BI1_HUMAN
ID BI1_HUMAN Reviewed; 237 AA.
AC P55061; B2R5M4; F8W034; O14938; Q643A7; Q96J50;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Bax inhibitor 1;
DE Short=BI-1;
DE AltName: Full=Testis-enhanced gene transcript protein;
DE AltName: Full=Transmembrane BAX inhibitor motif-containing protein 6;
GN Name=TMBIM6; Synonyms=BI1, TEGT;
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 TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=8530040; DOI=10.1006/geno.1995.1145;
RA Walter L., Marynen P., Szpirer J., Levan G., Guenther E.;
RT "Identification of a novel conserved human gene, TEGT.";
RL Genomics 28:301-304(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Cowling R.T., Birnboim H.C.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Kim J.-H., Jeong M.-Y., Cho S.-G.;
RT "Eukaryotic homologs of BAX inhibitor-1 (BI-1) suppresses BAX- and hydrogen
RT peroxide-induced cell death in endothelial cell lines.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta, and Testis;
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 [8]
RP CHARACTERIZATION, AND INTERACTION WITH BCL2 AND BCL2L1.
RX PubMed=9660918; DOI=10.1016/s1097-2765(00)80034-9;
RA Xu Q., Reed J.C.;
RT "Bax inhibitor-1, a mammalian apoptosis suppressor identified by functional
RT screening in yeast.";
RL Mol. Biol. Cell 1:337-346(1998).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21075086; DOI=10.1016/j.brainres.2010.11.015;
RA Krajewska M., Xu L., Xu W., Krajewski S., Kress C.L., Cui J., Yang L.,
RA Irie F., Yamaguchi Y., Lipton S.A., Reed J.C.;
RT "Endoplasmic reticulum protein BI-1 modulates unfolded protein response
RT signaling and protects against stroke and traumatic brain injury.";
RL Brain Res. 1370:227-237(2011).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, CALCIUM PORE DOMAIN, AND
RP MUTAGENESIS OF ASP-209 AND ASP-213.
RX PubMed=22128171; DOI=10.1074/jbc.m111.275354;
RA Bultynck G., Kiviluoto S., Henke N., Ivanova H., Schneider L.,
RA Rybalchenko V., Luyten T., Nuyts K., De Borggraeve W., Bezprozvanny I.,
RA Parys J.B., De Smedt H., Missiaen L., Methner A.;
RT "The C terminus of Bax inhibitor-1 forms a Ca2+-permeable channel pore.";
RL J. Biol. Chem. 287:2544-2557(2012).
RN [11]
RP TOPOLOGY.
RX PubMed=22418439; DOI=10.1074/jbc.m111.336149;
RA Carrara G., Saraiva N., Gubser C., Johnson B.F., Smith G.L.;
RT "Six-transmembrane topology for Golgi anti-apoptotic protein (GAAP) and Bax
RT inhibitor 1 (BI-1) provides model for the transmembrane Bax inhibitor-
RT containing motif (TMBIM) family.";
RL J. Biol. Chem. 287:15896-15905(2012).
CC -!- FUNCTION: Suppressor of apoptosis (PubMed:21075086). Modulates unfolded
CC protein response signaling (PubMed:21075086). Modulates ER calcium
CC homeostasis by acting as a calcium-leak channel (PubMed:22128171).
CC Negatively regulates autophagy and autophagosome formation, especially
CC during periods of nutrient deprivation, and reduces cell survival
CC during starvation (By similarity). {ECO:0000250|UniProtKB:Q9D2C7,
CC ECO:0000269|PubMed:21075086, ECO:0000269|PubMed:22128171}.
CC -!- SUBUNIT: Interacts with BCL2 and BCL2L1. {ECO:0000269|PubMed:9660918}.
