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Protein

Elongator complex protein 2

Gene

ELP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • microtubule binding Source: SGD

GO - Biological processi

  • protein transport Source: UniProtKB-KW
  • protein urmylation Source: SGD
  • regulation of transcription from RNA polymerase II promoter Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
  • tRNA wobble uridine modification Source: SGD
Complete GO annotation...

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
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR200C.
SGDiS000003432. ELP2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • Elongator holoenzyme complex Source: SGD
  • nucleoplasm Source: Reactome
  • nucleus Source: SGD
Complete GO annotation...

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.
PeptideAtlasiP42935.

PTM databases

iPTMnetiP42935.

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

GO - Molecular functioni

  • microtubule binding Source: SGD

Protein-protein interaction databases

BioGridi33453. 288 interactions.
DIPiDIP-2386N.
IntActiP42935. 16 interactions.
MINTiMINT-613845.

Structurei

Secondary structure

1
788
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128Combined sources
Beta strandi21 – 233Combined sources
Turni25 – 273Combined sources
Beta strandi30 – 345Combined sources
Beta strandi37 – 415Combined sources
Beta strandi51 – 566Combined sources
Beta strandi62 – 676Combined sources
Beta strandi71 – 8111Combined sources
Beta strandi83 – 9210Combined sources
Beta strandi94 – 1007Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi116 – 1205Combined sources
Beta strandi124 – 1318Combined sources
Beta strandi133 – 14513Combined sources
Beta strandi153 – 1608Combined sources
Beta strandi162 – 18322Combined sources
Beta strandi190 – 1989Combined sources
Beta strandi205 – 2128Combined sources
Beta strandi214 – 2174Combined sources
Beta strandi219 – 22810Combined sources
Beta strandi230 – 2367Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi269 – 2768Combined sources
Beta strandi284 – 2896Combined sources
Beta strandi291 – 2944Combined sources
Beta strandi296 – 30914Combined sources
Beta strandi318 – 3247Combined sources
Beta strandi343 – 3486Combined sources
Beta strandi353 – 3586Combined sources
Beta strandi384 – 3863Combined sources
Beta strandi388 – 3936Combined sources
Beta strandi400 – 4045Combined sources
Beta strandi409 – 4157Combined sources
Beta strandi428 – 4369Combined sources
Beta strandi442 – 4498Combined sources
Beta strandi452 – 46615Combined sources
Helixi469 – 47810Combined sources
Helixi540 – 5434Combined sources
Beta strandi550 – 5545Combined sources
Beta strandi561 – 5666Combined sources
Beta strandi570 – 5778Combined sources
Turni582 – 5843Combined sources
Beta strandi587 – 5915Combined sources
Turni592 – 5943Combined sources
Beta strandi611 – 6144Combined sources
Beta strandi618 – 6247Combined sources
Beta strandi626 – 6283Combined sources
Beta strandi630 – 6356Combined sources
Turni637 – 6393Combined sources
Beta strandi642 – 6498Combined sources
Beta strandi656 – 6616Combined sources
Turni664 – 6663Combined sources
Beta strandi668 – 6747Combined sources
Beta strandi677 – 6859Combined sources
Beta strandi687 – 69913Combined sources
Beta strandi704 – 7096Combined sources
Beta strandi714 – 72613Combined sources
Beta strandi729 – 7357Combined sources
Beta strandi738 – 7447Combined sources
Turni747 – 7493Combined sources
Beta strandi755 – 76410Combined sources
Beta strandi769 – 7757Combined sources
Beta strandi778 – 7858Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XFVX-ray3.20A1-788[»]
ProteinModelPortaliP42935.
SMRiP42935. Positions 3-786.
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

GeneTreeiENSGT00390000000916.
HOGENOMiHOG000200623.
InParanoidiP42935.
KOiK11374.
OMAiEIDHPPF.
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. 5 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

        10         20         30         40         50
MVECITPEAI FIGANKQTQV SDIHKVKKIV AFGAGKTIAL WDPIEPNNKG
60 70 80 90 100
VYATLKGHEA EVTCVRFVPD SDFMVSASED HHVKIWKFTD YSHLQCIQTI
110 120 130 140 150
QHYSKTIVAL SALPSLISVG CADGTISIWR QNIQNDEFGL AHEFTIKKGF
160 170 180 190 200
FYPLCLSLSK VEEKKYLLAI GGTNVNVFIA SFILSDSGIE KCRVVAELEG
210 220 230 240 250
HEDWVKSLAF RHQETPGDYL LCSGSQDRYI RLWRIRINDL IDDSEEDSKK
260 270 280 290 300
LTLLSNKQYK FQIDDELRVG INFEALIMGH DDWISSLQWH ESRLQLLAAT
310 320 330 340 350
ADTSLMVWEP DETSGIWVCS LRLGEMSSKG ASTATGSSGG FWSCLWFTHE
360 370 380 390 400
RMDFFLTNGK TGSWRMWATK DNIICDQRLG ISGATKDVTD IAWSPSGEYL
410 420 430 440 450
LATSLDQTTR LFAPWIYDAS GRKREIATWH EFSRPQIHGY DMICVETVTD
460 470 480 490 500
TRFVSGGDEK ILRSFDLPKG VAGMLQKFVG IQFEEKSEMP DSATVPVLGL
510 520 530 540 550
SNKAGEDDAN EDDEEEEGGN KETPDITDPL SLLECPPMED QLQRHLLWPE
560 570 580 590 600
VEKLYGHGFE ITCLDISPDQ KLIASACRSN NVQNAVIRIF STENWLEIKP
610 620 630 640 650
ALPFHSLTIT RLKFSKDGKF LLSVCRDRKW ALWERNMEDN TFELRFKNEK
660 670 680 690 700
PHTRIIWDAD WAPLEFGNVF VTASRDKTVK VWRHQKEPAD DYVLEASIKH
710 720 730 740 750
TKAVTAISIH DSMIREKILI SVGLENGEIY LYSYTLGKFE LITQLNEDIT
760 770 780
PADKITRLRW SHLKRNGKLF LGVGSSDLST RIYSLAYE
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XFVX-ray3.20A1-788[»]
ProteinModelPortaliP42935.
SMRiP42935. Positions 3-786.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33453. 288 interactions.
DIPiDIP-2386N.
IntActiP42935. 16 interactions.
MINTiMINT-613845.

PTM databases

iPTMnetiP42935.

Proteomic databases

MaxQBiP42935.
PeptideAtlasiP42935.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YGR200C.
SGDiS000003432. ELP2.

Phylogenomic databases

GeneTreeiENSGT00390000000916.
HOGENOMiHOG000200623.
InParanoidiP42935.
KOiK11374.
OMAiEIDHPPF.
OrthoDBiEOG7TQV9M.

Enzyme and pathway databases

BioCyciYEAST:G3O-30885-MONOMER.

Miscellaneous databases

PROiP42935.

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. 5 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 8, 2016
This is version 144 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

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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.