ELP3

ELP3 is the catalytic subunit of the histone acetyltransferase elongator complex, which contributes to transcript elongation and also regulates the maturation of projection neurons (Creppe et al., 2009 [PubMed 19185337]).[supplied by OMIM, Apr 2009]

Full Name

Elongator Acetyltransferase Complex Subunit 3

Research Area

Catalytic tRNA acetyltransferase subunit of the RNA polymerase II elongator complex, which is a component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation (PubMed:11714725, PubMed:11818576, PubMed:15902492, PubMed:16713582).

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:29415125).

In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity).

May also act as a protein lysine acetyltransferase by mediating acetylation of target proteins; such activity is however unclear in vivo and recent evidences suggest that ELP3 primarily acts as a tRNA acetyltransferase (PubMed:29415125).

Involved in neurogenesis: regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation (PubMed:19185337).

Required for acetylation of GJA1 in the developing cerebral cortex (By similarity).

Biological Process

Central nervous system development Source: UniProtKB
Neuron migration Source: UniProtKB
Positive regulation of cell migration Source: UniProtKB
Regulation of transcription by RNA polymerase II Source: UniProtKB
tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation Source: GO_Central
tRNA wobble uridine modification Source: UniProtKB

Cellular Location

Nucleus; Cytoplasm
Isoform 1: Nucleus
Isoform 2: Nucleus; Cytoplasm

Involvement in disease

Amyotrophic lateral sclerosis (ALS):
A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.