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BH3-interacting domain death agonist (p22 BID) (BID) [Cleaved into: BH3-interacting domain death agonist p15 (p15 BID); BH3-interacting domain death agonist p13 (p13 BID); BH3-interacting domain death agonist p11 (p11 BID)]

 BID_HUMAN               Reviewed;         195 AA.
P55957; Q549M7; Q71T04; Q7Z4M9; Q8IY86;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
18-JUL-2018, entry version 186.
RecName: Full=BH3-interacting domain death agonist;
AltName: Full=p22 BID;
Short=BID;
Contains:
RecName: Full=BH3-interacting domain death agonist p15;
AltName: Full=p15 BID;
Contains:
RecName: Full=BH3-interacting domain death agonist p13;
AltName: Full=p13 BID;
Contains:
RecName: Full=BH3-interacting domain death agonist p11;
AltName: Full=p11 BID;
Name=BID;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
PubMed=8918887; DOI=10.1101/gad.10.22.2859;
Wang K., Yin X.-M., Chao D.T., Milliman C.L., Korsmeyer S.J.;
"BID: a novel BH3 domain-only death agonist.";
Genes Dev. 10:2859-2869(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9721221; DOI=10.1006/geno.1998.5392;
Footz T.K., Birren B., Minoshima S., Asakawa S., Shimizu N.,
Riazi M.A., McDermid H.E.;
"The gene for death agonist BID maps to the region of human 22q11.2
duplicated in cat eye syndrome chromosomes and to mouse chromosome
6.";
Genomics 51:472-475(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
PubMed=14583606; DOI=10.1074/jbc.M309769200;
Renshaw S.A., Dempsey C.E., Barnes F.A., Bagstaff S.M., Dower S.K.,
Bingle C.D., Whyte M.K.;
"Three novel Bid proteins generated by alternative splicing of the
human Bid gene.";
J. Biol. Chem. 279:2846-2855(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Dai F.Y., Yu L., Huang H.B., Jiang C.L., Cui Y.Y., Zhao S.Y.;
"Cloning and expression of a new human cDNA homology to murine apoptic
death agonist (BID) mRNA.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-10.
NIEHS SNPs program;
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
GLN-162.
TISSUE=Brain, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-54, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
INTERACTION WITH ITCH, AND UBIQUITINATION BY ITCH.
PubMed=20392206; DOI=10.1111/j.1742-4658.2010.07562.x;
Azakir B.A., Desrochers G., Angers A.;
"The ubiquitin ligase Itch mediates the antiapoptotic activity of
epidermal growth factor by promoting the ubiquitylation and
degradation of the truncated C-terminal portion of Bid.";
FEBS J. 277:1319-1330(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[16]
STRUCTURE BY NMR.
PubMed=10089877; DOI=10.1016/S0092-8674(00)80572-3;
Chou J.J., Li H., Salvesen G.S., Yuan J., Wagner G.;
"Solution structure of BID, an intracellular amplifier of apoptotic
signaling.";
Cell 96:615-624(1999).
-!- FUNCTION: The major proteolytic product p15 BID allows the release
of cytochrome c (By similarity). Isoform 1, isoform 2 and isoform
4 induce ICE-like proteases and apoptosis. Isoform 3 does not
induce apoptosis. Counters the protective effect of Bcl-2.
{ECO:0000250, ECO:0000269|PubMed:14583606}.
-!- SUBUNIT: Forms heterodimers either with the pro-apoptotic protein
BAX or the anti-apoptotic protein Bcl-2 (By similarity). p15 BID
interacts with ITCH. {ECO:0000250, ECO:0000269|PubMed:20392206}.
-!- INTERACTION:
O43865:AHCYL1; NbExp=3; IntAct=EBI-10215147, EBI-2371423;
Q16611:BAK1; NbExp=4; IntAct=EBI-519672, EBI-519866;
Q07812:BAX; NbExp=17; IntAct=EBI-519672, EBI-516580;
P10415:BCL2; NbExp=9; IntAct=EBI-519672, EBI-77694;
Q07440:Bcl2a1 (xeno); NbExp=3; IntAct=EBI-519672, EBI-707754;
Q07817:BCL2L1; NbExp=2; IntAct=EBI-519672, EBI-78035;
Q07817-1:BCL2L1; NbExp=7; IntAct=EBI-519672, EBI-287195;
Q92843:BCL2L2; NbExp=5; IntAct=EBI-519672, EBI-707714;
Q03135:CAV1; NbExp=3; IntAct=EBI-519672, EBI-603614;
Q07820:MCL1; NbExp=2; IntAct=EBI-519672, EBI-1003422;
Q04864:REL; NbExp=3; IntAct=EBI-10215147, EBI-307352;
P17361:VACWR028 (xeno); NbExp=2; IntAct=EBI-519672, EBI-7115640;
P31946:YWHAB; NbExp=2; IntAct=EBI-519672, EBI-359815;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion
membrane {ECO:0000250}. Note=When uncleaved, it is predominantly
cytoplasmic. {ECO:0000269|PubMed:14583606}.
