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Q02884 (ELP4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 4
Alternative name(s):
Gamma-toxin target 7
HAT-associated protein 1
Gene names
Name:ELP4
Synonyms:HAP1, TOT7
Ordered Locus Names:YPL101W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length456 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. ELP4 is required for the complex integrity and the complex HAT activity but is not required for the association of the complex with nascent RNA transcript. 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.3 Ref.4 Ref.7 Ref.8 Ref.9 Ref.11 Ref.14

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). ELP4 interacts with KTI12. Ref.5 Ref.6 Ref.7 Ref.12

Subcellular location

Cytoplasm. Nucleus Ref.3 Ref.13.

Miscellaneous

Present with 358 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ELP4 family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Elongator complex protein 4
PRO_0000235812

Amino acid modifications

Modified residue2221Phosphoserine Ref.15

Secondary structure

........................................................... 456
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02884 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 276F0D1538EAA8FA

FASTA45651,156
        10         20         30         40         50         60 
MSFRKRGEIL NDRGSGLRGP LLRGPPRTSS TPLRTGNRRA PGNVPLSDTT ARLKKLNIAD 

        70         80         90        100        110        120 
ESKTKMGLDS SHVGVRPSPA TSQPTTSTGS ADLDSILGHM GLPLGNSVLV EEQSTTEFHS 

       130        140        150        160        170        180 
ILGKLFAAQG IVHNRISDSS ADKTRNGDTH VIVLSLNQMF AKELPGIYKG SRKQMKKNLI 

       190        200        210        220        230        240 
SEEESKVTVQ NLNETQRSTP SRYKDLKIAW KYKLADEKRL GSPDRDDIQQ NSEYKDYNHQ 

       250        260        270        280        290        300 
FDITTRLMPA PIASELTFIA PTQPVSTILS QIEQTIKRND KKLIRIVIPS LLHPAMYPPK 

       310        320        330        340        350        360 
MFESSEIIGL MHGVRSLVKK YYERVVLFAS ISIDIITPPL LVLLRNMFDS VINLEPFNQE 

       370        380        390        400        410        420 
MTEFLERVYK SQPGKIQHGL VHILKLPVFT DRGEMRVLKS EWAFKNGRKK FEIEQWGIPV 

       430        440        450 
DDAEGSAASE QSHSHSHSDE ISHNIPAKKT KISLDY 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(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]"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.
[4]"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.
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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].
[11]"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.
[12]"Physical and functional interaction between Elongator and the chromatin-associated Kti12 protein."
Petrakis T.G., Soegaard T.M.M., Erdjument-Bromage H., Tempst P., Svejstrup J.Q.
J. Biol. Chem. 280:19454-19460(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KTI12.
[13]"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.
[14]"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.
[15]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U43281 Genomic DNA. Translation: AAB68198.1.
BK006949 Genomic DNA. Translation: DAA11331.1.
PIRS61965.
RefSeqNP_015224.1. NM_001183915.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4A8JX-ray2.10A/D66-426[»]
4EJSX-ray2.61A67-438[»]
ProteinModelPortalQ02884.
SMRQ02884. Positions 67-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36079. 217 interactions.
DIPDIP-6718N.
IntActQ02884. 6 interactions.
MINTMINT-672307.
STRING4932.YPL101W.

Proteomic databases

PaxDbQ02884.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL101W; YPL101W; YPL101W.
GeneID856002.
KEGGsce:YPL101W.

Organism-specific databases

CYGDYPL101w.
SGDS000006022. ELP4.

Phylogenomic databases

eggNOGNOG250551.
HOGENOMHOG000175573.
KOK11375.
OMAWRYGLNK.
OrthoDBEOG7WDNCM.

Enzyme and pathway databases

BioCycYEAST:G3O-34004-MONOMER.

Gene expression databases

GenevestigatorQ02884.

Family and domain databases

InterProIPR008728. Elongator_complex_protein_4.
[Graphical view]
PfamPF05625. PAXNEB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio980875.
PROQ02884.

Entry information

Entry nameELP4_YEAST
AccessionPrimary (citable) accession number: Q02884
Secondary accession number(s): D6W3R5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 103 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 XVI

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references