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IID00987
 UniprotQ6ZNE5
ProteinBeclin 1-associated autophagy-related key regulator
GeneATG14
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
492
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 429-443 Hetero tetramer : IID01017Complex
 Evidence X-RAY 6hol C Reference
       Region 6hol C 429-433 disorder
       Region 6hol C 434-443 order
 Evidence X-RAY 6hol D Reference
       Region 6hol D 429-433 disorder
       Region 6hol D 434-443 order
SeqProS predicted 434-443 This region is predicted to be disordered by NeProc and AlphaFold (pLDDT < 68.5). Hetero tetramer : IID01017Complex
       Region 6hol C 434-443 order
       Region 6hol D 434-443 order
Seqphosphorylation
    416-416 Phosphoserine
    429-429 Phosphothreonine
    29-29 Phosphoserine
 
Prediction
NeProc
Disorder 1-21,218-229,291-303,406-481,488-492
Order 22-217,230-290,304-405,482-487
ProS 18-21,218-229,297-303,406-413,429-453,471-481,488-492
AlphaFold
Disorder 1-45,47-54,67-67,69-69,213-231,241-258,289-297,405-434,438-492
Order 46-46,55-66,68-68,70-212,232-240,259-288,298-404,435-437
SEG 220-235 ,448-480
Function
Function in SwissProt
Required for both basal and inducible autophagy. Determines the localization of the autophagy-specific PI3-kinase complex PI3KC3-C1 (PubMed:18843052, PubMed:19050071). Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine (PubMed:19270696, PubMed:20713597). Promotes BECN1 translocation from the trans-Golgi network to autophagosomes (PubMed:20713597). Enhances PIK3C3 activity in a BECN1-dependent manner. Essential for the autophagy-dependent phosphorylation of BECN1 (PubMed:23878393). Stimulates the phosphorylation of BECN1, but suppresses the phosphorylation PIK3C3 by AMPK (PubMed:23878393). Binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP8 interaction to promote autophagosome-endolysosome fusion (PubMed:25686604, PubMed:37632749). Modulates the hepatic lipid metabolism (By similarity).