-!- SUBCELLULAR LOCATION: BH3-interacting domain death agonist p15:
Mitochondrion membrane {ECO:0000250}. Note=Translocates to
mitochondria as an integral membrane protein. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: BH3-interacting domain death agonist p13:
Mitochondrion membrane {ECO:0000250}. Note=Associated with the
mitochondrial membrane. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 2: Mitochondrion membrane. Note=A
significant proportion of isoform 2 localizes to mitochondria, it
may be cleaved constitutively.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=BID(L);
IsoId=P55957-1; Sequence=Displayed;
Name=2; Synonyms=BID(EL);
IsoId=P55957-2; Sequence=VSP_017267;
Name=3; Synonyms=BID(S);
IsoId=P55957-3; Sequence=VSP_017268, VSP_017269;
Name=4; Synonyms=BID(ES);
IsoId=P55957-4; Sequence=VSP_017266;
-!- TISSUE SPECIFICITY: Isoform 2 and isoform 3 are expressed in
spleen, bone marrow, cerebral and cerebellar cortex. Isoform 2 is
expressed in spleen, pancreas and placenta (at protein level).
Isoform 3 is expressed in lung, pancreas and spleen (at protein
level). Isoform 4 is expressed in lung and pancreas (at protein
level). {ECO:0000269|PubMed:14583606}.
-!- DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX
for their pro-apoptotic activity and for their interaction with
anti-apoptotic members of the Bcl-2 family.
-!- PTM: TNF-alpha induces a caspase-mediated cleavage of p22 BID into
a major p15 and minor p13 and p11 products. {ECO:0000250}.
-!- PTM: p15 BID is ubiquitinated by ITCH; ubiquitination results in
proteasome-dependent degradation. {ECO:0000269|PubMed:20392206}.
-!- SEQUENCE CAUTION:
Sequence=AAH22072.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/bid/";
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EMBL; AF042083; AAC34365.1; -; mRNA.
EMBL; AF250233; AAO32633.1; -; mRNA.
EMBL; AY005151; AAF89091.1; -; mRNA.
EMBL; AF087891; AAP97190.1; -; mRNA.
EMBL; CR456389; CAG30275.1; -; mRNA.
EMBL; CR407603; CAG28531.1; -; mRNA.
EMBL; AY309922; AAP50259.1; -; Genomic_DNA.
EMBL; BC009197; AAH09197.1; -; mRNA.
EMBL; BC022072; AAH22072.2; ALT_INIT; mRNA.
EMBL; BC033634; AAH33634.1; -; mRNA.
EMBL; BC036364; AAH36364.2; -; mRNA.
CCDS; CCDS13747.1; -. [P55957-2]
CCDS; CCDS13748.1; -. [P55957-1]
CCDS; CCDS13749.1; -. [P55957-4]
RefSeq; NP_001187.1; NM_001196.3. [P55957-1]
RefSeq; NP_001231496.1; NM_001244567.1. [P55957-1]
RefSeq; NP_001231498.1; NM_001244569.1. [P55957-4]
RefSeq; NP_001231499.1; NM_001244570.1. [P55957-4]
RefSeq; NP_001231501.1; NM_001244572.1. [P55957-4]
RefSeq; NP_932070.1; NM_197966.2. [P55957-2]
RefSeq; NP_932071.1; NM_197967.2. [P55957-4]
UniGene; Hs.591054; -.
PDB; 1ZY3; NMR; -; B=82-101.
PDB; 2BID; NMR; -; A=1-195.
PDB; 2KBW; NMR; -; B=76-106.
PDB; 2M5B; NMR; -; B=80-101.
PDB; 2M5I; NMR; -; A=61-195.
PDB; 4BD2; X-ray; 2.21 A; C=76-109.
PDB; 4QVE; X-ray; 2.05 A; B=76-109.
PDB; 4ZEQ; X-ray; 1.80 A; B=79-104.
PDB; 4ZIG; X-ray; 2.20 A; B=79-98.
PDB; 4ZII; X-ray; 2.19 A; C=76-109.
PDB; 5AJJ; X-ray; 1.75 A; B=79-112.
PDB; 5C3F; X-ray; 1.43 A; B=80-101.
PDBsum; 1ZY3; -.
PDBsum; 2BID; -.