CC -!- INTERACTION:
CC P55061; Q86V24: ADIPOR2; NbExp=3; IntAct=EBI-1045825, EBI-1769445;
CC P55061; Q9HD20-3: ATP13A1; NbExp=3; IntAct=EBI-1045825, EBI-12069500;
CC P55061; Q6UXG3: CD300LG; NbExp=3; IntAct=EBI-1045825, EBI-10254587;
CC P55061; P11912: CD79A; NbExp=3; IntAct=EBI-1045825, EBI-7797864;
CC P55061; Q8TCZ2: CD99L2; NbExp=3; IntAct=EBI-1045825, EBI-2824782;
CC P55061; O00311: CDC7; NbExp=3; IntAct=EBI-1045825, EBI-374980;
CC P55061; Q8N7P3: CLDN22; NbExp=3; IntAct=EBI-1045825, EBI-17766761;
CC P55061; A0A7P0TAB9: COBLL1; NbExp=3; IntAct=EBI-1045825, EBI-23326314;
CC P55061; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-1045825, EBI-6942903;
CC P55061; Q15125: EBP; NbExp=3; IntAct=EBI-1045825, EBI-3915253;
CC P55061; Q9Y6X5: ENPP4; NbExp=3; IntAct=EBI-1045825, EBI-17442870;
CC P55061; P30040: ERP29; NbExp=3; IntAct=EBI-1045825, EBI-946830;
CC P55061; Q96AP7: ESAM; NbExp=3; IntAct=EBI-1045825, EBI-4314670;
CC P55061; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-1045825, EBI-18304435;
CC P55061; Q9BYJ0: FGFBP2; NbExp=3; IntAct=EBI-1045825, EBI-12911356;
CC P55061; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-1045825, EBI-12175685;
CC P55061; P36382: GJA5; NbExp=3; IntAct=EBI-1045825, EBI-750433;
CC P55061; P48165: GJA8; NbExp=3; IntAct=EBI-1045825, EBI-17458373;
CC P55061; Q9NTQ9: GJB4; NbExp=3; IntAct=EBI-1045825, EBI-12831526;
CC P55061; Q86YW7: GPHB5; NbExp=3; IntAct=EBI-1045825, EBI-11659720;
CC P55061; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-1045825, EBI-11955647;
CC P55061; O15529: GPR42; NbExp=3; IntAct=EBI-1045825, EBI-18076404;
CC P55061; Q8TED1: GPX8; NbExp=3; IntAct=EBI-1045825, EBI-11721746;
CC P55061; P02724: GYPA; NbExp=3; IntAct=EBI-1045825, EBI-702665;
CC P55061; P49863: GZMK; NbExp=3; IntAct=EBI-1045825, EBI-3910072;
CC P55061; Q9BSE4: HERPUD2; NbExp=5; IntAct=EBI-1045825, EBI-2868124;
CC P55061; Q6ZVN8-3: HJV; NbExp=3; IntAct=EBI-1045825, EBI-12827977;
CC P55061; P28335: HTR2C; NbExp=3; IntAct=EBI-1045825, EBI-994141;
CC P55061; P46695: IER3; NbExp=3; IntAct=EBI-1045825, EBI-1748945;
CC P55061; Q96MG2: JSRP1; NbExp=3; IntAct=EBI-1045825, EBI-11305455;
CC P55061; Q16322: KCNA10; NbExp=3; IntAct=EBI-1045825, EBI-12265328;
CC P55061; P48547: KCNC1; NbExp=3; IntAct=EBI-1045825, EBI-12830942;
CC P55061; Q9H400: LIME1; NbExp=3; IntAct=EBI-1045825, EBI-2830566;
CC P55061; Q96AG4: LRRC59; NbExp=3; IntAct=EBI-1045825, EBI-358888;
CC P55061; Q9NQG1: MANBAL; NbExp=3; IntAct=EBI-1045825, EBI-3867271;
CC P55061; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-1045825, EBI-373355;
CC P55061; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-1045825, EBI-6163737;
CC P55061; Q96HJ5: MS4A3; NbExp=3; IntAct=EBI-1045825, EBI-12806656;
CC P55061; Q2M2E3: ODF4; NbExp=6; IntAct=EBI-1045825, EBI-12382569;
CC P55061; P35372-10: OPRM1; NbExp=3; IntAct=EBI-1045825, EBI-12807478;
CC P55061; Q6UXB8: PI16; NbExp=3; IntAct=EBI-1045825, EBI-12810028;
CC P55061; Q8IYJ0: PIANP; NbExp=3; IntAct=EBI-1045825, EBI-12204277;
CC P55061; P49768: PSEN1; NbExp=12; IntAct=EBI-1045825, EBI-297277;
CC P55061; P15151: PVR; NbExp=3; IntAct=EBI-1045825, EBI-3919694;
CC P55061; Q9BRK0: REEP2; NbExp=3; IntAct=EBI-1045825, EBI-11337973;
