Q9QY01 · ULK2_MOUSE
- ProteinSerine/threonine-protein kinase ULK2
- GeneUlk2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1037 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | autophagosome | |
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic vesicle membrane | |
Cellular Component | cytosol | |
Cellular Component | phagophore assembly site | |
Cellular Component | phagophore assembly site membrane | |
Molecular Function | ATP binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | autophagosome assembly | |
Biological Process | autophagy | |
Biological Process | autophagy of mitochondrion | |
Biological Process | axon extension | |
Biological Process | axon guidance | |
Biological Process | collateral sprouting | |
Biological Process | negative regulation of collateral sprouting | |
Biological Process | piecemeal microautophagy of the nucleus | |
Biological Process | positive regulation of autophagy | |
Biological Process | protein localization | |
Biological Process | response to starvation | |
Biological Process | reticulophagy | |
Biological Process | signal transduction | |
Biological Process | somatic sensory system development |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase ULK2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9QY01
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle membrane ; Peripheral membrane protein
Note: Localizes to pre-autophagosomal membrane.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 39 | Decreased kinase activity. | ||||
Sequence: K → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 25 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000086783 | 1-1037 | Serine/threonine-protein kinase ULK2 | |||
Sequence: MEVVGDFEYCKRDLVGHGAFAVVFRGRHRQKTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQELPNSVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLHQIAAAMRILHSKGIIHRDLKPQNILLSYANRRKSNVSGIRIKIADFGFARYLHSNTMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNRSLMPSIPRETSPYLANLLLGLLQRNQKDRMDFEAFFSHPFLEQVPVKKSCPVPVPVYSGPVPGSSCSSSPSCRFASPPSLPDMQHIQEENLSSPPLGPPNYLQVSKDSASNSSKNSSCDTDDFVLVPHNISSDHSYDMPMGTTARRASNEFFMCGGQCQPTVSPHSETAPIPVPTQVRNYQRIEQNLISTASSGTNPHGSPRSAVVRRSNTSPMGFLRVGSCSPVPGDTVQTGGRRLSTGSSRPYSPSPLVGTIPEQFSQCCCGHPQGHEARSRHSSGSPVPQTQAPQSLLLGARLQSAPTLTDIYQNKQKLRKQHSDPVCPSHAGAGYSYSPQPSRPGSLGTSPTKHTGSSPRNSDWFFKTPLPTIIGSPTKTTAPFKIPKTQASSNLLALVTRHGPAESQSKDGNDPRECSHCLSVQGSERHRSEQQQSKAVFGRSVSTGKLSEQQVKAPLGGHQGSTDSLNTERPMDVAPAGACGVMLALPAGTAASARAVLFTVGSPPHSATAPTCTHMVLRTRTTSVGSSSSGGSLCSASGRVCVGSPPGPGLGSSPPGAEGAPSLRYVPYGASPPSLEGLITFEAPELPEETLMEREHTDTLRHLNMMLMFTECVLDLTAVRGGNPELCTSAVSLYQIQESVVVDQISQLSKDWGRVEQLVLYMKAAQLLAASLHLAKAQVKSGKLSPSMAVKQVVKNLNERYKFCITMCKKLTEKLNRFFSDKQRFIDEINSVTAEKLIYNCAVEMVQSAALDEMFQQTEDIVYRYHKAALLLEGLSKILQDPTDVENVHKYKCSIERRLSALCCSTATV | ||||||
Modified residue | 430 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 772 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 781 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Autophosphorylated. In response to nutrient limitation, probably phosphorylated and activated by AMPK, leading to activate autophagy.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of a complex consisting of ATG13/KIAA0652, ULK1 and RB1CC1/FIP200. Interacts (via C-terminus) with ATG13/KIAA0652. Associates with the mammalian target of rapamycin complex 1 (mTORC1) through an interaction with RPTOR (By similarity).
