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Protein

Beclin-2

Gene

BECN2

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

Functioni

Involved in 2 distinct lysosomal degradation pathways: acts as a regulator of autophagy and as a regulator of G-protein coupled receptors turnover. Regulates degradation in lysosomes of a variety of G-protein coupled receptors via its interaction with GPRASP1/GASP1.1 Publication

GO - Molecular functioni

GO - Biological processi

  • autophagosome assembly Source: GO_Central
  • autophagy Source: UniProtKB
  • autophagy of nucleus Source: GO_Central
  • cellular response to nitrogen starvation Source: GO_Central
  • endosome to lysosome transport Source: UniProtKB
  • glucose homeostasis Source: Ensembl
  • G-protein coupled receptor catabolic process Source: UniProtKB
  • late endosome to vacuole transport Source: GO_Central

Keywordsi

Biological processAutophagy

Names & Taxonomyi

Protein namesi
Recommended name:
Beclin-21 Publication
Alternative name(s):
Beclin-1 autophagy-related pseudogene 1Imported
Beclin-1-like protein 1Imported
Gene namesi
Name:BECN21 PublicationImported
Synonyms:BECN1L1Imported, BECN1P1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000196289.7.
HGNCiHGNC:38606. BECN2.

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi80I → S: Abolishes interaction with GPRASP1/GASP1 and ability to degrade G-protein coupled receptor. Does not affect function in autophagy. 1 Publication1
Mutagenesisi173E → L: Decreases homodimerization. Decreases interaction with ATG14. 1 Publication1
Mutagenesisi187N → L: Increases strongly homodimerization. Decreases interaction with ATG14. 1 Publication1
Mutagenesisi190A → L: Decreases interaction with ATG14. Increases slightly homodimerization; when associated with L-215. 1 Publication1
Mutagenesisi197A → L: Decreases interaction with ATG14. Probably strongly increases homodimerization; when associated with L-208. 1 Publication1
Mutagenesisi208E → L: Decreases interaction with ATG14. Probably strongly increases homodimerization; when associated with L-197. 1 Publication1
Mutagenesisi211H → L: Increases homodimerization. Decreases interaction with ATG14. 1 Publication1
Mutagenesisi215Y → L: Decreases interaction with ATG14. Increases slightly homodimerization; when associated with L-190. 1 Publication1
Mutagenesisi222Q → L: Decreases homodimerization. Decreases interaction with ATG14. 1 Publication1
Mutagenesisi243R → L: Decreases homodimerization. Decreases interaction with ATG14. 1 Publication1

Organism-specific databases

DisGeNETi441925.
OpenTargetsiENSG00000196289.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003322441 – 431Beclin-2Add BLAST431

Proteomic databases

PRIDEiA8MW95.

PTM databases

iPTMnetiA8MW95.
PhosphoSitePlusiA8MW95.

Expressioni

Tissue specificityi

Present in fetal and adult brain (at protein level).1 Publication

Interactioni

Subunit structurei

Homodimer (via coiled-coil domain) (PubMed:28218432). Interacts (via coiled-coil domain) with ATG14 (via coiled-coil domain); this interaction is tighter than BECN2 self-association (PubMed:23954414, PubMed:28218432). Interacts with AMBRA1, UVRAG and PIK3C3/VPS34; these interactions are not disrupted by starvation (PubMed:23954414). Does not interact with RUBCN (PubMed:23954414). Interacts (via N-terminus) with GPRASP1/GASP1; the interaction is direct (PubMed:23954414).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GPRASP1Q5JY774EBI-8839517,EBI-2514717

GO - Molecular functioni

Protein-protein interaction databases

IntActiA8MW95. 6 interactors.

Structurei

Secondary structure

1431
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi161 – 244Combined sources84

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5K7BX-ray2.30A/B/C/D160-246[»]
5K9LX-ray2.52A/B/C/D158-246[»]
ProteinModelPortaliA8MW95.
SMRiA8MW95.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni173 – 243Required for homodimer formation1 PublicationAdd BLAST71

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili125 – 248Sequence analysisAdd BLAST124

Sequence similaritiesi

Belongs to the beclin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00390000008164.
HOVERGENiHBG003181.
InParanoidiA8MW95.
KOiK08334.
OMAiVGWNEIN.

Family and domain databases

InterProiView protein in InterPro
IPR007243. Atg6/Beclin.
IPR032912. BECN2.
PANTHERiPTHR12768. PTHR12768. 1 hit.
PTHR12768:SF5. PTHR12768:SF5. 1 hit.
PfamiView protein in Pfam
PF04111. APG6. 1 hit.

Sequencei

Sequence statusi: Complete.

A8MW95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSIRFLCQR CHQALKLSGS SESRSLPAAP APTSGQAEPG DTREPGVTTR
60 70 80 90 100
EVTDAEEQQD GASSRSPPGD GSVSKGHANI FTLLGELGAM HMLSSIQKAA
110 120 130 140 150
GDIFDIVSGQ AVVDHPLCEE CTDSLLEQLD IQLALTEADS QNYQRCLETG
160 170 180 190 200
ELATSEDEAA ALRAELRDLE LEEARLVQEL EDVDRNNARA AADLQAAQAE
210 220 230 240 250
AAELDQQERQ HYRDYSALKR QQLELLDQLG NVENQLQYAR VQRDRLKEIN
260 270 280 290 300
CFTATFEIWV EGPLGVINNF RLGRLPTVRV GWNEINTAWG QAALLLLTLA
310 320 330 340 350
NTIGLQFQRY RLIPCGNHSY LKSLTDDRTE LPLFCYGGQD VFLNNKYDRA
360 370 380 390 400
MVAFLDCMQQ FKEEAEKGEL GLSLPYGIQV ETGLMEDVGG RGECYSIRTH
410 420 430
LNTQELWTKA LKFMLINFKW SLIWVASRYQ K
Length:431
Mass (Da):48,153
Last modified:October 31, 2012 - v2
Checksum:i9DB4184BE5C7A574
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HM031116 mRNA. Translation: ADM47406.1.
BX571673 Genomic DNA. No translation available.
CCDSiCCDS81433.1.
RefSeqiNP_001277622.1. NM_001290693.1.
UniGeneiHs.731347.

Genome annotation databases

EnsembliENST00000419583; ENSP00000488361; ENSG00000196289.
GeneIDi441925.
KEGGihsa:441925.

Similar proteinsi

Entry informationi

Entry nameiBECN2_HUMAN
AccessioniPrimary (citable) accession number: A8MW95
Secondary accession number(s): E9KNW0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: October 31, 2012
Last modified: October 25, 2017
This is version 62 of the entry and version 2 of the sequence. See 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families