CC P55061; Q9NX52-3: RHBDL2; NbExp=3; IntAct=EBI-1045825, EBI-12908426;
CC P55061; Q96GF1: RNF185; NbExp=4; IntAct=EBI-1045825, EBI-2340249;
CC P55061; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-1045825, EBI-17247926;
CC P55061; Q9Y3P8: SIT1; NbExp=3; IntAct=EBI-1045825, EBI-6977215;
CC P55061; Q96DU3: SLAMF6; NbExp=3; IntAct=EBI-1045825, EBI-14058448;
CC P55061; Q9Y666-2: SLC12A7; NbExp=3; IntAct=EBI-1045825, EBI-12854384;
CC P55061; Q96GZ6: SLC41A3; NbExp=3; IntAct=EBI-1045825, EBI-7225508;
CC P55061; P30825: SLC7A1; NbExp=3; IntAct=EBI-1045825, EBI-4289564;
CC P55061; O75908: SOAT2; NbExp=3; IntAct=EBI-1045825, EBI-9055438;
CC P55061; Q6NZ63: STEAP1B; NbExp=3; IntAct=EBI-1045825, EBI-12952093;
CC P55061; Q86SS6: SYT9; NbExp=3; IntAct=EBI-1045825, EBI-19129467;
CC P55061; Q8N6K0: TEX29; NbExp=3; IntAct=EBI-1045825, EBI-19027521;
CC P55061; Q9BVT8: TMUB1; NbExp=3; IntAct=EBI-1045825, EBI-11425701;
CC P55061; Q9Y320: TMX2; NbExp=3; IntAct=EBI-1045825, EBI-6447886;
CC P55061; Q02223: TNFRSF17; NbExp=3; IntAct=EBI-1045825, EBI-519945;
CC P55061; Q86YW5: TREML1; NbExp=3; IntAct=EBI-1045825, EBI-17245072;
CC P55061; O75310: UGT2B11; NbExp=3; IntAct=EBI-1045825, EBI-12891746;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21075086, ECO:0000269|PubMed:22128171}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:21075086,
CC ECO:0000269|PubMed:22128171}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P55061-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55061-2; Sequence=VSP_055119;
CC -!- TISSUE SPECIFICITY: Highly abundant in testis.
CC {ECO:0000269|PubMed:8530040}.
CC -!- DOMAIN: The intra-membrane loop at the C-terminus acts as a calcium
CC pore, mediating calcium leak from the ER into the cytosol.
CC {ECO:0000269|PubMed:22128171}.
CC -!- SIMILARITY: Belongs to the BI1 family. {ECO:0000305}.
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DR EMBL; X75861; CAA53472.1; -; mRNA.
DR EMBL; AF033095; AAB87479.1; -; mRNA.
DR EMBL; AY736129; AAU29521.1; -; mRNA.
DR EMBL; AK312238; BAG35171.1; -; mRNA.
DR EMBL; AC020612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW58089.1; -; Genomic_DNA.
DR EMBL; BC000916; AAH00916.1; -; mRNA.
DR EMBL; BC036203; AAH36203.2; -; mRNA.
DR CCDS; CCDS31797.1; -. [P55061-1]
DR CCDS; CCDS44875.1; -. [P55061-2]
DR PIR; I38334; I38334.
DR RefSeq; NP_001092046.1; NM_001098576.1. [P55061-2]
DR RefSeq; NP_003208.2; NM_003217.2. [P55061-1]
DR RefSeq; XP_005269183.1; XM_005269126.3. [P55061-2]
DR AlphaFoldDB; P55061; -.
DR SMR; P55061; -.
DR BioGRID; 112868; 117.
DR IntAct; P55061; 88.
DR MINT; P55061; -.
DR STRING; 9606.ENSP00000389277; -.
DR TCDB; 1.A.14.1.1; the calcium transporter a (cata) (formerly the testis-enhanced gene transfer (tegt) family.
DR GlyGen; P55061; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P55061; -.
DR PhosphoSitePlus; P55061; -.
DR SwissPalm; P55061; -.
DR BioMuta; TMBIM6; -.
DR DMDM; 20981681; -.
DR EPD; P55061; -.
DR jPOST; P55061; -.
DR MassIVE; P55061; -.
DR MaxQB; P55061; -.
DR PaxDb; P55061; -.
DR PeptideAtlas; P55061; -.
DR PRIDE; P55061; -.
DR ProteomicsDB; 29424; -.
DR ProteomicsDB; 56774; -. [P55061-1]
DR TopDownProteomics; P55061-1; -. [P55061-1]
DR Antibodypedia; 26071; 218 antibodies from 23 providers.
DR DNASU; 7009; -.
