Q23023 · UNC51_CAEEL
- ProteinSerine/threonine-protein kinase unc-51
- Geneunc-51
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids856 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Protein kinase important for axonal elongation and axonal guidance (PubMed:15539493, PubMed:7958904).
Functions in the CAN axons to direct both anterior and posterior migrations (PubMed:15539493).
Phosphorylates both unc-14 and vab-8 (PubMed:15539493).
Component of the unc-51/atg-13 complex that is probably recruited by lgg-1 to preautophagosomes and is required for autophagosome formation (PubMed:12958363, PubMed:17890369, PubMed:19377305, PubMed:26687600).
Interaction with autophagy related proteins such as atg-13 links it to the autophagy machinery to in turn promote P-granule degradation in somatic cells (PubMed:19377305).
Plays a role in mitophagy during limited food availability (PubMed:30133321).
Regulates cell size (PubMed:17890369).
Plays a role in male tail ray pattern formation (PubMed:17890369).
May be required for normal dauer morphogenesis (PubMed:12958363).
Functions in the CAN axons to direct both anterior and posterior migrations (PubMed:15539493).
Phosphorylates both unc-14 and vab-8 (PubMed:15539493).
Component of the unc-51/atg-13 complex that is probably recruited by lgg-1 to preautophagosomes and is required for autophagosome formation (PubMed:12958363, PubMed:17890369, PubMed:19377305, PubMed:26687600).
Interaction with autophagy related proteins such as atg-13 links it to the autophagy machinery to in turn promote P-granule degradation in somatic cells (PubMed:19377305).
Plays a role in mitophagy during limited food availability (PubMed:30133321).
Regulates cell size (PubMed:17890369).
Plays a role in male tail ray pattern formation (PubMed:17890369).
May be required for normal dauer morphogenesis (PubMed:12958363).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Features
Showing features for binding site, active site, site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase unc-51
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionQ23023
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Worms exhibit various abnormalities in axonal elongation and axonal structures (PubMed:7958904).
RNAi-mediated knockdown causes abnormalities in constitutive dauer formation in daf-2 e1370 mutant including a lack of autophagosome formation (PubMed:12958363).
RNAi-mediated knockdown causes abnormalities in constitutive dauer formation in daf-2 e1370 mutant including a lack of autophagosome formation (PubMed:12958363).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 37-41 | Abrogates kinase activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 39 | In KSEX9; variable effects. | ||||
Sequence: K → M | ||||||
Mutagenesis | 39 | Impairs kinase activity. | ||||
Sequence: K → R | ||||||
Mutagenesis | 358 | Impairs the interaction with lgg-1. | ||||
Sequence: F → A | ||||||
Mutagenesis | 360 | Impairs the interaction with lgg-1. | ||||
Sequence: F → A | ||||||
Mutagenesis | 841 | In E1120; paralyzed, egg laying defective and dumpy. | ||||
Sequence: R → H |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000086785 | 1-856 | Serine/threonine-protein kinase unc-51 | |||
Sequence: MEQFDGFEYSKRDLLGHGAFAIVYRGRYVDRTDVPVAIKAIAKKNISKSKNLLTKEIKILKELSSLKHENLVGLLKCTETPTHVYLVMEFCNGGDLADYLQQKTTLNEDTIQHFVVQIAHALEAINKKGIVHRDLKPQNILLCNNSRTQNPHFTDIVIKLADFGFARFLNDGVMAATLCGSPMYMAPEVIMSMQYDAKADLWSIGTILFQCLTGKAPFVAQTPPQLKAYYEKTRELRPNIPEWCSPNLRDLLLRLLKRNAKDRISFEDFFNHPFLTSPLLPSPSKRILESARSPLLANRRIITPQSSLPVPKRAGSTKLDSPTPVRRIGESPRVQRRVITPGMPSPVPGAPMQESTDFTFLPPRQESSPVKQVQVHTNVSPSLTTCKPVPVPSQRLTYQKMEERLAAARKTAVPSSSSPTGSAVSAQHQHQHQQQQEPASSPVVQRIERPDQLPRRTTLQDPNAHDIERMTMPNPTFVVCGSSTKPSPNNANRVRRSTITSPADTQDMVAADQMLSNLDPTTTTTTIPKSATTANIQGIPRGARDRSVTSPPQPTIHENEPLDNAKYQQTDVNNSPTAPTEPFIIKNQTTCSTSSTSSSVVEEEEAMSLPFASGSHLAAGFKKTPAEVPMDHGALPPALDQEIVLGEEHKQILAKLRFVAELVDTLIHVAEQKDNPLASAMASRRQLLTTGTSTTNTSSPYRRAEQLVVYVRALHMLSSALLLAQTNVANRVLHPSVAVQQVLNQLNDKYHQCLVRSQELASLGLPGQDPAMAVISAERIMYRHAIELCQAAALDELFGNPQLCSQRYQTAYMMLHTLAEQVNCDQDKTVLTRYKVAVEKRLRILERQGFVAAVNT |
Proteomic databases
PTM databases
Expression
Developmental stage
During embryonic development unc-51 is expressed extensively, particularly in the head region of late embryos. In the larval stages, expression appears to be restricted to neurons.
