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Protein

Beclin-1

Gene

BECN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a central role in autophagy (PubMed:23184933). Acts as 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 abcission step in cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20643123, PubMed:20208530). Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis (PubMed:25275521). Protects against infection by a neurovirulent strain of Sindbis virus (PubMed:9765397). May play a role in antiviral host defense.Curated5 Publications
Beclin-1-C 35 kDa localized to mitochondria can promote apoptosis; it induces the mitochondrial translocation of BAX and the release of proapoptotic factors.2 Publications

GO - Molecular functioni

  • phosphatidylinositol 3-kinase binding Source: ParkinsonsUK-UCL
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • autophagosome assembly Source: UniProtKB
  • autophagy Source: CACAO
  • beta-amyloid metabolic process Source: Ensembl
  • cellular defense response Source: ProtInc
  • cellular response to aluminum ion Source: Ensembl
  • cellular response to epidermal growth factor stimulus Source: Ensembl
  • cellular response to glucose starvation Source: UniProtKB
  • cellular response to nitrogen starvation Source: GO_Central
  • CVT pathway Source: GO_Central
  • cytokinesis Source: UniProtKB
  • defense response to virus Source: UniProtKB-KW
  • engulfment of apoptotic cell Source: Ensembl
  • late endosome to vacuole transport Source: GO_Central
  • lysosome organization Source: Ensembl
  • macroautophagy Source: UniProtKB
  • mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • mitotic metaphase plate congression Source: CACAO
  • negative regulation of apoptotic process Source: ProtInc
  • negative regulation of cell death Source: MGI
  • negative regulation of cell proliferation Source: Ensembl
  • negative regulation of reactive oxygen species metabolic process Source: Ensembl
  • neuron development Source: Ensembl
  • nucleophagy Source: GO_Central
  • positive regulation of attachment of mitotic spindle microtubules to kinetochore Source: CACAO
  • positive regulation of autophagy Source: UniProtKB
  • positive regulation of mitophagy Source: ParkinsonsUK-UCL
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: ParkinsonsUK-UCL
  • receptor catabolic process Source: UniProtKB
  • regulation of catalytic activity Source: Ensembl
  • regulation of cytokinesis Source: UniProtKB
  • response to drug Source: Ensembl
  • response to hypoxia Source: Ensembl
  • response to vitamin E Source: Ensembl
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Apoptosis, Autophagy, Cell cycle, Cell division, Endocytosis, Host-virus interaction

Enzyme and pathway databases

ReactomeiR-HSA-1632852. Macroautophagy.
SIGNORiQ14457.

Names & Taxonomyi

Protein namesi
Recommended name:
Beclin-1
Alternative name(s):
Coiled-coil myosin-like BCL2-interacting protein
Protein GT197
Cleaved into the following 2 chains:
Beclin-1-C 35 kDa1 Publication
Beclin-1-C 37 kDa1 Publication
Gene namesi
Name:BECN1
Synonyms:GT197
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:1034. BECN1.

Subcellular locationi

Beclin-1-C 35 kDa :
Beclin-1-C 37 kDa :
  • Mitochondrion By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901S → A: Complete loss of phosphorylation. Complete loss of phosphorylation and defective autophagic function; when associated with Ala-93. 1 Publication
Mutagenesisi93 – 931S → A: Partial loss of phosphorylation. Complete loss of phosphorylation and defective autophagic function; when associated with Ala-90. 1 Publication
Mutagenesisi112 – 1121L → A: Weakly decreases interaction with MUHV-4 M11, greatly decreases interaction with BCL2L1 isoform Bcl-X(L). 2 Publications
Mutagenesisi116 – 1161L → A: Decreases interaction with BCL2L1 isoform Bcl-X(L). 3 Publications
Mutagenesisi117 – 1171K → A: Weakly decreases interaction with MUHV-4 M11, greatly decreases interaction with BCL2L1 isoform Bcl-X(L). 1 Publication
Mutagenesisi120 – 1212GD → EA: Weakly decreases interaction with MUHV-4 M11, disrupts interaction with BCL2L1 isoform Bcl-X(L). 1 Publication
Mutagenesisi120 – 1201G → E: Decreases interaction with MUHV-4 M11, disrupts interaction with BCL2L1 isoform Bcl-X(L). 1 Publication
Mutagenesisi121 – 1211D → A: No effect on interaction with MUHV-4 M11, disrupts interaction with BCL2L1 isoform Bcl-X(L). 1 Publication
Mutagenesisi123 – 1231F → A: Weakly decreases interaction with MUHV-4 M11, disrupts interaction with BCL2 and decreases interaction with BCL2L1 isoform Bcl-X(L). 4 Publications
Mutagenesisi133 – 1331D → A: Abolishes in vitro cleavage by CASP3 and CASP8; when associated with A-149. 1 Publication
Mutagenesisi133 – 1331D → A: Abolishes in vitro cleavage by CASP8; when associated with A-146. 1 Publication
Mutagenesisi146 – 1461D → A: Abolishes in vitro cleavage by CASP8; when associated with A-133. 1 Publication
Mutagenesisi149 – 1491D → A: Abolishes in vitro cleavage by CASP3 and CASP8; when associated with A-133. 1 Publication
Mutagenesisi149 – 1491D → E: Abolishes in vitro cleavage by CASP3. 1 Publication
Mutagenesisi352 – 3521Y → A: Significantly reduces ubiquitination. 1 Publication
Mutagenesisi425 – 4251W → A: Decrease in membrane-association. 1 Publication

