BID_HUMAN
ID BID_HUMAN Reviewed; 195 AA.
AC P55957; Q549M7; Q71T04; Q7Z4M9; Q8IY86;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=BH3-interacting domain death agonist;
DE AltName: Full=p22 BID;
DE Short=BID;
DE Contains:
DE RecName: Full=BH3-interacting domain death agonist p15;
DE AltName: Full=p15 BID;
DE Contains:
DE RecName: Full=BH3-interacting domain death agonist p13;
DE AltName: Full=p13 BID;
DE Contains:
DE RecName: Full=BH3-interacting domain death agonist p11;
DE AltName: Full=p11 BID;
GN Name=BID;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX PubMed=8918887; DOI=10.1101/gad.10.22.2859;
RA Wang K., Yin X.-M., Chao D.T., Milliman C.L., Korsmeyer S.J.;
RT "BID: a novel BH3 domain-only death agonist.";
RL Genes Dev. 10:2859-2869(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9721221; DOI=10.1006/geno.1998.5392;
RA Footz T.K., Birren B., Minoshima S., Asakawa S., Shimizu N., Riazi M.A.,
RA McDermid H.E.;
RT "The gene for death agonist BID maps to the region of human 22q11.2
RT duplicated in cat eye syndrome chromosomes and to mouse chromosome 6.";
RL Genomics 51:472-475(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=14583606; DOI=10.1074/jbc.m309769200;
RA Renshaw S.A., Dempsey C.E., Barnes F.A., Bagstaff S.M., Dower S.K.,
RA Bingle C.D., Whyte M.K.;
RT "Three novel Bid proteins generated by alternative splicing of the human
RT Bid gene.";
RL J. Biol. Chem. 279:2846-2855(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Dai F.Y., Yu L., Huang H.B., Jiang C.L., Cui Y.Y., Zhao S.Y.;
RT "Cloning and expression of a new human cDNA homology to murine apoptic
RT death agonist (BID) mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-10.
RG NIEHS SNPs program;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP GLN-162.
RC TISSUE=Brain, and Skin;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH HUMANIN.
RX PubMed=15661737; DOI=10.1074/jbc.m411902200;
RA Zhai D., Luciano F., Zhu X., Guo B., Satterthwait A.C., Reed J.C.;
RT "Humanin binds and nullifies Bid activity by blocking its activation of Bax
RT and Bak.";
RL J. Biol. Chem. 280:15815-15824(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-54, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [12]
RP INTERACTION WITH ITCH, AND UBIQUITINATION BY ITCH.
RX PubMed=20392206; DOI=10.1111/j.1742-4658.2010.07562.x;
RA Azakir B.A., Desrochers G., Angers A.;
RT "The ubiquitin ligase Itch mediates the antiapoptotic activity of epidermal
RT growth factor by promoting the ubiquitylation and degradation of the
RT truncated C-terminal portion of Bid.";
RL FEBS J. 277:1319-1330(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PLEKHN1.
RX PubMed=29531808; DOI=10.1038/s41420-017-0006-5;
RA Kuriyama S., Tsuji T., Sakuma T., Yamamoto T., Tanaka M.;
RT "PLEKHN1 promotes apoptosis by enhancing Bax-Bak hetero-oligomerization
RT through interaction with Bid in human colon cancer.";
RL Cell. Death. Discov. 4:11-11(2018).
RN [18]
RP FORMATION OF FIBERS WITH HUMANIN.
RX PubMed=33106313; DOI=10.1074/jbc.ra120.013023;
RA Morris D.L., Johnson S., Bleck C.K.E., Lee D.Y., Tjandra N.;
RT "Humanin selectively prevents the activation of pro-apoptotic protein BID
RT by sequestering it into fibers.";
RL J. Biol. Chem. 295:18226-18238(2020).
RN [19]
RP FUNCTION (BH3-INTERACTING DOMAIN DEATH AGONIST P15), AND PROTEOLYTIC
RP CLEAVAGE.
RX PubMed=32029622; DOI=10.1126/science.aay0542;
RA Zhao P., Sun X., Chaggan C., Liao Z., In Wong K., He F., Singh S.,
RA Loomba R., Karin M., Witztum J.L., Saltiel A.R.;
RT "An AMPK-caspase-6 axis controls liver damage in nonalcoholic
RT steatohepatitis.";
RL Science 367:652-660(2020).
RN [20]
RP STRUCTURE BY NMR.
