BIK_HUMAN
ID BIK_HUMAN Reviewed; 160 AA.
AC Q13323; Q16582; Q6FH93;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Bcl-2-interacting killer;
DE AltName: Full=Apoptosis inducer NBK;
DE AltName: Full=BIP1;
DE AltName: Full=BP4;
GN Name=BIK; Synonyms=NBK;
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].
RC TISSUE=B-cell;
RX PubMed=7478623;
RA Boyd J.M., Gallo G.J., Elangovan B., Houghton A.B., Malstrom S.,
RA Avery B.J., Ebb R.G., Subramanian T., Chittenden T., Lutz R.J.,
RA Chinnadurai G.;
RT "Bik, a novel death-inducing protein shares a distinct sequence motif with
RT Bcl-2 family proteins and interacts with viral and cellular survival-
RT promoting proteins.";
RL Oncogene 11:1921-1928(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8816500; DOI=10.1128/mcb.16.10.5857;
RA Han J., Sabbatini P., White E.;
RT "Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that
RT interacts with E1B 19K.";
RL Mol. Cell. Biol. 16:5857-5864(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoid tissue;
RA Pun K.-T., Farrow S.N., Raven T., Wride C.J., White J.H.M., Brown R.;
RT "E1B-19K interacts with a novel apoptotic inducer, NBK.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10500065; DOI=10.1016/s0016-5085(99)70341-0;
RA Castells A., Ino Y., Louis D.N., Ramesh V., Gusella J.F., Rustgi A.K.;
RT "Mapping of a target region of allelic loss to a 0.5-cM interval on
RT chromosome 22q13 in human colorectal cancer.";
RL Gastroenterology 117:831-837(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-19.
RG NIEHS SNPs program;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [10]
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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [12]
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 [13]
RP CLEAVAGE BY RHBDD1, INTERACTION WITH RHBDD1, AND MUTAGENESIS OF
RP 153-GLY-PHE-154.
RX PubMed=18953687; DOI=10.1007/s00018-008-8452-0;
RA Wang Y., Guan X., Fok K.L., Li S., Zhang X., Miao S., Zong S., Koide S.S.,
RA Chan H.C., Wang L.;
RT "A novel member of the Rhomboid family, RHBDD1, regulates BIK-mediated
RT apoptosis.";
RL Cell. Mol. Life Sci. 65:3822-3829(2008).
RN [14]
RP INTERACTION WITH BCL2L10.
RX PubMed=23235460; DOI=10.1038/cddis.2012.178;
RA Rautureau G.J., Yabal M., Yang H., Huang D.C., Kvansakul M., Hinds M.G.;
RT "The restricted binding repertoire of Bcl-B leaves Bim as the universal
RT BH3-only prosurvival Bcl-2 protein antagonist.";
RL Cell Death Dis. 3:e443-e443(2012).
RN [15]
RP INTERACTION WITH BCL2L10.
RX PubMed=23563182; DOI=10.1038/onc.2013.99;
RA van de Kooij B., Rooswinkel R.W., Kok F., Herrebout M., de Vries E.,
RA Paauwe M., Janssen G.M., van Veelen P.A., Borst J.;
RT "Polyubiquitination and proteasomal turnover controls the anti-apoptotic
RT activity of Bcl-B.";
RL Oncogene 32:5439-5448(2013).
CC -!- FUNCTION: Accelerates programmed cell death. Association to the
CC apoptosis repressors Bcl-X(L), BHRF1, Bcl-2 or its adenovirus homolog
CC E1B 19k protein suppresses this death-promoting activity. Does not
CC interact with BAX. {ECO:0000269|PubMed:8521816}.
CC -!- SUBUNIT: Interacts with RHBDL4/RHBDD1 (PubMed:18953687). Interacts with
CC BCL2L10/BCL-B (PubMed:23235460, PubMed:23563182).
CC {ECO:0000269|PubMed:18953687, ECO:0000269|PubMed:23235460,
CC ECO:0000269|PubMed:23563182}.
