BECN1

gene
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Also known as ATG6VPS30

Summary

BECN1 (beclin 1, HGNC:1034) is a protein-coding gene on chromosome 17q21.31, encoding Beclin-1 (Q14457). Plays a central role in autophagy.

This gene encodes a protein that regulates autophagy, a catabolic process of degradation induced by starvation. The encoded protein is a component of the phosphatidylinositol-3-kinase (PI3K) complex which mediates vesicle-trafficking processes. This protein is thought to play a role in multiple cellular processes, including tumorigenesis, neurodegeneration and apoptosis. Alternative splicing results in multiple transcript variants.

Source: NCBI Gene 8678 — RefSeq curated summary.

At a glance

  • GWAS associations: 1
  • Clinical variants (ClinVar): 55 total
  • Druggable target: yes — 1 molecules with ChEMBL bioactivity
  • MANE Select transcript: NM_001313998

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:1034
Approved symbolBECN1
Namebeclin 1
Location17q21.31
Locus typegene with protein product
StatusApproved
AliasesATG6, VPS30
Ensembl geneENSG00000126581
Ensembl biotypeprotein_coding
OMIM604378
Entrez8678

Gene structure

Transcript identifiers

Ensembl transcripts: 39 — 28 protein_coding, 8 retained_intron, 2 nonsense_mediated_decay, 1 protein_coding_CDS_not_defined

ENST00000361523, ENST00000438274, ENST00000543382, ENST00000585515, ENST00000586589, ENST00000586754, ENST00000587880, ENST00000588276, ENST00000589492, ENST00000589493, ENST00000589636, ENST00000589663, ENST00000590099, ENST00000590185, ENST00000590764, ENST00000590852, ENST00000591085, ENST00000591307, ENST00000593112, ENST00000593205, ENST00000612631, ENST00000617806, ENST00000893287, ENST00000893288, ENST00000893289, ENST00000893290, ENST00000893291, ENST00000893292, ENST00000893293, ENST00000893294, ENST00000893295, ENST00000922825, ENST00000967385, ENST00000967386, ENST00000967387, ENST00000967388, ENST00000967389, ENST00000967390, ENST00000967391

RefSeq mRNA: 4 — MANE Select: NM_001313998 NM_001313998, NM_001313999, NM_001314000, NM_003766

CCDS: CCDS11441, CCDS82132

Canonical transcript exons

ENST00000590099 — 12 exons

ExonStartEnd
ENSE000027765434281013442810928
ENSE000028250264282415542824282
ENSE000034867214281452442814673
ENSE000034885574281590842816054
ENSE000035036964281394842814008
ENSE000035137984281854442818680
ENSE000035822144282077442820841
ENSE000036000574282374842823879
ENSE000036107784281878742818877
ENSE000036118974281822142818415
ENSE000036466804281165542811797
ENSE000036922904281954842819609

Expression profiles

Bgee: expression breadth ubiquitous, 295 present calls, max score 97.31.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 58.7304 / max 267.3426, expressed in 1827 samples.

FANTOM5 promoters (1 alternative TSS)

Promoter IDTPM avgSamples expressed
16618958.73041827

Top tissues by expression

295 total, by Bgee expression score (0-100, higher = more expressed):

TissueAnatomy IDExpression scoreQuality
rectumUBERON:000105297.31gold quality
colonic epitheliumUBERON:000039797.08gold quality
monocyteCL:000057696.99gold quality
mononuclear cellCL:000084296.81gold quality
leukocyteCL:000073896.74gold quality
calcaneal tendonUBERON:000370196.67gold quality
mucosa of stomachUBERON:000119996.61gold quality
lower esophagus muscularis layerUBERON:003583396.50gold quality
lower esophagusUBERON:001347396.48gold quality
skeletal muscle tissue of rectus abdominisUBERON:000451196.26gold quality
gastrocnemiusUBERON:000138896.17gold quality
olfactory segment of nasal mucosaUBERON:000538696.15gold quality
muscle of legUBERON:000138396.13gold quality
muscle layer of sigmoid colonUBERON:003580596.09gold quality
stromal cell of endometriumCL:000225596.08gold quality
Brodmann (1909) area 10UBERON:001354196.04gold quality
transverse colonUBERON:000115796.01gold quality
sigmoid colonUBERON:000115995.95gold quality
colonUBERON:000115595.91gold quality
large intestineUBERON:000005995.87gold quality
esophagogastric junction muscularis propriaUBERON:003584195.82gold quality
mucosa of transverse colonUBERON:000499195.79gold quality
islet of LangerhansUBERON:000000695.77gold quality
jejunal mucosaUBERON:000039995.75gold quality
granulocyteCL:000009495.74gold quality
muscle organUBERON:000163095.73gold quality
intestineUBERON:000016095.67gold quality
frontal poleUBERON:000279595.66gold quality
nasal cavity mucosaUBERON:000182695.58gold quality
esophagusUBERON:000104395.51gold quality

Single-cell (SCXA)

Detected in 2 experiment(s), a significant marker in 1.

ExperimentMarker?Max mean expression
E-ANND-3yes10.94
E-HCAD-31no1.88

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): ADNP, APP, ATF3, HBP1, JUN, NFKBID, PEG3, RELA, RELB, ROCK1, SIRT5, STAT3, TXK

miRNA regulators (miRDB)

57 targeting BECN1, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNAMax scoreAvg scoremiRNA target_count
HSA-MIR-30A-5P100.0076.313233
HSA-MIR-30B-5P100.0076.293248
HSA-MIR-30C-5P100.0076.293248
HSA-MIR-30D-5P100.0076.323233
HSA-MIR-30E-5P100.0076.323242
HSA-MIR-188-3P100.0068.761240
HSA-MIR-4668-3P100.0068.742635
HSA-MIR-520D-5P99.9873.344883
HSA-MIR-524-5P99.9873.434882
HSA-MIR-477599.9875.006394
HSA-MIR-4482-3P99.9872.503147
HSA-MIR-570-3P99.9672.414910
HSA-MIR-311999.9271.342390
HSA-MIR-10527-5P99.9172.283754
HSA-MIR-548E-5P99.8972.734486
HSA-MIR-391999.8769.452489
HSA-MIR-132399.8369.892471
HSA-MIR-498-5P99.7669.641807
HSA-MIR-556-3P99.7468.751203
HSA-MIR-548O-3P99.7469.302228
HSA-MIR-519A-3P99.6771.671868
HSA-MIR-519B-3P99.6771.671868
HSA-MIR-519C-3P99.6771.671870
HSA-MIR-452-5P99.6569.631762
HSA-MIR-4676-3P99.6569.311733
HSA-MIR-892C-3P99.6569.381745
HSA-MIR-875-3P99.6369.472548
HSA-MIR-129099.5969.902079
HSA-MIR-513A-3P99.3970.633620
HSA-MIR-513C-3P99.3970.633620

Literature-anchored findings (GeneRIF, showing 40)

