Q04868 (ELP6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongator complex protein 6

Alternative name(s):
Gamma-toxin target 6
HAT-associated protein 3

Gene names

Name:	ELP6
Synonyms:	HAP3, TOT6
Ordered Locus Names:	YMR312W
ORF Names:	YM9924.04

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	273 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. ELP6 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.4 Ref.5 Ref.8 Ref.9 Ref.10 Ref.12
Subunit structure	Component of the RNA polymerase II elongator complex, which consists of IKI3, ELP2, ELP3, ELP4, IKI1 and ELP6. ELP4, IKI1 and ELP6 form a distinct subcomplex (HAP). Ref.6 Ref.7 Ref.8
Subcellular location	Cytoplasm. Nucleus Ref.4 Ref.11.
Sequence similarities	Belongs to the ELP6 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from direct assay PubMed 22343726. Source: GOC 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 electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ELP4	Q02884	4	EBI-27653,EBI-35277
IKI1	P38874	4	EBI-27653,EBI-9061

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 273

273

Elongator complex protein 6

PRO_0000203355

Secondary structure

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273

Helix Strand Turn

Details...

Helix

20 – 23

4

Beta strand

25 – 27

3

Beta strand

30 – 36

7

Helix

43 – 55

13

Helix

59 – 62

4

Beta strand

76 – 84

9

Helix

86 – 95

10

Helix

100 – 102

3

Beta strand

103 – 109

7

Helix

112 – 116

5

Turn

117 – 119

3

Helix

122 – 138

17

Beta strand

143 – 149

7

Helix

151 – 153

3

Helix

154 – 157

4

Helix

163 – 169

7

Helix

171 – 176

6

Beta strand

179 – 186

8

Helix

188 – 190

3

Helix

197 – 200

4

Helix

202 – 214

13

Beta strand

216 – 222

7

Beta strand

234 – 240

7

Beta strand

257 – 264

8

Beta strand

267 – 271

5

Sequences

	Sequence		Length	Mass (Da)
	Q04868 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 1A5062465AF67F47	FASTA	273	30,574
	10 20 30 40 50 60 MGSVQRQDLV LFSDQSVLPA HFFQDSNSHN LFFITHQSCT QPLWMINALV ETHVLGSPSS 70 80 90 100 110 120 LNESSSSMLP SSTRSHAVLA SFIHEQNYFT NSLNKLKIPS NNYNVLDFLS DFIVNNIHNK 130 140 150 160 170 180 PRDKILSDVL AKFSAAIQNN PTDTIVIIEQ PELLLSLVSG LTCSELNNKF ITPLLRQCKV 190 200 210 220 230 240 LIIVSNSDIF NIDEYDASVH SSNLQNFYKS SFIKSMINLN LNPLKTGFAK DVTGSLHVCR 250 260 270 GGAPIATSNT SLHVVENEYL YLNEKESTKL FYR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"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.
[4]	"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.
[5]	"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.
[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]	"A multiprotein complex that interacts with RNA polymerase II elongator." Li Y., Takagi Y., Jiang Y., Tokunaga M., Erdjument-Bromage H., Tempst P., Kornberg R.D. J. Biol. Chem. 276:29628-29631(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR COMPLEX, MASS SPECTROMETRY.
[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]	"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.
[10]	"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.
[11]	"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: SUBCELLULAR LOCATION.
[12]	"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

Z54141 Genomic DNA. Translation: CAA90830.1.
AY557983 Genomic DNA. Translation: AAS56309.1.
BK006946 Genomic DNA. Translation: DAA10213.1.

PIR

S59305.

RefSeq

NP_014043.1. NM_001182823.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4A8J	X-ray	2.10	C/F	1-273	[»]
4EJS	X-ray	2.61	C	1-273	[»]

ProteinModelPortal

Q04868.

SMR

Q04868. Positions 2-272.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1966N.

IntAct

Q04868. 7 interactions.

MINT

MINT-385455.

STRING

4932.YMR312W.

Proteomic databases

PaxDb

Q04868.

PeptideAtlas

Q04868.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YMR312W; YMR312W; YMR312W.

GeneID

855360.

KEGG

sce:YMR312W.

Organism-specific databases

CYGD

YMR312w.

SGD

S000004929. ELP6.

Phylogenomic databases

eggNOG

NOG302847.

HOGENOM

HOG000248084.

KO

K11377.

OMA

VVENEYL.

OrthoDB

EOG4MGWHR.

Gene expression databases

Genevestigator

Q04868.

GermOnline

YMR312W. Saccharomyces cerevisiae.

Family and domain databases

ProtoNet

Search...

Other

NextBio

979130.

Entry information

Entry name

ELP6_YEAST

Accession

Primary (citable) accession number: Q04868
Secondary accession number(s): D6W0D9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	April 3, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program