CC -!- INTERACTION:
CC Q13323; Q9UHX3: ADGRE2; NbExp=3; IntAct=EBI-700794, EBI-11277970;
CC Q13323; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-700794, EBI-10827839;
CC Q13323; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-700794, EBI-11957045;
CC Q13323; Q9BVK2: ALG8; NbExp=3; IntAct=EBI-700794, EBI-3921603;
CC Q13323; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-700794, EBI-12109402;
CC Q13323; P05090: APOD; NbExp=3; IntAct=EBI-700794, EBI-715495;
CC Q13323; P10415: BCL2; NbExp=6; IntAct=EBI-700794, EBI-77694;
CC Q13323; Q16548: BCL2A1; NbExp=10; IntAct=EBI-700794, EBI-1003550;
CC Q13323; A0A0S2Z3D2: BCL2L1; NbExp=3; IntAct=EBI-700794, EBI-16431449;
CC Q13323; Q07817: BCL2L1; NbExp=12; IntAct=EBI-700794, EBI-78035;
CC Q13323; Q07817-1: BCL2L1; NbExp=4; IntAct=EBI-700794, EBI-287195;
CC Q13323; Q9HD36: BCL2L10; NbExp=8; IntAct=EBI-700794, EBI-2126349;
CC Q13323; Q92843: BCL2L2; NbExp=22; IntAct=EBI-700794, EBI-707714;
CC Q13323; O95393: BMP10; NbExp=3; IntAct=EBI-700794, EBI-3922513;
CC Q13323; Q12983: BNIP3; NbExp=3; IntAct=EBI-700794, EBI-749464;
CC Q13323; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-700794, EBI-12244618;
CC Q13323; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-700794, EBI-8648738;
CC Q13323; O14523: C2CD2L; NbExp=3; IntAct=EBI-700794, EBI-12822627;
CC Q13323; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-700794, EBI-12003442;
CC Q13323; Q06432: CACNG1; NbExp=3; IntAct=EBI-700794, EBI-9686780;
CC Q13323; P19397: CD53; NbExp=3; IntAct=EBI-700794, EBI-6657396;
CC Q13323; P21854: CD72; NbExp=3; IntAct=EBI-700794, EBI-307924;
CC Q13323; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-700794, EBI-12256978;
CC Q13323; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-700794, EBI-11522780;
CC Q13323; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-700794, EBI-2807956;
CC Q13323; O95406: CNIH1; NbExp=3; IntAct=EBI-700794, EBI-12172273;
CC Q13323; Q8TBE1: CNIH3; NbExp=3; IntAct=EBI-700794, EBI-12208021;
CC Q13323; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-700794, EBI-12019274;
CC Q13323; P49447: CYB561; NbExp=3; IntAct=EBI-700794, EBI-8646596;
CC Q13323; O43169: CYB5B; NbExp=3; IntAct=EBI-700794, EBI-1058710;
CC Q13323; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-700794, EBI-18535450;
CC Q13323; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-700794, EBI-781551;
CC Q13323; Q2M3D2: EXOC3L2; NbExp=3; IntAct=EBI-700794, EBI-14890134;
CC Q13323; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-700794, EBI-18304435;
CC Q13323; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-700794, EBI-12118888;
CC Q13323; Q92520: FAM3C; NbExp=3; IntAct=EBI-700794, EBI-2876774;
CC Q13323; Q969F0: FATE1; NbExp=8; IntAct=EBI-700794, EBI-743099;
CC Q13323; P12314: FCGR1A; NbExp=3; IntAct=EBI-700794, EBI-2869867;
CC Q13323; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-700794, EBI-11991950;
CC Q13323; Q8TED1: GPX8; NbExp=3; IntAct=EBI-700794, EBI-11721746;
CC Q13323; Q14416: GRM2; NbExp=3; IntAct=EBI-700794, EBI-10232876;
CC Q13323; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-700794, EBI-8503746;
CC Q13323; O15554: KCNN4; NbExp=3; IntAct=EBI-700794, EBI-2924473;
CC Q13323; Q9NX47: MARCHF5; NbExp=3; IntAct=EBI-700794, EBI-2341610;
CC Q13323; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-700794, EBI-12070086;
CC Q13323; Q9UHE5: NAT8; NbExp=3; IntAct=EBI-700794, EBI-2863634;
CC Q13323; Q8N912: NRAC; NbExp=3; IntAct=EBI-700794, EBI-12051377;
CC Q13323; Q8IXM6: NRM; NbExp=3; IntAct=EBI-700794, EBI-10262547;
CC Q13323; Q96AL5: PBX3; NbExp=3; IntAct=EBI-700794, EBI-741171;
CC Q13323; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-700794, EBI-12092917;
CC Q13323; O00264: PGRMC1; NbExp=3; IntAct=EBI-700794, EBI-1045534;
CC Q13323; P26678: PLN; NbExp=3; IntAct=EBI-700794, EBI-692836;
CC Q13323; P60201-2: PLP1; NbExp=3; IntAct=EBI-700794, EBI-12188331;
CC Q13323; Q04941: PLP2; NbExp=3; IntAct=EBI-700794, EBI-608347;
CC Q13323; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-700794, EBI-10485931;
CC Q13323; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-700794, EBI-7545592;