  • expression of three (Beclin 1, RbAp48 and Pir51) were increased and one (aldolase b) was decreased in liver tumor tissues. (PMID:14966907)
  • C(2)-ceramide stimulated macroautophagy in colon cancer cells, stimulated the expression of the autophagy gene product beclin 1, and mediated tamoxifen-dependent accumulation of autophagic vacuoles in breast cancer MCF-7 cells (PMID:14970205)
  • BECLIN 1 augmented cisplatin-induced apoptosis via enhancing caspase 9 activity. (PMID:15922724)
  • VPS30/ATG6 complemented A1PiZ degradation-deficient (add3) yeast mutants (PMID:16267277)
  • Results argue against a role for Beclin 1 as an essential chaperone or adaptor for hVps34 in normal vesicular trafficking, and they support the hypothesis that Beclin 1 functions mainly to engage hVps34 in the autophagic pathway. (PMID:16390869)
  • age-dependent decrease of beclin 1 expression may lead to a reduction of autophagic activity during aging, which in turn promotes the accumulation of mutant Htt and the progression of the disease (PMID:16522639)
  • Partial Beclin 1 silencing aggravates mitochondrial permeabilization and apoptosis in HepG2 cells treated with an anti-Fas antibody or with doxorubicin (PMID:16718815)
  • Evolutionarily conserved domain of Beclin 1 is essential for Vps34 interaction, autophagy function, and tumor suppressor function. (PMID:16874027)
  • Beclin 1 has different roles in different histotypes of human brain tumours (PMID:17203225)
  • Expression of autophagy gene Beclin 1 decreases in cervical aquamous cell carcinoma. (PMID:17236580)
  • Kringle 5 of human plasminogen has a role in autophagic survival by up-regulating Beclin 1 and complexing Bcl-2 to Beclin 1 (PMID:17272502)
  • Beclin1 expression is down-regulated in epithelial ovarian cancer tissues, and overexpression can inhibit proliferation and induce apoptosis of SKOV3 cells. (PMID:17355787)
  • BH3-only proteins and BH3 mimetics induce autophagy by competitively disrupting the interaction between BECN1 and Bcl-2/Bcl-X(L). (PMID:17438366)
  • The constructed vector significantly inhibited the expression of the mRNA and protein of Beclin 1 in the HeLa cells. (PMID:17441324)
  • Beclin 1 expression is down-regulated in epithelial ovarian cancer tissue while the p110alpha, hvps34 and p-PKB are having the abnormal expressions on PI3K/PKB signaling pathway. (PMID:17441338)
  • The functional and physical interaction between Bcl-X(L) and a BH3-like domain in BECN1 was studied. (PMID:17446862)
  • this is the first report on BECN1 gene mutations in human cancer tissues, and the data suggest that point mutations are a rare event in common human cancers and probably do not play a major role in cancer pathogenesis (PMID:17550384)
  • These results indicate that Beclin 1 can inhibit the growth of colorectal cancer cells. (PMID:17595761)
  • Differential interactions between BECN1 and Bcl-2 family members are reported. (PMID:17643073)
  • Analysis of all known Bcl-xL/BH3 domain complexes. (PMID:17659302)
  • Autophagy also plays an essential role in tumorigenesis, as the essential autophagy regulator BECN1 is monoallelically deleted. (PMID:17786023)
  • Data suggest that beclin 1 plays important roles in the regulation of the life span of human CL and ovarian androgen-secreting cells, by maintaining autophagy at levels promoting cell survival rather than cell death. (PMID:17999086)
  • Data suggest that ICP34.5-mediated antagonism of the autophagy function of Beclin 1 is essential for viral neurovirulence, and the antiviral signaling molecule PKR lies genetically upstream of Beclin 1 in host defense against HSV-1. (PMID:18005679)
  • beclin-1 inactivation by loss of expression may not occur in colorectal and gastric cancers (PMID:18184403)
  • The positive rates of Beclin1 and MAPLC3 were significantly lower in non-small cell lung cancer tissues than in adjacent non-cancerous tissues and normal tissues. (PMID:18184459)
  • Abeta pathology is regulated by beclin 1 through a pathway that involves autophagy (PMID:18497881)
  • beclin 1 deficiency disrupts neuronal autophagy, modulates APP metabolism, and promotes neurodegeneration (PMID:18497889)
  • Data suggest that a Beclin1-binding autophagic tumour suppressor, UVRAG, interacts with the class C Vps complex, a key component of the endosomal fusion machinery. (PMID:18552835)
  • beclin 1 has a role in vitamin D3-induced autophagy of human myeloid leukemia cells (PMID:18628207)
  • Bcl-xL and UVRAG cause a monomer-dimer switch in Beclin1 (PMID:18641390)
  • These results demonstrate that Beclin 1 is essential for autophagy, differentiation and antiapoptosis, and may play an important role in coordinating inputs for cellular decisions to signaling machinery that mediates different cellular cascades. (PMID:18769161)
  • gamma-Herpesvirus protein M11 inhibits autophagy through a mechanism that involves the binding of the Beclin 1 BH3 domain in the M11 hydrophobic surface groove. (PMID:18797192)
  • Beclin 1 can down-regulate estrogenic signaling and growth response, and contribute to the development of antiestrogen resistance. (PMID:18829541)
  • These results suggest that mammalian cells have at least two distinct class III PI3-kinase complexes, and that beclin 1 interacts distinctly with mammalian Atg14 and UVRAG in two of these complexes. (PMID:18843052)
  • study defines a regulatory signaling pathway mediated by Barkor (KIAA0831) that positively controls autophagy through Beclin 1 (PMID:19050071)
  • activation of JNK pathway can mediate Beclin 1 expression, which plays a key role in autophagic cell death in cancer cells (PMID:19060920)
  • beclin 1 has a role in favorable prognosis in stage IIIB colon cancers (PMID:19066461)
  • beclin-1 and HIF-1alpha expression are important determinants of survival in esophageal squamous cell carcinoma (PMID:19130303)
  • Beclin 1-dependent apoptotic activity has a role in preventing progression of hepatocellular carcinoma (PMID:19145109)
  • Data show that DAPK phosphorylates beclin 1 on Thr 119 located at a crucial position within its BH3 domain, and thus promotes the dissociation of beclin 1 from Bcl-XL and the induction of autophagy. (PMID:19180116)

Cross-species orthologs

5 orthologs

OrganismSymbolGene ID
danio_reriobecn1ENSDARG00000079128
mus_musculusBecn1ENSMUSG00000035086
rattus_norvegicusBecn1ENSRNOG00000020513
drosophila_melanogasterAtg6FBGN0264325
caenorhabditis_elegansWBGENE00000247

Paralogs (1): BECN2 (ENSG00000196289)

Protein

Protein identifiers

Beclin-1Q14457 (reviewed: Q14457)

Alternative names: Coiled-coil myosin-like BCL2-interacting protein, Protein GT197

All UniProt accessions (13): Q14457, A0A024R1X5, A0A087WVZ2, E7EV84, K7EKK2, K7EL88, K7ELY9, K7EMA2, K7EN35, K7EQQ7, K7ER46, K7ERY0, K7ES83

UniProt curated annotations — full annotation on UniProt →

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. Beclin-1-C 35 kDa localized to mitochondria can promote apoptosis; it induces the mitochondrial translocation of BAX and the release of proapoptotic factors. (Microbial infection) Protects against infection by a neurovirulent strain of Sindbis virus.

