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Q02884

- ELP4_YEAST

UniProt

Q02884 - ELP4_YEAST

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Protein

Elongator complex protein 4

Gene

ELP4

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

Functioni

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.7 Publications

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. regulation of transcription from RNA polymerase II promoter Source: SGD
  3. transcription, DNA-templated Source: UniProtKB-KW
  4. tRNA wobble uridine modification Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-34004-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongator complex protein 4
Alternative name(s):
Gamma-toxin target 7
HAT-associated protein 1
Gene namesi
Name:ELP4
Synonyms:HAP1, TOT7
Ordered Locus Names:YPL101W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

CYGDiYPL101w.
SGDiS000006022. ELP4.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. Elongator holoenzyme complex Source: SGD
  3. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Elongator complex protein 4PRO_0000235812Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei222 – 2221Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ02884.
PaxDbiQ02884.

Expressioni

Gene expression databases

GenevestigatoriQ02884.

Interactioni

Subunit structurei

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 KTI12.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ELP2P429357EBI-35277,EBI-23459
ELP6Q0486810EBI-35277,EBI-27653
IKI1P3887410EBI-35277,EBI-9061
IKI3Q067069EBI-35277,EBI-9068

Protein-protein interaction databases

BioGridi36079. 219 interactions.
DIPiDIP-6718N.
IntActiQ02884. 6 interactions.
MINTiMINT-672307.
STRINGi4932.YPL101W.

Structurei

Secondary structure

1
456
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi75 – 773Combined sources
Turni79 – 813Combined sources
Beta strandi84 – 863Combined sources
Helixi91 – 966Combined sources
Beta strandi99 – 1035Combined sources
Beta strandi107 – 1126Combined sources
Helixi119 – 13517Combined sources
Beta strandi149 – 1546Combined sources
Helixi158 – 1636Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi241 – 2466Combined sources
Turni253 – 2553Combined sources
Beta strandi256 – 2594Combined sources
Beta strandi261 – 2633Combined sources
Helixi265 – 27814Combined sources
Turni279 – 2813Combined sources
Beta strandi282 – 2887Combined sources
Turni289 – 2924Combined sources
Turni294 – 2963Combined sources
Helixi299 – 3024Combined sources
Helixi304 – 32017Combined sources
Turni321 – 3244Combined sources
Beta strandi325 – 3328Combined sources
Helixi333 – 3353Combined sources
Helixi338 – 34710Combined sources
Beta strandi349 – 3568Combined sources
Helixi359 – 36810Combined sources
Turni369 – 3713Combined sources
Helixi373 – 3753Combined sources
Beta strandi379 – 3857Combined sources
Helixi389 – 3924Combined sources
Beta strandi398 – 4069Combined sources
Beta strandi411 – 4155Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A8JX-ray2.10A/D66-426[»]
4EJSX-ray2.61A67-438[»]
ProteinModelPortaliQ02884.
SMRiQ02884. Positions 67-168, 234-419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ELP4 family.Curated

Phylogenomic databases

eggNOGiNOG250551.
HOGENOMiHOG000175573.
InParanoidiQ02884.
KOiK11375.
OMAiWRYGLNK.
OrthoDBiEOG7WDNCM.

Family and domain databases

InterProiIPR008728. Elongator_complex_protein_4.
[Graphical view]
PfamiPF05625. PAXNEB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02884-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSFRKRGEIL NDRGSGLRGP LLRGPPRTSS TPLRTGNRRA PGNVPLSDTT
60 70 80 90 100
ARLKKLNIAD ESKTKMGLDS SHVGVRPSPA TSQPTTSTGS ADLDSILGHM
110 120 130 140 150
GLPLGNSVLV EEQSTTEFHS ILGKLFAAQG IVHNRISDSS ADKTRNGDTH
160 170 180 190 200
VIVLSLNQMF AKELPGIYKG SRKQMKKNLI SEEESKVTVQ NLNETQRSTP
210 220 230 240 250
SRYKDLKIAW KYKLADEKRL GSPDRDDIQQ NSEYKDYNHQ FDITTRLMPA
260 270 280 290 300
PIASELTFIA PTQPVSTILS QIEQTIKRND KKLIRIVIPS LLHPAMYPPK
310 320 330 340 350
MFESSEIIGL MHGVRSLVKK YYERVVLFAS ISIDIITPPL LVLLRNMFDS
360 370 380 390 400
VINLEPFNQE MTEFLERVYK SQPGKIQHGL VHILKLPVFT DRGEMRVLKS
410 420 430 440 450
EWAFKNGRKK FEIEQWGIPV DDAEGSAASE QSHSHSHSDE ISHNIPAKKT

KISLDY
Length:456
Mass (Da):51,156
Last modified:November 1, 1996 - v1
Checksum:i276F0D1538EAA8FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43281 Genomic DNA. Translation: AAB68198.1.
BK006949 Genomic DNA. Translation: DAA11331.1.
PIRiS61965.
RefSeqiNP_015224.1. NM_001183915.1.

Genome annotation databases

EnsemblFungiiYPL101W; YPL101W; YPL101W.
GeneIDi856002.
KEGGisce:YPL101W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43281 Genomic DNA. Translation: AAB68198.1 .
BK006949 Genomic DNA. Translation: DAA11331.1 .
PIRi S61965.
RefSeqi NP_015224.1. NM_001183915.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4A8J X-ray 2.10 A/D 66-426 [» ]
4EJS X-ray 2.61 A 67-438 [» ]
ProteinModelPortali Q02884.
SMRi Q02884. Positions 67-168, 234-419.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36079. 219 interactions.
DIPi DIP-6718N.
IntActi Q02884. 6 interactions.
MINTi MINT-672307.
STRINGi 4932.YPL101W.

Proteomic databases

MaxQBi Q02884.
PaxDbi Q02884.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YPL101W ; YPL101W ; YPL101W .
GeneIDi 856002.
KEGGi sce:YPL101W.

Organism-specific databases

CYGDi YPL101w.
SGDi S000006022. ELP4.

Phylogenomic databases

eggNOGi NOG250551.
HOGENOMi HOG000175573.
InParanoidi Q02884.
KOi K11375.
OMAi WRYGLNK.
OrthoDBi EOG7WDNCM.

Enzyme and pathway databases

BioCyci YEAST:G3O-34004-MONOMER.

Miscellaneous databases

NextBioi 980875.
PROi Q02884.

Gene expression databases

Genevestigatori Q02884.

Family and domain databases

InterProi IPR008728. Elongator_complex_protein_4.
[Graphical view ]
Pfami PF05625. PAXNEB. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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. 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.

Entry informationi

Entry nameiELP4_YEAST
AccessioniPrimary (citable) accession number: Q02884
Secondary accession number(s): D6W3R5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 108 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 358 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3