RX PubMed=10089877; DOI=10.1016/s0092-8674(00)80572-3;
RA Chou J.J., Li H., Salvesen G.S., Yuan J., Wagner G.;
RT "Solution structure of BID, an intracellular amplifier of apoptotic
RT signaling.";
RL Cell 96:615-624(1999).
CC -!- FUNCTION: Induces caspases and apoptosis (PubMed:14583606). Counters
CC the protective effect of BCL2 (By similarity).
CC {ECO:0000250|UniProtKB:P70444, ECO:0000269|PubMed:14583606}.
CC -!- FUNCTION: [BH3-interacting domain death agonist p15]: Induces caspase
CC activation and apoptosis (PubMed:15661737, PubMed:32029622). Allows the
CC release of cytochrome c (PubMed:32029622).
CC {ECO:0000269|PubMed:15661737, ECO:0000269|PubMed:32029622}.
CC -!- FUNCTION: [Isoform 1]: Induces ICE-like proteases and apoptosis.
CC {ECO:0000269|PubMed:14583606}.
CC -!- FUNCTION: [Isoform 2]: Induces ICE-like proteases and apoptosis.
CC {ECO:0000269|PubMed:14583606}.
CC -!- FUNCTION: [Isoform 3]: Does not induce apoptosis.
CC {ECO:0000269|PubMed:14583606}.
CC -!- FUNCTION: [Isoform 4]: Induces ICE-like proteases and apoptosis.
CC {ECO:0000269|PubMed:14583606}.
CC -!- SUBUNIT: Forms heterodimers either with the pro-apoptotic protein BAX
CC or the anti-apoptotic protein BCL2 (By similarity). Interacts with
CC PLEKHN1 (PubMed:29531808). {ECO:0000250|UniProtKB:P70444,
CC ECO:0000269|PubMed:29531808}.
CC -!- SUBUNIT: [BH3-interacting domain death agonist]: Interacts with
CC humanin; forms fibers with humanin which results in BID conformational
CC changes and sequestering of BID into the fibers, preventing BID
CC activation. {ECO:0000269|PubMed:15661737, ECO:0000269|PubMed:33106313}.
CC -!- SUBUNIT: [BH3-interacting domain death agonist p15]: Interacts with
CC ITCH (PubMed:20392206). Interacts with humanin; the interaction
CC prevents BID-induced apoptosis (PubMed:15661737). Interacts with MTCH2
CC (By similarity). {ECO:0000250|UniProtKB:P70444,
CC ECO:0000269|PubMed:15661737, ECO:0000269|PubMed:20392206}.
CC -!- INTERACTION:
CC P55957; O43865: AHCYL1; NbExp=3; IntAct=EBI-519672, EBI-2371423;
CC P55957; Q16611: BAK1; NbExp=4; IntAct=EBI-519672, EBI-519866;
CC P55957; Q07812: BAX; NbExp=17; IntAct=EBI-519672, EBI-516580;
CC P55957; P10415: BCL2; NbExp=9; IntAct=EBI-519672, EBI-77694;
CC P55957; Q07817: BCL2L1; NbExp=2; IntAct=EBI-519672, EBI-78035;
CC P55957; Q07817-1: BCL2L1; NbExp=7; IntAct=EBI-519672, EBI-287195;
CC P55957; Q92843: BCL2L2; NbExp=5; IntAct=EBI-519672, EBI-707714;
CC P55957; Q03135: CAV1; NbExp=3; IntAct=EBI-519672, EBI-603614;
CC P55957; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-519672, EBI-742054;
CC P55957; Q07820: MCL1; NbExp=2; IntAct=EBI-519672, EBI-1003422;
CC P55957; Q04864: REL; NbExp=3; IntAct=EBI-519672, EBI-307352;
CC P55957; Q07440: Bcl2a1; Xeno; NbExp=3; IntAct=EBI-519672, EBI-707754;
CC P55957; P17361: VACWR028; Xeno; NbExp=2; IntAct=EBI-519672, EBI-7115640;
CC P55957-2; O43865: AHCYL1; NbExp=3; IntAct=EBI-10215147, EBI-2371423;
CC P55957-2; Q04864: REL; NbExp=3; IntAct=EBI-10215147, EBI-307352;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14583606}.
CC Mitochondrion membrane {ECO:0000269|PubMed:14583606}. Mitochondrion
CC outer membrane {ECO:0000269|PubMed:29531808}. Note=When uncleaved, it
CC is predominantly cytoplasmic. {ECO:0000269|PubMed:14583606}.
