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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

GO - Molecular functioni

  • phosphatidylinositol 3-kinase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • activation of mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • autophagosome assembly Source: UniProtKB
  • autophagy Source: CACAO
  • beta-amyloid metabolic process Source: Ensembl
  • cellular defense response Source: ProtInc
  • 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
  • mitotic metaphase plate congression Source: CACAO
  • negative regulation of apoptotic process Source: ProtInc
  • 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 macroautophagy Source: Ensembl
  • positive regulation of mitochondrion degradation Source: ParkinsonsUK-UCL
  • receptor catabolic process Source: UniProtKB
  • regulation of catalytic activity Source: Ensembl
  • regulation of cytokinesis Source: UniProtKB
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Beclin-1
Alternative name(s):
Coiled-coil myosin-like BCL2-interacting protein
Protein GT197
Gene namesi
Name:BECN1
Synonyms:GT197
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:1034. BECN1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

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
Mutagenesisi116 – 1161L → A: Decreases interaction with BCL2L1 isoform Bcl-X(L). 1 Publication
Mutagenesisi123 – 1231F → A: Disrupts interaction with BCL2 and decreases interaction with BCL2L1 isoform Bcl-X(L). 2 Publications
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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
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

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ14457.
PaxDbiQ14457.
PRIDEiQ14457.

PTM databases

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

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 KIAA0226/Rubicon, 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 human cytomegalovirus/HHV-5 protein TRS1 (PubMed:22205736).By similarityCurated18 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AMBRA1Q9C0C78EBI-949378,EBI-2512975
ATG14Q6ZNE522EBI-949378,EBI-2690371
BCL2P1041516EBI-949378,EBI-77694
BCL2L1Q07817-14EBI-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
PIK3C3Q8NEB915EBI-949378,EBI-1056470
RAB39AQ149642EBI-949378,EBI-3048577
TAB2Q9NYJ811EBI-949378,EBI-358708
TAB3Q8N5C89EBI-949378,EBI-359964
UVRAGQ9P2Y517EBI-949378,EBI-2952704
v-bcl-2P898842EBI-949378,EBI-8849581From a different organism.
WASH1A8K0Z33EBI-949378,EBI-6160405
ZWINTO952296EBI-949378,EBI-1001132

Protein-protein interaction databases

BioGridi114226. 58 interactions.
DIPiDIP-44611N.
IntActiQ14457. 84 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 176-447.
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

Sequence similaritiesi

Belongs to the beclin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG285533.
GeneTreeiENSGT00390000008164.
HOGENOMiHOG000158093.
HOVERGENiHBG003181.
InParanoidiQ14457.
KOiK08334.
OMAiYIPPARM.
OrthoDBiEOG7D2FDG.
PhylomeDBiQ14457.
TreeFamiTF314282.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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_003757.1. NM_003766.3.
XP_005257815.1. XM_005257758.2.
UniGeneiHs.716464.

Genome annotation databases

EnsembliENST00000361523; ENSP00000355231; ENSG00000126581.
ENST00000590099; ENSP00000465364; ENSG00000126581.
GeneIDi8678.
KEGGihsa:8678.
UCSCiuc002ibn.2. 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_003757.1. NM_003766.3.
XP_005257815.1. XM_005257758.2.
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 176-447.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114226. 58 interactions.
DIPiDIP-44611N.
IntActiQ14457. 84 interactions.
MINTiMINT-2865445.
STRINGi9606.ENSP00000355231.

PTM databases

PhosphoSiteiQ14457.

Polymorphism and mutation databases

BioMutaiBECN1.
DMDMi13124704.

Proteomic databases

MaxQBiQ14457.
PaxDbiQ14457.
PRIDEiQ14457.

Protocols and materials databases

DNASUi8678.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361523; ENSP00000355231; ENSG00000126581.
ENST00000590099; ENSP00000465364; ENSG00000126581.
GeneIDi8678.
KEGGihsa:8678.
UCSCiuc002ibn.2. human.

Organism-specific databases

CTDi8678.
GeneCardsiGC17M040963.
HGNCiHGNC:1034. BECN1.
HPAiCAB010143.
HPA028949.
MIMi604378. gene.
neXtProtiNX_Q14457.
PharmGKBiPA25337.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG285533.
GeneTreeiENSGT00390000008164.
HOGENOMiHOG000158093.
HOVERGENiHBG003181.
InParanoidiQ14457.
KOiK08334.
OMAiYIPPARM.
OrthoDBiEOG7D2FDG.
PhylomeDBiQ14457.
TreeFamiTF314282.

Miscellaneous databases

ChiTaRSiBECN1. human.
EvolutionaryTraceiQ14457.
GeneWikiiBECN1.
GenomeRNAii8678.
NextBioi32555.
PROiQ14457.
SOURCEiSearch...

Gene expression databases

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

Family and domain databases

InterProiIPR007243. Atg6/Beclin.
IPR029318. BH3_dom.
[Graphical view]
PANTHERiPTHR12768. PTHR12768. 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. "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.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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; KIAA0226; PIK3C3; PIK3R4 AND UVRAG.
  16. Cited for: INTERACTION WITH HMGB1.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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.
  24. "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.
  25. "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.
  26. "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.
  27. "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.
  28. "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.
  29. "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.

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: July 22, 2015
This is version 148 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

External Data

Dasty 3

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 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.