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Protein

Beclin-1

Gene

Becn1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a central role in autophagy. 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. Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis. May play a role in antiviral host defense (By similarity).By similarity
Beclin-1-C 35 kDa localized to mitochondria can promote apoptosis; it induces the mitochondrial translocation of BAX and the release of proapoptotic factors.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Apoptosis, Autophagy, Cell cycle, Cell division

Enzyme and pathway databases

ReactomeiR-RNO-1632852. Macroautophagy.

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:
Gene namesi
Name:Becn1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi620190. Becn1.

Subcellular locationi

  • Cytoplasm By similarity
  • Golgi apparatustrans-Golgi network membrane By similarity; Peripheral membrane protein By similarity
  • Endosome membrane By similarity; Peripheral membrane protein By similarity
  • Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity
  • Mitochondrion membrane By similarity; Peripheral membrane protein By similarity
  • Cytoplasmic vesicleautophagosome Curated

  • Note: Interaction with ATG14 promotes translocation to autophagosomes. Expressed in dendrites and cell bodies of cerebellar Purkinje cells.By similarity
Beclin-1-C 35 kDa :
  • Mitochondrion By similarity
  • Nucleus By similarity
  • Cytoplasm By similarity
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)DescriptionActionsGraphical viewLength
Mutagenesisi178L → A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-192. 1 Publication1
Mutagenesisi178L → A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-196. 1 Publication1
Mutagenesisi178L → A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-259. 1 Publication1
Mutagenesisi189E → L: Decreases interaction with ATG14, no effect on interaction with UVRAG; when associated with L-217, L-224 and L-255. 1 Publication1
Mutagenesisi192L → A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-178. 1 Publication1
Mutagenesisi196L → A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-178. 1 Publication1
Mutagenesisi217A → L: Decreases interaction with ATG14, no effect on interaction with UVRAG; when associated with L-189, L-224 and L-255. 1 Publication1
Mutagenesisi224E → L: Decreases interaction with ATG14, no effect on interaction with UVRAG; when associated with L-189, L-217 and L-255. 1 Publication1
Mutagenesisi255A → L: Decreases interaction with ATG14, no effect on interaction with UVRAG; when associated with L-189, L-217 and L-224. 1 Publication1
Mutagenesisi259L → A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-178. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003162901 – 448Beclin-1Add BLAST448
ChainiPRO_0000435044132 – 448Beclin-1-C 37 kDaBy similarityAdd BLAST317
ChainiPRO_0000435045148 – 448Beclin-1-C 35 kDaBy similarityAdd BLAST301

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei29PhosphoserineBy similarity1
Modified residuei88Phosphoserine; by AMPKBy similarity1
Modified residuei91Phosphoserine; by AMPKBy similarity1
Modified residuei94Phosphoserine; by AMPKBy similarity1
Modified residuei117Phosphothreonine; by DAPK1By similarity1

Post-translational modificationi

Phosphorylation at Thr-117 by DAPK1 reduces its interaction with BCL2 and BCL2L1 and promotes induction of autophagy. In response to autophagic stimuli, phosphorylated at serine residues by AMPK in an ATG14-dependent manner, and this phosphorylation is critical for maximally efficient autophagy.By similarity
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 (By similarity).By similarity
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.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ91XJ1.
PRIDEiQ91XJ1.

PTM databases

iPTMnetiQ91XJ1.
PhosphoSitePlusiQ91XJ1.

Expressioni

Gene expression databases

BgeeiENSRNOG00000020513.
GenevisibleiQ91XJ1. RN.

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 (PubMed:22314358). 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. 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. Interacts with AMBRA1, GOPC, GRID2. Interacts with BCL2 and BCL2L1; 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, DAPK1, RAB39A. Interacts with SLAMF1 (By similarity). Interacts with VMP1 (PubMed:17724469). Interacts with TRIM5; the interaction causes activation of BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2 (By similarity). Interacts with active ULK1 (phosphorylated on 'Ser-317') and MEFV simultaneously (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi250376. 1 interactor.
DIPiDIP-61888N.
STRINGi10116.ENSRNOP00000027868.

