Q23023 · UNC51_CAEEL

  • Protein
    Serine/threonine-protein kinase unc-51
  • Gene
    unc-51
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site15-23ATP (UniProtKB | ChEBI)
Binding site39ATP (UniProtKB | ChEBI)
Active site134Proton acceptor
Site357Required for interaction with lgg-1

GO annotations

AspectTerm
Cellular Componentautophagosome
Cellular Componentaxon
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentneuron projection
Cellular Componentneuronal cell body
Cellular Componentphagophore assembly site
Cellular Componentphagophore assembly site membrane
Cellular Componentserine/threonine protein kinase complex
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionprotein kinase activity
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Biological Processapoptotic cell clearance
Biological Processautophagosome assembly
Biological Processautophagy
Biological Processautophagy of mitochondrion
Biological Processaxon extension
Biological Processaxon guidance
Biological Processaxonogenesis
Biological Processcell migration
Biological Processdauer larval development
Biological Processdetermination of adult lifespan
Biological Processembryo development ending in birth or egg hatching
Biological Processmacroautophagy
Biological Processnematode male tail tip morphogenesis
Biological Processpiecemeal microautophagy of the nucleus
Biological Processpositive regulation of autophagy
Biological Processprogrammed cell death
Biological Processregulation of axon extension
Biological Processregulation of cell size
Biological Processregulation of multicellular organism growth
Biological Processregulation of protein localization
Biological Processresponse to starvation
Biological Processreticulophagy

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine/threonine-protein kinase unc-51
  • EC number
  • Alternative names
    • Uncoordinated protein 51

Gene names

    • Name
      unc-51
    • ORF names
      Y60A3A.1

Organism names

  • Taxonomic identifier
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    Q23023

Proteomes

Organism-specific databases

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).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis37-41Abrogates kinase activity.
Mutagenesis39In KSEX9; variable effects.
Mutagenesis39Impairs kinase activity.
Mutagenesis358Impairs the interaction with lgg-1.
Mutagenesis360Impairs the interaction with lgg-1.
Mutagenesis841In E1120; paralyzed, egg laying defective and dumpy.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000867851-856Serine/threonine-protein kinase unc-51

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

    • WBGene00006786Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues

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).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q23023unc-14 G5ECQ14EBI-329049, EBI-2419199
BINARY Q23023vab-8 Q214414EBI-329049, EBI-2412191

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, motif, compositional bias.

TypeIDPosition(s)Description
Domain9-275Protein kinase
Region304-327Disordered
Motif358-361LIR
Region362-391Disordered
Region405-471Disordered
Compositional bias411-442Polar residues
Compositional bias520-537Polar residues
Region520-582Disordered
Compositional bias548-582Polar residues
Region750-856Required for interaction with unc-14 and vab-8

Domain

The LIR motif (LC3-interacting region) is required for its interaction with lgg-1.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    856
  • Mass (Da)
    94,893
  • Last updated
    1996-11-01 v1
  • Checksum
    721F6F6FB0399F6E
MEQFDGFEYSKRDLLGHGAFAIVYRGRYVDRTDVPVAIKAIAKKNISKSKNLLTKEIKILKELSSLKHENLVGLLKCTETPTHVYLVMEFCNGGDLADYLQQKTTLNEDTIQHFVVQIAHALEAINKKGIVHRDLKPQNILLCNNSRTQNPHFTDIVIKLADFGFARFLNDGVMAATLCGSPMYMAPEVIMSMQYDAKADLWSIGTILFQCLTGKAPFVAQTPPQLKAYYEKTRELRPNIPEWCSPNLRDLLLRLLKRNAKDRISFEDFFNHPFLTSPLLPSPSKRILESARSPLLANRRIITPQSSLPVPKRAGSTKLDSPTPVRRIGESPRVQRRVITPGMPSPVPGAPMQESTDFTFLPPRQESSPVKQVQVHTNVSPSLTTCKPVPVPSQRLTYQKMEERLAAARKTAVPSSSSPTGSAVSAQHQHQHQQQQEPASSPVVQRIERPDQLPRRTTLQDPNAHDIERMTMPNPTFVVCGSSTKPSPNNANRVRRSTITSPADTQDMVAADQMLSNLDPTTTTTTIPKSATTANIQGIPRGARDRSVTSPPQPTIHENEPLDNAKYQQTDVNNSPTAPTEPFIIKNQTTCSTSSTSSSVVEEEEAMSLPFASGSHLAAGFKKTPAEVPMDHGALPPALDQEIVLGEEHKQILAKLRFVAELVDTLIHVAEQKDNPLASAMASRRQLLTTGTSTTNTSSPYRRAEQLVVYVRALHMLSSALLLAQTNVANRVLHPSVAVQQVLNQLNDKYHQCLVRSQELASLGLPGQDPAMAVISAERIMYRHAIELCQAAALDELFGNPQLCSQRYQTAYMMLHTLAEQVNCDQDKTVLTRYKVAVEKRLRILERQGFVAAVNT

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias411-442Polar residues
Compositional bias520-537Polar residues
Compositional bias548-582Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z38016
EMBL· GenBank· DDBJ
CAA86114.1
EMBL· GenBank· DDBJ
mRNA
BX284605
EMBL· GenBank· DDBJ
CAB60406.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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