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P42935

- ELP2_YEAST

UniProt

P42935 - ELP2_YEAST

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Protein

Elongator complex protein 2

Gene

ELP2

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. ELP2 is dispensable for the complex integrity and, in vitro, is not required for complex HAT activity. It is not required for the association of the complex with nascent RNA transcript. Independently, ELP2 may be involved in polarized exocytosis. 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.8 Publications

GO - Biological processi

  1. protein transport Source: UniProtKB-KW
  2. protein urmylation Source: SGD
  3. regulation of transcription from RNA polymerase II promoter Source: SGD
  4. transcription, DNA-templated Source: UniProtKB-KW
  5. tRNA wobble uridine modification Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transcription, Transcription regulation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-30885-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongator complex protein 2
Alternative name(s):
Gamma-toxin target 2
Gene namesi
Name:ELP2
Synonyms:TOT2
Ordered Locus Names:YGR200C
ORF Names:G7725
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR200c.
SGDiS000003432. ELP2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. Elongator holoenzyme complex Source: SGD
  3. nucleoplasm Source: Reactome
  4. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 788788Elongator complex protein 2PRO_0000051474Add
BLAST

Proteomic databases

MaxQBiP42935.
PaxDbiP42935.
PeptideAtlasiP42935.

Expressioni

Gene expression databases

GenevestigatoriP42935.

Interactioni

Subunit structurei

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, ELP2 interacts with IKI3.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ELP4Q028847EBI-23459,EBI-35277
IKI1P388746EBI-23459,EBI-9061

Protein-protein interaction databases

BioGridi33453. 287 interactions.
DIPiDIP-2386N.
IntActiP42935. 15 interactions.
MINTiMINT-613845.
STRINGi4932.YGR200C.

Structurei

3D structure databases

ProteinModelPortaliP42935.
SMRiP42935. Positions 27-310, 387-413.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati57 – 8731WD 1Add
BLAST
Repeati101 – 13030WD 2Add
BLAST
Repeati141 – 18141WD 3Add
BLAST
Repeati200 – 23435WD 4Add
BLAST
Repeati279 – 30931WD 5Add
BLAST
Repeati383 – 41331WD 6Add
BLAST
Repeati438 – 46629WD 7Add
BLAST
Repeati604 – 63431WD 8Add
BLAST
Repeati651 – 68333WD 9Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat ELP2 family.Curated
Contains 9 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00390000000916.
HOGENOMiHOG000200623.
InParanoidiP42935.
KOiK11374.
OMAiDQVPEIN.
OrthoDBiEOG7TQV9M.

