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Q02908 (ELP3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 111. 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 3

EC=2.3.1.48
Alternative name(s):
Gamma-toxin target 3
Gene names
Name:ELP3
Synonyms:HPA1, TOT3
Ordered Locus Names:YPL086C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length557 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as catalytic subunit of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (Pol II) 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. ELP3 is required for the complex integrity and for the association of the complex with nascent RNA transcript. Independently, ELP3 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.3 Ref.4 Ref.5 Ref.7 Ref.8 Ref.9 Ref.13 Ref.15 Ref.16

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Cofactor

Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

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. ELP3 interacts with KTI12. Ref.5 Ref.6 Ref.7 Ref.14

Subcellular location

Cytoplasm. Nucleus Ref.3 Ref.11 Ref.15.

Miscellaneous

Present with 4760 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ELP3 family.

Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
   Biological processProtein transport
Transcription
Transcription regulation
Transport
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   LigandIron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionAcyltransferase
Chromatin regulator
Transferase
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistone acetylation

Inferred from direct assay Ref.5. Source: GOC

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.7. Source: SGD

tRNA wobble uridine modification

Inferred from mutant phenotype PubMed 18755837. Source: SGD

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentElongator holoenzyme complex

Inferred from direct assay Ref.7. Source: SGD

cytoplasm

Inferred from direct assay PubMed 12139626. Source: SGD

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 12139626. Source: SGD

   Molecular_functionhistone acetyltransferase activity

Inferred from direct assay Ref.5. Source: SGD

iron-sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.7PubMed 16429126PubMed 18467557PubMed 21179020. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IKI1P388746EBI-33957,EBI-9061

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 557557Elongator complex protein 3
PRO_0000235811

Regions

Domain405 – 557153N-acetyltransferase

Sites

Metal binding1081Iron-sulfur (4Fe-4S-S-AdoMet) Probable
Metal binding1181Iron-sulfur (4Fe-4S-S-AdoMet) Probable
Metal binding1211Iron-sulfur (4Fe-4S-S-AdoMet) Probable

Amino acid modifications

Cross-link453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10

Experimental info

Mutagenesis1081C → S: Eliminates iron contents; when associated with S-118 and S-121. Ref.17
Mutagenesis1181C → S: Eliminates iron contents; when associated with S-108 and S-121. Ref.17
Mutagenesis1211C → S: Eliminates iron contents; when associated with S-108 and S-118. Ref.17

Sequences

Sequence LengthMass (Da)Tools
Q02908 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 64EF8B42D3C3102E

FASTA55763,657
        10         20         30         40         50         60 
MARHGKGPKT NKKKLAPEKE RFIQCCADIT LELTDSLTSG TTREINLNGL ITKYSKKYKL 

        70         80         90        100        110        120 
KQQPRLTDII NSIPDQYKKY LLPKLKAKPV RTASGIAVVA VMCKPHRCPH IAYTGNICVY 

       130        140        150        160        170        180 
CPGGPDSDFE YSTQSYTGYE PTSMRAIRAR YDPYEQARGR VEQLKQLGHS IDKVEYVLMG 

       190        200        210        220        230        240 
GTFMSLPKEY REDFIVKLHN ALSGFNGNDI DEAILYSQQS LTKCVGITIE TRPDYCTQTH 

       250        260        270        280        290        300 
LDDMLKYGCT RLEIGVQSLY EDVARDTNRG HTVRSVCETF AVSKDAGYKV VSHMMPDLPN 

       310        320        330        340        350        360 
VGMERDIEQF KEYFENPDFR TDGLKIYPTL VIRGTGLYEL WKTGRYKSYS ANALVDLVAR 

       370        380        390        400        410        420 
ILALVPPWTR IYRVQRDIPM PLVTSGVDNG NLRELALARM KDLGTTCRDV RTREVGIQEV 

       430        440        450        460        470        480 
HHKVQPDQVE LIRRDYYANG GWETFLSYED PKKDILIGLL RLRKASKKYT YRKEFTSQRT 

       490        500        510        520        530        540 
SIVRELHVYG SVVPLHSRDP RKFQHQGFGT LLMEEAERIA KEEHGSEKIS VISGVGVRNY 

       550 
YGKLGYELDG PYMSKRI 

« 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme."
Wittschieben B.O., Otero G., de Bizemont T., Fellows J., Erdjument-Bromage H., Ohba R., Li Y., Allis C.D., Tempst P., Svejstrup J.Q.
Mol. Cell 4:123-128(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR COMPLEX.
[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]"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]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-453.
Strain: SUB592.
[11]"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].
[12]"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].
[13]"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.
[14]"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.
[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]"The Elongator subunit Elp3 contains a Fe4S4 cluster and binds S-adenosylmethionine."
Paraskevopoulou C., Fairhurst S.A., Lowe D.J., Brick P., Onesti S.
Mol. Microbiol. 59:795-806(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: S-ADENOSYLMETHIONINE-BINDING, MUTAGENESIS OF CYS-108; CYS-118 AND CYS-121.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U43281 Genomic DNA. Translation: AAB68213.1.
BK006949 Genomic DNA. Translation: DAA11347.1.
PIRS61980.
RefSeqNP_015239.1. NM_001183900.1.

3D structure databases

ProteinModelPortalQ02908.
SMRQ02908. Positions 501-550.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36095. 304 interactions.
DIPDIP-2385N.
IntActQ02908. 16 interactions.
MINTMINT-645857.
STRING4932.YPL086C.

Proteomic databases

MaxQBQ02908.
PaxDbQ02908.
PeptideAtlasQ02908.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL086C; YPL086C; YPL086C.
GeneID856019.
KEGGsce:YPL086C.

Organism-specific databases

CYGDYPL086c.
SGDS000006007. ELP3.

Phylogenomic databases

eggNOGCOG1243.
GeneTreeENSGT00390000013141.
HOGENOMHOG000227514.
KOK07739.
OMAGYKVVSH.
OrthoDBEOG7Z95VX.

Enzyme and pathway databases

BioCycYEAST:G3O-33992-MONOMER.

Gene expression databases

GenevestigatorQ02908.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
3.80.30.20. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR006638. Elp3/MiaB/NifB.
IPR000182. GNAT_dom.
IPR005910. Hist_AcTrfase_ELP3.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
TIGRFAMsTIGR01211. ELP3. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio980923.
PROQ02908.

Entry information

Entry nameELP3_YEAST
AccessionPrimary (citable) accession number: Q02908
Secondary accession number(s): D6W3T1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 111 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