CC Q13323; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-700794, EBI-8636004;
CC Q13323; Q969E2: SCAMP4; NbExp=3; IntAct=EBI-700794, EBI-4403649;
CC Q13323; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-700794, EBI-8652744;
CC Q13323; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-700794, EBI-9679163;
CC Q13323; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-700794, EBI-10329948;
CC Q13323; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-700794, EBI-749270;
CC Q13323; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-700794, EBI-10262251;
CC Q13323; Q96G79: SLC35A4; NbExp=3; IntAct=EBI-700794, EBI-12363689;
CC Q13323; Q7Z769: SLC35E3; NbExp=3; IntAct=EBI-700794, EBI-13389236;
CC Q13323; O43826: SLC37A4; NbExp=3; IntAct=EBI-700794, EBI-6269684;
CC Q13323; Q92504: SLC39A7; NbExp=3; IntAct=EBI-700794, EBI-1051105;
CC Q13323; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-700794, EBI-12188413;
CC Q13323; P0DN84: STRIT1; NbExp=3; IntAct=EBI-700794, EBI-12200293;
CC Q13323; Q9UNK0: STX8; NbExp=3; IntAct=EBI-700794, EBI-727240;
CC Q13323; Q969X1: TMBIM1; NbExp=3; IntAct=EBI-700794, EBI-2820569;
CC Q13323; Q6UX40: TMEM107; NbExp=3; IntAct=EBI-700794, EBI-12845616;
CC Q13323; P17152: TMEM11; NbExp=3; IntAct=EBI-700794, EBI-723946;
CC Q13323; Q9BXJ8: TMEM120A; NbExp=3; IntAct=EBI-700794, EBI-727322;
CC Q13323; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-700794, EBI-8638294;
CC Q13323; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-700794, EBI-2339195;
CC Q13323; Q8N511: TMEM199; NbExp=3; IntAct=EBI-700794, EBI-10265825;
CC Q13323; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-700794, EBI-347385;
CC Q13323; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-700794, EBI-12195227;
CC Q13323; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-700794, EBI-12887458;
CC Q13323; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-700794, EBI-11956809;
CC Q13323; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-700794, EBI-2852148;
CC Q13323; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-700794, EBI-11742770;
CC Q13323; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-700794, EBI-2548832;
CC Q13323; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-700794, EBI-12111910;
CC Q13323; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-700794, EBI-12195249;
CC Q13323; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-700794, EBI-10243654;
CC Q13323; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-700794, EBI-11988865;
CC Q13323; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-700794, EBI-2819725;
CC Q13323; Q15836: VAMP3; NbExp=3; IntAct=EBI-700794, EBI-722343;
CC Q13323; O95183: VAMP5; NbExp=3; IntAct=EBI-700794, EBI-10191195;
CC Q13323; Q9BQB6: VKORC1; NbExp=3; IntAct=EBI-700794, EBI-6256462;
CC Q13323; O95159: ZFPL1; NbExp=3; IntAct=EBI-700794, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Single-pass membrane
CC protein. Mitochondrion membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Note=Around the nuclear envelope, and in
CC cytoplasmic membranes.
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: Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced
CC cleavage is a necessary step prior its degradation by the proteosome-
CC dependent mechanism. {ECO:0000269|PubMed:18953687}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/bik/";
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DR EMBL; U34584; AAC50413.1; -; mRNA.
DR EMBL; U49730; AAC79124.1; -; mRNA.
DR EMBL; X89986; CAA62013.1; -; mRNA.
DR EMBL; AF174424; AAF01156.1; -; Genomic_DNA.
DR EMBL; AF174421; AAF01156.1; JOINED; Genomic_DNA.
DR EMBL; AF174422; AAF01156.1; JOINED; Genomic_DNA.
DR EMBL; AF174423; AAF01156.1; JOINED; Genomic_DNA.
DR EMBL; CR456390; CAG30276.1; -; mRNA.
DR EMBL; BT006728; AAP35374.1; -; mRNA.
DR EMBL; AY245248; AAO61089.1; -; Genomic_DNA.
DR EMBL; CR541863; CAG46661.1; -; mRNA.
DR EMBL; CR541883; CAG46681.1; -; mRNA.
DR EMBL; AL022237; CAA18260.2; -; Genomic_DNA.
DR EMBL; CH471138; EAW73282.1; -; Genomic_DNA.
DR EMBL; BC001599; AAH01599.1; -; mRNA.
DR CCDS; CCDS14044.1; -.
DR PIR; S58214; S58214.
DR RefSeq; NP_001188.1; NM_001197.4.
