Becn1
entrez
114558
canonical
uniprot
Q91XJ1
canonical
ensembl
ENSRNOG00000020513
resolver
ensembl
ENSRNOG00055032831
resolver
ensembl
ENSRNOG00060013552
resolver
ensembl
ENSRNOG00065030974
resolver
ensp
ENSRNOP00000071966
resolver
ensp
ENSRNOP00055046889
resolver
ensp
ENSRNOP00060018342
resolver
ensp
ENSRNOP00065043920
resolver
enst
ENSRNOT00000082010
resolver
enst
ENSRNOT00055056789
resolver
enst
ENSRNOT00060023142
resolver
enst
ENSRNOT00065053430
resolver
genesymbol
Becn1
resolver
uniprot_entry
BECN1_RAT
resolver
amino_acid_sequence
MEGSKASSSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGESQEEEANSGEEPFIETRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEMLEQMNEGDSEQLQRELKELALEEERLIQELEDVEKNRKVVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQMQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSAPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK
uniprot
proteins
function
FUNCTION: Plays a central role in autophagy. Acts as a core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abscission step in cytokinesis, probably in the context of PI3KC3-C2. Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis. May play a role in antiviral host defense (By similarity). {ECO:0000250|UniProtKB:O88597, ECO:0000250|UniProtKB:Q14457}.; FUNCTION: Beclin-1-C 35 kDa localized to mitochondria can promote apoptosis; it induces the mitochondrial translocation of BAX and the release of proapoptotic factors. {ECO:0000250|UniProtKB:O88597, ECO:0000250|UniProtKB:Q14457}.
uniprot
proteins
mass_dalton
51557
uniprot
proteins
mutagenesis
MUTAGEN 178; /note="L->A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-192."; /evidence="ECO:0000269|PubMed:22314358"; MUTAGEN 178; /note="L->A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-196."; /evidence="ECO:0000269|PubMed:22314358"; MUTAGEN 178; /note="L->A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-259."; /evidence="ECO:0000269|PubMed:22314358"; MUTAGEN 189; /note="E->L: Decreases interaction with ATG14, no effect on interaction with UVRAG; when associated with L-217, L-224 and L-255."; /evidence="ECO:0000269|PubMed:22314358"; MUTAGEN 192; /note="L->A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-178."; /evidence="ECO:0000269|PubMed:22314358"; MUTAGEN 196; /note="L->A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-178."; /evidence="ECO:0000269|PubMed:22314358"; MUTAGEN 217; /note="A->L: Decreases interaction with ATG14, no effect on interaction with UVRAG; when associated with L-189, L-224 and L-255."; /evidence="ECO:0000269|PubMed:22314358"; MUTAGEN 224; /note="E->L: Decreases interaction with ATG14, no effect on interaction with UVRAG; when associated with L-189, L-217 and L-255."; /evidence="ECO:0000269|PubMed:22314358"; MUTAGEN 255; /note="A->L: Decreases interaction with ATG14, no effect on interaction with UVRAG; when associated with L-189, L-217 and L-224."; /evidence="ECO:0000269|PubMed:22314358"; MUTAGEN 259; /note="L->A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-178."; /evidence="ECO:0000269|PubMed:22314358
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-117 by DAPK1 reduces its interaction with BCL2 and BCL2L1 and promotes induction of autophagy. In response to autophagic stimuli, phosphorylated at serine residues by AMPK in an ATG14-dependent manner, and this phosphorylation is critical for maximally efficient autophagy. {ECO:0000250|UniProtKB:O88597, ECO:0000250|UniProtKB:Q14457}.; PTM: Polyubiquitinated by NEDD4, both with 'Lys-11'- and 'Lys-63'-linkages (By similarity). 'Lys-11'-linked polyubiquitination leads to degradation and is enhanced when the stabilizing interaction partner VPS34 is depleted (By similarity). Deubiquitinated by USP10 and USP13, leading to stabilize the PIK3C3/VPS34-containing complexes (By similarity). Polyubiquitinated at Lys-400 with 'Lys-48'-linkages (By similarity). 'Lys-48'-linked polyubiquitination of Lys-400 leads to degradation (By similarity). Deubiquitinated by ATXN3, leading to stabilization (By similarity). Ubiquitinated at Lys-435 via 'Lys-63'-linkage by the DCX(AMBRA1) complex, thereby increasing the association between BECN1 and PIK3C3 to promote PIK3C3 activity (By similarity). 'Lys-48'-linked ubiquitination by RNF216 leads to proteasomal degradation and autophagy inhibition (By similarity). {ECO:0000250|UniProtKB:Q14457}.; PTM: Proteolytically processed by caspases including CASP8 and CASP3; the C-terminal fragments lack autophagy-inducing capacity and are proposed to induce apoptosis. Thus the cleavage is proposed to be an determinant to switch from autophagy to apoptosis pathways affecting cellular homeostasis including viral infections and survival of tumor cells. {ECO:0000250|UniProtKB:O88597, ECO:0000250|UniProtKB:Q14457}.
uniprot
proteins
protein_family
Beclin family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17724469
uniprot
proteins
pubmed
22314358
uniprot
proteins
sequence_length
448
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O88597}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endosome membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Note=Interaction with ATG14 promotes translocation to autophagosomes. Expressed in dendrites and cell bodies of cerebellar Purkinje cells. {ECO:0000250|UniProtKB:O88597, ECO:0000250|UniProtKB:Q14457}.; SUBCELLULAR LOCATION: [Beclin-1-C 35 kDa]: Mitochondrion {ECO:0000250|UniProtKB:O88597, ECO:0000250|UniProtKB:Q14457}. Nucleus {ECO:0000250|UniProtKB:Q14457}. Cytoplasm {ECO:0000250|UniProtKB:Q14457}.; SUBCELLULAR LOCATION: [Beclin-1-C 37 kDa]: Mitochondrion {ECO:0000250|UniProtKB:O88597}.
uniprot
proteins