PDBsum; 2KBW; -.
PDBsum; 2M5B; -.
PDBsum; 2M5I; -.
PDBsum; 4BD2; -.
PDBsum; 4QVE; -.
PDBsum; 4ZEQ; -.
PDBsum; 4ZIG; -.
PDBsum; 4ZII; -.
PDBsum; 5AJJ; -.
PDBsum; 5C3F; -.
ProteinModelPortal; P55957; -.
SMR; P55957; -.
BioGrid; 107106; 55.
ComplexPortal; CPX-1984; BID:BCL-2 complex.
ComplexPortal; CPX-1991; BID:BCL-XL complex.
CORUM; P55957; -.
DIP; DIP-34937N; -.
IntAct; P55957; 37.
MINT; P55957; -.
STRING; 9606.ENSP00000318822; -.
iPTMnet; P55957; -.
PhosphoSitePlus; P55957; -.
BioMuta; BID; -.
DMDM; 2493285; -.
OGP; P55957; -.
EPD; P55957; -.
MaxQB; P55957; -.
PaxDb; P55957; -.
PeptideAtlas; P55957; -.
PRIDE; P55957; -.
ProteomicsDB; 12613; -. [P55957-4]
ProteomicsDB; 56882; -.
ProteomicsDB; 56883; -. [P55957-2]
ProteomicsDB; 56884; -. [P55957-3]
ProteomicsDB; 56885; -. [P55957-4]
TopDownProteomics; P55957-1; -. [P55957-1]
TopDownProteomics; P55957-4; -. [P55957-4]
DNASU; 637; -.
Ensembl; ENST00000317361; ENSP00000318822; ENSG00000015475. [P55957-2]
Ensembl; ENST00000342111; ENSP00000344594; ENSG00000015475. [P55957-3]
Ensembl; ENST00000399765; ENSP00000382667; ENSG00000015475. [P55957-4]
Ensembl; ENST00000399767; ENSP00000382669; ENSG00000015475. [P55957-4]
Ensembl; ENST00000399774; ENSP00000382674; ENSG00000015475. [P55957-1]
Ensembl; ENST00000551952; ENSP00000449236; ENSG00000015475. [P55957-1]
Ensembl; ENST00000611040; ENSP00000483709; ENSG00000015475. [P55957-4]
Ensembl; ENST00000614949; ENSP00000477773; ENSG00000015475. [P55957-4]
Ensembl; ENST00000615414; ENSP00000483534; ENSG00000015475. [P55957-4]
Ensembl; ENST00000622694; ENSP00000480414; ENSG00000015475. [P55957-1]
GeneID; 637; -.
KEGG; hsa:637; -.
UCSC; uc002znc.3; human. [P55957-1]
CTD; 637; -.
DisGeNET; 637; -.
EuPathDB; HostDB:ENSG00000015475.18; -.
GeneCards; BID; -.
HGNC; HGNC:1050; BID.
HPA; CAB003771; -.
HPA; HPA000722; -.
MIM; 601997; gene.
neXtProt; NX_P55957; -.
OpenTargets; ENSG00000015475; -.
PharmGKB; PA25353; -.
eggNOG; ENOG410IVZ7; Eukaryota.
eggNOG; ENOG410ZF8F; LUCA.
GeneTree; ENSGT00390000002868; -.
HOGENOM; HOG000010016; -.
HOVERGEN; HBG001703; -.
InParanoid; P55957; -.
KO; K04726; -.
OMA; RDVFRTT; -.
OrthoDB; EOG091G0LRX; -.
PhylomeDB; P55957; -.
TreeFam; TF102047; -.
Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
Reactome; R-HSA-111452; Activation and oligomerization of BAK protein.
Reactome; R-HSA-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
Reactome; R-HSA-114294; Activation, translocation and oligomerization of BAX.
Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
Reactome; R-HSA-75108; Activation, myristolyation of BID and translocation to mitochondria.
SIGNOR; P55957; -.
ChiTaRS; BID; human.
EvolutionaryTrace; P55957; -.
GeneWiki; BH3_interacting-domain_death_agonist; -.
GeneWiki; BH3_interacting_domain_death_agonist; -.
GenomeRNAi; 637; -.
PMAP-CutDB; P55957; -.
PRO; PR:P55957; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000015475; -.
CleanEx; HS_BID; -.
ExpressionAtlas; P55957; baseline and differential.
Genevisible; P55957; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0032592; C:integral component of mitochondrial membrane; IEA:Ensembl.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; TAS:ProtInc.
GO; GO:0005123; F:death receptor binding; TAS:ProtInc.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0008637; P:apoptotic mitochondrial changes; TAS:ProtInc.