DR AlphaFoldDB; Q13323; -.
DR BioGRID; 107107; 99.
DR ComplexPortal; CPX-309; BIK:BCL-w complex.
DR DIP; DIP-928N; -.
DR ELM; Q13323; -.
DR IntAct; Q13323; 103.
DR MINT; Q13323; -.
DR STRING; 9606.ENSP00000216115; -.
DR iPTMnet; Q13323; -.
DR PhosphoSitePlus; Q13323; -.
DR BioMuta; BIK; -.
DR DMDM; 2493284; -.
DR MassIVE; Q13323; -.
DR PaxDb; Q13323; -.
DR PeptideAtlas; Q13323; -.
DR PRIDE; Q13323; -.
DR ProteomicsDB; 59311; -.
DR Antibodypedia; 13376; 559 antibodies from 37 providers.
DR DNASU; 638; -.
DR Ensembl; ENST00000216115.3; ENSP00000216115.2; ENSG00000100290.3.
DR GeneID; 638; -.
DR KEGG; hsa:638; -.
DR MANE-Select; ENST00000216115.3; ENSP00000216115.2; NM_001197.5; NP_001188.1.
DR UCSC; uc003bdk.3; human.
DR CTD; 638; -.
DR DisGeNET; 638; -.
DR GeneCards; BIK; -.
DR HGNC; HGNC:1051; BIK.
DR HPA; ENSG00000100290; Tissue enhanced (salivary).
DR MIM; 603392; gene.
DR neXtProt; NX_Q13323; -.
DR OpenTargets; ENSG00000100290; -.
DR PharmGKB; PA25354; -.
DR VEuPathDB; HostDB:ENSG00000100290; -.
DR eggNOG; ENOG502TF5K; Eukaryota.
DR GeneTree; ENSGT00530000064453; -.
DR HOGENOM; CLU_139842_0_0_1; -.
DR InParanoid; Q13323; -.
DR OMA; LECMEGS; -.
DR OrthoDB; 1487465at2759; -.
DR PhylomeDB; Q13323; -.
DR TreeFam; TF338339; -.
DR PathwayCommons; Q13323; -.
DR SignaLink; Q13323; -.
DR SIGNOR; Q13323; -.
DR BioGRID-ORCS; 638; 12 hits in 1066 CRISPR screens.
DR ChiTaRS; BIK; human.
DR GeneWiki; Bcl-2-interacting_killer; -.
DR GenomeRNAi; 638; -.
DR Pharos; Q13323; Tbio.
DR PRO; PR:Q13323; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q13323; protein.
DR Bgee; ENSG00000100290; Expressed in nasal cavity epithelium and 128 other tissues.
DR ExpressionAtlas; Q13323; baseline and differential.
DR Genevisible; Q13323; HS.
DR GO; GO:0097136; C:Bcl-2 family protein complex; IPI:ComplexPortal.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:BHF-UCL.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IDA:BHF-UCL.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:ComplexPortal.
DR InterPro; IPR024579; Bcl2-int_killer.
DR InterPro; IPR020728; Bcl2_BH3_motif_CS.
DR PANTHER; PTHR15018; PTHR15018; 1.
DR Pfam; PF12201; bcl-2I13; 1.
DR PROSITE; PS01259; BH3; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Membrane; Mitochondrion; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..160
FT /note="Bcl-2-interacting killer"
FT /id="PRO_0000143100"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 137..158
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255"
FT MOTIF 57..71
FT /note="BH3"
FT SITE 153..154
FT /note="Cleavage; by RHBDL4/RHBDD1"
FT /evidence="ECO:0000305"
FT VARIANT 19
FT /note="E -> K (in dbSNP:rs4988415)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_029179"
FT VARIANT 26
FT /note="T -> I (in dbSNP:rs11090143)"
FT /id="VAR_048420"
FT VARIANT 148
FT /note="L -> P (in dbSNP:rs11574527)"
FT /id="VAR_029180"
FT MUTAGEN 153..154
FT /note="GG->FF: Inhibits RHBDL4/RHBDD1-induced cleavage."
FT /evidence="ECO:0000269|PubMed:18953687"
SQ SEQUENCE 160 AA; 18016 MW; 89034F4443F5A136 CRC64;
MSEVRPLSRD ILMETLLYEQ LLEPPTMEVL GMTDSEEDLD PMEDFDSLEC MEGSDALALR
LACIGDEMDV SLRAPRLAQL SEVAMHSLGL AFIYDQTEDI RDVLRSFMDG FTTLKENIMR
FWRSPNPGSW VSCEQVLLAL LLLLALLLPL LSGGLHLLLK
