ID   BECN1_HUMAN             Reviewed;         450 AA.
AC   Q14457; O75595; Q9UNA8;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   16-DEC-2008, entry version 78.
DE   RecName: Full=Beclin-1;
DE   AltName: Full=Coiled-coil myosin-like BCL2-interacting protein;
DE   AltName: Full=Protein GT197;
GN   Name=BECN1; Synonyms=GT197;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH BCL-2.
RC   TISSUE=Brain;
RX   MEDLINE=98440516; PubMed=9765397;
RA   Liang X.H., Kleeman L.K., Jiang H.H., Gordon G., Goldman J.E.,
RA   Berry G., Herman B., Levine B.;
RT   "Protection against fatal Sindbis virus encephalitis by beclin, a
RT   novel Bcl-2-interacting protein.";
RL   J. Virol. 72:8586-8596(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99326523; PubMed=10395800; DOI=10.1006/geno.1999.5851;
RA   Aita V.M., Liang X.H., Murty V.V.V.S., Pincus D.L., Yu W., Cayanis E.,
RA   Kalachikov S., Gilliam T.C., Levine B.;
RT   "Cloning and genomic organization of beclin 1, a candidate tumor
RT   suppressor gene on chromosome 17q21.";
RL   Genomics 59:59-65(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cervix;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 150-450.
RC   TISSUE=Mammary gland;
RX   MEDLINE=96039267; PubMed=7490091; DOI=10.1006/geno.1995.1185;
RA   Rommens J.M., Durocher F., McArthur J., Tonin P., Leblanc J.-F.,
RA   Allen T., Samson C., Ferri L., Narod S., Morgan K., Simard J.;
RT   "Generation of a transcription map at the HSD17B locus centromeric to
RT   BRCA1 at 17q21.";
RL   Genomics 28:530-542(1995).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57 AND SER-64, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 107-135 IN COMPLEX WITH
RP   BCL2L1.
RX   PubMed=17337444; DOI=10.1074/jbc.M700492200;
RA   Oberstein A., Jeffrey P.D., Shi Y.;
RT   "Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is
RT   a novel BH3-only protein.";
RL   J. Biol. Chem. 282:13123-13132(2007).
RN   [7]
RP   STRUCTURE BY NMR OF 106-128 IN COMPLEX WITH BCL2L1.
RX   PubMed=17659302; DOI=10.1016/j.jmb.2007.06.069;
RA   Feng W., Huang S., Wu H., Zhang M.;
RT   "Molecular basis of Bcl-xL's target recognition versatility revealed
RT   by the structure of Bcl-xL in complex with the BH3 domain of beclin-
RT   1.";
RL   J. Mol. Biol. 372:223-235(2007).
CC   -!- FUNCTION: Plays a central role in autophagy (By similarity). May
CC       play a role in antiviral host defense. Protects against infection
CC       by a neurovirulent strain of Sindbis virus.
CC   -!- SUBUNIT: Interacts with GOPC and GRID2. Interacts with AMBRA1.
CC       Probably forms a complex with AMBRA1 and PIK3C3 (By similarity).
CC       Interacts with BCL2 and BCL2L1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). Golgi apparatus
CC       membrane; Peripheral membrane protein (By similarity).
CC       Note=Expressed in dendrites and cell bodies of cerebellar Purkinje
CC       cells (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the beclin family.
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DR   EMBL; AF077301; AAC68653.1; -; mRNA.
DR   EMBL; AF139131; AAD27650.1; -; mRNA.
DR   EMBL; BC010276; AAH10276.1; -; mRNA.
DR   EMBL; L38932; AAB59573.1; -; mRNA.
DR   PIR; I54209; I54209.
DR   RefSeq; NP_003757.1; -.
DR   UniGene; Hs.12272; -.
DR   PDB; 2P1L; X-ray; 2.50 A; B/D/F/H=107-135.
DR   PDB; 2PON; NMR; -; A=106-128.
DR   PDBsum; 2P1L; -.
DR   PDBsum; 2PON; -.
DR   IntAct; Q14457; 1.
DR   PhosphoSite; Q14457; -.
DR   PRIDE; Q14457; -.
DR   Ensembl; ENSG00000126581; Homo sapiens.
DR   GeneID; 8678; -.
DR   KEGG; hsa:8678; -.
DR   GeneCards; GC17M038215; -.
DR   H-InvDB; HIX0018211; -.
DR   HGNC; HGNC:1034; BECN1.
DR   HPA; CAB010143; -.
DR   MIM; 604378; gene.
DR   PharmGKB; PA25337; -.
DR   HOVERGEN; Q14457; -.
DR   LinkHub; Q14457; -.
DR   NextBio; 32555; -.
DR   ArrayExpress; Q14457; -.
DR   CleanEx; HS_BECN1; -.
DR   GermOnline; ENSG00000126581; Homo sapiens.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006916; P:anti-apoptosis; TAS:ProtInc.
DR   GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR   GO; GO:0009615; P:response to virus; IEA:UniProtKB-KW.
DR   InterPro; IPR007243; Autophagy_prot_6.
DR   PANTHER; PTHR12768; APG6; 1.
DR   Pfam; PF04111; APG6; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; Autophagy; Coiled coil; Cytoplasm;
KW   Golgi apparatus; Membrane; Phosphoprotein; Polymorphism.
FT   CHAIN         1    450       Beclin-1.
FT                                /FTId=PRO_0000218555.
FT   COILED      142    270       Potential.
FT   MOD_RES      57     57       Phosphothreonine.
FT   MOD_RES      64     64       Phosphoserine.
FT   VARIANT     103    103       A -> V.
FT                                /FTId=VAR_010384.
FT   VARIANT     403    403       I -> T.
FT                                /FTId=VAR_005236.
FT   CONFLICT    150    150       T -> A (in Ref. 4; AAB59573).
FT   HELIX       107    125
SQ   SEQUENCE   450 AA;  51896 MW;  ABF0C2DD7087473C CRC64;
     MEGSKTSNNS TMQVSFVCQR CSQPLKLDTS FKILDRVTIQ ELTAPLLTTA QAKPGETQEE
     ETNSGEEPFI ETPRQDGVSR RFIPPARMMS TESANSFTLI GEASDGGTME NLSRRLKVTG
     DLFDIMSGQT DVDHPLCEEC TDTLLDQLDT QLNVTENECQ NYKRCLEILE QMNEDDSEQL
     QMELKELALE EERLIQELED VEKNRKIVAE NLEKVQAEAE RLDQEEAQYQ REYSEFKRQQ
     LELDDELKSV ENQMRYAQTQ LDKLKKTNVF NATFHIWHSG QFGTINNFRL GRLPSVPVEW
     NEINAAWGQT VLLLHALANK MGLKFQRYRL VPYGNHSYLE SLTDKSKELP LYCSGGLRFF
     WDNKFDHAMV AFLDCVQQFK EEVEKGETRF CLPYRMDVEK GKIEDTGGSG GSYSIKTQFN
     SEEQWTKALK FMLTNLKWGL AWVSSQFYNK
//