UniProt functional annotation for P42935



	UniProt functional annotation for P42935

UniProt code: P42935.

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

Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.

Function: Component of the RNA polymerase II elongator complex, a multiprotein complex associated with the RNA polymerase II (Pol II) holoenzyme, and which is involved in transcriptional elongation (PubMed:10024884, PubMed:11296232, PubMed:11689709, PubMed:11904415). The elongator complex is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5- methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:15769872, PubMed:18755837). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:29332244). It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin) (PubMed:11904415). May also be involved in sensitivity to Pichia inositovora toxin (PubMed:13680368). Independently, ELP2 may be involved in polarized exocytosis (PubMed:15138274, PubMed:15780940). {ECO:0000269|PubMed:10024884, ECO:0000269|PubMed:11296232, ECO:0000269|PubMed:11689709, ECO:0000269|PubMed:11904415, ECO:0000269|PubMed:13680368, ECO:0000269|PubMed:15138274, ECO:0000269|PubMed:15769872, ECO:0000269|PubMed:15780940, ECO:0000269|PubMed:18755837, ECO:0000303|PubMed:29332244}.

Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000269|PubMed:15769872, ECO:0000269|PubMed:18755837}.

Subunit: Component of the RNA polymerase II elongator complex, which consists of ELP1/IKI3, ELP2, ELP3, ELP4, ELP5/IKI1 and ELP6 (PubMed:11435442, PubMed:11689709, PubMed:27974378, PubMed:27872205). The elongator complex is composed of two copies of the Elp123 subcomplex (composed of ELP1/IKI3, ELP2 and ELP3) and two copies of the Elp456 subcomplex (composed of ELP4, ELP5/IKI1 and ELP6) (PubMed:27974378, PubMed:27872205). The Elp123 subcomplex forms a two- lobed scaffold, which binds the Elp456 subcomplex asymmetrically (PubMed:27974378, PubMed:27872205). In the complex, ELP2 interacts with ELP1/IKI3 (PubMed:12139626). {ECO:0000269|PubMed:11435442, ECO:0000269|PubMed:11689709, ECO:0000269|PubMed:12139626, ECO:0000269|PubMed:27872205, ECO:0000269|PubMed:27974378}.

Subcellular location: Cytoplasm. Nucleus.

Miscellaneous: Present with 6090 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.

Similarity: Belongs to the WD repeat ELP2 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Taxonomy:		Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.



Function:		Component of the RNA polymerase II elongator complex, a multiprotein complex associated with the RNA polymerase II (Pol II) holoenzyme, and which is involved in transcriptional elongation (PubMed:10024884, PubMed:11296232, PubMed:11689709, PubMed:11904415). The elongator complex is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5- methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:15769872, PubMed:18755837). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:29332244). It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin) (PubMed:11904415). May also be involved in sensitivity to Pichia inositovora toxin (PubMed:13680368). Independently, ELP2 may be involved in polarized exocytosis (PubMed:15138274, PubMed:15780940). {ECO:0000269\|PubMed:10024884, ECO:0000269\|PubMed:11296232, ECO:0000269\|PubMed:11689709, ECO:0000269\|PubMed:11904415, ECO:0000269\|PubMed:13680368, ECO:0000269\|PubMed:15138274, ECO:0000269\|PubMed:15769872, ECO:0000269\|PubMed:15780940, ECO:0000269\|PubMed:18755837, ECO:0000303\|PubMed:29332244}.


Pathway:		tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000269\|PubMed:15769872, ECO:0000269\|PubMed:18755837}.
Subunit:		Component of the RNA polymerase II elongator complex, which consists of ELP1/IKI3, ELP2, ELP3, ELP4, ELP5/IKI1 and ELP6 (PubMed:11435442, PubMed:11689709, PubMed:27974378, PubMed:27872205). The elongator complex is composed of two copies of the Elp123 subcomplex (composed of ELP1/IKI3, ELP2 and ELP3) and two copies of the Elp456 subcomplex (composed of ELP4, ELP5/IKI1 and ELP6) (PubMed:27974378, PubMed:27872205). The Elp123 subcomplex forms a two- lobed scaffold, which binds the Elp456 subcomplex asymmetrically (PubMed:27974378, PubMed:27872205). In the complex, ELP2 interacts with ELP1/IKI3 (PubMed:12139626). {ECO:0000269\|PubMed:11435442, ECO:0000269\|PubMed:11689709, ECO:0000269\|PubMed:12139626, ECO:0000269\|PubMed:27872205, ECO:0000269\|PubMed:27974378}.
Subcellular location:		Cytoplasm. Nucleus.
Miscellaneous:		Present with 6090 molecules/cell in log phase SD medium. {ECO:0000269\|PubMed:14562106}.
Similarity:		Belongs to the WD repeat ELP2 family. {ECO:0000305}.