BECN1
entrez
8678
canonical
uniprot
Q14457
canonical
ensembl
ENSG00000126581
resolver
ensp
ENSP00000355231
resolver
ensp
ENSP00000416173
resolver
ensp
ENSP00000465364
resolver
ensp
ENSP00000563347
resolver
ensp
ENSP00000592884
resolver
ensp
ENSP00000637444
resolver
ensp
ENSP00000637445
resolver
ensp
ENSP00000646342
resolver
enst
ENST00000361523
resolver
enst
ENST00000438274
resolver
enst
ENST00000590099
resolver
enst
ENST00000893288
resolver
enst
ENST00000967385
resolver
enst
ENST00000967386
resolver
genesymbol
BECN1
resolver
genesymbol_syn
GT197
resolver
hgnc
HGNC:1034
resolver
uniprot
A0A024R1X5
resolver
uniprot
B2R6N7
resolver
uniprot
B4DQ36
resolver
uniprot
E7EV84
resolver
uniprot
O75595
resolver
uniprot
Q9UNA8
resolver
uniprot
W0FFG4
resolver
uniprot_entry
A0A024R1X5_HUMAN
resolver
uniprot_entry
B4DQ36_HUMAN
resolver
uniprot_entry
BECN1_HUMAN
resolver
uniprot_entry
E7EV84_HUMAN
resolver
uniprot_entry
W0FFG4_HUMAN
resolver
uniprot_sec
B2R6N7
resolver
uniprot_sec
O75595
resolver
uniprot_sec
Q9UNA8
resolver
amino_acid_sequence
MEGSKTSNNSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQMELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQTQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK
uniprot
proteins
function
FUNCTION: Plays a central role in autophagy (PubMed:18570871, PubMed:21358617, PubMed:23184933, PubMed:23974797, PubMed:25484083, PubMed:28445460, PubMed:37776275). 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 (PubMed:20208530, PubMed:20643123, PubMed:23974797, PubMed:26783301). Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis (PubMed:25275521). May play a role in antiviral host defense. {ECO:0000269|PubMed:18570871, ECO:0000269|PubMed:20208530, ECO:0000269|PubMed:20643123, ECO:0000269|PubMed:21358617, ECO:0000269|PubMed:23184933, ECO:0000269|PubMed:23974797, ECO:0000269|PubMed:25275521, ECO:0000269|PubMed:25484083, ECO:0000269|PubMed:26783301, ECO:0000269|PubMed:28445460, ECO:0000269|PubMed:37776275, ECO:0000269|PubMed:9765397}.; 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:0000269|PubMed:21364619, ECO:0000269|PubMed:26263979}.; FUNCTION: (Microbial infection) Protects against infection by a neurovirulent strain of Sindbis virus. {ECO:0000269|PubMed:9765397}.
uniprot
proteins
mass_dalton
51896
uniprot
proteins
mutagenesis
MUTAGEN 90; /note="S->A: Complete loss of phosphorylation. Complete loss of phosphorylation and defective autophagic function; when associated with Ala-93."; /evidence="ECO:0000269|PubMed:23878393"; MUTAGEN 93; /note="S->A: Partial loss of phosphorylation. Complete loss of phosphorylation and defective autophagic function; when associated with Ala-90."; /evidence="ECO:0000269|PubMed:23878393"; MUTAGEN 112; /note="L->A: Weakly decreases interaction with MUHV-4 M11, greatly decreases interaction with BCL2L1 isoform Bcl-X(L)."; /evidence="ECO:0000269|PubMed:18797192, ECO:0000269|PubMed:24443581"; MUTAGEN 116; /note="L->A: Decreases interaction with BCL2L1 isoform Bcl-X(L)."; /evidence="ECO:0000269|PubMed:17446862, ECO:0000269|PubMed:18797192, ECO:0000269|PubMed:24443581"; MUTAGEN 117; /note="K->A: Weakly decreases interaction with MUHV-4 M11, greatly decreases interaction with BCL2L1 isoform Bcl-X(L)."; /evidence="ECO:0000269|PubMed:24443581"; MUTAGEN 117; /note="K->R: Does not affect ubiquitination by the DCX(AMBRA1) complex."; /evidence="ECO:0000269|PubMed:23974797"; MUTAGEN 120..121; /note="GD->EA: