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Protein

Elongator complex protein 3

Gene

ELP3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.9 Publications

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi108 – 1081Iron-sulfur (4Fe-4S-S-AdoMet)Curated
Metal bindingi118 – 1181Iron-sulfur (4Fe-4S-S-AdoMet)Curated
Metal bindingi121 – 1211Iron-sulfur (4Fe-4S-S-AdoMet)Curated

GO - Molecular functioni

  • histone acetyltransferase activity Source: SGD
  • iron-sulfur cluster binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • histone acetylation Source: GOC
  • protein transport Source: UniProtKB-KW
  • regulation of transcription from RNA polymerase II promoter Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
  • tRNA wobble uridine modification Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

Protein transport, Transcription, Transcription regulation, Transport

Keywords - Ligandi

Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-33992-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongator complex protein 3 (EC:2.3.1.48)
Alternative name(s):
Gamma-toxin target 3
Gene namesi
Name:ELP3
Synonyms:HPA1, TOT3
Ordered Locus Names:YPL086C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XVI

Organism-specific databases

CYGDiYPL086c.
EuPathDBiFungiDB:YPL086C.
SGDiS000006007. ELP3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • Elongator holoenzyme complex Source: SGD
  • nucleoplasm Source: Reactome
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1081C → S: Eliminates iron contents; when associated with S-118 and S-121. 1 Publication
Mutagenesisi118 – 1181C → S: Eliminates iron contents; when associated with S-108 and S-121. 1 Publication
Mutagenesisi121 – 1211C → S: Eliminates iron contents; when associated with S-108 and S-118. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 557557Elongator complex protein 3PRO_0000235811Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki453 – 453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ02908.
PaxDbiQ02908.
PeptideAtlasiQ02908.

Expressioni

Gene expression databases

GenevestigatoriQ02908.

Interactioni

Subunit structurei

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 KTI12.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IKI1P388746EBI-33957,EBI-9061

Protein-protein interaction databases

BioGridi36095. 308 interactions.
DIPiDIP-2385N.
IntActiQ02908. 17 interactions.
MINTiMINT-645857.
STRINGi4932.YPL086C.

Structurei

3D structure databases

ProteinModelPortaliQ02908.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini405 – 557153N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ELP3 family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1243.
GeneTreeiENSGT00390000013141.
HOGENOMiHOG000227514.
InParanoidiQ02908.
KOiK07739.
OMAiGYKVVSH.
OrthoDBiEOG7Z95VX.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
3.80.30.20. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR006638. Elp3/MiaB/NifB.
IPR000182. GNAT_dom.
IPR005910. Hist_AcTrfase_ELP3.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
TIGRFAMsiTIGR01211. ELP3. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02908-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARHGKGPKT NKKKLAPEKE RFIQCCADIT LELTDSLTSG TTREINLNGL
60 70 80 90 100
ITKYSKKYKL KQQPRLTDII NSIPDQYKKY LLPKLKAKPV RTASGIAVVA
110 120 130 140 150
VMCKPHRCPH IAYTGNICVY CPGGPDSDFE YSTQSYTGYE PTSMRAIRAR
160 170 180 190 200
YDPYEQARGR VEQLKQLGHS IDKVEYVLMG GTFMSLPKEY REDFIVKLHN
210 220 230 240 250
ALSGFNGNDI DEAILYSQQS LTKCVGITIE TRPDYCTQTH LDDMLKYGCT
260 270 280 290 300
RLEIGVQSLY EDVARDTNRG HTVRSVCETF AVSKDAGYKV VSHMMPDLPN
310 320 330 340 350
VGMERDIEQF KEYFENPDFR TDGLKIYPTL VIRGTGLYEL WKTGRYKSYS
360 370 380 390 400
ANALVDLVAR ILALVPPWTR IYRVQRDIPM PLVTSGVDNG NLRELALARM
410 420 430 440 450
KDLGTTCRDV RTREVGIQEV HHKVQPDQVE LIRRDYYANG GWETFLSYED
460 470 480 490 500
PKKDILIGLL RLRKASKKYT YRKEFTSQRT SIVRELHVYG SVVPLHSRDP
510 520 530 540 550
RKFQHQGFGT LLMEEAERIA KEEHGSEKIS VISGVGVRNY YGKLGYELDG

PYMSKRI
Length:557
Mass (Da):63,657
Last modified:November 1, 1996 - v1
Checksum:i64EF8B42D3C3102E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43281 Genomic DNA. Translation: AAB68213.1.
BK006949 Genomic DNA. Translation: DAA11347.1.
PIRiS61980.
RefSeqiNP_015239.1. NM_001183900.1.

Genome annotation databases

EnsemblFungiiYPL086C; YPL086C; YPL086C.
GeneIDi856019.
KEGGisce:YPL086C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43281 Genomic DNA. Translation: AAB68213.1.
BK006949 Genomic DNA. Translation: DAA11347.1.
PIRiS61980.
RefSeqiNP_015239.1. NM_001183900.1.

3D structure databases

ProteinModelPortaliQ02908.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36095. 308 interactions.
DIPiDIP-2385N.
IntActiQ02908. 17 interactions.
MINTiMINT-645857.
STRINGi4932.YPL086C.

Proteomic databases

MaxQBiQ02908.
PaxDbiQ02908.
PeptideAtlasiQ02908.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL086C; YPL086C; YPL086C.
GeneIDi856019.
KEGGisce:YPL086C.

Organism-specific databases

CYGDiYPL086c.
EuPathDBiFungiDB:YPL086C.
SGDiS000006007. ELP3.

Phylogenomic databases

eggNOGiCOG1243.
GeneTreeiENSGT00390000013141.
HOGENOMiHOG000227514.
InParanoidiQ02908.
KOiK07739.
OMAiGYKVVSH.
OrthoDBiEOG7Z95VX.

Enzyme and pathway databases

BioCyciYEAST:G3O-33992-MONOMER.

Miscellaneous databases

NextBioi980923.
PROiQ02908.

Gene expression databases

GenevestigatoriQ02908.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
3.80.30.20. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR006638. Elp3/MiaB/NifB.
IPR000182. GNAT_dom.
IPR005910. Hist_AcTrfase_ELP3.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
TIGRFAMsiTIGR01211. ELP3. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-453.
    Strain: SUB592.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. 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.

Entry informationi

Entry nameiELP3_YEAST
AccessioniPrimary (citable) accession number: Q02908
Secondary accession number(s): D6W3T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: November 1, 1996
Last modified: May 27, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4760 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.