Subunit / interactions. 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. 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/auxiliary subunits to form alternative complex forms. Alternative complex forms containing a fourth 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. Both, PI3KC3-C1 and PI3KC3-C2, can associate with further regulatory subunits, such as RUBCN, SH3GLB1/Bif-1 and AMBRA1. PI3KC3-C1 probably associates with PIK3CB. Forms a complex with PPP2CA and AMBRA1; AMBRA1 and BECN1 components of the complex regulate MYC stability via different pathways. Component of the complex, at least composed of LRPPRC, BECN1 and BCL2; the interactions prevent BECN1 from forming an autophagy-inducing complex with PIK3C3. Interacts with AMBRA1, GOPC, GRID2. 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. Interacts with cytosolic HMGB1; inhibits the interaction of BECN1 and BCL2 leading to promotion of autophagy. Interacts with USP10, USP13, VMP1, DAPK1, RAB39A. Interacts with the poly-Gln domain of ATXN3; the interaction causes deubiquitination at Lys-402 and stabilizes BECN1. Interacts with SLAMF1. Interacts with TRIM5; the interaction causes activation of BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. Interacts with active ULK1 (phosphorylated on ‘Ser-317’) and MEFV simultaneously. Interacts with WDR81 and WDR91; negatively regulates the PI3 kinase/PI3K activity associated with endosomal membranes. Interacts with LAPTM4B; competes with EGFR for LAPTM4B binding; regulates EGFR activity. Interacts with TRIM50. Interacts with TRIM16. Interacts with ATG14; this interaction is increased in the absence of TMEM39A. Interacts with WASHC1; preventing interaction with AMBRA1 and the DCX(AMBRA1) complex and subsequent ubiquitination. Interacts with TRIM17. Interacts with BCL2L10/BCL-B (via BH1 domain). Interacts with SH3BGRL. Interacts with IRGM; enhancing BECN1-interacting partners and influencing the composition of the BECN1 complex. Interacts with ARMC3. Interacts with LRPPRC. (Microbial infection) Interacts with human cytomegalovirus/HHV-5 protein TRS1. (Microbial infection) Interacts with murine gammaherpesvirus 68 M11. (Microbial infection) Interacts with herpes simplex virus 1 (HHV-1) protein ICP34.5; this interaction antagonizes the host autophagy response. (Microbial infection) Interacts with Epstein-Barr virus protein BHRF1; this interaction inhibits BECN1-mediated autophagy induction.

Subcellular location. Cytoplasm. Golgi apparatus. trans-Golgi network membrane. Endosome membrane. Endoplasmic reticulum membrane. Mitochondrion membrane. Endosome. Cytoplasmic vesicle. Autophagosome Mitochondrion. Nucleus. Cytoplasm Mitochondrion.

Tissue specificity. Ubiquitous.

Post-translational modifications. Phosphorylation at Thr-119 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. Polyubiquitinated by NEDD4, both with ‘Lys-11’- and ‘Lys-63’-linkages. ‘Lys-11’-linked polyubiquitination 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. Polyubiquitinated at Lys-402 with ‘Lys-48’-linkages. ‘Lys-48’-linked polyubiquitination of Lys-402 leads to degradation. Deubiquitinated by ATXN3, leading to stabilization. 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. ‘Lys-48’-linked ubiquitination by RNF216 leads to proteasomal degradation and autophagy inhibition. 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.

Domain organisation. 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. The C-terminal evolutionary conserved domain (ECD) contains poly-Gln-binding domains such as the ATXN3 poly-Gln motif, consistent with structural docking models revealing two highly scored poly-Gln-binding pockets in the ECD. As some binding is observed with BECN1 lacking the ECD, other domains of BECN1 may also interact with ATXN3.

Miscellaneous. Expanded poly-Gln tracts inhibit ATXN3-BECN1 interaction, decrease BECN1 levels and impair starvation-induced autophagy.

Similarity. Belongs to the beclin family.

RefSeq proteins (4): NP_001300927, NP_001300928, NP_001300929, NP_003757 (=MANE)

Domains & families (InterPro)

IDNameType
IPR007243Atg6/BeclinFamily
IPR029318BH3_domDomain
IPR038274Atg6/Beclin_C_sfHomologous_superfamily
IPR040455Atg6_BARADomain
IPR041691Atg6/beclin_CCDomain

Pfam: PF04111, PF15285, PF17675

UniProt features (63 total): mutagenesis site 19, strand 10, helix 9, modified residue 7, region of interest 4, chain 3, sequence conflict 3, cross-link 2, sequence variant 2, turn 2, coiled-coil region 1, short sequence motif 1

Structure

Experimental structures (PDB)

31 structures, top 30 by resolution.

PDBMethodResolution (Å)
6HOIX-RAY DIFFRACTION1.14
5HHEX-RAY DIFFRACTION1.46
6HOJX-RAY DIFFRACTION1.51
4DDPX-RAY DIFFRACTION1.55
6HOKX-RAY DIFFRACTION1.61
5VAUX-RAY DIFFRACTION1.75
5VAYX-RAY DIFFRACTION1.8
5EFMX-RAY DIFFRACTION1.95
5VAXX-RAY DIFFRACTION2
4MI8X-RAY DIFFRACTION2.1
6DCOX-RAY DIFFRACTION2.2
6DCNX-RAY DIFFRACTION2.44
2P1LX-RAY DIFFRACTION2.5
3DVUX-RAY DIFFRACTION2.5
9MHFELECTRON MICROSCOPY2.73
9RX5ELECTRON MICROSCOPY3.15
9MHGELECTRON MICROSCOPY3.2
9ZPDELECTRON MICROSCOPY3.38
9RX6ELECTRON MICROSCOPY3.52
13BVELECTRON MICROSCOPY3.77
9ZPCELECTRON MICROSCOPY3.83
9RX8ELECTRON MICROSCOPY3.87
9RX9ELECTRON MICROSCOPY3.99
9RXAELECTRON MICROSCOPY4
9RXBELECTRON MICROSCOPY4.03
9MHHELECTRON MICROSCOPY4.5
9C82ELECTRON MICROSCOPY6.84
7BL1ELECTRON MICROSCOPY9.8
9S47ELECTRON MICROSCOPY9.88
2PONSOLUTION NMR

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-Q14457-F177.370.40

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Post-translational modifications (9): 15, 30, 90, 93, 96, 119, 402, 437, 1

Mutagenesis-validated functional residues (19):

