P42935 (ELP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	788 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Protein transport Transcription Transcription regulation Transport
Cellular component	Cytoplasm Nucleus
Domain	Repeat WD repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein transport Inferred from electronic annotation. Source: UniProtKB-KW protein urmylation Inferred from mutant phenotype PubMed 14551258. Source: SGD regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.8. Source: SGD tRNA wobble uridine modification Inferred from mutant phenotype PubMed 18755837. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Elongator holoenzyme complex Inferred from direct assay Ref.8. Source: SGD cytoplasm Inferred from direct assay Ref.9. Source: SGD nucleus Inferred from direct assay Ref.9. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ELP4	Q02884	7	EBI-23459,EBI-35277
IKI1	P38874	6	EBI-23459,EBI-9061

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 788	788	Elongator complex protein 2		PRO_0000051474
Regions
	Repeat	57 – 87	31	WD 1
	Repeat	101 – 130	30	WD 2
	Repeat	141 – 181	41	WD 3
	Repeat	200 – 234	35	WD 4
	Repeat	279 – 309	31	WD 5
	Repeat	383 – 413	31	WD 6
	Repeat	438 – 466	29	WD 7
	Repeat	604 – 634	31	WD 8
	Repeat	651 – 683	33	WD 9
Amino acid modifications
	Modified residue	152	1	Phosphotyrosine Ref.17
	Modified residue	157	1	Phosphoserine Ref.17
Experimental info
	Sequence conflict	579	1	S → P in AAS56426. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P42935 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 5371908FE2E6EC0D	FASTA	788	89,411
	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

References

	« Hide 'large scale' referencesShow '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. , 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 96604 / S288c / FY1679.
[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. , 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.
[17]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-152 AND SER-157, MASS SPECTROMETRY.
+	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.
PIR	S53923.
RefSeq	NP_011716.3. NM_001181329.3.
3D structure databases
ProteinModelPortal	P42935.
SMR	P42935. Positions 27-309, 342-414, 585-684.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2386N.
IntAct	P42935. 17 interactions.
MINT	MINT-613845.
STRING	4932.YGR200C.
Proteomic databases
PaxDb	P42935.
PeptideAtlas	P42935.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR200C; YGR200C; YGR200C.
GeneID	853114.
KEGG	sce:YGR200C. sce:YGR205W.
Organism-specific databases
CYGD	YGR200c.
SGD	S000003432. ELP2.
Phylogenomic databases
eggNOG	COG2319.
GeneTree	ENSGT00390000000916.
HOGENOM	HOG000200623.
KO	K11374. K15918.
OMA	HGYDMIC.
OrthoDB	EOG42C1HT.
Gene expression databases
Genevestigator	P42935.
GermOnline	YGR200C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.130.10.10. 3 hits.
InterPro	IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR017986. WD40_repeat_dom. [Graphical view]
Pfam	PF00400. WD40. 8 hits. [Graphical view]
SMART	SM00320. WD40. 11 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. False negative. PS50082. WD_REPEATS_2. 6 hits. PS50294. WD_REPEATS_REGION. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	973136.

Entry information

Entry name

ELP2_YEAST

Accession

Primary (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:	May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program