Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00410
Entry Name
UniProt Accession
Theoretical PI
4.69
Molecular Weight
21951.6
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
BH3-interacting domain death agonist p11
Protein Synonyms/Alias
p22 BID; BID; p15 BID; p13 BID; p11 BID;
Gene Name
Bid
Gene Synonyms/Alias
Created Date
01-NOV-1997
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
60
Canonical
EDELQTDGSQASRSF
[1][2]
N-Myristoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Maurer-Stroh S, Eisenhaber B, Eisenhaber F. N-terminal N-myristoylation ofproteins: prediction of substrate proteins from amino acid sequence. J Mol Biol. 2002 Apr 5;317(4):541-57.[PMID:11955008]
[2] Zha J, Weiler S, Oh KJ, Wei MC, Korsmeyer SJ. PosttranslationalN-myristoylation of BID as a molecular switch for targeting mitochondria andapoptosis. Science. 2000 Dec 1;290(5497):1761-5.[PMID:11099414]
Functional Description
Induces caspases and apoptosis. Counters the protective effect of Bcl-2. The major proteolytic product p15 BID allows the release of cytochrome c.
Sequence Annotation
Motif: 87 100 BH3.
Functional site: 60 61 Cleavage.
Functional site: 75 76 Cleavage.
Functional site: 98 99 Cleavage.
Modified residue: 1 1 N-acetylmethionine.
Modified residue: 78 78 Phosphoserine.
Protein Length
195 AA.
Protein Sequence
(Canonical)
MDSEVSNGSG LGAEHITDLL VFGFLQSSGC TRQELEVLGR ELPVQAYWEA DLEDELQTDG  60
SQASRSFNQG RIEPDSESQE EIIHNIARHL AQIGDEMDHN IQPTLVRQLA AQFMNGSLSE  120
EDKRNCLAKA LDEVKTAFPR DMENDKAMLI MTMLLAKKVA SHAPSLLRDV FHTTVNFINQ  180
NLFSYVRNLV RNEMD                                                   195
FASTA
(Canonical)
>LipidDB-10090-00410|P70444
MDSEVSNGSGLGAEHITDLLVFGFLQSSGCTRQELEVLGRELPVQAYWEADLEDELQTDG
SQASRSFNQGRIEPDSESQEEIIHNIARHLAQIGDEMDHNIQPTLVRQLAAQFMNGSLSE
EDKRNCLAKALDEVKTAFPRDMENDKAMLIMTMLLAKKVASHAPSLLRDVFHTTVNFINQ
NLFSYVRNLVRNEMD
Gene Ontology
GO:0005737; C:cytoplasm; IDA:MGI
GO:0005829; C:cytosol; IDA:MGI
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0032592; C:integral component of mitochondrial membrane; IDA:BHF-UCL
GO:0016020; C:membrane; IDA:MGI
GO:0005739; C:mitochondrion; IDA:MGI
GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB
GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI
GO:0008637; P:apoptotic mitochondrial changes; IDA:MGI
GO:0007420; P:brain development; IEA:Ensembl
GO:0090150; P:establishment of protein localization to membrane; IEA:Ensembl
GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI
GO:0034349; P:glial cell apoptotic process; IEA:Ensembl
GO:0097284; P:hepatocyte apoptotic process; IGI:MGI
GO:0097345; P:mitochondrial outer membrane permeabilization; IGI:MGI
GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl
GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl
GO:0032464; P:positive regulation of protein homooligomerization; IDA:BHF-UCL
GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IGI:BHF-UCL
GO:0051260; P:protein homooligomerization; IDA:BHF-UCL
GO:0006626; P:protein targeting to mitochondrion; IMP:MGI
GO:0042127; P:regulation of cell proliferation; IMP:MGI
GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IMP:MGI
GO:1902108; P:regulation of mitochondrial membrane permeability involved in apoptotic process; IGI:MGI
GO:0032459; P:regulation of protein oligomerization; IDA:UniProtKB
GO:0001836; P:release of cytochrome c from mitochondria; IDA:MGI
GO:0032355; P:response to estradiol; IEA:Ensembl
GO:0042770; P:signal transduction in response to DNA damage; TAS:UniProtKB
Interpro
InterPro; IPR020728; Bcl2_BH3_motif_CS
InterPro; IPR010479; BID
Pfam
Pfam; PF06393; BID;
SMART
PROSITE
PROSITE; PS01259; BH3;
PRINTS