Q6ZNE5 · BAKOR_HUMAN
- ProteinBeclin 1-associated autophagy-related key regulator
- GeneATG14
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids492 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
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).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBeclin 1-associated autophagy-related key regulator
- Short namesBarkor
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6ZNE5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Peripheral membrane protein
Preautophagosomal structure membrane ; Peripheral membrane protein
Cytoplasmic vesicle, autophagosome membrane ; Peripheral membrane protein
Note: Cytosolic under nutrient-rich conditions (PubMed:19050071).
Following autophagy stimuli, such as starvation or rapamycin induction, predominantly detected in cytoplasmic foci, identified as isolation membranes and autophagosomes (PubMed:19050071).
Accumulates on highly curved PtdIns3P enriched autophagic membrane via its BATS domain to sense and maintain membrane curvature (By similarity).
Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme (By similarity).
Following autophagy stimuli, such as starvation or rapamycin induction, predominantly detected in cytoplasmic foci, identified as isolation membranes and autophagosomes (PubMed:19050071).
Accumulates on highly curved PtdIns3P enriched autophagic membrane via its BATS domain to sense and maintain membrane curvature (By similarity).
Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme (By similarity).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 43 | In Atg14L4C4A; fails to localize to the endoplasmic reticulum; when associated with A-46; A-55 and A-58. | ||||
Sequence: C → A | ||||||
Mutagenesis | 46 | In Atg14L4C4A; fails to localize to the endoplasmic reticulum; when associated with A-43; A-55 and A-58. | ||||
Sequence: C → A | ||||||
Mutagenesis | 55 | In Atg14L4C4A; fails to localize to the endoplasmic reticulum; when associated with A-43; A-46 and A-58. | ||||
Sequence: C → A | ||||||
Mutagenesis | 58 | In Atg14L4C4A; fails to localize to the endoplasmic reticulum; when associated with A-43; A-46 and A-55. | ||||
Sequence: C → A | ||||||
Natural variant | VAR_061240 | 59 | in dbSNP:rs57295720 | |||
Sequence: V → I | ||||||
Natural variant | VAR_049514 | 131 | in dbSNP:rs17675076 | |||
Sequence: N → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 561 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000050774 | 1-492 | UniProt | Beclin 1-associated autophagy-related key regulator | |||
Sequence: MASPSGKGARALEAPGCGPRPLARDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCVQSGDFVYFDGRDRERFIDKKERLSRLKSKQEEFQKEVLKAMEGKWITDQLRWKIMSCKMRIEQLKQTICKGNEEMEKNSEGLLKTKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKTIDLRSHYERLANLRRSHILELTSVIFPIEEVKTGVRDPADVSSESDSAMTSSTVSKLAEARRTTYLSGRWVCDDHNGDTSISITGPWISLPNNGDYSAYYSWVEEKKTTQGPDMEQSNPAYTISAALCYATQLVNILSHILDVNLPKKLCNSEFCGENLSKQKFTRAVKKLNANILYLCFSQHVNLDQLQPLHTLRNLMYLVSPSSEHLGRSGPFEVRADLEESMEFVDPGVAGESDESGDERVSDEETDLGTDWENLPSPRFCDIPSQSVEVSQSQSTQASPPIASSSAGGMISSAAASVTSWFKAYTGHR | |||||||
Modified residue | 29 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 29 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 416 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 425 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 429 | UniProt | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Ubiquitinated via 'Lys-6', 'Lys-11' and 'Lys-63'-linked polyubiquitin chains on multiple lysines by MARCHF7, leading to ATG14 aggregation and loss of interaction with STX17.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Forms homooligomers; homo-oligomerization is essential for the roles in membrane tethering and enhancement of SNARE-mediated fusion (PubMed:25686604).
Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex I (PI3KC3-C1) in which the core composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 is associated with ATG14 (PubMed:18843052, PubMed:19050071, PubMed:19270696, PubMed:22314358, PubMed:23878393).
PI3KC3-C1 displays a V-shaped architecture with PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1 subcomplex (PubMed:25490155).
PI3KC3-C1 can associate with further regulatory subunits. Interacts with PIK3CB (By similarity).
Interacts (via coiled-coil domain) with BECN2 (via coiled-coil domain); this interaction is tighter than BECN2 self-association (PubMed:23954414, PubMed:28218432).
Interacts with the STX17-SNAP29 binary t-SNARE complex (PubMed:25686604, PubMed:37632749).
Interacts with NRBF2 (By similarity).
