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   27-MAR-2024, entry version 221.
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: OPG035; 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   PDB; 7P33; X-ray; 2.79 A; F/G/H/I/J=76-109.
DR   PDB; 7QTW; X-ray; 1.41 A; B=76-109.
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   PDBsum; 7P33; -.
DR   PDBsum; 7QTW; -.
DR   AlphaFoldDB; P55957; -.
DR   BMRB; P55957; -.
DR   SMR; P55957; -.
DR   BioGRID; 107106; 103.
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   BindingDB; P55957; -.
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; 9606-ENSP00000318822; -.
DR   PeptideAtlas; P55957; -.
DR   ProteomicsDB; 56882; -. [P55957-1]
DR   ProteomicsDB; 56883; -. [P55957-2]
DR   ProteomicsDB; 56884; -. [P55957-3]
DR   ProteomicsDB; 56885; -. [P55957-4]
DR   Pumba; P55957; -.
DR   TopDownProteomics; P55957-1; -. [P55957-1]
DR   TopDownProteomics; P55957-4; -. [P55957-4]
DR   Antibodypedia; 263; 1509 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   AGR; HGNC:1050; -.
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   OrthoDB; 5322479at2759; -.
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; 30 hits in 1174 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 170 other cell types or tissues.
DR   ExpressionAtlas; P55957; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
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:0043028; F:cysteine-type endopeptidase regulator activity involved in apoptotic process; TAS:UniProt.
DR   GO; GO:0005123; F:death receptor binding; TAS:ProtInc.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
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; Blc2-like; 1.
DR   InterPro; IPR036834; Bcl-2-like_sf.
DR   InterPro; IPR020728; Bcl2_BH3_motif_CS.
DR   InterPro; IPR010479; BID.
DR   PANTHER; PTHR35447; BH3-INTERACTING DOMAIN DEATH AGONIST; 1.
DR   PANTHER; PTHR35447:SF1; BH3-INTERACTING DOMAIN DEATH AGONIST; 1.
DR   Pfam; PF06393; BID; 1.
DR   PIRSF; PIRSF038018; BID; 1.
DR   SUPFAM; SSF56854; Bcl-2 inhibitors of programmed cell death; 1.
DR   PROSITE; PS01259; BH3; 1.
DR   Genevisible; P55957; HS.
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   HELIX           101..105
FT                   /evidence="ECO:0007829|PDB:7P33"
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
//