    GeneIDi 853114.
    KEGGi sce:YGR200C.

    Organism-specific databases

    CYGDi YGR200c.
    SGDi S000003432. ELP2.

    Phylogenomic databases

    eggNOGi COG2319.
    GeneTreei ENSGT00390000000916.
    HOGENOMi HOG000200623.
    KOi K11374.
    OMAi DQVPEIN.
    OrthoDBi EOG7TQV9M.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30885-MONOMER.

    Miscellaneous databases

    NextBioi 973136.
    PROi P42935.

    Gene expression databases

    Genevestigatori P42935.

    Family and domain databases

    Gene3Di 2.130.10.10. 3 hits.
    InterProi IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00400. WD40. 8 hits.
    [Graphical view ]
    SMARTi SM00320. WD40. 11 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 4 hits.
    PROSITEi PS50082. WD_REPEATS_2. 6 hits.
    PS50294. WD_REPEATS_REGION. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the yeast PMT and EF1G genes, of the human and bacterial electron-transferring flavoproteins (beta-chain) and of the Escherichia coli phosphoserine phosphohydrolase, and five new ORFs."
      Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A., Rodrigues-Pousada C.
      Yeast 12:273-280(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "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.
    6. "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.
    7. "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.
    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. "Protein interactions within Saccharomyces cerevisiae Elongator, a complex essential for Kluyveromyces lactis zymocicity."
      Fichtner L., Frohloff F., Jablonowski D., Stark M.J.R., Schaffrath R.
      Mol. Microbiol. 45:817-826(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IKI3.
    10. "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.
    11. "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.
    12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    14. "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.
    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.

    Entry informationi

    Entry nameiELP2_YEAST
    AccessioniPrimary (citable) accession number: P42935
    Secondary accession number(s): D6VUY2, E9P8V1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 130 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 6090 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 VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3