BAK_HUMAN
ID BAK_HUMAN Reviewed; 211 AA.
AC Q16611; C0H5Y7; Q6I9T6; Q92533;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=Bcl-2 homologous antagonist/killer;
DE AltName: Full=Apoptosis regulator BAK;
DE AltName: Full=Bcl-2-like protein 7;
DE Short=Bcl2-L-7;
GN Name=BAK1; Synonyms=BAK, BCL2L7, CDN1;
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 [MRNA] (ISOFORM 1), AND INTERACTION WITH ADENOVIRUS E1B
RP 19K PROTEIN.
RC TISSUE=B-cell;
RX PubMed=7715729; DOI=10.1038/374731a0;
RA Farrow S.N., White J.H.M., Martinou I., Raven T., Pun K.-T., Grinham C.J.,
RA Martinou J.-C., Brown R.;
RT "Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K.";
RL Nature 374:731-733(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7715730; DOI=10.1038/374733a0;
RA Chittenden T., Harrington E.A., O'Connor R., Flemington C., Lutz R.J.,
RA Evan G.I., Guild B.C.;
RT "Induction of apoptosis by the Bcl-2 homologue Bak.";
RL Nature 374:733-736(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7715731; DOI=10.1038/374736a0;
RA Kiefer M.C., Brauer M.J., Powers V.C., Wu J.J., Umansky S.R., Tomei L.D.,
RA Barr P.J.;
RT "Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak.";
RL Nature 374:736-739(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-28 AND ARG-69.
RG NIEHS SNPs program;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Lung;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 96-206.
RA Eguchi H., Hayashi S.;
RT "Estrogen alters expression of apoptosis-regulators, Bcl-2, Bcl-xL and Bak,
RT as well as susceptibility to therapeutic agents of human breast cancer
RT cells.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP MUTAGENESIS, AND FUNCTION OF BH3 MOTIF.
RX PubMed=8521816; DOI=10.1002/j.1460-2075.1995.tb00246.x;
RA Chittenden T., Flemington C., Houghton A.B., Ebb R.G., Gallo G.J.,
RA Elangovan B., Chinnadurai G., Lutz R.J.;
RT "A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death
RT and protein binding functions.";
RL EMBO J. 14:5589-5596(1995).
RN [11]
RP INTERACTION WITH EPSTEIN-BARR VIRUS PROTEIN BALF1.
RX PubMed=10233985; DOI=10.1128/jvi.73.6.5181-5185.1999;
RA Marshall W.L., Yim C., Gustafson E., Graf T., Sage D.R., Hanify K.,
RA Williams L., Fingeroth J., Finberg R.W.;
RT "Epstein-Barr virus encodes a novel homolog of the bcl-2 oncogene that
RT inhibits apoptosis and associates with Bax and Bak.";
RL J. Virol. 73:5181-5185(1999).
RN [12]
RP INTERACTION WITH VACCINIA VIRUS PROTEIN F1.
RX PubMed=16439990; DOI=10.1038/sj.cdd.4401853;
RA Postigo A., Cross J.R., Downward J., Way M.;
RT "Interaction of F1L with the BH3 domain of Bak is responsible for
RT inhibiting vaccinia-induced apoptosis.";
RL Cell Death Differ. 13:1651-1662(2006).
RN [13]
RP INTERACTION WITH GIMAP3 AND GIMAP5.
RX PubMed=16509771; DOI=10.1371/journal.pbio.0040103;
RA Nitta T., Nasreen M., Seike T., Goji A., Ohigashi I., Miyazaki T., Ohta T.,
RA Kanno M., Takahama Y.;
RT "IAN family critically regulates survival and development of T
RT lymphocytes.";
RL PLoS Biol. 4:593-605(2006).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
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 [16]
RP INTERACTION WITH RTL10/BOP.
RX PubMed=23055042; DOI=10.1007/s13238-012-2069-7;
RA Zhang X., Weng C., Li Y., Wang X., Jiang C., Li X., Xu Y., Chen Q., Pan L.,
RA Tang H.;
RT "Human Bop is a novel BH3-only member of the Bcl-2 protein family.";
RL Protein Cell 3:790-801(2012).
RN [17]
RP INTERACTION WITH VDAC1.
