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P42935 (ELP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongator complex protein 2
Alternative name(s):
Gamma-toxin target 2
Gene names
Name:ELP2
Synonyms:TOT2
Ordered Locus Names:YGR200C
ORF Names:G7725
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length788 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.8 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16

Subunit structure

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. Ref.7 Ref.8 Ref.9

Subcellular location

Cytoplasm. Nucleus Ref.5 Ref.12 Ref.15.

Miscellaneous

Present with 6090 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the WD repeat ELP2 family.

Contains 9 WD repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ELP4Q028847EBI-23459,EBI-35277
IKI1P388746EBI-23459,EBI-9061

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 788788Elongator complex protein 2
PRO_0000051474

Regions

Repeat57 – 8731WD 1
Repeat101 – 13030WD 2
Repeat141 – 18141WD 3
Repeat200 – 23435WD 4
Repeat279 – 30931WD 5
Repeat383 – 41331WD 6
Repeat438 – 46629WD 7
Repeat604 – 63431WD 8
Repeat651 – 68333WD 9

Experimental info

Sequence conflict5791S → P in AAS56426. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P42935 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 5371908FE2E6EC0D

FASTA78889,411
        10         20         30         40         50         60 
MVECITPEAI FIGANKQTQV SDIHKVKKIV AFGAGKTIAL WDPIEPNNKG VYATLKGHEA 

        70         80         90        100        110        120 
EVTCVRFVPD SDFMVSASED HHVKIWKFTD YSHLQCIQTI QHYSKTIVAL SALPSLISVG 

       130        140        150        160        170        180 
CADGTISIWR QNIQNDEFGL AHEFTIKKGF FYPLCLSLSK VEEKKYLLAI GGTNVNVFIA 

       190        200        210        220        230        240 
SFILSDSGIE KCRVVAELEG HEDWVKSLAF RHQETPGDYL LCSGSQDRYI RLWRIRINDL 

       250        260        270        280        290        300 
IDDSEEDSKK LTLLSNKQYK FQIDDELRVG INFEALIMGH DDWISSLQWH ESRLQLLAAT 

       310        320        330        340        350        360 
ADTSLMVWEP DETSGIWVCS LRLGEMSSKG ASTATGSSGG FWSCLWFTHE RMDFFLTNGK 

       370        380        390        400        410        420 
TGSWRMWATK DNIICDQRLG ISGATKDVTD IAWSPSGEYL LATSLDQTTR LFAPWIYDAS 

       430        440        450        460        470        480 
GRKREIATWH EFSRPQIHGY DMICVETVTD TRFVSGGDEK ILRSFDLPKG VAGMLQKFVG 

       490        500        510        520        530        540 
IQFEEKSEMP DSATVPVLGL SNKAGEDDAN EDDEEEEGGN KETPDITDPL SLLECPPMED 

       550        560        570        580        590        600 
QLQRHLLWPE VEKLYGHGFE ITCLDISPDQ KLIASACRSN NVQNAVIRIF STENWLEIKP 

       610        620        630        640        650        660 
ALPFHSLTIT RLKFSKDGKF LLSVCRDRKW ALWERNMEDN TFELRFKNEK PHTRIIWDAD 

       670        680        690        700        710        720 
WAPLEFGNVF VTASRDKTVK VWRHQKEPAD DYVLEASIKH TKAVTAISIH DSMIREKILI 

       730        740        750        760        770        780 
SVGLENGEIY LYSYTLGKFE LITQLNEDIT PADKITRLRW SHLKRNGKLF LGVGSSDLST 


RIYSLAYE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[13]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49133 Genomic DNA. Translation: CAA88993.1.
Z72985 Genomic DNA. Translation: CAA97227.1.
AY558100 Genomic DNA. Translation: AAS56426.1.
BK006941 Genomic DNA. Translation: DAA08293.1.
PIRS53923.
RefSeqNP_011716.3. NM_001181329.3.

3D structure databases

ProteinModelPortalP42935.
SMRP42935. Positions 27-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33453. 286 interactions.
DIPDIP-2386N.
IntActP42935. 15 interactions.
MINTMINT-613845.
STRING4932.YGR200C.

Proteomic databases

PaxDbP42935.
PeptideAtlasP42935.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR200C; YGR200C; YGR200C.
GeneID853114.
KEGGsce:YGR200C.

Organism-specific databases

CYGDYGR200c.
SGDS000003432. ELP2.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00390000000916.
HOGENOMHOG000200623.
KOK11374.
OMANRQRFGD.
OrthoDBEOG7TQV9M.

Enzyme and pathway databases

BioCycYEAST:G3O-30885-MONOMER.

Gene expression databases

GenevestigatorP42935.

Family and domain databases

Gene3D2.130.10.10. 3 hits.
InterProIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 8 hits.
[Graphical view]
SMARTSM00320. WD40. 11 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 4 hits.
PROSITEPS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio973136.
PROP42935.

Entry information

Entry nameELP2_YEAST
AccessionPrimary (citable) accession number: P42935
Secondary accession number(s): D6VUY2, E9P8V1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families