Organism-specific databases

PharmGKBiPA25337.

Polymorphism and mutation databases

BioMutaiBECN1.
DMDMi13124704.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Beclin-1PRO_0000218555Add
BLAST
Chaini134 – 450317Beclin-1-C 37 kDa1 PublicationPRO_0000435036Add
BLAST
Chaini150 – 450301Beclin-1-C 35 kDa2 PublicationsPRO_0000435037Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei90 – 901Phosphoserine; by AMPK1 Publication
Modified residuei93 – 931Phosphoserine; by AMPK1 Publication
Modified residuei96 – 961Phosphoserine; by AMPKBy similarity
Modified residuei119 – 1191Phosphothreonine; by DAPK11 Publication

Post-translational modificationi

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).2 Publications
Polyubiquitinated by NEDD4, both with 'Lys11'- and 'Lys63'-linkages. 'Lys'-11-linked poyubiquitination leads to degradation and is enhanced when the stabilizing interaction partner VPS34 is depleted. Deubiquitinated by USP10 and USP13, leading to stabilize the PIK3C3/VPS34-containing complexes.2 Publications
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.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ14457.
MaxQBiQ14457.
PaxDbiQ14457.
PRIDEiQ14457.

PTM databases

iPTMnetiQ14457.
PhosphoSiteiQ14457.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ14457.
CleanExiHS_BECN1.
ExpressionAtlasiQ14457. baseline and differential.
GenevisibleiQ14457. HS.

Organism-specific databases

HPAiCAB010143.
HPA028949.

