Q06706 (ELP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongator complex protein 1

Alternative name(s):
Gamma-toxin target 1
Protein IKI3

Gene names

Name:	IKI3
Synonyms:	ELP1, TOT1
Ordered Locus Names:	YLR384C
ORF Names:	L3502.7

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	1349 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. Independently, ELP3 may be involved in polarized exocytosis. It is required for the polarized localization of GTPase-activating protein SEC2. 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.7 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15
Subunit structure	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. In the complex, IKI3 interacts with ELP2. Ref.6 Ref.7 Ref.8 Ref.14
Subcellular location	Cytoplasm. Nucleus Ref.4 Ref.12 Ref.14.
Miscellaneous	Present with 10500 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the ELP1/IKA1 family.

Ontologies

Keywords
Biological process	Protein transport Transcription Transcription regulation Transport
Cellular component	Cytoplasm Nucleus
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein transport Inferred from electronic annotation. Source: UniProtKB-KW 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 Ref.8. Source: SGD nucleus Inferred from direct assay Ref.8. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ELP4	Q02884	9	EBI-9068,EBI-35277
IKI1	P38874	8	EBI-9068,EBI-9061

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1349	1349	Elongator complex protein 1		PRO_0000084179

Sequences

	Sequence		Length	Mass (Da)
	Q06706 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 7AEB1C0BA99282F6	FASTA	1,349	152,990
	10 20 30 40 50 60 MVEHDKSGSK RQELRSNMRN LITLNKGKFK PTASTAEGDE DDLSFTLLDS VFDTLSDSIT 70 80 90 100 110 120 CVLGSTDIGA IEVQQFMKDG SRNVLASFNI QTFDDKLLSF VHFADINQLV FVFEQGDIIT 130 140 150 160 170 180 ATYDPVSLDP AETLIEIMGT IDNGIAAAQW SYDEETLAMV TKDRNVVVLS KLFEPISEYH 190 200 210 220 230 240 LEVDDLKISK HVTVGWGKKE TQFRGKGARA MEREALASLK ASGLVGNQLR DPTMPYMVDT 250 260 270 280 290 300 GDVTALDSHE ITISWRGDCD YFAVSSVEEV PDEDDETKSI KRRAFRVFSR EGQLDSASEP 310 320 330 340 350 360 VTGMEHQLSW KPQGSLIASI QRKTDLGEED SVDVIFFERN GLRHGEFDTR LPLDEKVESV 370 380 390 400 410 420 CWNSNSEALA VVLANRIQLW TSKNYHWYLK QELYASDISY VKWHPEKDFT LMFSDAGFIN 430 440 450 460 470 480 IVDFAYKMAQ GPTLEPFDNG TSLVVDGRTV NITPLALANV PPPMYYRDFE TPGNVLDVAC 490 500 510 520 530 540 SFSNEIYAAI NKDVLIFAAV PSIEEMKKGK HPSIVCEFPK SEFTSEVDSL RQVAFINDSI 550 560 570 580 590 600 VGVLLDTDNL SRIALLDIQD ITQPTLITIV EVYDKIVLLR SDFDYNHLVY ETRDGTVCQL 610 620 630 640 650 660 DAEGQLMEIT KFPQLVRDFR VKRVHNTSAE DDDNWSAESS ELVAFGITNN GKLFANQVLL 670 680 690 700 710 720 ASAVTSLEIT DSFLLFTTAQ HNLQFVHLNS TDFKPLPLVE EGVEDERVRA IERGSILVSV 730 740 750 760 770 780 IPSKSSVVLQ ATRGNLETIY PRIMVLAEVR KNIMAKRYKE AFIVCRTHRI NLDILHDYAP 790 800 810 820 830 840 ELFIENLEVF INQIGRVDYL NLFISCLSED DVTKTKYKET LYSGISKSFG MEPAPLTEMQ 850 860 870 880 890 900 IYMKKKMFDP KTSKVNKICD AVLNVLLSNP EYKKKYLQTI ITAYASQNPQ NLSAALKLIS 910 920 930 940 950 960 ELENSEEKDS CVTYLCFLQD VNVVYKSALS LYDVSLALLV AQKSQMDPRE YLPFLQELQD 970 980 990 1000 1010 1020 NEPLRRKFLI DDYLGNYEKA LEHLSEIDKD GNVSEEVIDY VESHDLYKHG LALYRYDSEK 1030 1040 1050 1060 1070 1080 QNVIYNIYAK HLSSNQMYTD AAVAYEMLGK LKEAMGAYQS AKRWREAMSI AVQKFPEEVE 1090 1100 1110 1120 1130 1140 SVAEELISSL TFEHRYVDAA DIQLEYLDNV KEAVALYCKA YRYDIASLVA IKAKKDELLE 1150 1160 1170 1180 1190 1200 EVVDPGLGEG FGIIAELLAD CKGQINSQLR RLRELRAKKE ENPYAFYGQE TEQADDVSVA 1210 1220 1230 1240 1250 1260 PSETSTQESF FTRYTGKTGG TAKTGASRRT AKNKRREERK RARGKKGTIY EEEYLVQSVG 1270 1280 1290 1300 1310 1320 RLIERLNQTK PDAVRVVEGL CRRNMREQAH QIQKNFVEVL DLLKANVKEI YSISEKDRER 1330 1340 VNENGEVYYI PEIPVPEIHD FPKSHIVDF