PositionPhenotype
90complete loss of phosphorylation. complete loss of phosphorylation and defective autophagic function; when associated wi
93partial loss of phosphorylation. complete loss of phosphorylation and defective autophagic function; when associated wit
112weakly decreases interaction with muhv-4 m11, greatly decreases interaction with bcl2l1 isoform bcl-x(l).
116decreases interaction with bcl2l1 isoform bcl-x(l).
117weakly decreases interaction with muhv-4 m11, greatly decreases interaction with bcl2l1 isoform bcl-x(l).
117does not affect ubiquitination by the dcx(ambra1) complex.
120–121weakly decreases interaction with muhv-4 m11, disrupts interaction with bcl2l1 isoform bcl-x(l).
120decreases interaction with muhv-4 m11, disrupts interaction with bcl2l1 isoform bcl-x(l).
121no effect on interaction with muhv-4 m11, disrupts interaction with bcl2l1 isoform bcl-x(l).
123weakly decreases interaction with muhv-4 m11, disrupts interaction with bcl2 and decreases interaction with bcl2l1 isofo
133abolishes in vitro cleavage by casp3 and casp8; when associated with a-149.
133abolishes in vitro cleavage by casp8; when associated with a-146.
146abolishes in vitro cleavage by casp8; when associated with a-133.
149abolishes in vitro cleavage by casp3 and casp8; when associated with a-133.
149abolishes in vitro cleavage by casp3.
352significantly reduces ubiquitination.
402decreases k48 polyubiquitination and stabilizes becn1.
425decrease in membrane-association.
437abolished ubiquitination by the dcx(ambra1) complex.

Function

Pathways and Gene Ontology

Reactome pathways

28 pathways

IDPathway
R-HSA-1169408ISG15 antiviral mechanism
R-HSA-1632852Macroautophagy
R-HSA-5689880Ub-specific processing proteases
R-HSA-9679504Translation of Replicase and Assembly of the Replication Transcription Complex
R-HSA-9694676Translation of Replicase and Assembly of the Replication Transcription Complex
R-HSA-9705671SARS-CoV-2 activates/modulates innate and adaptive immune responses
R-HSA-983170Antigen Presentation: Folding, assembly and peptide loading of class I MHC
R-HSA-9833110RSV-host interactions
R-HSA-9920951Dengue virus modulates apoptosis
R-HSA-1169410Antimicrobial mechanism of IFN-stimulated genes
R-HSA-1280215Cytokine Signaling in Immune system
R-HSA-1280218Adaptive Immune System
R-HSA-1643685Disease
R-HSA-168256Immune System
R-HSA-392499Metabolism of proteins
R-HSA-5663205Infectious disease
R-HSA-5688426Deubiquitination
R-HSA-597592Post-translational protein modification
R-HSA-913531Interferon Signaling
R-HSA-9612973Autophagy
R-HSA-9678108SARS-CoV-1 Infection
R-HSA-9679506SARS-CoV Infections
R-HSA-9694516SARS-CoV-2 Infection
R-HSA-9705683SARS-CoV-2-host interactions
R-HSA-9772572Early SARS-CoV-2 Infection Events
R-HSA-9820952Respiratory Syncytial Virus Infection Pathway
R-HSA-9824446Viral Infection Pathways
R-HSA-983169Class I MHC mediated antigen processing & presentation

MSigDB gene sets: 427 (showing top): GSE18804_SPLEEN_MACROPHAGE_VS_TUMORAL_MACROPHAGE_UP, GSE18804_BRAIN_VS_COLON_TUMORAL_MACROPHAGE_UP, GOBP_CIRCADIAN_RHYTHM, GOBP_SMAD_PROTEIN_SIGNAL_TRANSDUCTION, GOBP_CHROMOSOME_ORGANIZATION, GOBP_ATTACHMENT_OF_SPINDLE_MICROTUBULES_TO_KINETOCHORE, GOBP_REGULATION_OF_AUTOPHAGY, GOBP_PHOSPHOLIPID_METABOLIC_PROCESS, GOBP_PHOSPHATIDYLINOSITOL_METABOLIC_PROCESS, GOBP_LYSOSOMAL_TRANSPORT, GOBP_VACUOLE_ORGANIZATION, REACTOME_ADAPTIVE_IMMUNE_SYSTEM, GOBP_SKELETAL_SYSTEM_DEVELOPMENT, GOBP_INTRACELLULAR_PROTEIN_TRANSPORT, REACTOME_CYTOKINE_SIGNALING_IN_IMMUNE_SYSTEM

GO Biological Process (60): autophagosome assembly (GO:0000045), mitophagy (GO:0000423), response to hypoxia (GO:0001666), cytoplasmic pattern recognition receptor signaling pathway (GO:0002753), protein targeting to lysosome (GO:0006622), autophagy (GO:0006914), apoptotic process (GO:0006915), cellular defense response (GO:0006968), cellular response to nitrogen starvation (GO:0006995), lysosome organization (GO:0007040), mitotic metaphase chromosome alignment (GO:0007080), JNK cascade (GO:0007254), circadian rhythm (GO:0007623), negative regulation of cell population proliferation (GO:0008285), protein secretion (GO:0009306), response to xenobiotic stimulus (GO:0009410), response to iron(II) ion (GO:0010040), response to lead ion (GO:0010288), regulation of autophagy (GO:0010506), positive regulation of autophagy (GO:0010508), positive regulation of cardiac muscle hypertrophy (GO:0010613), macroautophagy (GO:0016236), regulation of macroautophagy (GO:0016241), regulation of cytokinesis (GO:0032465), receptor catabolic process (GO:0032801), response to vitamin E (GO:0033197), cellular response to amino acid starvation (GO:0034198), phosphatidylinositol-3-phosphate biosynthetic process (GO:0036092), p38MAPK cascade (GO:0038066), cellular response to glucose starvation (GO:0042149), negative regulation of apoptotic process (GO:0043066), negative regulation of programmed cell death (GO:0043069), engulfment of apoptotic cell (GO:0043652), early endosome to late endosome transport (GO:0045022), late endosome to vacuole transport (GO:0045324), neuron development (GO:0048666), amyloid-beta metabolic process (GO:0050435), cell division (GO:0051301), defense response to virus (GO:0051607), positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction (GO:0051897)

GO Molecular Function (8): protein kinase binding (GO:0019901), protein-macromolecule adaptor activity (GO:0030674), ubiquitin protein ligase binding (GO:0031625), identical protein binding (GO:0042802), phosphatidylinositol 3-kinase binding (GO:0043548), GTPase binding (GO:0051020), molecular adaptor activity (GO:0060090), protein binding (GO:0005515)

GO Cellular Component (23): phagophore assembly site (GO:0000407), cytoplasm (GO:0005737), endosome (GO:0005768), autophagosome (GO:0005776), endoplasmic reticulum (GO:0005783), endoplasmic reticulum membrane (GO:0005789), trans-Golgi network (GO:0005802), cytosol (GO:0005829), endosome membrane (GO:0010008), nuclear body (GO:0016604), dendrite (GO:0030425), cytoplasmic side of mitochondrial outer membrane (GO:0032473), phosphatidylinositol 3-kinase complex, class III, type I (GO:0034271), phosphatidylinositol 3-kinase complex, class III, type II (GO:0034272), phosphatidylinositol 3-kinase complex, class III (GO:0035032), phagocytic vesicle (GO:0045335), nucleus (GO:0005634), mitochondrion (GO:0005739), Golgi apparatus (GO:0005794), membrane (GO:0016020), cytoplasmic vesicle (GO:0031410), mitochondrial membrane (GO:0031966), protein-containing complex (GO:0032991)