Gene expression databases
Interaction
Subunit
Interacts with unc-14 and vab-8 (PubMed:15539493).
Interacts (via C-terminus) with atg-13 (PubMed:19377305).
Interacts (via the LIR motif) with lgg-1; the interaction is direct (PubMed:26687600).
Interacts (via C-terminus) with atg-13 (PubMed:19377305).
Interacts (via the LIR motif) with lgg-1; the interaction is direct (PubMed:26687600).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q23023 | unc-14 G5ECQ1 | 4 | EBI-329049, EBI-2419199 | |
BINARY | Q23023 | vab-8 Q21441 | 4 | EBI-329049, EBI-2412191 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 9-275 | Protein kinase | ||||
Sequence: YSKRDLLGHGAFAIVYRGRYVDRTDVPVAIKAIAKKNISKSKNLLTKEIKILKELSSLKHENLVGLLKCTETPTHVYLVMEFCNGGDLADYLQQKTTLNEDTIQHFVVQIAHALEAINKKGIVHRDLKPQNILLCNNSRTQNPHFTDIVIKLADFGFARFLNDGVMAATLCGSPMYMAPEVIMSMQYDAKADLWSIGTILFQCLTGKAPFVAQTPPQLKAYYEKTRELRPNIPEWCSPNLRDLLLRLLKRNAKDRISFEDFFNHPFL | ||||||
Region | 304-327 | Disordered | ||||
Sequence: PQSSLPVPKRAGSTKLDSPTPVRR | ||||||
Motif | 358-361 | LIR | ||||
Sequence: FTFL | ||||||
Region | 362-391 | Disordered | ||||
Sequence: PPRQESSPVKQVQVHTNVSPSLTTCKPVPV | ||||||
Region | 405-471 | Disordered | ||||
Sequence: LAAARKTAVPSSSSPTGSAVSAQHQHQHQQQQEPASSPVVQRIERPDQLPRRTTLQDPNAHDIERMT | ||||||
Compositional bias | 411-442 | Polar residues | ||||
Sequence: TAVPSSSSPTGSAVSAQHQHQHQQQQEPASSP | ||||||
Compositional bias | 520-537 | Polar residues | ||||
Sequence: PTTTTTTIPKSATTANIQ | ||||||
Region | 520-582 | Disordered | ||||
Sequence: PTTTTTTIPKSATTANIQGIPRGARDRSVTSPPQPTIHENEPLDNAKYQQTDVNNSPTAPTEP | ||||||
Compositional bias | 548-582 | Polar residues | ||||
Sequence: VTSPPQPTIHENEPLDNAKYQQTDVNNSPTAPTEP | ||||||
Region | 750-856 | Required for interaction with unc-14 and vab-8 | ||||
Sequence: YHQCLVRSQELASLGLPGQDPAMAVISAERIMYRHAIELCQAAALDELFGNPQLCSQRYQTAYMMLHTLAEQVNCDQDKTVLTRYKVAVEKRLRILERQGFVAAVNT |
Domain
The LIR motif (LC3-interacting region) is required for its interaction with lgg-1.
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
- Length856
- Mass (Da)94,893
- Last updated1996-11-01 v1
- Checksum721F6F6FB0399F6E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 411-442 | Polar residues | ||||
Sequence: TAVPSSSSPTGSAVSAQHQHQHQQQQEPASSP | ||||||
Compositional bias | 520-537 | Polar residues | ||||
Sequence: PTTTTTTIPKSATTANIQ | ||||||
Compositional bias | 548-582 | Polar residues | ||||
Sequence: VTSPPQPTIHENEPLDNAKYQQTDVNNSPTAPTEP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z38016 EMBL· GenBank· DDBJ | CAA86114.1 EMBL· GenBank· DDBJ | mRNA | ||
BX284605 EMBL· GenBank· DDBJ | CAB60406.1 EMBL· GenBank· DDBJ | Genomic DNA |