RX PubMed=25296756; DOI=10.1074/jbc.m114.567792;
RA Li L., Yao Y.C., Gu X.Q., Che D., Ma C.Q., Dai Z.Y., Li C., Zhou T.,
RA Cai W.B., Yang Z.H., Yang X., Gao G.Q.;
RT "Plasminogen kringle 5 induces endothelial cell apoptosis by triggering a
RT voltage-dependent anion channel 1 (VDAC1) positive feedback loop.";
RL J. Biol. Chem. 289:32628-32638(2014).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [19]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
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 [20]
RP STRUCTURE BY NMR OF 72-87 IN COMPLEX WITH BCL2L1 ISOFORM BCL-X(L).
RX PubMed=9020082; DOI=10.1126/science.275.5302.983;
RA Sattler M., Liang H., Nettesheim D., Meadows R.P., Harlan J.E.,
RA Eberstadt M., Yoon H.S., Shuker S.B., Chang B.S., Minn A.J., Thompson C.B.,
RA Fesik S.W.;
RT "Structure of Bcl-xL-Bak peptide complex: recognition between regulators of
RT apoptosis.";
RL Science 275:983-986(1997).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 16-186, FUNCTION, SUBUNIT,
RP MUTAGENESIS OF HIS-164, AND ZINC-BINDING.
RX PubMed=17157251; DOI=10.1016/j.molcel.2006.10.014;
RA Moldoveanu T., Liu Q., Tocilj A., Watson M., Shore G., Gehring K.;
RT "The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding
RT site.";
RL Mol. Cell 24:677-688(2006).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 67-92 IN COMPLEX WITH MYXOMA
RP VIRUS PROTEIN M11L.
RX PubMed=17386268; DOI=10.1016/j.molcel.2007.02.004;
RA Kvansakul M., van Delft M.F., Lee E.F., Gulbis J.M., Fairlie W.D.,
RA Huang D.C.S., Colman P.M.;
RT "A structural viral mimic of prosurvival Bcl-2: a pivotal role for
RT sequestering proapoptotic Bax and Bak.";
RL Mol. Cell 25:933-942(2007).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of MS0836.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- FUNCTION: Plays a role in the mitochondrial apoptosic process. Upon
CC arrival of cell death signals, promotes mitochondrial outer membrane
CC (MOM) permeabilization by oligomerizing to form pores within the MOM.
CC This releases apoptogenic factors into the cytosol, including
CC cytochrome c, promoting the activation of caspase 9 which in turn
CC processes and activates the effector caspases.
CC {ECO:0000269|PubMed:17157251, ECO:0000269|PubMed:8521816}.
CC -!- SUBUNIT: Homodimer. Formation of the homodimer is zinc-dependent
CC (PubMed:17157251). Forms heterodimers with BCL2 and BCL2L1 isoform Bcl-
CC X(L) (PubMed:9020082). Forms heterooligomers with BAX
CC (PubMed:29531808). Interacts with BCL2A1 (By similarity). Interacts
CC with RTL10/BOP (PubMed:23055042). Interacts with VDAC1
CC (PubMed:25296756). Interacts with GIMAP3/IAN4 and GIMAP5/IAN5
CC (PubMed:16509771). {ECO:0000250|UniProtKB:O08734,
CC ECO:0000269|PubMed:16509771, ECO:0000269|PubMed:17157251,
CC ECO:0000269|PubMed:23055042, ECO:0000269|PubMed:25296756,
CC ECO:0000269|PubMed:29531808, ECO:0000269|PubMed:9020082}.
CC -!- SUBUNIT: (Microbial infection) Interacts with vaccinia virus protein
CC F1. {ECO:0000269|PubMed:16439990}.
CC -!- SUBUNIT: (Microbial infection) Interacts with myxoma virus protein
CC M11L. {ECO:0000269|PubMed:17386268}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
CC protein BALF1. {ECO:0000269|PubMed:10233985}.
CC -!- SUBUNIT: (Microbial infection) Interacts with adenovirus protein E1B
CC 19K. {ECO:0000269|PubMed:7715729}.