GO; GO:0090150; P:establishment of protein localization to membrane; IDA:BHF-UCL.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; TAS:ProtInc.
GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IEA:Ensembl.
GO; GO:0097345; P:mitochondrial outer membrane permeabilization; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; TAS:HGNC.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; IEA:Ensembl.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IEA:Ensembl.
GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0032464; P:positive regulation of protein homooligomerization; IDA:BHF-UCL.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0032461; P:positive regulation of protein oligomerization; IDA:UniProtKB.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0006626; P:protein targeting to mitochondrion; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:HGNC.
GO; GO:0042770; P:signal transduction in response to DNA damage; TAS:UniProtKB.
Gene3D; 1.10.437.10; -; 1.
InterPro; IPR020728; Bcl2_BH3_motif_CS.
InterPro; IPR010479; BID.
InterPro; IPR036834; Blc2-like_sf.
PANTHER; PTHR35447; PTHR35447; 1.
Pfam; PF06393; BID; 1.
PIRSF; PIRSF038018; BID; 1.
SUPFAM; SSF56854; SSF56854; 1.
PROSITE; PS01259; BH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Complete proteome; Cytoplasm; Membrane; Mitochondrion; Phosphoprotein;
Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 195 BH3-interacting domain death agonist.
/FTId=PRO_0000143101.
CHAIN 62 195 BH3-interacting domain death agonist p15.
{ECO:0000250}.
/FTId=PRO_0000223233.
CHAIN 77 195 BH3-interacting domain death agonist p13.
{ECO:0000250}.
/FTId=PRO_0000223232.
CHAIN 100 195 BH3-interacting domain death agonist p11.
{ECO:0000250}.
/FTId=PRO_0000223231.
MOTIF 86 100 BH3.
SITE 61 62 Cleavage. {ECO:0000250}.
SITE 76 77 Cleavage. {ECO:0000250}.
SITE 99 100 Cleavage. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 54 54 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 78 78 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
VAR_SEQ 1 96 Missing (in isoform 4).
{ECO:0000303|PubMed:14583606}.
/FTId=VSP_017266.
VAR_SEQ 1 1 M -> MCSGAGVMMARWAARGRAGWRSTVRILSPLGHCEPG
VSRSCRAAQAM (in isoform 2).
{ECO:0000303|PubMed:14583606,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_017267.
VAR_SEQ 75 137 DSESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGLALQLRN
TSRSEEDRNRDLATALEQLLQA -> GASDNNTASAEEETE
AAGSVAVERGLHGAATVILKVKKTSSGILPGTSPRSGTAWT
VASLRAW (in isoform 3).
{ECO:0000303|PubMed:14583606}.
/FTId=VSP_017268.
VAR_SEQ 138 195 Missing (in isoform 3).
{ECO:0000303|PubMed:14583606}.
/FTId=VSP_017269.
VARIANT 10 10 S -> G (in dbSNP:rs8190315).
{ECO:0000269|Ref.7}.
/FTId=VAR_018845.
VARIANT 162 162 H -> Q (in dbSNP:rs17853595).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_025332.
VARIANT 194 194 M -> T (in dbSNP:rs59225839).
/FTId=VAR_061041.
HELIX 15 27 {ECO:0000244|PDB:2BID}.
STRAND 31 33 {ECO:0000244|PDB:2BID}.
HELIX 34 40 {ECO:0000244|PDB:2BID}.
HELIX 41 43 {ECO:0000244|PDB:2BID}.
HELIX 81 100 {ECO:0000244|PDB:5C3F}.
TURN 102 105 {ECO:0000244|PDB:2KBW}.
HELIX 106 114 {ECO:0000244|PDB:2BID}.
HELIX 116 118 {ECO:0000244|PDB:2BID}.
HELIX 119 135 {ECO:0000244|PDB:2BID}.
HELIX 145 162 {ECO:0000244|PDB:2BID}.
HELIX 167 179 {ECO:0000244|PDB:2BID}.
TURN 180 182 {ECO:0000244|PDB:2BID}.
HELIX 183 191 {ECO:0000244|PDB:2BID}.
SEQUENCE 195 AA; 21995 MW; B17A07334C1AFBEF CRC64;
MDCEVNNGSS LRDECITNLL VFGFLQSCSD NSFRRELDAL GHELPVLAPQ WEGYDELQTD
GNRSSHSRLG RIEADSESQE DIIRNIARHL AQVGDSMDRS IPPGLVNGLA LQLRNTSRSE
EDRNRDLATA LEQLLQAYPR DMEKEKTMLV LALLLAKKVA SHTPSLLRDV FHTTVNFINQ
NLRTYVRSLA RNGMD


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