P38874 (ELP5_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 104.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Elongator complex protein 5 Alternative name(s): Gamma-toxin target 5 HAT-associated protein 2 Protein IKI1 | ||||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome] | ||||||
| Taxonomic identifier | 559292 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › ![]() |
Protein attributes
| Sequence length | 309 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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. 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. Ref.4 Ref.5 Ref.8 Ref.9 Ref.10 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). Ref.6 Ref.7 Ref.8 |
| Subcellular location | |
| Miscellaneous | Present with 3870 molecules/cell in log phase SD medium. |
| Sequence similarities | Belongs to the ELP5 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Cellular component | Cytoplasm Nucleus |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | ATP catabolic process Inferred from direct assay PubMed 22343726. Source: GOC regulation of transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW tRNA modificationInferred from mutant phenotype Ref.14. Source: SGD transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | Elongator holoenzyme complex Inferred from direct assay Ref.8. Source: SGD cytoplasmInferred from direct assay PubMed 12139626. Source: SGD nucleusInferred from direct assay PubMed 12139626. Source: SGD |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ELP2 | P42935 | 6 | EBI-9061,EBI-23459 | |
| ELP3 | Q02908 | 6 | EBI-9061,EBI-33957 | |
| ELP4 | Q02884 | 6 | EBI-9061,EBI-35277 | |
| ELP6 | Q04868 | 4 | EBI-9061,EBI-27653 | |
| IKI3 | Q06706 | 8 | EBI-9061,EBI-9068 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 309 | 309 | Elongator complex protein 5 | PRO_0000084178 | ||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 8 – 16 | 9 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 23 – 30 | 8 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 36 – 48 | 13 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 55 – 61 | 7 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 70 – 74 | 5 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 80 – 89 | 10 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 102 – 107 | 6 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 109 – 111 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 114 – 116 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 117 – 124 | 8 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 129 – 136 | 8 | ||||||||||||||||||||||||||||||||||||||||||
| Turn | 151 – 153 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 157 – 164 | 8 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 166 – 173 | 8 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 181 – 189 | 9 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 200 – 209 | 10 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 215 – 223 | 9 | ||||||||||||||||||||||||||||||||||||||||||
| Turn | 224 – 227 | 4 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 228 – 231 | 4 | ||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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] | "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. Vaudin M.Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972. |
| [3] | Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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, 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] | "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] | "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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | D83267 Genomic DNA. Translation: BAA20087.1. U00030 Genomic DNA. Translation: AAB68362.1. BK006934 Genomic DNA. Translation: DAA06879.1. | ||||||||||||||||||
| PIR | S46684. | ||||||||||||||||||
| RefSeq | NP_012057.3. NM_001179318.3. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P38874. | ||||||||||||||||||
| SMR | P38874. Positions 7-234. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| DIP | DIP-1967N. | ||||||||||||||||||
| IntAct | P38874. 8 interactions. | ||||||||||||||||||
| MINT | MINT-385467. | ||||||||||||||||||
| STRING | 4932.YHR187W. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PaxDb | P38874. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| EnsemblFungi | YHR187W; YHR187W; YHR187W. | ||||||||||||||||||
| GeneID | 856594. | ||||||||||||||||||
| KEGG | sce:YHR187W. sce:YHR189W. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CYGD | YHR187w. | ||||||||||||||||||
| SGD | S000001230. IKI1. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | NOG72129. | ||||||||||||||||||
| HOGENOM | HOG000248152. | ||||||||||||||||||
| KO | K01056. K11376. | ||||||||||||||||||
| OMA | EEDPYED. | ||||||||||||||||||
| OrthoDB | EOG45HW6T. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| Genevestigator | P38874. | ||||||||||||||||||
| GermOnline | YHR187W. Saccharomyces cerevisiae. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR019519. Histone_acetylation_protein_2. [Graphical view] | ||||||||||||||||||
| Pfam | PF10483. Hap2_elong. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| NextBio | 982478. | ||||||||||||||||||
Entry information
| Entry name | ELP5_YEAST | ||||||||
| Accession | Primary (citable) accession number: P38874 Secondary accession number(s): D3DLD5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome VIII Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