Interacts with SYNGAP1
Interacts with SYNGAP1
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 9-271 | Protein kinase | ||||
Sequence: YCKRDLVGHGAFAVVFRGRHRQKTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQELPNSVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLHQIAAAMRILHSKGIIHRDLKPQNILLSYANRRKSNVSGIRIKIADFGFARYLHSNTMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNRSLMPSIPRETSPYLANLLLGLLQRNQKDRMDFEAFFSHPFL | ||||||
Region | 319-350 | Disordered | ||||
Sequence: ENLSSPPLGPPNYLQVSKDSASNSSKNSSCDT | ||||||
Region | 452-480 | Disordered | ||||
Sequence: CSPVPGDTVQTGGRRLSTGSSRPYSPSPL | ||||||
Compositional bias | 455-480 | Polar residues | ||||
Sequence: VPGDTVQTGGRRLSTGSSRPYSPSPL | ||||||
Region | 494-515 | Disordered | ||||
Sequence: GHPQGHEARSRHSSGSPVPQTQ | ||||||
Region | 540-594 | Disordered | ||||
Sequence: QKLRKQHSDPVCPSHAGAGYSYSPQPSRPGSLGTSPTKHTGSSPRNSDWFFKTPL | ||||||
Compositional bias | 559-589 | Polar residues | ||||
Sequence: YSYSPQPSRPGSLGTSPTKHTGSSPRNSDWF | ||||||
Region | 626-697 | Disordered | ||||
Sequence: HGPAESQSKDGNDPRECSHCLSVQGSERHRSEQQQSKAVFGRSVSTGKLSEQQVKAPLGGHQGSTDSLNTER | ||||||
Compositional bias | 631-660 | Basic and acidic residues | ||||
Sequence: SQSKDGNDPRECSHCLSVQGSERHRSEQQQ | ||||||
Compositional bias | 661-696 | Polar residues | ||||
Sequence: SKAVFGRSVSTGKLSEQQVKAPLGGHQGSTDSLNTE | ||||||
Region | 813-1037 | CTD-like region | ||||
Sequence: ELPEETLMEREHTDTLRHLNMMLMFTECVLDLTAVRGGNPELCTSAVSLYQIQESVVVDQISQLSKDWGRVEQLVLYMKAAQLLAASLHLAKAQVKSGKLSPSMAVKQVVKNLNERYKFCITMCKKLTEKLNRFFSDKQRFIDEINSVTAEKLIYNCAVEMVQSAALDEMFQQTEDIVYRYHKAALLLEGLSKILQDPTDVENVHKYKCSIERRLSALCCSTATV |
Domain
The CTD-like region mediates membrane-binding and incorporation into large protein complexes.
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. APG1/unc-51/ULK1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,037
- Mass (Da)112,877
- Last updated2000-05-01 v1
- Checksum2E7DC3B0B87E9607
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 455-480 | Polar residues | ||||
Sequence: VPGDTVQTGGRRLSTGSSRPYSPSPL | ||||||
Compositional bias | 559-589 | Polar residues | ||||
Sequence: YSYSPQPSRPGSLGTSPTKHTGSSPRNSDWF | ||||||
Compositional bias | 631-660 | Basic and acidic residues | ||||
Sequence: SQSKDGNDPRECSHCLSVQGSERHRSEQQQ | ||||||
Compositional bias | 661-696 | Polar residues | ||||
Sequence: SKAVFGRSVSTGKLSEQQVKAPLGGHQGSTDSLNTE | ||||||
Sequence conflict | 998 | in Ref. 2; BAA77341 | ||||
Sequence: L → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF145922 EMBL· GenBank· DDBJ | AAF18325.1 EMBL· GenBank· DDBJ | mRNA | ||
AB019577 EMBL· GenBank· DDBJ | BAA77341.1 EMBL· GenBank· DDBJ | mRNA | ||
AK146620 EMBL· GenBank· DDBJ | BAE27309.1 EMBL· GenBank· DDBJ | mRNA | ||
AK122331 EMBL· GenBank· DDBJ | BAC65613.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC046778 EMBL· GenBank· DDBJ | AAH46778.1 EMBL· GenBank· DDBJ | mRNA | ||
BC053029 EMBL· GenBank· DDBJ | AAH53029.1 EMBL· GenBank· DDBJ | mRNA |