Weakly decreases interaction with MUHV-4 M11, disrupts interaction with BCL2L1 isoform Bcl-X(L)."; /evidence="ECO:0000269|PubMed:24443581"; MUTAGEN 120; /note="G->E: Decreases interaction with MUHV-4 M11, disrupts interaction with BCL2L1 isoform Bcl-X(L)."; /evidence="ECO:0000269|PubMed:24443581"; MUTAGEN 121; /note="D->A: No effect on interaction with MUHV-4 M11, disrupts interaction with BCL2L1 isoform Bcl-X(L)."; /evidence="ECO:0000269|PubMed:24443581"; MUTAGEN 123; /note="F->A: Weakly decreases interaction with MUHV-4 M11, disrupts interaction with BCL2 and decreases interaction with BCL2L1 isoform Bcl-X(L). Reduces interaction with BCL2L10."; /evidence="ECO:0000269|PubMed:16179260, ECO:0000269|PubMed:17446862, ECO:0000269|PubMed:18797192, ECO:0000269|PubMed:22498477, ECO:0000269|PubMed:24443581"; MUTAGEN 133; /note="D->A: Abolishes in vitro cleavage by CASP3 and CASP8; when associated with A-149."; /evidence="ECO:0000269|PubMed:21364619"; MUTAGEN 133; /note="D->A: Abolishes in vitro cleavage by CASP8; when associated with A-146."; /evidence="ECO:0000269|PubMed:21444671"; MUTAGEN 146; /note="D->A: Abolishes in vitro cleavage by CASP8; when associated with A-133."; /evidence="ECO:0000269|PubMed:21444671"; MUTAGEN 149; /note="D->A: Abolishes in vitro cleavage by CASP3 and CASP8; when associated with A-133."; /evidence="ECO:0000269|PubMed:21364619"; MUTAGEN 149; /note="D->E: Abolishes in vitro cleavage by CASP3."; /evidence="ECO:0000269|PubMed:19713971"; MUTAGEN 352; /note="Y->A: Significantly reduces ubiquitination."; /evidence="ECO:0000269|PubMed:21936852"; MUTAGEN 402; /note="K->R: Decreases K48 polyubiquitination and stabilizes BECN1."; /evidence="ECO:0000269|PubMed:28445460"; MUTAGEN 425; /note="W->A: Decrease in membrane-association."; /evidence="ECO:0000269|PubMed:23878393"; MUTAGEN 437; /note="K->R: Abolished ubiquitination by the DCX(AMBRA1) complex."; /evidence="ECO:0000269|PubMed:23974797
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-119 by DAPK1 reduces its interaction with BCL2 and BCL2L1 and promotes induction of autophagy (PubMed:19180116). 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 (PubMed:23878393, PubMed:25891078). {ECO:0000269|PubMed:19180116, ECO:0000269|PubMed:23878393, ECO:0000269|PubMed:25891078}.; PTM: Polyubiquitinated by NEDD4, both with 'Lys-11'- and 'Lys-63'-linkages (PubMed:21936852). 'Lys-11'-linked polyubiquitination leads to degradation and is enhanced when the stabilizing interaction partner VPS34 is depleted (PubMed:21936852). Deubiquitinated by USP10 and USP13, leading to stabilize the PIK3C3/VPS34-containing complexes (PubMed:21962518). Polyubiquitinated at Lys-402 with 'Lys-48'-linkages (PubMed:28445460). 'Lys-48'-linked polyubiquitination of Lys-402 leads to degradation (PubMed:28445460). Deubiquitinated by ATXN3, leading to stabilization (PubMed:28445460). Ubiquitinated at Lys-437 via 'Lys-63'-linkage by the DCX(AMBRA1) complex, thereby increasing the association between BECN1 and PIK3C3 to promote PIK3C3 activity (PubMed:23974797). 'Lys-48'-linked ubiquitination by RNF216 leads to proteasomal degradation and autophagy inhibition (PubMed:25484083). {ECO:0000269|PubMed:21936852, ECO:0000269|PubMed:21962518, ECO:0000269|PubMed:23974797, ECO:0000269|PubMed:25484083, ECO:0000269|PubMed:28445460}.; 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:0000305|PubMed:19713971, ECO:0000305|PubMed:21364619}.
