ULK2

This gene encodes a protein that is similar to a serine/threonine kinase in C. elegans which is involved in axonal elongation. The structure of this protein is similar to the C. elegans protein in that both proteins have an N-terminal kinase domain, a central proline/serine rich (PS) domain, and a C-terminal (C) domain. The gene is located within the Smith-Magenis syndrome region on chromosome 17. Alternatively spliced transcript variants encoding the same protein have been identified. [provided by RefSeq]

unc-51-like kinase 2 (C. elegans)

Serine/threonine-protein kinase involved in autophagy in response to starvation. Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes. Part of regulatory feedback loops in autophagy: acts both as a downstream effector and a negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK, also acts as a negative regulator of AMPK through phosphorylation of the AMPK subunits PRKAA1, PRKAB2 and PRKAG1. May phosphorylate ATG13/KIAA0652, FRS2, FRS3 and RPTOR; however such data need additional evidences. Not involved in ammonia-induced autophagy or in autophagic response of cerebellar granule neurons (CGN) to low potassium concentration. Plays a role early in neuronal differentiation and is required for granule cell axon formation: may govern axon formation via Ras-like GTPase signaling and through regulation of the Rab5-mediated endocytic pathways within developing axons.

Biological Process autophagosome assembly Source:GO_Central1 Publication
Biological Process autophagy Source:GO_Central1 Publication
Biological Process autophagy of mitochondrion Source:GO_Central1 Publication
Biological Process axon extension Source:GO_Central1 Publication
Biological Process collateral sprouting Source:Ensembl
Biological Process late nucleophagy Source:GO_Central1 Publication
Biological Process negative regulation of collateral sprouting Source:GO_Central1 Publication
Biological Process peptidyl-serine phosphorylation Source:GO_Central1 Publication
Biological Process piecemeal microautophagy of the nucleus Source:GO_Central1 Publication
Biological Process positive regulation of autophagy Source:GO_Central1 Publication
Biological Process protein autophosphorylation Source:UniProtKB1 Publication
Biological Process response to starvation Source:UniProtKB
Biological Process reticulophagy Source:GO_Central1 Publication
Biological Process signal transduction Source:InterPro

Cytoplasmic vesicle membrane
Localizes to pre-autophagosomal membrane.

Autophosphorylated. In response to nutrient limitation, probably phosphorylated and activated by AMPK, leading to activate autophagy.