Structurei

Secondary structure

1448
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi174 – 263Combined sources90

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3Q8TX-ray1.90A/B174-264[»]
ProteinModelPortaliQ91XJ1.
SMRiQ91XJ1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni110 – 157Interaction with BCL2 and BCL2L1 isoform Bcl-X(L)By similarityAdd BLAST48
Regioni423 – 448Required for membrane-associationBy similarityAdd BLAST26

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili140 – 267Sequence analysisAdd BLAST128

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi106 – 125BH3By similarityAdd BLAST20

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.1 Publication

Sequence similaritiesi

Belongs to the beclin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2751. Eukaryota.
ENOG410XQ85. LUCA.
GeneTreeiENSGT00390000008164.
HOGENOMiHOG000158093.
HOVERGENiHBG003181.
InParanoidiQ91XJ1.
KOiK08334.
OMAiYIPPARM.
PhylomeDBiQ91XJ1.
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.

Q91XJ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGSKASSST MQVSFVCQRC SQPLKLDTSF KILDRVTIQE LTAPLLTTAQ
60 70 80 90 100
AKPGESQEEE ANSGEEPFIE TRQDGVSRRF IPPARMMSTE SANSFTLIGE
110 120 130 140 150
ASDGGTMENL SRRLKVTGDL FDIMSGQTDV DHPLCEECTD TLLDQLDTQL
160 170 180 190 200
NVTENECQNY KRCLEMLEQM NEGDSEQLQR ELKELALEEE RLIQELEDVE
210 220 230 240 250
KNRKVVAENL EKVQAEAERL DQEEAQYQRE YSEFKRQQLE LDDELKSVEN
260 270 280 290 300
QMRYAQMQLD KLKKTNVFNA TFHIWHSGQF GTINNFRLGR LPSAPVEWNE
310 320 330 340 350
INAAWGQTVL LLHALANKMG LKFQRYRLVP YGNHSYLESL TDKSKELPLY
360 370 380 390 400
CSGGLRFFWD NKFDHAMVAF LDCVQQFKEE VEKGETRFCL PYRMDVEKGK
410 420 430 440
IEDTGGSGGS YSIKTQFNSE EQWTKALKFM LTNLKWGLAW VSSQFYNK
Length:448
Mass (Da):51,557
Last modified:December 1, 2001 - v1
Checksum:i34981BE560F3354B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY033824 mRNA. Translation: AAK56548.1.
BC074011 mRNA. Translation: AAH74011.1.
RefSeqiNP_001029289.1. NM_001034117.1.
NP_446191.1. NM_053739.2.
UniGeneiRn.2776.

Genome annotation databases

EnsembliENSRNOT00000027868; ENSRNOP00000027868; ENSRNOG00000020513.
ENSRNOT00000082010; ENSRNOP00000071966; ENSRNOG00000020513.
GeneIDi114558.
KEGGirno:114558.
UCSCiRGD:620190. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY033824 mRNA. Translation: AAK56548.1.
BC074011 mRNA. Translation: AAH74011.1.
RefSeqiNP_001029289.1. NM_001034117.1.
NP_446191.1. NM_053739.2.
UniGeneiRn.2776.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3Q8TX-ray1.90A/B174-264[»]
ProteinModelPortaliQ91XJ1.
SMRiQ91XJ1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250376. 1 interactor.
DIPiDIP-61888N.
STRINGi10116.ENSRNOP00000027868.

PTM databases

iPTMnetiQ91XJ1.
PhosphoSitePlusiQ91XJ1.

Proteomic databases

PaxDbiQ91XJ1.
PRIDEiQ91XJ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027868; ENSRNOP00000027868; ENSRNOG00000020513.
ENSRNOT00000082010; ENSRNOP00000071966; ENSRNOG00000020513.
GeneIDi114558.
KEGGirno:114558.
UCSCiRGD:620190. rat.

Organism-specific databases

CTDi8678.
RGDi620190. Becn1.

Phylogenomic databases

eggNOGiKOG2751. Eukaryota.
ENOG410XQ85. LUCA.
GeneTreeiENSGT00390000008164.
HOGENOMiHOG000158093.
HOVERGENiHBG003181.
InParanoidiQ91XJ1.
KOiK08334.
OMAiYIPPARM.
PhylomeDBiQ91XJ1.
TreeFamiTF314282.

Enzyme and pathway databases

ReactomeiR-RNO-1632852. Macroautophagy.

Miscellaneous databases

PROiQ91XJ1.

Gene expression databases

BgeeiENSRNOG00000020513.
GenevisibleiQ91XJ1. RN.

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...

Entry informationi

Entry nameiBECN1_RAT
AccessioniPrimary (citable) accession number: Q91XJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.