CC -!- SUBCELLULAR LOCATION: [BH3-interacting domain death agonist p15]:
CC Mitochondrion membrane {ECO:0000250|UniProtKB:P70444}.
CC Note=Translocates to mitochondria as an integral membrane protein.
CC {ECO:0000250|UniProtKB:P70444}.
CC -!- SUBCELLULAR LOCATION: [BH3-interacting domain death agonist p13]:
CC Mitochondrion membrane {ECO:0000250|UniProtKB:P70444}. Note=Associated
CC with the mitochondrial membrane. {ECO:0000250|UniProtKB:P70444}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:14583606}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC {ECO:0000269|PubMed:14583606}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion membrane
CC {ECO:0000269|PubMed:14583606}. Note=A significant proportion of isoform
CC 2 localizes to mitochondria, it may be cleaved constitutively.
CC {ECO:0000269|PubMed:14583606}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=BID(L);
CC IsoId=P55957-1; Sequence=Displayed;
CC Name=2; Synonyms=BID(EL);
CC IsoId=P55957-2; Sequence=VSP_017267;
CC Name=3; Synonyms=BID(S);
CC IsoId=P55957-3; Sequence=VSP_017268, VSP_017269;
CC Name=4; Synonyms=BID(ES);
CC IsoId=P55957-4; Sequence=VSP_017266;
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in spleen, pancreas and
CC placenta (at protein level). {ECO:0000269|PubMed:14583606}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in lung, pancreas and spleen
CC (at protein level). {ECO:0000269|PubMed:14583606}.
CC -!- TISSUE SPECIFICITY: [Isoform 4]: Expressed in lung and pancreas (at
CC protein level). {ECO:0000269|PubMed:14583606}.
CC -!- DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for
CC their pro-apoptotic activity and for their interaction with anti-
CC apoptotic members of the Bcl-2 family.
CC -!- PTM: [BH3-interacting domain death agonist]: TNF-alpha induces caspase-
CC mediated cleavage into a major p15 and minor p13 and p11 products (By
CC similarity). Cleaved by CASP6 into a major p15 and minor p13 products,
CC leading to release of cytochrome c and subsequent nonalcoholic
CC steatohepatitis (PubMed:32029622). {ECO:0000250|UniProtKB:P70444,
CC ECO:0000269|PubMed:32029622}.
CC -!- PTM: [BH3-interacting domain death agonist p15]: Ubiquitinated by ITCH;
CC ubiquitination results in proteasome-dependent degradation.
CC {ECO:0000269|PubMed:20392206}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22072.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/bid/";
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DR EMBL; AF042083; AAC34365.1; -; mRNA.
DR EMBL; AF250233; AAO32633.1; -; mRNA.
DR EMBL; AY005151; AAF89091.1; -; mRNA.
DR EMBL; AF087891; AAP97190.1; -; mRNA.
DR EMBL; CR456389; CAG30275.1; -; mRNA.
DR EMBL; CR407603; CAG28531.1; -; mRNA.
DR EMBL; AY309922; AAP50259.1; -; Genomic_DNA.
DR EMBL; BC009197; AAH09197.1; -; mRNA.
DR EMBL; BC022072; AAH22072.2; ALT_INIT; mRNA.
DR EMBL; BC033634; AAH33634.1; -; mRNA.
DR EMBL; BC036364; AAH36364.2; -; mRNA.
DR CCDS; CCDS13747.1; -. [P55957-2]
DR CCDS; CCDS13748.1; -. [P55957-1]
DR CCDS; CCDS13749.1; -. [P55957-4]
DR RefSeq; NP_001187.1; NM_001196.3. [P55957-1]
DR RefSeq; NP_001231496.1; NM_001244567.1. [P55957-1]
DR RefSeq; NP_001231498.1; NM_001244569.1. [P55957-4]
DR RefSeq; NP_001231499.1; NM_001244570.1. [P55957-4]
DR RefSeq; NP_001231501.1; NM_001244572.1. [P55957-4]
DR RefSeq; NP_932070.1; NM_197966.2. [P55957-2]
DR RefSeq; NP_932071.1; NM_197967.2. [P55957-4]
DR PDB; 1ZY3; NMR; -; B=82-101.
DR PDB; 2BID; NMR; -; A=1-195.
DR PDB; 2KBW; NMR; -; B=76-106.
DR PDB; 2M5B; NMR; -; B=80-101.
DR PDB; 2M5I; NMR; -; A=61-195.
DR PDB; 4BD2; X-ray; 2.21 A; C=76-109.