Interactioni

Subunit structurei

A homodimeric form is proposed to exist; this metastable form readily transits to ATG14- or UVRAG-containing complexes with BECN1:UVRAG being more stable than BECN1:ATG14 (By similarity). Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex the core of which is composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 associating with additional regulatory/auxilliary subunits to form alternative complex forms. Alternative complex forms containing a forth regulatory subunit in a mutually exclusive manner are PI3K complex I (PI3KC3-C1) containing ATG14, and PI3K complex II (PI3KC3-C2) containing UVRAG. PI3KC3-C1 displays a V-shaped architecture with PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1 subcomplex (PubMed:18843052, PubMed:19050071, PubMed:19270696, PubMed:23878393, PubMed:25490155). Both, PI3KC3-C1 and PI3KC3-C2, can associate with further regulatory subunits, such as RUBCN, SH3GLB1/Bif-1 and AMBRA1 (PubMed:20643123, PubMed:19270696). PI3KC3-C1 probably associates with PIK3CB (By similarity). Interacts with AMBRA1, GOPC, GRID2 (By similarity). Interacts with BCL2 and BCL2L1 isoform Bcl-X(L); the interaction inhibits BECN1 function in promoting autophagy by interfering with the formation of the PI3K complex (PubMed:9765397, PubMed:16179260, PubMed:17446862, PubMed:17337444, PubMed:17659302). Interacts with cytosolic HMGB1; inhibits the interaction of BECN1 and BCL2 leading to promotion of autophagy (PubMed:20819940). Interacts with USP10, USP13, VMP1, DAPK1, RAB39A (PubMed:19180116, PubMed:17724469, PubMed:17337444, PubMed:21962518, PubMed:24349490). Interacts with SLAMF1 (PubMed:22493499). Interacts with TRIM5; the interaction causes activation of BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2 (PubMed:25127057). Interacts with active ULK1 (phosphorylated on 'Ser-317') and MEFV simultaneously (PubMed:26347139). Interacts with human cytomegalovirus/HHV-5 protein TRS1 (PubMed:22205736). Interacts with murine gammaherpesvirus 68 M11 (PubMed:18797192, PubMed:24443581).By similarityCurated22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AMBRA1Q9C0C78EBI-949378,EBI-2512975
ATG14Q6ZNE528EBI-949378,EBI-2690371
BCL2P1041516EBI-949378,EBI-77694
BCL2L1Q07817-15EBI-949378,EBI-287195
BIRC5O153923EBI-949378,EBI-518823
DAPK1P533554EBI-949378,EBI-358616
EGFRP005337EBI-949378,EBI-297353
EXOC8Q8IYI64EBI-949378,EBI-742102
HMGB1P094292EBI-949378,EBI-389432
MCL1Q078202EBI-949378,EBI-1003422
PIK3C3Q8NEB924EBI-949378,EBI-1056470
RAB39AQ149642EBI-949378,EBI-3048577
RUBCNQ9262215EBI-949378,EBI-2952709
Slamf1Q9QUM48EBI-949378,EBI-7910086From a different organism.
TAB2Q9NYJ811EBI-949378,EBI-358708
TAB3Q8N5C89EBI-949378,EBI-359964
UVRAGQ9P2Y527EBI-949378,EBI-2952704
v-bcl-2P898844EBI-949378,EBI-8849581From a different organism.
VMP1Q96GC93EBI-949378,EBI-2800296
Vmp1Q91ZQ06EBI-949378,EBI-11163586From a different organism.
WASH1A8K0Z33EBI-949378,EBI-6160405
ZWINTO952296EBI-949378,EBI-1001132

GO - Molecular functioni

  • phosphatidylinositol 3-kinase binding Source: ParkinsonsUK-UCL
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114226. 79 interactions.
DIPiDIP-44611N.
IntActiQ14457. 96 interactions.
MINTiMINT-2865445.
STRINGi9606.ENSP00000355231.

Structurei

Secondary structure

1
450
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi109 – 12315Combined sources
Turni124 – 1263Combined sources
Helixi250 – 26213Combined sources
Beta strandi276 – 2794Combined sources
Beta strandi282 – 2854Combined sources
Helixi300 – 32122Combined sources
Beta strandi326 – 3316Combined sources
Helixi334 – 3363Combined sources
Beta strandi338 – 3436Combined sources
Beta strandi349 – 3513Combined sources
Helixi358 – 3603Combined sources
Helixi364 – 38421Combined sources
Turni398 – 4014Combined sources
Beta strandi402 – 4043Combined sources
Turni406 – 4094Combined sources
Beta strandi412 – 4154Combined sources
Helixi422 – 44625Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P1LX-ray2.50B/D/F/H107-135[»]
2PONNMR-A106-128[»]
3DVUX-ray2.50C/D105-130[»]
4DDPX-ray1.55A241-450[»]
4MI8X-ray2.10C/D107-130[»]
ProteinModelPortaliQ14457.
SMRiQ14457. Positions 112-447.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14457.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni112 – 15948Interaction with BCL2 and BCL2L1 isoform Bcl-X(L)1 PublicationAdd
BLAST
Regioni425 – 45026Required for membrane-association1 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili142 – 270129Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi108 – 12720BH3Add
BLAST

Domaini

The coiled coil domain can form antiparallel homodimers and mediates dimerization with the coiled coil domains of ATG14 or UVRAG involved in the formation of PI3K complexes.By similarity

Sequence similaritiesi

Belongs to the beclin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2751. Eukaryota.
ENOG410XQ85. LUCA.
GeneTreeiENSGT00390000008164.
HOGENOMiHOG000158093.
HOVERGENiHBG003181.
InParanoidiQ14457.
KOiK08334.
OMAiYIPPARM.
OrthoDBiEOG7D2FDG.
PhylomeDBiQ14457.
TreeFamiTF314282.