uniprot
proteins
protein_family
Beclin family
uniprot
proteins
pubmed
10395800
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16179260
uniprot
proteins
pubmed
17337444
uniprot
proteins
pubmed
17446862
uniprot
proteins
pubmed
17659302
uniprot
proteins
pubmed
17724469
uniprot
proteins
pubmed
18005679
uniprot
proteins
pubmed
18570871
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18797192
uniprot
proteins
pubmed
18843052
uniprot
proteins
pubmed
19050071
uniprot
proteins
pubmed
19180116
uniprot
proteins
pubmed
19270696
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19713971
uniprot
proteins
pubmed
19759141
uniprot
proteins
pubmed
20208530
uniprot
proteins
pubmed
20643123
uniprot
proteins
pubmed
20819940
uniprot
proteins
pubmed
21358617
uniprot
proteins
pubmed
21364619
uniprot
proteins
pubmed
21444671
uniprot
proteins
pubmed
21936852
uniprot
proteins
pubmed
21962518
uniprot
proteins
pubmed
22205736
uniprot
proteins
pubmed
22493499
uniprot
proteins
pubmed
22498477
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23184933
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23822101
uniprot
proteins
pubmed
23878393
uniprot
proteins
pubmed
23974797
uniprot
proteins
pubmed
24349490
uniprot
proteins
pubmed
24443581
uniprot
proteins
pubmed
25127057
uniprot
proteins
pubmed
25275521
uniprot
proteins
pubmed
25484083
uniprot
proteins
pubmed
25490155
uniprot
proteins
pubmed
25803737
uniprot
proteins
pubmed
25891078
uniprot
proteins
pubmed
26263979
uniprot
proteins
pubmed
26347139
uniprot
proteins
pubmed
26783301
uniprot
proteins
pubmed
27562068
uniprot
proteins
pubmed
27693506
uniprot
proteins
pubmed
28445460
uniprot
proteins
pubmed
28479384
uniprot
proteins
pubmed
29604308
uniprot
proteins
pubmed
31123703
uniprot
proteins
pubmed
31806350
uniprot
proteins
pubmed
31937766
uniprot
proteins
pubmed
34870550
uniprot
proteins
pubmed
37776275
uniprot
proteins
pubmed
7490091
uniprot
proteins
pubmed
9765397
uniprot
proteins
sequence_length
450
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19713971, ECO:0000269|PubMed:21364619, ECO:0000269|PubMed:22498477, ECO:0000269|PubMed:25484083}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:19050071}; Peripheral membrane protein {ECO:0000269|PubMed:19050071}. Endosome membrane {ECO:0000269|PubMed:23878393}; Peripheral membrane protein {ECO:0000269|PubMed:23878393}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23878393}; Peripheral membrane protein {ECO:0000269|PubMed:23878393}. Mitochondrion membrane {ECO:0000269|PubMed:23878393}; Peripheral membrane protein {ECO:0000269|PubMed:23878393}. Endosome {ECO:0000250|UniProtKB:O88597}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Note=Interaction with ATG14 promotes translocation to autophagosomes. Expressed in dendrites and cell bodies of cerebellar Purkinje cells (By similarity). {ECO:0000250|UniProtKB:O88597, ECO:0000269|PubMed:19050071}.; SUBCELLULAR LOCATION: [Beclin-1-C 35 kDa]: Mitochondrion {ECO:0000269|PubMed:21364619, ECO:0000269|PubMed:26263979}. Nucleus {ECO:0000269|PubMed:19713971}. Cytoplasm {ECO:0000269|PubMed:19713971}.; SUBCELLULAR LOCATION: [Beclin-1-C 37 kDa]: Mitochondrion {ECO:0000250|UniProtKB:O88597}.
uniprot
proteins