Reactome top-level categories

Rollup of top-15 pathways:

CategoryPathways
Immune System2
Antimicrobial mechanism of IFN-stimulated genes1
Autophagy1
Deubiquitination1
SARS-CoV-1 Infection1
Early SARS-CoV-2 Infection Events1
SARS-CoV-2-host interactions1
Class I MHC mediated antigen processing & presentation1
Respiratory Syncytial Virus Infection Pathway1
Dengue Virus-Host Interactions1
Interferon Signaling1
Disease1
Post-translational protein modification1
Metabolism of proteins1
Cytokine Signaling in Immune system1

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
cytoplasm5
cellular anatomical structure4
intracellular membrane-bounded organelle4
protein binding3
endomembrane system3
autophagy2
binding2
phosphatidylinositol 3-kinase complex, class III2
Atg12 activating enzyme activity1
protein-phosphatidylethanolamide deconjugating activity1
Atg12 conjugating enzyme activity1
Atg12 ligase activity1
organelle assembly1
Atg1/ULK1 kinase complex assembly1
autophagosome organization1
autophagy of mitochondrion1
macroautophagy1
response to stress1
response to decreased oxygen levels1
positive regulation of cytokine production1
pattern recognition receptor signaling pathway1
intracellular receptor signaling pathway1
protein targeting to vacuole1
lysosomal transport1
protein localization to lysosome1
catabolic process1
transmembrane transport1
process utilizing autophagic mechanism1
programmed cell death1
apoptotic signaling pathway1
execution phase of apoptosis1
defense response1
cellular response to starvation1
cellular response to nitrogen levels1
lytic vacuole organization1
mitotic sister chromatid segregation1
mitotic cell cycle1
metaphase chromosome alignment1
mitotic cell cycle process1
MAPK cascade1

Protein interactions and networks

STRING

3790 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
BECN1ATG14Q6ZNE5999
BECN1PIK3C3Q8NEB9999
BECN1UVRAGQ9P2Y5999
BECN1PIK3R4Q99570999
BECN1BCL2P10415999
BECN1AMBRA1Q9C0C7999
BECN1RUBCNQ92622998
BECN1BCL2L1Q07817996
BECN1ULK1O75385995
BECN1NRBF2Q96F24994
BECN1MCL1Q07820994
BECN1VMP1Q96GC9993
BECN1SH3GLB1Q9Y371993
BECN1MYD88P78397990
BECN1HMGB1P09429988

IntAct

452 interactions, top by confidence:

ABTypeScore
ATG14BECN1psi-mi:“MI:0915”(physical association)0.980
ATG14BECN1psi-mi:“MI:0407”(direct interaction)0.980
BECN1ATG14psi-mi:“MI:0914”(association)0.980
ATG14BECN1psi-mi:“MI:0914”(association)0.980
BECN1ATG14psi-mi:“MI:0915”(physical association)0.980
BECN1ATG14psi-mi:“MI:0407”(direct interaction)0.980

BioGRID (682): BECN1 (Co-purification), BCL2 (Co-purification), BCL2 (Reconstituted Complex), BCL2L1 (Reconstituted Complex), BECN1 (Reconstituted Complex), UVRAG (Reconstituted Complex), BECN1 (Affinity Capture-Western), BCL2L1 (Affinity Capture-Western), UVRAG (Affinity Capture-Western), ATG14 (Affinity Capture-Western), BECN1 (Affinity Capture-Western), BECN1 (Affinity Capture-Western), BECN1 (Affinity Capture-Western), PIK3C3 (Affinity Capture-Western), BECN1 (Affinity Capture-Western)

ESM2 similar proteins: A0AUQ6, A2BE76, O14645, O18973, O35427, O35473, O55003, O88447, O88597, P50503, Q05B58, Q12983, Q13901, Q14457, Q14AM7, Q14CZ0, Q28HY5, Q32KN2, Q32PE4, Q4A1L3, Q4A1L4, Q4A1L5, Q4R3K5, Q4R8N2, Q4RLT3, Q52LA3, Q5JSJ4, Q5NVP8, Q5R878, Q5RBU4, Q5TKA1, Q5ZHS3, Q5ZJQ3, Q68FJ8, Q6DKA1, Q6GMH0, Q6GP52, Q6PAX8, Q6X4M3, Q7TSU0

Diamond homologs: A5DIV5, A8MW95, I1S4N7, O88597, P0DM65, P87117, Q14457, Q22592, Q4A1L3, Q4A1L4, Q4A1L5, Q54JI9, Q55CC5, Q5R878, Q5ZKS6, Q6GP52, Q91XJ1, Q9VCE1, F1RCP1, Q9M367, W0TD11, Q02948, Q6FP39

SIGNOR signaling

42 interactions.

AEffectBMechanism
UVRAG“up-regulates activity”BECN1binding
BCL2down-regulatesBECN1binding
BCL2L1down-regulatesBECN1binding
AMBRA1“up-regulates activity”BECN1binding
GOPCup-regulatesBECN1binding
SH3GLB1up-regulatesBECN1binding
DAPK1up-regulatesBECN1phosphorylation
BECN1up-regulatesAutophagosome_formation
USP13“up-regulates quantity by stabilization”BECN1deubiquitination
BECN1“up-regulates quantity by stabilization”USP13deubiquitination
BECN1“up-regulates quantity by stabilization”USP10deubiquitination
USP10“up-regulates quantity by stabilization”BECN1deubiquitination
SIRT5“up-regulates quantity by expression”BECN1“transcriptional regulation”
CHEK2“up-regulates activity”BECN1phosphorylation
STYK1“up-regulates activity”BECN1phosphorylation
BECN1“up-regulates activity”ZWINTbinding
KLHL20“down-regulates quantity by destabilization”BECN1binding
“Cullin 3-RBX1-Skp1”“down-regulates quantity by destabilization”BECN1polyubiquitination
JAK2“up-regulates activity”BECN1phosphorylation
ROCK1“up-regulates activity”BECN1phosphorylation
JAK2“up-regulates quantity”BECN1phosphorylation
MAPKAPK2“up-regulates activity”BECN1phosphorylation
EGFR“down-regulates activity”BECN1phosphorylation
STK4“up-regulates activity”BECN1phosphorylation

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 86 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

PathwayPartnersFoldFDR
Activation of BAD and translocation to mitochondria559.5×9e-06
Activation of BH3-only proteins538.8×2e-05
RHO GTPases activate PKNs629.7×1e-05
Intrinsic Pathway for Apoptosis627.4×1e-05
Apoptosis615.7×2e-04
FCGR3A-mediated phagocytosis514.6×9e-04
Translocation of SLC2A4 (GLUT4) to the plasma membrane614.5×2e-04
Programmed Cell Death613.7×2e-04