Family and domain databases

InterProiIPR007243. Atg6/Beclin.
IPR032913. BECN1.
IPR029318. BH3_dom.
[Graphical view]
PANTHERiPTHR12768. PTHR12768. 1 hit.
PTHR12768:SF6. PTHR12768:SF6. 1 hit.
PfamiPF04111. APG6. 1 hit.
PF15285. BH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q14457-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGSKTSNNS TMQVSFVCQR CSQPLKLDTS FKILDRVTIQ ELTAPLLTTA
60 70 80 90 100
QAKPGETQEE ETNSGEEPFI ETPRQDGVSR RFIPPARMMS TESANSFTLI
110 120 130 140 150
GEASDGGTME NLSRRLKVTG DLFDIMSGQT DVDHPLCEEC TDTLLDQLDT
160 170 180 190 200
QLNVTENECQ NYKRCLEILE QMNEDDSEQL QMELKELALE EERLIQELED
210 220 230 240 250
VEKNRKIVAE NLEKVQAEAE RLDQEEAQYQ REYSEFKRQQ LELDDELKSV
260 270 280 290 300
ENQMRYAQTQ LDKLKKTNVF NATFHIWHSG QFGTINNFRL GRLPSVPVEW
310 320 330 340 350
NEINAAWGQT VLLLHALANK MGLKFQRYRL VPYGNHSYLE SLTDKSKELP
360 370 380 390 400
LYCSGGLRFF WDNKFDHAMV AFLDCVQQFK EEVEKGETRF CLPYRMDVEK
410 420 430 440 450
GKIEDTGGSG GSYSIKTQFN SEEQWTKALK FMLTNLKWGL AWVSSQFYNK
Length:450
Mass (Da):51,896
Last modified:February 21, 2001 - v2
Checksum:iABF0C2DD7087473C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501T → A in AAB59573 (PubMed:7490091).Curated
Sequence conflicti161 – 1611N → S in BAG35534 (PubMed:14702039).Curated
Sequence conflicti314 – 3141L → H in BAG35534 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031A → V.
VAR_010384
Natural varianti403 – 4031I → T.
VAR_005236

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077301 mRNA. Translation: AAC68653.1.
AF139131 mRNA. Translation: AAD27650.1.
AK312651 mRNA. Translation: BAG35534.1.
BC010276 mRNA. Translation: AAH10276.1.
L38932 mRNA. Translation: AAB59573.1.
CCDSiCCDS11441.1.
PIRiI54209.
RefSeqiNP_001300927.1. NM_001313998.1.
NP_001300928.1. NM_001313999.1.
NP_001300929.1. NM_001314000.1.
NP_003757.1. NM_003766.4.
UniGeneiHs.716464.

Genome annotation databases

EnsembliENST00000361523; ENSP00000355231; ENSG00000126581.
ENST00000590099; ENSP00000465364; ENSG00000126581.
GeneIDi8678.
KEGGihsa:8678.
UCSCiuc002ibn.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077301 mRNA. Translation: AAC68653.1.
AF139131 mRNA. Translation: AAD27650.1.
AK312651 mRNA. Translation: BAG35534.1.
BC010276 mRNA. Translation: AAH10276.1.
L38932 mRNA. Translation: AAB59573.1.
CCDSiCCDS11441.1.
PIRiI54209.
RefSeqiNP_001300927.1. NM_001313998.1.
NP_001300928.1. NM_001313999.1.
NP_001300929.1. NM_001314000.1.
NP_003757.1. NM_003766.4.
UniGeneiHs.716464.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P1LX-ray2.50B/D/F/H107-135[»]
2PONNMR-A106-128[»]
3DVUX-ray2.50C/D105-130[»]
4DDPX-ray1.55A241-450[»]
4MI8X-ray2.10C/D107-130[»]
ProteinModelPortaliQ14457.
SMRiQ14457. Positions 112-447.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114226. 79 interactions.
DIPiDIP-44611N.
IntActiQ14457. 96 interactions.
MINTiMINT-2865445.
STRINGi9606.ENSP00000355231.

PTM databases

iPTMnetiQ14457.
PhosphoSiteiQ14457.

Polymorphism and mutation databases

BioMutaiBECN1.
DMDMi13124704.

Proteomic databases

EPDiQ14457.
MaxQBiQ14457.
PaxDbiQ14457.
PRIDEiQ14457.