DR PDB; 4QVE; X-ray; 2.05 A; B=76-109.
DR PDB; 4ZEQ; X-ray; 1.80 A; B=79-104.
DR PDB; 4ZIG; X-ray; 2.20 A; B=79-98.
DR PDB; 4ZII; X-ray; 2.19 A; C=76-109.
DR PDB; 5AJJ; X-ray; 1.75 A; B=79-112.
DR PDB; 5C3F; X-ray; 1.43 A; B=80-101.
DR PDB; 7M5A; X-ray; 1.50 A; B=80-100.
DR PDB; 7M5B; X-ray; 1.85 A; B/D=80-100.
DR PDBsum; 1ZY3; -.
DR PDBsum; 2BID; -.
DR PDBsum; 2KBW; -.
DR PDBsum; 2M5B; -.
DR PDBsum; 2M5I; -.
DR PDBsum; 4BD2; -.
DR PDBsum; 4QVE; -.
DR PDBsum; 4ZEQ; -.
DR PDBsum; 4ZIG; -.
DR PDBsum; 4ZII; -.
DR PDBsum; 5AJJ; -.
DR PDBsum; 5C3F; -.
DR PDBsum; 7M5A; -.
DR PDBsum; 7M5B; -.
DR AlphaFoldDB; P55957; -.
DR BMRB; P55957; -.
DR SMR; P55957; -.
DR BioGRID; 107106; 93.
DR ComplexPortal; CPX-1984; BID:BCL-2 complex.
DR ComplexPortal; CPX-1991; BID:BCL-XL complex.
DR DIP; DIP-34937N; -.
DR IntAct; P55957; 39.
DR MINT; P55957; -.
DR STRING; 9606.ENSP00000318822; -.
DR ChEMBL; CHEMBL1250414; -.
DR GlyGen; P55957; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P55957; -.
DR PhosphoSitePlus; P55957; -.
DR BioMuta; BID; -.
DR DMDM; 2493285; -.
DR OGP; P55957; -.
DR EPD; P55957; -.
DR jPOST; P55957; -.
DR MassIVE; P55957; -.
DR MaxQB; P55957; -.
DR PaxDb; P55957; -.
DR PeptideAtlas; P55957; -.
DR PRIDE; P55957; -.
DR ProteomicsDB; 56882; -. [P55957-1]
DR ProteomicsDB; 56883; -. [P55957-2]
DR ProteomicsDB; 56884; -. [P55957-3]
DR ProteomicsDB; 56885; -. [P55957-4]
DR TopDownProteomics; P55957-1; -. [P55957-1]
DR TopDownProteomics; P55957-4; -. [P55957-4]
DR Antibodypedia; 263; 1351 antibodies from 50 providers.
DR DNASU; 637; -.
DR Ensembl; ENST00000317361.11; ENSP00000318822.7; ENSG00000015475.19. [P55957-2]
DR Ensembl; ENST00000342111.9; ENSP00000344594.5; ENSG00000015475.19. [P55957-3]
DR Ensembl; ENST00000399765.5; ENSP00000382667.1; ENSG00000015475.19. [P55957-4]
DR Ensembl; ENST00000399767.6; ENSP00000382669.1; ENSG00000015475.19. [P55957-4]
DR Ensembl; ENST00000551952.5; ENSP00000449236.1; ENSG00000015475.19. [P55957-1]
DR Ensembl; ENST00000614949.4; ENSP00000477773.1; ENSG00000015475.19. [P55957-4]
DR Ensembl; ENST00000622694.5; ENSP00000480414.1; ENSG00000015475.19. [P55957-1]
DR GeneID; 637; -.
DR KEGG; hsa:637; -.
DR MANE-Select; ENST00000622694.5; ENSP00000480414.1; NM_001196.4; NP_001187.1.
DR UCSC; uc002znc.3; human. [P55957-1]
DR CTD; 637; -.
DR DisGeNET; 637; -.
DR GeneCards; BID; -.
DR HGNC; HGNC:1050; BID.
DR HPA; ENSG00000015475; Tissue enhanced (bone).
DR MIM; 601997; gene.
DR neXtProt; NX_P55957; -.
DR OpenTargets; ENSG00000015475; -.
DR PharmGKB; PA25353; -.
DR VEuPathDB; HostDB:ENSG00000015475; -.
DR eggNOG; ENOG502SAN7; Eukaryota.
DR GeneTree; ENSGT00390000002868; -.
DR HOGENOM; CLU_090524_0_0_1; -.
DR InParanoid; P55957; -.