GO biological processes:

GO termPartnersFoldFDR
autophagy811.9×1e-04
actin cytoskeleton organization77.5×6e-03
negative regulation of apoptotic process136.1×9e-05

Disease & clinical

Clinical variants and AI predictions

ClinVar

55 variants total. Per-class counts are floors (≥ shown; pagination cap):

ClassificationCount (floor)
Pathogenic0
Likely pathogenic0
Uncertain significance38
Likely benign3
Benign1

Top pathogenic / likely-pathogenic (0)

SpliceAI

1640 predictions. Top by Δscore:

VariantEffectΔscore
17:42810924:CCATC:Cacceptor_gain1.0000
17:42810925:CATC:Cacceptor_gain1.0000
17:42810925:CATCC:Cacceptor_gain1.0000
17:42810926:ATCC:Aacceptor_loss1.0000
17:42810927:TC:Tacceptor_gain1.0000
17:42810927:TCCTG:Tacceptor_loss1.0000
17:42810928:CC:Cacceptor_gain1.0000
17:42810929:C:CCacceptor_gain1.0000
17:42810929:C:CGacceptor_loss1.0000
17:42810930:T:Aacceptor_loss1.0000
17:42810935:A:ACacceptor_gain1.0000
17:42814523:CCT:Cdonor_gain1.0000
17:42814547:ATTGG:Adonor_gain1.0000
17:42814669:TGTGC:Tacceptor_gain1.0000
17:42815953:T:Cdonor_gain1.0000
17:42816054:CCTG:Cacceptor_loss1.0000
17:42816056:T:Aacceptor_loss1.0000
17:42816066:C:CTacceptor_gain1.0000
17:42816067:A:Tacceptor_gain1.0000
17:42818216:CTCA:Cdonor_gain1.0000
17:42818217:TCAC:Tdonor_loss1.0000
17:42818218:CA:Cdonor_loss1.0000
17:42818219:A:ACdonor_gain1.0000
17:42818219:AC:Adonor_loss1.0000
17:42818220:C:CCdonor_gain1.0000
17:42818220:CT:Cdonor_gain1.0000
17:42818220:CTG:Cdonor_gain1.0000
17:42818220:CTGA:Cdonor_gain1.0000
17:42818220:CTGAG:Cdonor_gain1.0000
17:42818223:AGCTT:Adonor_gain1.0000

AlphaMissense

3001 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
17:42810794:A:GL440P1.000
17:42810801:A:GW438R1.000
17:42810801:A:TW438R1.000
17:42810802:C:AK437N1.000
17:42810802:C:GK437N1.000
17:42810804:T:CK437E1.000
17:42810806:A:GL436P1.000
17:42810808:A:CN435K1.000
17:42810808:A:TN435K1.000
17:42810815:A:GL433P1.000
17:42810823:C:AK430N1.000
17:42810823:C:GK430N1.000
17:42810825:T:CK430E1.000
17:42810827:A:GL429P1.000
17:42810827:A:TL429H1.000
17:42810836:G:AT426I1.000
17:42810838:C:AW425C1.000
17:42810838:C:GW425C1.000
17:42810839:C:GW425S1.000
17:42810840:A:GW425R1.000
17:42810840:A:TW425R1.000
17:42810865:T:AK416N1.000
17:42810865:T:GK416N1.000
17:42810869:A:TI415N1.000
17:42811714:A:CC375W1.000
17:42811721:A:GL373P1.000
17:42811736:G:TA368E1.000
17:42811742:T:AD366V1.000
17:42811742:T:GD366A1.000
17:42811743:C:GD366H1.000

dbSNP variants (sampled 300 via entrez): RS1000319622 (17:42815410 C>T), RS1000350652 (17:42815205 T>A), RS1000846044 (17:42825278 C>T), RS1001133326 (17:42823331 T>C), RS1001748491 (17:42819023 G>C,T), RS1001750012 (17:42825532 C>A,G), RS1001904751 (17:42823620 A>G), RS1002023231 (17:42816731 G>A), RS1002522443 (17:42812825 G>C), RS1002675834 (17:42820120 C>T), RS1002702838 (17:42821099 C>T), RS1003170034 (17:42825007 C>G,T), RS1003669856 (17:42819008 G>A), RS1003972017 (17:42811044 T>G), RS1003981614 (17:42813258 G>A,C)

Disease associations

OMIM: gene MIM:604378 | disease phenotypes:

GenCC curated gene-disease

Mondo (0):

Orphanet (0):

HPO phenotypes

0 total (0 of 0 shown, HPO-id order):

GWAS associations

1 associations (top):

StudyTraitp-value
GCST004125_13Type 2 diabetes (age of onset)3.000000e-06

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (2): CHEMBL4296010 (SINGLE PROTEIN), CHEMBL6066579 (PROTEIN COMPLEX)

Molecules with ChEMBL bioactivity

1 molecules (phase ≥1), by development phase (incl. off-target/promiscuous compounds). Patent mentions across the top 20 by phase: 4,288 (via chembl_molecule»patent_compound — counts attach to the compound, not the gene–compound relationship, so off-target/promiscuous molecules can dominate).

MoleculeNamePhasePatents
CHEMBL376408ABT 73714,288

PharmGKB: 1 entry (VIP=true, CPIC=false)

ChEMBL bioactivities

44 potent at pChembl≥5 of 52 total, top 44 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChemblTypeValueUnitMolecule
7.20IC5063nMCHEMBL5203263
7.00Kd100nMCHEMBL5091207
6.74IC50184nMCHEMBL5201326
6.56IC50274nMCHEMBL5188416
6.48Kd330nMCHEMBL5083528
6.46IC50349nMCHEMBL5179160
6.46IC50349nMCHEMBL5203263
6.34IC50455nMCHEMBL5196601
6.21Kd610nMCHEMBL5086210
6.15Kd710nMCHEMBL5078220
6.07Kd860nMCHEMBL5077489
6.04IC50905nMCHEMBL5757533
6.01IC50982nMCHEMBL5184993
5.94Kd1140nMCHEMBL5094688
5.91IC501244nMCHEMBL5822152
5.89Kd1290nMCHEMBL5083800
5.78IC501676nMCHEMBL5204089
5.77IC501700nMABT 737
5.75IC501800nMCHEMBL5190824
5.74IC501801nMCHEMBL5787211
5.69Kd2030nMCHEMBL5069538
5.67Kd2140nMCHEMBL5085821
5.67IC502140nMCHEMBL5949126
5.66Kd2200nMCHEMBL5093197
5.62Kd2410nMCHEMBL5089668
5.62IC502421nMCHEMBL5183356
5.62IC502390nMCHEMBL5201193
5.60IC502500nMCHEMBL5184262
5.57IC502680nMCHEMBL6018840
5.56IC502765nMCHEMBL5198074
5.55Kd2840nMCHEMBL5089306
5.55IC502794nMCHEMBL5204882
5.54IC502879nMCHEMBL5201389
5.52IC503000nMCHEMBL5201820
5.49Kd3210nMCHEMBL5088512
5.39IC504100nMCHEMBL5185435
5.29IC505138nMCHEMBL5850575
5.26IC505520nMCHEMBL5174166
5.17IC506770nMCHEMBL6032390
5.14IC507227nMCHEMBL5183128
5.04IC509100nMCHEMBL5209197
5.01IC509830nMCHEMBL5170063
5.00IC509895nMCHEMBL5171960
5.00IC501e+04nMCHEMBL5202782