Protocols and materials databases

DNASUi8678.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361523; ENSP00000355231; ENSG00000126581.
ENST00000590099; ENSP00000465364; ENSG00000126581.
GeneIDi8678.
KEGGihsa:8678.
UCSCiuc002ibn.3. human.

Organism-specific databases

CTDi8678.
GeneCardsiBECN1.
HGNCiHGNC:1034. BECN1.
HPAiCAB010143.
HPA028949.
MIMi604378. gene.
neXtProtiNX_Q14457.
PharmGKBiPA25337.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2751. Eukaryota.
ENOG410XQ85. LUCA.
GeneTreeiENSGT00390000008164.
HOGENOMiHOG000158093.
HOVERGENiHBG003181.
InParanoidiQ14457.
KOiK08334.
OMAiYIPPARM.
OrthoDBiEOG7D2FDG.
PhylomeDBiQ14457.
TreeFamiTF314282.

Enzyme and pathway databases

ReactomeiR-HSA-1632852. Macroautophagy.
SIGNORiQ14457.

Miscellaneous databases

ChiTaRSiBECN1. human.
EvolutionaryTraceiQ14457.
GeneWikiiBECN1.
GenomeRNAii8678.
PROiQ14457.
SOURCEiSearch...

Gene expression databases

BgeeiQ14457.
CleanExiHS_BECN1.
ExpressionAtlasiQ14457. baseline and differential.
GenevisibleiQ14457. HS.