DR PhylomeDB; P55957; -.
DR TreeFam; TF102047; -.
DR PathwayCommons; P55957; -.
DR Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-HSA-111452; Activation and oligomerization of BAK protein.
DR Reactome; R-HSA-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
DR Reactome; R-HSA-114294; Activation, translocation and oligomerization of BAX.
DR Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR Reactome; R-HSA-75108; Activation, myristolyation of BID and translocation to mitochondria.
DR SignaLink; P55957; -.
DR SIGNOR; P55957; -.
DR BioGRID-ORCS; 637; 28 hits in 1083 CRISPR screens.
DR ChiTaRS; BID; human.
DR EvolutionaryTrace; P55957; -.
DR GeneWiki; BH3_interacting-domain_death_agonist; -.
DR GeneWiki; BH3_interacting_domain_death_agonist; -.
DR GenomeRNAi; 637; -.
DR Pharos; P55957; Tbio.
DR PRO; PR:P55957; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P55957; protein.
DR Bgee; ENSG00000015475; Expressed in monocyte and 169 other tissues.
DR ExpressionAtlas; P55957; baseline and differential.
DR Genevisible; P55957; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005123; F:death receptor binding; TAS:ProtInc.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
DR GO; GO:0090150; P:establishment of protein localization to membrane; IDA:BHF-UCL.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; TAS:ProtInc.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IDA:UniProtKB.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IEA:Ensembl.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; IEA:Ensembl.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; TAS:HGNC-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; IEA:Ensembl.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IEA:Ensembl.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0042129; P:regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:HGNC-UCL.
DR GO; GO:0042770; P:signal transduction in response to DNA damage; TAS:UniProtKB.
DR GO; GO:0097435; P:supramolecular fiber organization; IDA:UniProtKB.
DR DisProt; DP01662; -.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR020728; Bcl2_BH3_motif_CS.
DR InterPro; IPR010479; BID.
DR PANTHER; PTHR35447; PTHR35447; 1.
DR Pfam; PF06393; BID; 1.
DR PIRSF; PIRSF038018; BID; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR PROSITE; PS01259; BH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cytoplasm;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..195
FT /note="BH3-interacting domain death agonist"
FT /id="PRO_0000143101"
FT CHAIN 61..195
FT /note="BH3-interacting domain death agonist p15"
FT /evidence="ECO:0000305|PubMed:32029622"
FT /id="PRO_0000223233"
FT CHAIN 76..195
FT /note="BH3-interacting domain death agonist p13"
FT /evidence="ECO:0000305|PubMed:32029622"
FT /id="PRO_0000223232"
FT CHAIN 100..195
FT /note="BH3-interacting domain death agonist p11"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT /id="PRO_0000223231"
FT MOTIF 86..100
FT /note="BH3"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT SITE 60..61
FT /note="Cleavage; by CASP6"
FT /evidence="ECO:0000269|PubMed:32029622"
FT SITE 75..76
FT /note="Cleavage;by CASP6"
FT /evidence="ECO:0000269|PubMed:32029622"
FT SITE 99..100
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 54
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VAR_SEQ 1..96
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14583606"
FT /id="VSP_017266"
FT VAR_SEQ 1
FT /note="M -> MCSGAGVMMARWAARGRAGWRSTVRILSPLGHCEPGVSRSCRAAQAM
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14583606,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017267"
FT VAR_SEQ 75..137
FT /note="DSESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGLALQLRNTSRSEEDRNRD
FT LATALEQLLQA -> GASDNNTASAEEETEAAGSVAVERGLHGAATVILKVKKTSSGIL
FT PGTSPRSGTAWTVASLRAW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14583606"
FT /id="VSP_017268"
FT VAR_SEQ 138..195
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14583606"
FT /id="VSP_017269"
FT VARIANT 10
FT /note="S -> G (in dbSNP:rs8190315)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_018845"
FT VARIANT 162
FT /note="H -> Q (in dbSNP:rs17853595)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025332"
FT VARIANT 194
FT /note="M -> T (in dbSNP:rs59225839)"
FT /id="VAR_061041"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:2BID"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2BID"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:2BID"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2BID"
FT HELIX 81..100
FT /evidence="ECO:0007829|PDB:5C3F"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:2KBW"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:2BID"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2BID"
FT HELIX 119..135
FT /evidence="ECO:0007829|PDB:2BID"
FT HELIX 145..162
FT /evidence="ECO:0007829|PDB:2BID"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:2BID"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:2BID"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:2BID"
SQ 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