CC -!- INTERACTION:
CC Q16611; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-519866, EBI-702390;
CC Q16611; Q16611: BAK1; NbExp=5; IntAct=EBI-519866, EBI-519866;
CC Q16611; Q07812: BAX; NbExp=5; IntAct=EBI-519866, EBI-516580;
CC Q16611; P10415: BCL2; NbExp=3; IntAct=EBI-519866, EBI-77694;
CC Q16611; Q16548: BCL2A1; NbExp=6; IntAct=EBI-519866, EBI-1003550;
CC Q16611; Q07817: BCL2L1; NbExp=27; IntAct=EBI-519866, EBI-78035;
CC Q16611; Q07817-1: BCL2L1; NbExp=13; IntAct=EBI-519866, EBI-287195;
CC Q16611; Q92843: BCL2L2; NbExp=8; IntAct=EBI-519866, EBI-707714;
CC Q16611; P55957: BID; NbExp=4; IntAct=EBI-519866, EBI-519672;
CC Q16611; G5E9A7: DMWD; NbExp=3; IntAct=EBI-519866, EBI-10976677;
CC Q16611; P28799: GRN; NbExp=3; IntAct=EBI-519866, EBI-747754;
CC Q16611; P04792: HSPB1; NbExp=3; IntAct=EBI-519866, EBI-352682;
CC Q16611; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-519866, EBI-1055254;
CC Q16611; O60333-2: KIF1B; NbExp=3; IntAct=EBI-519866, EBI-10975473;
CC Q16611; Q07820: MCL1; NbExp=17; IntAct=EBI-519866, EBI-1003422;
CC Q16611; P49810: PSEN2; NbExp=3; IntAct=EBI-519866, EBI-2010251;
CC Q16611; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-519866, EBI-396669;
CC Q16611; Q7L3V2: RTL10; NbExp=2; IntAct=EBI-519866, EBI-10697720;
CC Q16611; P00441: SOD1; NbExp=3; IntAct=EBI-519866, EBI-990792;
CC Q16611; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-519866, EBI-5235340;
CC Q16611; Q86WV8: TSC1; NbExp=3; IntAct=EBI-519866, EBI-12806590;
CC Q16611; P97287: Mcl1; Xeno; NbExp=3; IntAct=EBI-519866, EBI-707292;
CC Q16611; Q80U63: Mfn2; Xeno; NbExp=3; IntAct=EBI-519866, EBI-8437663;
CC Q16611; P24356: VACWR040; Xeno; NbExp=6; IntAct=EBI-519866, EBI-8041400;
CC Q16611-1; Q16611-1: BAK1; NbExp=4; IntAct=EBI-26980661, EBI-26980661;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:29531808}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16611-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16611-2; Sequence=VSP_056551, VSP_056552;
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues, with
CC highest levels in the heart and skeletal muscle.
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 -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/bak1/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BAK1ID752ch6p21.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X84213; CAA58997.1; -; mRNA.
DR EMBL; U23765; AAA93066.1; -; mRNA.
DR EMBL; U16811; AAA74466.1; -; mRNA.
DR EMBL; AY260471; AAO74828.1; -; Genomic_DNA.
DR EMBL; CR457419; CAG33700.1; -; mRNA.
DR EMBL; Z93017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03740.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03742.1; -; Genomic_DNA.
DR EMBL; BC004431; AAH04431.1; -; mRNA.
DR EMBL; BC110337; AAI10338.1; -; mRNA.
DR EMBL; D88397; BAA13606.1; -; Genomic_DNA.
DR CCDS; CCDS4781.1; -. [Q16611-1]
DR PIR; S58873; S58873.
DR RefSeq; NP_001179.1; NM_001188.3. [Q16611-1]
DR RefSeq; XP_011513081.1; XM_011514779.2. [Q16611-1]
DR PDB; 1BXL; NMR; -; B=72-87.
DR PDB; 2IMS; X-ray; 1.48 A; A=16-186.
DR PDB; 2IMT; X-ray; 1.49 A; A=16-186.
DR PDB; 2JBY; X-ray; 2.41 A; B=67-92.
DR PDB; 2JCN; X-ray; 1.80 A; A=21-190.
DR PDB; 2LP8; NMR; -; B=72-87.
DR PDB; 2M5B; NMR; -; A=18-186.
DR PDB; 2XPX; X-ray; 2.05 A; B=67-92.
DR PDB; 2YV6; X-ray; 2.50 A; A=23-185.
DR PDB; 3I1H; X-ray; 2.20 A; B=72-87.