Family and domain databases

InterProiIPR007243. Atg6/Beclin.
IPR032913. BECN1.
IPR029318. BH3_dom.
[Graphical view]
PANTHERiPTHR12768. PTHR12768. 1 hit.
PTHR12768:SF6. PTHR12768:SF6. 1 hit.
PfamiPF04111. APG6. 1 hit.
PF15285. BH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Protection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein."
    Liang X.H., Kleeman L.K., Jiang H.H., Gordon G., Goldman J.E., Berry G., Herman B., Levine B.
    J. Virol. 72:8586-8596(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH BCL-2.
    Tissue: Brain.
  2. "Cloning and genomic organization of beclin 1, a candidate tumor suppressor gene on chromosome 17q21."
    Aita V.M., Liang X.H., Murty V.V.V.S., Pincus D.L., Yu W., Cayanis E., Kalachikov S., Gilliam T.C., Levine B.
    Genomics 59:59-65(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cervix.
  5. "Generation of a transcription map at the HSD17B locus centromeric to BRCA1 at 17q21."
    Rommens J.M., Durocher F., McArthur J., Tonin P., Leblanc J.-F., Allen T., Samson C., Ferri L., Narod S., Morgan K., Simard J.
    Genomics 28:530-542(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 150-450.
    Tissue: Mammary gland.
  6. "Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy."
    Pattingre S., Tassa A., Qu X., Garuti R., Liang X.H., Mizushima N., Packer M., Schneider M.D., Levine B.
    Cell 122:927-939(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCL2, MUTAGENESIS OF PHE-123.
  7. Cited for: INTERACTION WITH BCL2L1, MUTAGENESIS OF LEU-116 AND PHE-123.
  8. "Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG."
    Itakura E., Kishi C., Inoue K., Mizushima N.
    Mol. Biol. Cell 19:5360-5372(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATG14; PIK3C3; PIK3R4 AND UVRAG.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Reduced expression of vacuole membrane protein 1 affects the invasion capacity of tumor cells."
    Sauermann M., Sahin O., Sultmann H., Hahne F., Blaszkiewicz S., Majety M., Zatloukal K., Fuzesi L., Poustka A., Wiemann S., Arlt D.
    Oncogene 27:1320-1326(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VMP1.
  11. "Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase."
    Sun Q., Fan W., Chen K., Ding X., Chen S., Zhong Q.
    Proc. Natl. Acad. Sci. U.S.A. 105:19211-19216(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATG14; PIK3C3 AND UVRAG, SUBCELLULAR LOCATION.
  12. "DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy."
    Zalckvar E., Berissi H., Mizrachy L., Idelchuk Y., Koren I., Eisenstein M., Sabanay H., Pinkas-Kramarski R., Kimchi A.
    EMBO Rep. 10:285-292(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-119, INTERACTION WITH DAPK1.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "A phosphatidylinositol 3-kinase class III sub-complex containing VPS15, VPS34, Beclin 1, UVRAG and BIF-1 regulates cytokinesis and degradative endocytic traffic."
    Thoresen S.B., Pedersen N.M., Liestol K., Stenmark H.
    Exp. Cell Res. 316:3368-3378(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  15. "Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages."
    Matsunaga K., Saitoh T., Tabata K., Omori H., Satoh T., Kurotori N., Maejima I., Shirahama-Noda K., Ichimura T., Isobe T., Akira S., Noda T., Yoshimori T.
    Nat. Cell Biol. 11:385-396(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATG14; RUBCN; PIK3C3; PIK3R4 AND UVRAG.
  16. "Apoptosis blocks Beclin 1-dependent autophagosome synthesis: an effect rescued by Bcl-xL."
    Luo S., Rubinsztein D.C.
    Cell Death Differ. 17:268-277(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, MUTAGENESIS OF ASP-149.
  17. "Caspase-mediated cleavage of Beclin-1 inactivates Beclin-1-induced autophagy and enhances apoptosis by promoting the release of proapoptotic factors from mitochondria."
    Wirawan E., Vande Walle L., Kersse K., Cornelis S., Claerhout S., Vanoverberghe I., Roelandt R., De Rycke R., Verspurten J., Declercq W., Agostinis P., Vanden Berghe T., Lippens S., Vandenabeele P.
    Cell Death Dis. 1:E18-E18(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-133 AND ASP-149.
  18. Cited for: INTERACTION WITH HMGB1.
  19. "PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of FYVE-CENT to the midbody."
    Sagona A.P., Nezis I.P., Pedersen N.M., Liestol K., Poulton J., Rusten T.E., Skotheim R.I., Raiborg C., Stenmark H.
    Nat. Cell Biol. 12:362-371(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Following cytochrome c release, autophagy is inhibited during chemotherapy-induced apoptosis by caspase 8-mediated cleavage of Beclin 1."
    Li H., Wang P., Sun Q., Ding W.X., Yin X.M., Sobol R.W., Stolz D.B., Yu J., Zhang L.
    Cancer Res. 71:3625-3634(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC CLEAVAGE, MUTAGENESIS OF ASP-133 AND ASP-146.
  21. "Beclin1 controls the levels of p53 by regulating the deubiquitination activity of USP10 and USP13."
    Liu J., Xia H., Kim M., Xu L., Li Y., Zhang L., Cai Y., Norberg H.V., Zhang T., Furuya T., Jin M., Zhu Z., Wang H., Yu J., Li Y., Hao Y., Choi A., Ke H., Ma D., Yuan J.
    Cell 147:223-234(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH USP10 AND USP13.
  22. "Nedd4-dependent lysine-11-linked polyubiquitination of the tumour suppressor Beclin 1."
