Q02884 (ELP4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongator complex protein 4

Alternative name(s):
Gamma-toxin target 7
HAT-associated protein 1

Gene names

Name:	ELP4
Synonyms:	HAP1, TOT7
Ordered Locus Names:	YPL101W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	456 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. 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. Ref.3 Ref.4 Ref.7 Ref.8 Ref.9 Ref.11 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). ELP4 interacts with KTI12. Ref.5 Ref.6 Ref.7 Ref.12
Subcellular location	Cytoplasm. Nucleus Ref.3 Ref.13.
Miscellaneous	Present with 358 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the ELP4 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
PTM	Phosphoprotein
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 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Elongator holoenzyme complex Inferred from direct assay Ref.7. Source: SGD cytoplasm Inferred from direct assay PubMed 11914276. Source: SGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ELP2	P42935	7	EBI-35277,EBI-23459
ELP6	Q04868	4	EBI-35277,EBI-27653
IKI1	P38874	6	EBI-35277,EBI-9061
IKI3	Q06706	9	EBI-35277,EBI-9068

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 456

456

Elongator complex protein 4

PRO_0000235812

Amino acid modifications

Modified residue

222

1

Phosphoserine Ref.15 Ref.16

Secondary structure

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456

Helix Strand Turn

Details...

Beta strand

75 – 77

3

Turn

79 – 81

3

Beta strand

84 – 86

3

Helix

91 – 96

6

Beta strand

99 – 103

5

Beta strand

107 – 112

6

Helix

119 – 135

17

Beta strand

149 – 154

6

Helix

158 – 163

6

Beta strand

165 – 167

3

Beta strand

241 – 246

6

Turn

253 – 255

3

Beta strand

256 – 259

4

Beta strand

261 – 263

3

Helix

265 – 278

14

Turn

279 – 281

3

Beta strand

282 – 288

7

Turn

289 – 292

4

Turn

294 – 296

3

Helix

299 – 302

4

Helix

304 – 320

17

Turn

321 – 324

4

Beta strand

325 – 332

8

Helix

333 – 335

3

Helix

338 – 347

10

Beta strand

349 – 356

8

Helix

359 – 368

10

Turn

369 – 371

3

Helix

373 – 375

3

Beta strand

379 – 385

7

Helix

389 – 392

4

Beta strand

398 – 406

9

Beta strand

411 – 415

5

Sequences

	Sequence		Length	Mass (Da)
	Q02884 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 276F0D1538EAA8FA	FASTA	456	51,156
	10 20 30 40 50 60 MSFRKRGEIL NDRGSGLRGP LLRGPPRTSS TPLRTGNRRA PGNVPLSDTT ARLKKLNIAD 70 80 90 100 110 120 ESKTKMGLDS SHVGVRPSPA TSQPTTSTGS ADLDSILGHM GLPLGNSVLV EEQSTTEFHS 130 140 150 160 170 180 ILGKLFAAQG IVHNRISDSS ADKTRNGDTH VIVLSLNQMF AKELPGIYKG SRKQMKKNLI 190 200 210 220 230 240 SEEESKVTVQ NLNETQRSTP SRYKDLKIAW KYKLADEKRL GSPDRDDIQQ NSEYKDYNHQ 250 260 270 280 290 300 FDITTRLMPA PIASELTFIA PTQPVSTILS QIEQTIKRND KKLIRIVIPS LLHPAMYPPK 310 320 330 340 350 360 MFESSEIIGL MHGVRSLVKK YYERVVLFAS ISIDIITPPL LVLLRNMFDS VINLEPFNQE 370 380 390 400 410 420 MTEFLERVYK SQPGKIQHGL VHILKLPVFT DRGEMRVLKS EWAFKNGRKK FEIEQWGIPV 430 440 450 DDAEGSAASE QSHSHSHSDE ISHNIPAKKT KISLDY

References

	« Hide 'large scale' referencesShow '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. , 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 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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, 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]	"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].
[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, MASS SPECTROMETRY. Strain: ADR376.
[16]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U43281 Genomic DNA. Translation: AAB68198.1.
BK006949 Genomic DNA. Translation: DAA11331.1.

PIR

S61965.

RefSeq

NP_015224.1. NM_001183915.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4A8J	X-ray	2.10	A/D	66-426	[»]
4EJS	X-ray	2.61	A	67-438	[»]

ProteinModelPortal

Q02884.

SMR

Q02884. Positions 67-168, 234-419.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6718N.

IntAct

Q02884. 5 interactions.

MINT

MINT-672307.

STRING

4932.YPL101W.

Proteomic databases

PaxDb

Q02884.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPL101W; YPL101W; YPL101W.

GeneID

856002.

KEGG

sce:YPL101W.

Organism-specific databases

CYGD

YPL101w.

SGD

S000006022. ELP4.

Phylogenomic databases

eggNOG

NOG250551.

HOGENOM

HOG000175573.

KO

K11375.

OMA

IEEWGIP.

OrthoDB

EOG4BS0VP.

Enzyme and pathway databases

BioCyc

YEAST:G3O-34004-MONOMER.

Gene expression databases

Genevestigator

Q02884.

GermOnline

YPL101W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR008728. Elongator_complex_protein_4.
[Graphical view]

Pfam

PF05625. PAXNEB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

980875.

Entry information

Entry name

ELP4_YEAST

Accession

Primary (citable) accession number: Q02884
Secondary accession number(s): D6W3R5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program