Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q04868 (ELP6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length273 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. 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ELP4Q0288410EBI-27653,EBI-35277
IKI1P388746EBI-27653,EBI-9061

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 273273Elongator complex protein 6
PRO_0000203355

Secondary structure

................................................ 273
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04868 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 1A5062465AF67F47

FASTA27330,574
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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 204508 / S288c.
[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. 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.
[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, IDENTIFICATION BY 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.
PIRS59305.
RefSeqNP_014043.1. NM_001182823.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4A8JX-ray2.10C/F1-273[»]
4EJSX-ray2.61C1-273[»]
ProteinModelPortalQ04868.
SMRQ04868. Positions 2-272.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35492. 212 interactions.
DIPDIP-1966N.
IntActQ04868. 8 interactions.
MINTMINT-385455.
STRING4932.YMR312W.

Proteomic databases

PaxDbQ04868.
PeptideAtlasQ04868.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR312W; YMR312W; YMR312W.
GeneID855360.
KEGGsce:YMR312W.

Organism-specific databases

CYGDYMR312w.
SGDS000004929. ELP6.

Phylogenomic databases

eggNOGNOG302847.
HOGENOMHOG000248084.
KOK11377.
OMADFLVKLH.
OrthoDBEOG7QC87F.

Enzyme and pathway databases

BioCycYEAST:G3O-32976-MONOMER.

Gene expression databases

GenevestigatorQ04868.

Family and domain databases

ProtoNetSearch...

Other

NextBio979130.

Entry information

Entry nameELP6_YEAST
AccessionPrimary (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 16, 2014
This is version 97 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 XIII

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

Yeast

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

Uncharacterized protein families (UPF)

List of uncharacterized protein family (UPF) entries

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references