PubChem BioAssay actives

14 with measured affinity, of 24 total; 14 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

CompoundAssayTypeValueUnit
(3S)-3-[[(2S)-2-[[(2S,5S,8S,11S,14S,17S,20S,24E,32R)-32-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-5-carbamimidamidopentanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-methylbutanoyl]amino]-3-methylpentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-17-(4-aminobutyl)-8,11-bis[(2S)-butan-2-yl]-14-(2-carboxyethyl)-2-(2-methylpropyl)-3,6,9,12,15,18,33-heptaoxo-5-propan-2-yl-1,4,7,10,13,16,19-heptazacyclotritriacont-24-ene-20-carbonyl]amino]-5-carbamimidamidopentanoyl]amino]-4-[[(2S)-1-amino-3-methyl-1-oxobutan-2-yl]amino]-4-oxobutanoic acid1830131: Binding affinity to Beclin 1 coiled coil domain (unknown origin) by isothermal titration calorimetry assaykd0.1000uM
2-[(2S,5S,8S,11S,14S,17S,20S,24E,32R)-32-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-5-carbamimidamidopentanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-methylbutanoyl]amino]-4-methylpentanoyl]amino]-3-phenylpropanoyl]amino]-4-amino-4-oxobutanoyl]amino]-20-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-amino-3-methyl-1-oxobutan-2-yl]amino]-1-oxohexan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]carbamoyl]-17-(4-aminobutyl)-14-[(2S)-butan-2-yl]-2-(2-methylpropyl)-3,6,9,12,15,18,33-heptaoxo-5,11-di(propan-2-yl)-1,4,7,10,13,16,19-heptazacyclotritriacont-24-en-8-yl]acetic acid1830131: Binding affinity to Beclin 1 coiled coil domain (unknown origin) by isothermal titration calorimetry assaykd0.3300uM
(4S)-4-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-5-carbamimidamidopentanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoyl]amino]-5-[[(3S,6S,9S,12S,15S,18S,21R,28E,33S)-33-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-amino-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]carbamoyl]-3-(4-aminobutyl)-12-[(2S)-butan-2-yl]-18-(3-carbamimidamidopropyl)-6,15-bis(2-carboxyethyl)-2,5,8,11,14,17,20-heptaoxo-9-propan-2-yl-1,4,7,10,13,16,19-heptazacyclotritriacont-28-en-21-yl]amino]-5-oxopentanoic acid1830131: Binding affinity to Beclin 1 coiled coil domain (unknown origin) by isothermal titration calorimetry assaykd0.6100uM
3-[(3S,6S,9S,12S,15S,18S,21R,28E,33S)-21-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-5-carbamimidamidopentanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-33-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-amino-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]carbamoyl]-3,18-bis(4-aminobutyl)-15-[(2S)-butan-2-yl]-12-(carboxymethyl)-2,5,8,11,14,17,20-heptaoxo-9-propan-2-yl-1,4,7,10,13,16,19-heptazacyclotritriacont-28-en-6-yl]propanoic acid1830131: Binding affinity to Beclin 1 coiled coil domain (unknown origin) by isothermal titration calorimetry assaykd0.7100uM
3-[(3S,6S,9S,12S,15S,18S,21R,28E,33S)-21-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-5-carbamimidamidopentanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-3-(4-aminobutyl)-33-[[(2S)-1-[[(2S)-1-[[(2S)-1-amino-3-methyl-1-oxobutan-2-yl]amino]-1-oxopropan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]carbamoyl]-9,18-bis(3-carbamimidamidopropyl)-15-(2-carboxyethyl)-12-(carboxymethyl)-2,5,8,11,14,17,20-heptaoxo-1,4,7,10,13,16,19-heptazacyclotritriacont-28-en-6-yl]propanoic acid1830131: Binding affinity to Beclin 1 coiled coil domain (unknown origin) by isothermal titration calorimetry assaykd0.8600uM
3-[(2S,5S,8S,11S,14S,17S,20S,24E,32R)-32-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-5-carbamimidamidopentanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-4-methylpentanoyl]amino]-6-aminohexanoyl]amino]-5-amino-5-oxopentanoyl]amino]-20-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-amino-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]carbamoyl]-17-(4-aminobutyl)-14-(2-carboxyethyl)-8-(carboxymethyl)-2-(2-methylpropyl)-3,6,9,12,15,18,33-heptaoxo-11-propan-2-yl-1,4,7,10,13,16,19-heptazacyclotritriacont-24-en-5-yl]propanoic acid1830131: Binding affinity to Beclin 1 coiled coil domain (unknown origin) by isothermal titration calorimetry assaykd1.1400uM
3-[(2S,5S,8S,11S,14S,17S,20S,24E,32R)-32-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-5-carbamimidamidopentanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-20-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-amino-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]carbamoyl]-17-(4-aminobutyl)-14-(2-carboxyethyl)-8-(carboxymethyl)-2-(2-methylsulfanylethyl)-3,6,9,12,15,18,33-heptaoxo-11-propan-2-yl-1,4,7,10,13,16,19-heptazacyclotritriacont-24-en-5-yl]propanoic acid1830131: Binding affinity to Beclin 1 coiled coil domain (unknown origin) by isothermal titration calorimetry assaykd1.2900uM
4-[4-[[2-(4-chlorophenyl)phenyl]methyl]piperazin-1-yl]-N-[4-[[(2R)-4-(dimethylamino)-1-phenylsulfanylbutan-2-yl]amino]-3-nitrophenyl]sulfonylbenzamide2138372: Inhibition of Beclin-1/Bcl-2 (unknown origin) interaction by fluorescence polarization assayic501.7000uM
3-[(3S,6S,9S,12S,15S,18S,21R,28E,33S)-21-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-5-carbamimidamidopentanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-3-(4-aminobutyl)-33-[[(2S)-1-[[(2S)-1-[[(2S)-1-amino-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]carbamoyl]-9,18-bis(3-carbamimidamidopropyl)-15-(2-carboxyethyl)-12-(carboxymethyl)-2,5,8,11,14,17,20-heptaoxo-1,4,7,10,13,16,19-heptazacyclotritriacont-28-en-6-yl]propanoic acid1830131: Binding affinity to Beclin 1 coiled coil domain (unknown origin) by isothermal titration calorimetry assaykd2.0300uM
3-[(3S,6S,9S,12S,18S,21R,28E,33S)-21-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-5-carbamimidamidopentanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-33-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-amino-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]carbamoyl]-18-(4-aminobutyl)-12-(carboxymethyl)-3-(2-methylpropyl)-2,5,8,11,14,17,20-heptaoxo-9-propan-2-yl-1,4,7,10,13,16,19-heptazacyclotritriacont-28-en-6-yl]propanoic acid1830131: Binding affinity to Beclin 1 coiled coil domain (unknown origin) by isothermal titration calorimetry assaykd2.1400uM
3-[(2S,5S,8S,11S,14S,17S,20S,24E,32R)-32-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-5-carbamimidamidopentanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-methylpentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-20-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-amino-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]carbamoyl]-17-(4-aminobutyl)-8-(carboxymethyl)-14-(2-methylpropyl)-2-(2-methylsulfanylethyl)-3,6,9,12,15,18,33-heptaoxo-11-propan-2-yl-1,4,7,10,13,16,19-heptazacyclotritriacont-24-en-5-yl]propanoic acid1830131: Binding affinity to Beclin 1 coiled coil domain (unknown origin) by isothermal titration calorimetry assaykd2.2000uM
3-[(2S,5S,8S,11S,14S,17S,20S,24E,32R)-32-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-5-carbamimidamidopentanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-20-[[(2R)-1-[[(2S)-6-amino-1-[[(2S)-1-amino-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]carbamoyl]-2,17-bis(4-aminobutyl)-14-(2-carboxyethyl)-8-(carboxymethyl)-3,6,9,12,15,18,33-heptaoxo-11-propan-2-yl-1,4,7,10,13,16,19-heptazacyclotritriacont-24-en-5-yl]propanoic acid1830131: Binding affinity to Beclin 1 coiled coil domain (unknown origin) by isothermal titration calorimetry assaykd2.4100uM
(4S)-4-[[(2S)-2-[[(2S)-2-[[(2S,5S,8S,11S,14S,17S,20S,24E,32R)-32-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-5-carbamimidamidopentanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]-17-(4-aminobutyl)-2,11-bis(3-carbamimidamidopropyl)-5,14-bis(2-carboxyethyl)-8-(carboxymethyl)-3,6,9,12,15,18,33-heptaoxo-1,4,7,10,13,16,19-heptazacyclotritriacont-24-ene-20-carbonyl]amino]-5-carbamimidamidopentanoyl]amino]propanoyl]amino]-5-amino-5-oxopentanoic acid1830131: Binding affinity to Beclin 1 coiled coil domain (unknown origin) by isothermal titration calorimetry assaykd2.8400uM
(4S)-4-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-5-carbamimidamidopentanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]-5-[[(2S)-1-[[(3R,6R,9R,12R,15R,18R,21R,28E,33S)-9-(4-aminobutyl)-33-[[(2R)-1-amino-1-oxopropan-2-yl]carbamoyl]-6-(3-amino-3-oxopropyl)-3,15-bis(3-carbamimidamidopropyl)-12-(2-carboxyethyl)-18-(carboxymethyl)-2,5,8,11,14,17,20-heptaoxo-1,4,7,10,13,16,19-heptazacyclotritriacont-28-en-21-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-oxopentanoic acid1830131: Binding affinity to Beclin 1 coiled coil domain (unknown origin) by isothermal titration calorimetry assaykd3.2100uM

