Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Elongator complex protein 5

Gene

IKI1

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 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. IKI1 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.6 Publications

GO - Biological processi

  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
  • tRNA modification Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-31217-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongator complex protein 5
Alternative name(s):
Gamma-toxin target 5
HAT-associated protein 2
Protein IKI1
Gene namesi
Name:IKI1
Synonyms:ELP5, HAP2, TOT5
Ordered Locus Names:YHR187W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VIII

Organism-specific databases

CYGDiYHR187w.
EuPathDBiFungiDB:YHR187W.
SGDiS000001230. IKI1.

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Elongator complex protein 5PRO_0000084178Add
BLAST

Proteomic databases

MaxQBiP38874.
PaxDbiP38874.

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).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ELP2P429356EBI-9061,EBI-23459
ELP3Q029086EBI-9061,EBI-33957
ELP4Q0288410EBI-9061,EBI-35277
ELP6Q048686EBI-9061,EBI-27653
IKI3Q067068EBI-9061,EBI-9068

Protein-protein interaction databases

BioGridi36621. 118 interactions.
DIPiDIP-1967N.
IntActiP38874. 9 interactions.
MINTiMINT-385467.

Structurei

Secondary structure

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 169Combined sources
Beta strandi23 – 308Combined sources
Helixi36 – 4813Combined sources
Beta strandi55 – 617Combined sources
Beta strandi70 – 745Combined sources
Helixi80 – 8910Combined sources
Beta strandi102 – 1076Combined sources
Helixi109 – 1113Combined sources
Helixi114 – 1163Combined sources
Helixi117 – 1248Combined sources
Beta strandi129 – 1368Combined sources
Turni151 – 1533Combined sources
Helixi157 – 1648Combined sources
Beta strandi166 – 1738Combined sources
Helixi181 – 1899Combined sources
Beta strandi200 – 20910Combined sources
Beta strandi215 – 2239Combined sources
Turni224 – 2274Combined sources
Beta strandi228 – 2314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A8JX-ray2.10B/E1-270[»]
4EJSX-ray2.61B1-238[»]
ProteinModelPortaliP38874.
SMRiP38874. Positions 7-234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ELP5 family.Curated

Phylogenomic databases

eggNOGiNOG72129.
HOGENOMiHOG000248152.
InParanoidiP38874.
KOiK11376.
OMAiYEYEKDD.
OrthoDBiEOG7XWQ03.

Family and domain databases

InterProiIPR019519. Elp5.
[Graphical view]
PfamiPF10483. Elong_Iki1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38874-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSSHNPVI LLKRILSLTE SSPFILCLDS IAQTSYKLIQ EFVHQSKSKG
60 70 80 90 100
NEYPIVYISF ETVNKPSYCT QFIDATQMDF VHLVKQIISY LPAATATQAK
110 120 130 140 150
KHMVIIDSLN YISTEYITRF LSEIASPHCT MVATYHKDIK DENRTVIPDW
160 170 180 190 200
NNNYPDKLTL LQFMATTIVD IDVVLTGTLD TEEVSELLNE FRIPRGLNND
210 220 230 240 250
IFQLRLVNKR KSGRSLEYDF IVNSNTHEYE LLSTTKQEEE SSSNGLETPE
260 270 280 290 300
MLQGLTTFNL GTSNKQKLAK DQVALPFLEA QSFGQGGAIV YEYEKDDDYD

EEDPYEDPF
Length:309
Mass (Da):35,220
Last modified:February 1, 1995 - v1
Checksum:iDFD93D7BA583E2F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83267 Genomic DNA. Translation: BAA20087.1.
U00030 Genomic DNA. Translation: AAB68362.1.
BK006934 Genomic DNA. Translation: DAA06879.1.
PIRiS46684.
RefSeqiNP_012057.3. NM_001179318.3.

Genome annotation databases

EnsemblFungiiYHR187W; YHR187W; YHR187W.
GeneIDi856594.
KEGGisce:YHR187W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83267 Genomic DNA. Translation: BAA20087.1.
U00030 Genomic DNA. Translation: AAB68362.1.
BK006934 Genomic DNA. Translation: DAA06879.1.
PIRiS46684.
RefSeqiNP_012057.3. NM_001179318.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A8JX-ray2.10B/E1-270[»]
4EJSX-ray2.61B1-238[»]
ProteinModelPortaliP38874.
SMRiP38874. Positions 7-234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36621. 118 interactions.
DIPiDIP-1967N.
IntActiP38874. 9 interactions.
MINTiMINT-385467.

Proteomic databases

MaxQBiP38874.
PaxDbiP38874.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR187W; YHR187W; YHR187W.
GeneIDi856594.
KEGGisce:YHR187W.

Organism-specific databases

CYGDiYHR187w.
EuPathDBiFungiDB:YHR187W.
SGDiS000001230. IKI1.

Phylogenomic databases

eggNOGiNOG72129.
HOGENOMiHOG000248152.
InParanoidiP38874.
KOiK11376.
OMAiYEYEKDD.
OrthoDBiEOG7XWQ03.

Enzyme and pathway databases

BioCyciYEAST:G3O-31217-MONOMER.

Miscellaneous databases

NextBioi982478.
PROiP38874.

Family and domain databases

InterProiIPR019519. Elp5.
[Graphical view]
PfamiPF10483. Elong_Iki1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of IKI1 and IKI3 genes conferring pGKL killer sensitivity on Saccharomyces cerevisiae."
    Yajima H., Tokunaga M., Nakayama-Murayama A., Hishinuma F.
    Biosci. Biotechnol. Biochem. 61:704-709(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  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.

Entry informationi

Entry nameiELP5_YEAST
AccessioniPrimary (citable) accession number: P38874
Secondary accession number(s): D3DLD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 22, 2015
This is version 123 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 3870 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 VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: 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.