DR Ensembl; ENST00000267115.10; ENSP00000267115.5; ENSG00000139644.13. [P55061-1]
DR Ensembl; ENST00000395006.8; ENSP00000378454.4; ENSG00000139644.13. [P55061-1]
DR Ensembl; ENST00000423828.5; ENSP00000389277.1; ENSG00000139644.13. [P55061-2]
DR Ensembl; ENST00000549385.5; ENSP00000448036.1; ENSG00000139644.13. [P55061-1]
DR Ensembl; ENST00000552370.5; ENSP00000450158.2; ENSG00000139644.13. [P55061-1]
DR Ensembl; ENST00000552699.5; ENSP00000446734.1; ENSG00000139644.13. [P55061-2]
DR GeneID; 7009; -.
DR KEGG; hsa:7009; -.
DR MANE-Select; ENST00000267115.10; ENSP00000267115.5; NM_003217.3; NP_003208.2.
DR UCSC; uc001rux.3; human. [P55061-1]
DR CTD; 7009; -.
DR DisGeNET; 7009; -.
DR GeneCards; TMBIM6; -.
DR HGNC; HGNC:11723; TMBIM6.
DR HPA; ENSG00000139644; Tissue enhanced (liver).
DR MIM; 600748; gene.
DR neXtProt; NX_P55061; -.
DR OpenTargets; ENSG00000139644; -.
DR PharmGKB; PA36440; -.
DR VEuPathDB; HostDB:ENSG00000139644; -.
DR eggNOG; KOG1629; Eukaryota.
DR GeneTree; ENSGT01050000244940; -.
DR InParanoid; P55061; -.
DR OMA; MGDVIGM; -.
DR OrthoDB; 1275249at2759; -.
DR PhylomeDB; P55061; -.
DR TreeFam; TF323395; -.
DR PathwayCommons; P55061; -.
DR SignaLink; P55061; -.
DR BioGRID-ORCS; 7009; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; TMBIM6; human.
DR GeneWiki; TEGT; -.
DR GenomeRNAi; 7009; -.
DR Pharos; P55061; Tbio.
DR PRO; PR:P55061; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P55061; protein.
DR Bgee; ENSG00000139644; Expressed in islet of Langerhans and 213 other tissues.
DR ExpressionAtlas; P55061; baseline and differential.
DR Genevisible; P55061; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; NAS:ParkinsonsUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0060698; F:endoribonuclease inhibitor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0034620; P:cellular response to unfolded protein; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:ParkinsonsUK-UCL.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0010523; P:negative regulation of calcium ion transport into cytosol; IDA:MGI.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0060702; P:negative regulation of endoribonuclease activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0002638; P:negative regulation of immunoglobulin production; IEA:Ensembl.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0033119; P:negative regulation of RNA splicing; IDA:ParkinsonsUK-UCL.
DR GO; GO:1990441; P:negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:1902065; P:response to L-glutamate; IDA:ParkinsonsUK-UCL.
DR InterPro; IPR006213; Bax_inhbtr1_CS.
DR InterPro; IPR006214; Bax_inhibitor_1-related.
DR PANTHER; PTHR23291; PTHR23291; 1.
DR Pfam; PF01027; Bax1-I; 1.
DR PROSITE; PS01243; BI1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Autophagy; Calcium; Endoplasmic reticulum;
KW Isopeptide bond; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Unfolded protein response.
FT CHAIN 1..237
FT /note="Bax inhibitor 1"
FT /id="PRO_0000179078"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..52
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..112
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..166
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT VAR_SEQ 1
FT /note="M -> MSHSSVTREAPQLLSQRQRREVRGVWGWGCLPGPRGGPALFGLVTFG
FT QSGDCCTDSGTM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055119"
FT MUTAGEN 209
FT /note="D->A: Abolishes calcium flux properties."
FT /evidence="ECO:0000269|PubMed:22128171"
FT MUTAGEN 213
FT /note="D->A: Abolishes calcium flux properties."
FT /evidence="ECO:0000269|PubMed:22128171"
FT CONFLICT 118
FT /note="F -> L (in Ref. 2; AAU29521)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="L -> P (in Ref. 1; CAA53472)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="F -> V (in Ref. 1; CAA53472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 26538 MW; 6567E73A1AD6238E CRC64;
MNIFDRKINF DALLKFSHIT PSTQQHLKKV YASFALCMFV AAAGAYVHMV THFIQAGLLS
ALGSLILMIW LMATPHSHET EQKRLGLLAG FAFLTGVGLG PALEFCIAVN PSILPTAFMG
TAMIFTCFTL SALYARRRSY LFLGGILMSA LSLLLLSSLG NVFFGSIWLF QANLYVGLVV
MCGFVLFDTQ LIIEKAEHGD QDYIWHCIDL FLDFITVFRK LMMILAMNEK DKKKEKK