Family and domain databases

Gene3Di2.130.10.10. 3 hits.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 8 hits.
[Graphical view]
SMARTiSM00320. WD40. 11 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 4 hits.
PROSITEiPS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42935-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVECITPEAI FIGANKQTQV SDIHKVKKIV AFGAGKTIAL WDPIEPNNKG
60 70 80 90 100
VYATLKGHEA EVTCVRFVPD SDFMVSASED HHVKIWKFTD YSHLQCIQTI
110 120 130 140 150
QHYSKTIVAL SALPSLISVG CADGTISIWR QNIQNDEFGL AHEFTIKKGF
160 170 180 190 200
FYPLCLSLSK VEEKKYLLAI GGTNVNVFIA SFILSDSGIE KCRVVAELEG
210 220 230 240 250
HEDWVKSLAF RHQETPGDYL LCSGSQDRYI RLWRIRINDL IDDSEEDSKK
260 270 280 290 300
LTLLSNKQYK FQIDDELRVG INFEALIMGH DDWISSLQWH ESRLQLLAAT
310 320 330 340 350
ADTSLMVWEP DETSGIWVCS LRLGEMSSKG ASTATGSSGG FWSCLWFTHE
360 370 380 390 400
RMDFFLTNGK TGSWRMWATK DNIICDQRLG ISGATKDVTD IAWSPSGEYL
410 420 430 440 450
LATSLDQTTR LFAPWIYDAS GRKREIATWH EFSRPQIHGY DMICVETVTD
460 470 480 490 500
TRFVSGGDEK ILRSFDLPKG VAGMLQKFVG IQFEEKSEMP DSATVPVLGL
510 520 530 540 550
SNKAGEDDAN EDDEEEEGGN KETPDITDPL SLLECPPMED QLQRHLLWPE
560 570 580 590 600
VEKLYGHGFE ITCLDISPDQ KLIASACRSN NVQNAVIRIF STENWLEIKP
610 620 630 640 650
ALPFHSLTIT RLKFSKDGKF LLSVCRDRKW ALWERNMEDN TFELRFKNEK
660 670 680 690 700
PHTRIIWDAD WAPLEFGNVF VTASRDKTVK VWRHQKEPAD DYVLEASIKH
710 720 730 740 750
TKAVTAISIH DSMIREKILI SVGLENGEIY LYSYTLGKFE LITQLNEDIT
760 770 780
PADKITRLRW SHLKRNGKLF LGVGSSDLST RIYSLAYE
Length:788
Mass (Da):89,411
Last modified:November 1, 1995 - v1
Checksum:i5371908FE2E6EC0D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti579 – 5791S → P in AAS56426. (PubMed:17322287)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49133 Genomic DNA. Translation: CAA88993.1.
Z72985 Genomic DNA. Translation: CAA97227.1.
AY558100 Genomic DNA. Translation: AAS56426.1.
BK006941 Genomic DNA. Translation: DAA08293.1.
PIRiS53923.
RefSeqiNP_011716.3. NM_001181329.3.

Genome annotation databases

EnsemblFungiiYGR200C; YGR200C; YGR200C.
GeneIDi853114.
KEGGisce:YGR200C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49133 Genomic DNA. Translation: CAA88993.1 .
Z72985 Genomic DNA. Translation: CAA97227.1 .
AY558100 Genomic DNA. Translation: AAS56426.1 .
BK006941 Genomic DNA. Translation: DAA08293.1 .
PIRi S53923.
RefSeqi NP_011716.3. NM_001181329.3.

3D structure databases

ProteinModelPortali P42935.
SMRi P42935. Positions 27-310, 387-413.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33453. 287 interactions.
DIPi DIP-2386N.
IntActi P42935. 15 interactions.
MINTi MINT-613845.
STRINGi 4932.YGR200C.

Proteomic databases

MaxQBi P42935.
PaxDbi P42935.
PeptideAtlasi P42935.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR200C ; YGR200C ; YGR200C .
GeneIDi 853114.
KEGGi sce:YGR200C.

Organism-specific databases

CYGDi YGR200c.
SGDi S000003432. ELP2.

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00390000000916.
HOGENOMi HOG000200623.
InParanoidi P42935.
KOi K11374.
OMAi DQVPEIN.
OrthoDBi EOG7TQV9M.

Enzyme and pathway databases

BioCyci YEAST:G3O-30885-MONOMER.

Miscellaneous databases

NextBioi 973136.
PROi P42935.

Gene expression databases

Genevestigatori P42935.

Family and domain databases

Gene3Di 2.130.10.10. 3 hits.
InterProi IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF00400. WD40. 8 hits.
[Graphical view ]
SMARTi SM00320. WD40. 11 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 4 hits.
PROSITEi PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the yeast PMT and EF1G genes, of the human and bacterial electron-transferring flavoproteins (beta-chain) and of the Escherichia coli phosphoserine phosphohydrolase, and five new ORFs."
    Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A., Rodrigues-Pousada C.
    Yeast 12:273-280(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "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.
  6. "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.
  7. "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.
  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. "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 IKI3.
  10. "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.
  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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  14. "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.
  15. "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, SUBCELLULAR LOCATION.
  16. "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 nameiELP2_YEAST
AccessioniPrimary (citable) accession number: P42935
Secondary accession number(s): D6VUY2, E9P8V1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 131 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 6090 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3