    Platta H.W., Abrahamsen H., Thoresen S.B., Stenmark H.
    Biochem. J. 441:399-406(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY NEDD4, MUTAGENESIS OF TYR-352.
  23. "Receptor signaling lymphocyte-activation molecule family 1 (Slamf1) regulates membrane fusion and NADPH oxidase 2 (NOX2) activity by recruiting a Beclin-1/Vps34/ultraviolet radiation resistance-associated gene (UVRAG) complex."
    Ma C., Wang N., Detre C., Wang G., O'Keeffe M., Terhorst C.
    J. Biol. Chem. 287:18359-18365(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLAMF1.
  24. "The human cytomegalovirus protein TRS1 inhibits autophagy via its interaction with Beclin 1."
    Chaumorcel M., Lussignol M., Mouna L., Cavignac Y., Fahie K., Cotte-Laffitte J., Geballe A., Brune W., Beau I., Codogno P., Esclatine A.
    J. Virol. 86:2571-2584(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHV-5 PROTEIN TRS1.
  25. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "XBP1 mRNA splicing triggers an autophagic response in endothelial cells through BECLIN-1 transcriptional activation."
    Margariti A., Li H., Chen T., Martin D., Vizcay-Barrena G., Alam S., Karamariti E., Xiao Q., Zampetaki A., Zhang Z., Wang W., Jiang Z., Gao C., Ma B., Chen Y.G., Cockerill G., Hu Y., Xu Q., Zeng L.
    J. Biol. Chem. 288:859-872(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  27. "Role of membrane association and Atg14-dependent phosphorylation in beclin-1-mediated autophagy."
    Fogel A.I., Dlouhy B.J., Wang C., Ryu S.W., Neutzner A., Hasson S.A., Sideris D.P., Abeliovich H., Youle R.J.
    Mol. Cell. Biol. 33:3675-3688(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-90 AND SER-93, MUTAGENESIS OF SER-90; SER-93 AND TRP-425, SUBCELLULAR LOCATION, MEMBRANE-SPANNING REGION, INTERACTION WITH PIK3C3; PIK3R4; UVRAG AND ATG14.
  28. "Rab39a interacts with phosphatidylinositol 3-kinase and negatively regulates autophagy induced by lipopolysaccharide stimulation in macrophages."
    Seto S., Sugaya K., Tsujimura K., Nagata T., Horii T., Koide Y.
    PLoS ONE 8:E83324-E83324(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB39A.
  29. "TRIM proteins regulate autophagy and can target autophagic substrates by direct recognition."
    Mandell M.A., Jain A., Arko-Mensah J., Chauhan S., Kimura T., Dinkins C., Silvestri G., Munch J., Kirchhoff F., Simonsen A., Wei Y., Levine B., Johansen T., Deretic V.
    Dev. Cell 30:394-409(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM5.
  30. "Beclin 1 is required for neuron viability and regulates endosome pathways via the UVRAG-VPS34 complex."
    McKnight N.C., Zhong Y., Wold M.S., Gong S., Phillips G.R., Dou Z., Zhao Y., Heintz N., Zong W.X., Yue Z.
    PLoS Genet. 10:E1004626-E1004626(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  31. "Architecture and dynamics of the autophagic phosphatidylinositol 3-kinase complex."
    Baskaran S., Carlson L.A., Stjepanovic G., Young L.N., Kim do J., Grob P., Stanley R.E., Nogales E., Hurley J.H.
    Elife 3:0-0(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECONSTITUTION OF THE PI3K COMPLEX I, ELECTRON MICROSCOPY OF THE PI3K COMPLEX I.
  32. "RNase L cleavage products promote switch from autophagy to apoptosis by caspase-mediated cleavage of beclin-1."
    Siddiqui M.A., Mukherjee S., Manivannan P., Malathi K.
    Int. J. Mol. Sci. 16:17611-17636(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-133 AND ASP-149.
  33. "TRIM-mediated precision autophagy targets cytoplasmic regulators of innate immunity."
    Kimura T., Jain A., Choi S.W., Mandell M.A., Schroder K., Johansen T., Deretic V.
    J. Cell Biol. 210:973-989(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MEFV; TRIM21 AND ULK1.
  34. "Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein."
    Oberstein A., Jeffrey P.D., Shi Y.
    J. Biol. Chem. 282:13123-13132(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 107-135 IN COMPLEX WITH BCL2L1, DOMAIN BH3 MOTIF.
  35. "Molecular basis of Bcl-xL's target recognition versatility revealed by the structure of Bcl-xL in complex with the BH3 domain of beclin-1."
    Feng W., Huang S., Wu H., Zhang M.
    J. Mol. Biol. 372:223-235(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 106-128 IN COMPLEX WITH BCL2L1.
  36. "Molecular basis of the regulation of Beclin 1-dependent autophagy by the gamma-herpesvirus 68 Bcl-2 homolog M11."
    Sinha S., Colbert C.L., Becker N., Wei Y., Levine B.
    Autophagy 4:989-997(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 105-130 IN COMPLEX WITH MUHV-4 M11, MUTAGENESIS OF LEU-112; LEU-116; GLY-120; ASP-121 AND PHE-123.
  37. "Targeting gamma-herpesvirus 68 Bcl-2-mediated down-regulation of autophagy."
    Su M., Mei Y., Sanishvili R., Levine B., Colbert C.L., Sinha S.
    J. Biol. Chem. 289:8029-8040(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 107-130 IN COMPLEX WITH MUHV-4 M11, MUTAGENESIS OF LEU-112; LEU-116; LYS-117; GLY-120; ASP-121 AND PHE-123.

Entry informationi

Entry nameiBECN1_HUMAN
AccessioniPrimary (citable) accession number: Q14457
Secondary accession number(s): B2R6N7, O75595, Q9UNA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 21, 2001
Last modified: June 8, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.