DR PDB; 3QBR; X-ray; 2.60 A; B/Y=63-96.
DR PDB; 4D2L; X-ray; 2.90 A; B=67-91.
DR PDB; 4U2U; X-ray; 2.90 A; A/B=23-186.
DR PDB; 4U2V; X-ray; 2.30 A; A/B/C/D=68-148.
DR PDB; 4UF1; X-ray; 2.30 A; B=67-92.
DR PDB; 5AJK; X-ray; 2.55 A; B/D/F/H/J/L=67-92.
DR PDB; 5FMI; X-ray; 1.49 A; A=23-184.
DR PDB; 5FMK; X-ray; 1.73 A; B=63-96.
DR PDB; 5VWV; X-ray; 1.90 A; A=23-186.
DR PDB; 5VWW; X-ray; 2.80 A; A/B=23-186.
DR PDB; 5VWX; X-ray; 2.49 A; A/C=23-186.
DR PDB; 5VWY; X-ray; 1.55 A; A=23-186.
DR PDB; 5VWZ; X-ray; 1.62 A; A/C=23-186.
DR PDB; 5VX0; X-ray; 1.60 A; A/C=23-186.
DR PDB; 5VX1; X-ray; 1.22 A; A/B=23-186.
DR PDB; 6ODH; X-ray; 2.30 A; A/B/C/D/E/F=71-147.
DR PDB; 6UXM; X-ray; 2.49 A; A/B/C/D/E/F=68-148.
DR PDB; 6UXN; X-ray; 2.49 A; A/B/C/D/E/F/G/H/I/J/K/L=68-148.
DR PDB; 6UXO; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L=68-148.
DR PDB; 6UXP; X-ray; 2.49 A; A/B/C/D/E/F/G/H=68-148.
DR PDB; 6UXQ; X-ray; 1.70 A; A/B/C/D=68-148.
DR PDB; 6UXR; X-ray; 1.80 A; A/B=68-148.
DR PDB; 7K02; X-ray; 3.40 A; A/B/C/D/E/F=67-186.
DR PDB; 7LK4; X-ray; 3.10 A; P/Q/R/S=23-186.
DR PDB; 7M5A; X-ray; 1.50 A; A=21-186.
DR PDB; 7M5B; X-ray; 1.85 A; A/C=21-186.
DR PDB; 7OFM; NMR; -; A=183-211.
DR PDB; 7OFO; NMR; -; A=183-211.
DR PDBsum; 1BXL; -.
DR PDBsum; 2IMS; -.
DR PDBsum; 2IMT; -.
DR PDBsum; 2JBY; -.
DR PDBsum; 2JCN; -.
DR PDBsum; 2LP8; -.
DR PDBsum; 2M5B; -.
DR PDBsum; 2XPX; -.
DR PDBsum; 2YV6; -.
DR PDBsum; 3I1H; -.
DR PDBsum; 3QBR; -.
DR PDBsum; 4D2L; -.
DR PDBsum; 4U2U; -.
DR PDBsum; 4U2V; -.
DR PDBsum; 4UF1; -.
DR PDBsum; 5AJK; -.
DR PDBsum; 5FMI; -.
DR PDBsum; 5FMK; -.
DR PDBsum; 5VWV; -.
DR PDBsum; 5VWW; -.
DR PDBsum; 5VWX; -.
DR PDBsum; 5VWY; -.
DR PDBsum; 5VWZ; -.
DR PDBsum; 5VX0; -.
DR PDBsum; 5VX1; -.
DR PDBsum; 6ODH; -.
DR PDBsum; 6UXM; -.
DR PDBsum; 6UXN; -.
DR PDBsum; 6UXO; -.
DR PDBsum; 6UXP; -.
DR PDBsum; 6UXQ; -.
DR PDBsum; 6UXR; -.
DR PDBsum; 7K02; -.
DR PDBsum; 7LK4; -.
DR PDBsum; 7M5A; -.
DR PDBsum; 7M5B; -.
DR PDBsum; 7OFM; -.
DR PDBsum; 7OFO; -.
DR AlphaFoldDB; Q16611; -.
DR BMRB; Q16611; -.
DR SMR; Q16611; -.
DR BioGRID; 107054; 37.
DR ComplexPortal; CPX-1989; BAK1 oligomer.