CTD chemical–gene interactions

257 total (human), top 30 by PubMed support.

ChemicalActions (top 5)PubMed papers
3-methyladeninedecreases reaction, increases expression, decreases response to substance, decreases expression, affects binding (+2 more)21
Acetylcysteinedecreases reaction, increases expression, increases phosphorylation, affects cotreatment14
sodium arseniteincreases reaction, affects cotreatment, affects reaction, increases expression, decreases reaction (+1 more)13
Sirolimusdecreases expression, increases reaction, affects cotreatment, increases expression, decreases reaction (+1 more)10
Resveratrolaffects metabolic processing, decreases reaction, increases expression, increases degradation, affects cotreatment (+6 more)7
Arsenic Trioxideaffects binding, increases reaction, increases degradation, decreases reaction, increases expression7
Cisplatindecreases expression, decreases reaction, affects cotreatment, affects reaction, affects response to substance (+2 more)7
Doxorubicindecreases reaction, increases expression, affects cotreatment, affects response to substance, affects expression (+1 more)6
Hydrogen Peroxideincreases reaction, affects localization, increases abundance, increases lipidation, affects response to substance (+5 more)6
4-phenylbutyric aciddecreases reaction, increases expression5
Chloroquinedecreases expression, increases reaction, affects cotreatment, increases expression, decreases reaction (+1 more)5
Particulate Matterdecreases reaction, increases expression5
dorsomorphindecreases reaction, increases expression, increases reaction, decreases expression4
Paraquatincreases reaction, decreases reaction, affects cotreatment, increases expression, decreases expression4
Palmitic Aciddecreases reaction, increases expression, increases reaction, affects cotreatment, affects expression (+1 more)4
Nanotubes, Carbondecreases expression, increases expression4
tetrandrineaffects cotreatment, increases expression, decreases expression3
manganese chlorideaffects expression, increases expression, affects binding, affects reaction, decreases reaction (+1 more)3
hydroquinoneincreases expression, increases reaction, decreases reaction3
2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-onedecreases reaction, increases phosphorylation, increases expression, increases activity3
Ethanoldecreases reaction, increases expression, increases reaction, decreases expression, increases degradation3
Arsenicincreases expression, affects cotreatment, affects expression, affects methylation, decreases reaction (+1 more)3
Cannabidiolincreases expression, affects response to substance3
Cadmium Chloridedecreases reaction, increases expression, affects reaction, increases abundance3
bisphenol Aincreases expression, affects binding, increases reaction, affects reaction, decreases reaction2
arseniteincreases expression, affects reaction, decreases expression, increases lipidation2
2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-oneincreases expression, increases reaction, affects reaction2
U 0126decreases reaction, increases expression2
pyrazolanthroneaffects binding, decreases reaction, increases expression, increases reaction2
3-(4-methylphenylsulfonyl)-2-propenenitrileincreases expression, decreases reaction2

ChEMBL screening assays

7 unique, capped per target: 7 binding

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL4118772BindingBinding affinity to BECN1 in human NCI-H23 cells at 1 uM by mass spectrometry based pull down assayStudies of TAK1-centered polypharmacology with novel covalent TAK1 inhibitors. — Bioorg Med Chem

Cellosaurus cell lines

1 cell lines: 1 cancer cell line

First 10 cell lines (id-ordered, not curated):

CellosaurusNameCategorySex
CVCL_B1L8Abcam HeLa BECN1 KOCancer cell lineFemale

Clinical trials (associated diseases)

0 trials via MONDO — disease-level, not drug-specific.

  • Disease cohort memberships (association, not causation — diseases whose associated-gene cohort lists this gene; a subset are also under Associated diseases): type 2 diabetes mellitus