CPLM-011005

Genbank Nucleotide ID

Elongator complex protein 3

Protein Synonyms/Alias

Gamma-toxin target 3

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Position	Peptide	Type	References
289	VSKDAGYKVVSHMMP	acetylation	[1]
325	DFRTDGLKIYPTLVI	acetylation	[1]
423	GIQEVHHKVQPDQVE	acetylation	[1]
453	LSYEDPKKDILIGLL	ubiquitination	[2, 3, 4]
543	GVRNYYGKLGYELDG	acetylation	[1]
543	GVRNYYGKLGYELDG	ubiquitination	[5]

[1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
[2] A proteomics approach to understanding protein ubiquitination.
Peng J, Schwartz D, Elias JE, Thoreen CC, Cheng D, Marsischky G, Roelofs J, Finley D, Gygi SP.
Nat Biotechnol. 2003 Aug;21(8):921-6. [PMID: 12872131]
[3] Computational identification of ubiquitylation sites from protein sequences.
Tung CW, Ho SY.
BMC Bioinformatics. 2008 Jul 15;9:310. [PMID: 18625080]
[4] Identification, analysis, and prediction of protein ubiquitination sites.
Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269]
[5] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]

Functional Description

Acts as catalytic subunit of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (Pol II) 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. ELP3 is required for the complex integrity and for the association of the complex with nascent RNA transcript. Independently, ELP3 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.

DOMAIN 405 557 N-acetyltransferase.
METAL 108 108 Iron-sulfur (4Fe-4S-S-AdoMet) (Probable).
METAL 118 118 Iron-sulfur (4Fe-4S-S-AdoMet) (Probable).
METAL 121 121 Iron-sulfur (4Fe-4S-S-AdoMet) (Probable).
CROSSLNK 453 453 Glycyl lysine isopeptide (Lys-Gly)

Acyltransferase; Chromatin regulator; Complete proteome; Cytoplasm; Iron; Iron-sulfur; Isopeptide bond; Metal-binding; Nucleus; Protein transport; Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription; Transcription regulation; Transferase; Transport; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:SGD.
GO:0033588; C:Elongator holoenzyme complex; IDA:SGD.
GO:0005634; C:nucleus; IDA:SGD.
GO:0004402; F:histone acetyltransferase activity; IDA:SGD.
GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:SGD.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0002098; P:tRNA wobble uridine modification; IMP:SGD.

IPR016181; Acyl_CoA_acyltransferase.
IPR006638; Elp3/MiaB/NifB.
IPR000182; GNAT_dom.
IPR005910; Hist_AcTrfase_ELP3.
IPR007197; rSAM.
IPR023404; rSAM_horseshoe.

PF00583; Acetyltransf_1
PF04055; Radical_SAM