References

	« Hide 'large scale' referencesShow '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]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [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]	"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]	"Protein interactions within Saccharomyces cerevisiae Elongator, a complex essential for Kluyveromyces lactis zymocicity." Fichtner L., Frohloff F., Jablonowski D., Stark M.J.R., Schaffrath R. Mol. Microbiol. 45:817-826(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ELP2.
[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]	"Subunit communications crucial for the functional integrity of the yeast RNA polymerase II elongator (gamma-toxin target (TOT)) complex." Frohloff F., Jablonowski D., Fichtner L., Schaffrath R. J. Biol. Chem. 278:956-961(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"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.
[12]	"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].
[13]	"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].
[14]	"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, INTERACTION WITH SEC2, SUBCELLULAR LOCATION.
[15]	"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	D87841 Genomic DNA. Translation: BAA20120.1. U19104 Genomic DNA. Translation: AAB67278.1. BK006945 Genomic DNA. Translation: DAA09685.1.
PIR	S51471.
RefSeq	NP_013488.3. NM_001182273.3.
3D structure databases
ProteinModelPortal	Q06706.
SMR	Q06706. Positions 143-170, 354-423, 471-496, 661-686.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2384N.
IntAct	Q06706. 18 interactions.
MINT	MINT-567397.
Proteomic databases
PaxDb	Q06706.
PeptideAtlas	Q06706.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR384C; YLR384C; YLR384C.
GeneID	851100.
KEGG	sce:YLR384C. sce:YLR386W.
Organism-specific databases
CYGD	YLR384c.
SGD	S000004376. IKI3.
Phylogenomic databases
eggNOG	COG5290.
GeneTree	ENSGT00390000013344.
HOGENOM	HOG000188454.
KO	K11373. K15305.
OMA	HPVNQVT.
OrthoDB	EOG4578G4.
Gene expression databases
Genevestigator	Q06706.
GermOnline	YLR384C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.130.10.10. 3 hits.
InterPro	IPR006849. IKI3. IPR015943. WD40/YVTN_repeat-like_dom. [Graphical view]
PANTHER	PTHR12747. PTHR12747. 1 hit.
Pfam	PF04762. IKI3. 1 hit. [Graphical view]
PIRSF	PIRSF017233. IKAP. 1 hit.
ProtoNet	Search...
Other
NextBio	967788.

Entry information

Entry name

ELP1_YEAST

Accession

Primary (citable) accession number: Q06706
Secondary accession number(s): D6VZ19, O00036

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program