DR ComplexPortal; CPX-860; BAK1-Bcl-X complex.
DR CORUM; Q16611; -.
DR DIP; DIP-935N; -.
DR ELM; Q16611; -.
DR IntAct; Q16611; 39.
DR MINT; Q16611; -.
DR STRING; 9606.ENSP00000363591; -.
DR BindingDB; Q16611; -.
DR ChEMBL; CHEMBL5609; -.
DR TCDB; 1.A.21.1.3; the bcl-2 (bcl-2) family.
DR iPTMnet; Q16611; -.
DR PhosphoSitePlus; Q16611; -.
DR BioMuta; BAK1; -.
DR DMDM; 2493274; -.
DR EPD; Q16611; -.
DR jPOST; Q16611; -.
DR MassIVE; Q16611; -.
DR MaxQB; Q16611; -.
DR PaxDb; Q16611; -.
DR PeptideAtlas; Q16611; -.
DR PRIDE; Q16611; -.
DR ProteomicsDB; 60948; -. [Q16611-1]
DR ProteomicsDB; 7574; -.
DR TopDownProteomics; Q16611-1; -. [Q16611-1]
DR Antibodypedia; 3556; 762 antibodies from 46 providers.
DR DNASU; 578; -.
DR Ensembl; ENST00000374467.4; ENSP00000363591.3; ENSG00000030110.14. [Q16611-1]
DR Ensembl; ENST00000442998.6; ENSP00000391258.2; ENSG00000030110.14. [Q16611-2]
DR GeneID; 578; -.
DR KEGG; hsa:578; -.
DR MANE-Select; ENST00000374467.4; ENSP00000363591.3; NM_001188.4; NP_001179.1.
DR UCSC; uc003oes.4; human. [Q16611-1]
DR CTD; 578; -.
DR DisGeNET; 578; -.
DR GeneCards; BAK1; -.
DR HGNC; HGNC:949; BAK1.
DR HPA; ENSG00000030110; Low tissue specificity.
DR MIM; 600516; gene.
DR neXtProt; NX_Q16611; -.
DR OpenTargets; ENSG00000030110; -.
DR PharmGKB; PA25253; -.
DR VEuPathDB; HostDB:ENSG00000030110; -.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT01050000244872; -.
DR HOGENOM; CLU_145501_0_0_1; -.
DR InParanoid; Q16611; -.
DR OMA; NGGWVAA; -.
DR PhylomeDB; Q16611; -.
DR TreeFam; TF315834; -.
DR PathwayCommons; Q16611; -.
DR Reactome; R-HSA-111452; Activation and oligomerization of BAK protein.
DR Reactome; R-HSA-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-HSA-5620971; Pyroptosis.
DR SignaLink; Q16611; -.
DR SIGNOR; Q16611; -.
DR BioGRID-ORCS; 578; 160 hits in 1049 CRISPR screens.
DR EvolutionaryTrace; Q16611; -.
DR GeneWiki; Bcl-2_homologous_antagonist_killer; -.
DR GenomeRNAi; 578; -.
DR Pharos; Q16611; Tbio.
DR PRO; PR:Q16611; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q16611; protein.
DR Bgee; ENSG00000030110; Expressed in mucosa of transverse colon and 121 other tissues.
DR ExpressionAtlas; Q16611; baseline and differential.
DR Genevisible; Q16611; HS.
DR GO; GO:0097145; C:BAK complex; IDA:UniProtKB.
DR GO; GO:0097136; C:Bcl-2 family protein complex; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:BHF-UCL.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HGNC-UCL.
DR GO; GO:0046930; C:pore complex; IDA:HGNC-UCL.
DR GO; GO:0051400; F:BH domain binding; IEA:Ensembl.
DR GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
DR GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IDA:BHF-UCL.
DR GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0097190; P:apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0001783; P:B cell apoptotic process; IEA:Ensembl.
DR GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
DR GO; GO:0002352; P:B cell negative selection; IEA:Ensembl.
DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0060402; P:calcium ion transport into cytosol; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0034620; P:cellular response to unfolded protein; TAS:ParkinsonsUK-UCL.
DR GO; GO:0034644; P:cellular response to UV; IMP:UniProtKB.