Interacts with PIK3C3 and BECN1; this interaction is increased in the absence of TMEM39A (PubMed:31806350).
Interacts with STEEP1; the interaction is required for trafficking of STING1 from the endoplasmic reticulum (PubMed:32690950).
Interacts with ARMC3 (via ARM domains) (By similarity).
Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex I (PI3KC3-C1) in which the core composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 is associated with ATG14 (PubMed:18843052, PubMed:19050071, PubMed:19270696, PubMed:22314358, PubMed:23878393).
PI3KC3-C1 displays a V-shaped architecture with PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1 subcomplex (PubMed:25490155).
PI3KC3-C1 can associate with further regulatory subunits. Interacts with PIK3CB (By similarity).
Interacts (via coiled-coil domain) with BECN2 (via coiled-coil domain); this interaction is tighter than BECN2 self-association (PubMed:23954414, PubMed:28218432).
Interacts with the STX17-SNAP29 binary t-SNARE complex (PubMed:25686604, PubMed:37632749).
Interacts with NRBF2 (By similarity).
Interacts with PIK3C3 and BECN1; this interaction is increased in the absence of TMEM39A (PubMed:31806350).
Interacts with STEEP1; the interaction is required for trafficking of STING1 from the endoplasmic reticulum (PubMed:32690950).
Interacts with ARMC3 (via ARM domains) (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q6ZNE5 | BECN1 Q14457 | 51 | EBI-2690371, EBI-949378 | |
BINARY | Q6ZNE5 | FSD2 A1L4K1 | 3 | EBI-2690371, EBI-5661036 | |
BINARY | Q6ZNE5 | MIS18A Q9NYP9 | 4 | EBI-2690371, EBI-1104552 | |
BINARY | Q6ZNE5 | PIK3C3 Q8NEB9 | 31 | EBI-2690371, EBI-1056470 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, coiled coil, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 43-58 | Cysteine repeats | ||||
Sequence: CPLCNTTRRRLTCAKC | ||||||
Coiled coil | 71-180 | |||||
Sequence: DRERFIDKKERLSRLKSKQEEFQKEVLKAMEGKWITDQLRWKIMSCKMRIEQLKQTICKGNEEMEKNSEGLLKTKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKT | ||||||
Region | 410-473 | Disordered | ||||
Sequence: PGVAGESDESGDERVSDEETDLGTDWENLPSPRFCDIPSQSVEVSQSQSTQASPPIASSSAGGM | ||||||
Region | 413-492 | BATS | ||||
Sequence: AGESDESGDERVSDEETDLGTDWENLPSPRFCDIPSQSVEVSQSQSTQASPPIASSSAGGMISSAAASVTSWFKAYTGHR | ||||||
Compositional bias | 443-473 | Polar residues | ||||
Sequence: FCDIPSQSVEVSQSQSTQASPPIASSSAGGM |
Domain
The coiled-coil domain is required for BECN1- and PIK3C3-binding and for autophagy.
The final 80 residues in the C-terminus define a minimum required region for autophagosome binding called BATS.
The N-terminal cysteine repeats are required for proper localization to the endoplasmic reticulum.
Sequence similarities
Belongs to the ATG14 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q6ZNE5-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length492
- Mass (Da)55,309
- Last updated2004-07-05 v1
- ChecksumA3EAB0580077D7A6
Q6ZNE5-2
- Name2
- Differences from canonical
- 1-113: Missing
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_013931 | 1-113 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 256 | in Ref. 5; AAI09090 | ||||
Sequence: N → S | ||||||
Compositional bias | 443-473 | Polar residues | ||||
Sequence: FCDIPSQSVEVSQSQSTQASPPIASSSAGGM |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB020638 EMBL· GenBank· DDBJ | BAA74854.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK131251 EMBL· GenBank· DDBJ | BAD18430.1 EMBL· GenBank· DDBJ | mRNA | ||
AK292810 EMBL· GenBank· DDBJ | BAF85499.1 EMBL· GenBank· DDBJ | mRNA | ||
AL158801 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471061 EMBL· GenBank· DDBJ | EAW80673.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC109089 EMBL· GenBank· DDBJ | AAI09090.1 EMBL· GenBank· DDBJ | mRNA | ||
BC109090 EMBL· GenBank· DDBJ | AAI09091.1 EMBL· GenBank· DDBJ | mRNA | ||
BR000826 EMBL· GenBank· DDBJ | FAA00433.1 EMBL· GenBank· DDBJ | mRNA |