DR GO; GO:0031018; P:endocrine pancreas development; IEA:Ensembl.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; TAS:UniProtKB.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; IDA:HGNC-UCL.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR GO; GO:0044346; P:fibroblast apoptotic process; IEA:Ensembl.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; TAS:ParkinsonsUK-UCL.
DR GO; GO:0035108; P:limb morphogenesis; IEA:Ensembl.
DR GO; GO:0008053; P:mitochondrial fusion; IEA:Ensembl.
DR GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IDA:ComplexPortal.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IDA:ComplexPortal.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IEA:Ensembl.
DR GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; IMP:UniProtKB.
DR GO; GO:1903896; P:positive regulation of IRE1-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IC:ComplexPortal.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:HGNC-UCL.
DR GO; GO:0045862; P:positive regulation of proteolysis; IDA:BHF-UCL.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IC:ComplexPortal.
DR GO; GO:0048597; P:post-embryonic camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IDA:BHF-UCL.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IDA:HGNC-UCL.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:BHF-UCL.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0009620; P:response to fungus; IEA:Ensembl.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0010046; P:response to mycotoxin; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0010225; P:response to UV-C; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0070242; P:thymocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0060068; P:vagina development; IEA:Ensembl.
DR CDD; cd06845; Bcl-2_like; 1.
DR DisProt; DP02539; -.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR026308; BAK.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR046371; Bcl-2_BH1-3.
DR InterPro; IPR026298; Bcl-2_fam.
DR InterPro; IPR002475; Bcl2-like.
DR InterPro; IPR020717; Bcl2_BH1_motif_CS.
DR InterPro; IPR020726; Bcl2_BH2_motif_CS.
DR InterPro; IPR020728; Bcl2_BH3_motif_CS.
DR PANTHER; PTHR11256; PTHR11256; 1.
DR PANTHER; PTHR11256:SF41; PTHR11256:SF41; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR PRINTS; PR01862; BCL2FAMILY.
DR SMART; SM00337; BCL; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
DR PROSITE; PS01080; BH1; 1.
DR PROSITE; PS01258; BH2; 1.
DR PROSITE; PS01259; BH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis;
KW Host-virus interaction; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..211
FT /note="Bcl-2 homologous antagonist/killer"
FT /id="PRO_0000143059"
FT TRANSMEM 188..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 74..88
FT /note="BH3"
FT MOTIF 117..136
FT /note="BH1"
FT MOTIF 169..184
FT /note="BH2"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT VAR_SEQ 117..153
FT /note="SLFESGINWGRVVALLGFGYRLALHVYQHGLTGFLGQ -> RPAATPTACLR
FT VASIGAVWWLFWASATVWPYTSTSMA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056551"
FT VAR_SEQ 154..211
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056552"
FT VARIANT 28
FT /note="A -> V (in dbSNP:rs4987115)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_018829"
FT VARIANT 42
FT /note="R -> H (in dbSNP:rs1051911)"
FT /id="VAR_048417"
FT VARIANT 69
FT /note="S -> R (in dbSNP:rs5745592)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_018830"
FT MUTAGEN 164
FT /note="H->A: Strongly reduced zinc binding and
FT homodimerization."
FT /evidence="ECO:0000269|PubMed:17157251"
FT HELIX 24..47
FT /evidence="ECO:0007829|PDB:5VX1"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:5VX1"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:5VX1"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:5VX1"
FT HELIX 84..100
FT /evidence="ECO:0007829|PDB:5VX1"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:5VX1"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:5VX1"
FT HELIX 125..145
FT /evidence="ECO:0007829|PDB:5VX1"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:5VX1"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:5VX1"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:5VX1"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:5VX1"
FT HELIX 188..209
FT /evidence="ECO:0007829|PDB:7OFM"
SQ SEQUENCE 211 AA; 23409 MW; A2200FE72A46D04E CRC64;
MASGQGPGPP RQECGEPALP SASEEQVAQD TEEVFRSYVF YRHQQEQEAE GVAAPADPEM
VTLPLQPSST MGQVGRQLAI IGDDINRRYD SEFQTMLQHL QPTAENAYEY FTKIATSLFE
SGINWGRVVA LLGFGYRLAL HVYQHGLTGF LGQVTRFVVD FMLHHCIARW IAQRGGWVAA
LNLGNGPILN VLVVLGVVLL GQFVVRRFFK S
