B2CL2_HUMAN
ID B2CL2_HUMAN Reviewed; 193 AA.
AC Q92843; A8K0F4; Q2M3U0; Q5U0H4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Bcl-2-like protein 2;
DE Short=Bcl2-L-2;
DE AltName: Full=Apoptosis regulator Bcl-W;
GN Name=BCL2L2; Synonyms=BCLW, KIAA0271;
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), FUNCTION, AND VARIANT ARG-133.
RX PubMed=8761287;
RA Gibson L., Holmgreen S.P., Huang D.C., Bernard O., Copeland N.G.,
RA Jenkins N.A., Sutherland G.R., Baker E., Adams J.M., Cory S.;
RT "Bcl-w, a novel member of the Bcl-2 family, promotes cell survival.";
RL Oncogene 13:665-675(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-133.
RC TISSUE=Brain;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-133.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-133.
RC TISSUE=Cerebellum;
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=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-133.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ARG-133.
RC TISSUE=Brain, Lung, and Rhabdomyosarcoma;
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11423909; DOI=10.1038/sj.cdd.4400835;
RA O'Reilly L.A., Print C., Hausmann G., Moriishi K., Cory S., Huang D.C.S.,
RA Strasser A.;
RT "Tissue expression and subcellular localization of the pro-survival
RT molecule Bcl-w.";
RL Cell Death Differ. 8:486-494(2001).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=12952938; DOI=10.1083/jcb.200302144;
RA Wilson-Annan J., O'Reilly L.A., Crawford S.A., Hausmann G., Beaumont J.G.,
RA Parma L.P., Chen L., Lackmann M., Lithgow T., Hinds M.G., Day C.L.,
RA Adams J.M., Huang D.C.S.;
RT "Proapoptotic BH3-only proteins trigger membrane integration of prosurvival
RT Bcl-w and neutralize its activity.";
RL J. Cell Biol. 162:877-887(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262 (ISOFORM 3), AND
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 [17]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-286 AND ARG-290 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [18]
RP STRUCTURE BY NMR OF 1-183.
RX PubMed=12660157; DOI=10.1093/emboj/cdg144;
RA Hinds M.G., Lackmann M., Skea G.L., Harrison P.J., Huang D.C.S., Day C.L.;
RT "The structure of Bcl-w reveals a role for the C-terminal residues in
RT modulating biological activity.";
RL EMBO J. 22:1497-1507(2003).
RN [19]
RP STRUCTURE BY NMR OF 2-171.
RX PubMed=12651847; DOI=10.1074/jbc.m301798200;
RA Denisov A.Y., Madiraju M.S.R., Chen G., Khadir A., Beauparlant P.,
RA Attardo G., Shore G.C., Gehring K.;
RT "Solution structure of human BCL-w: modulation of ligand binding by the C-
RT terminal helix.";
RL J. Biol. Chem. 278:21124-21128(2003).
CC -!- FUNCTION: Promotes cell survival. Blocks dexamethasone-induced
CC apoptosis. Mediates survival of postmitotic Sertoli cells by
CC suppressing death-promoting activity of BAX.
CC {ECO:0000269|PubMed:8761287}.
CC -!- SUBUNIT: Interacts with HIF3A (via C-terminus domain). Interacts with
CC BOP. {ECO:0000250|UniProtKB:P70345}.
CC -!- INTERACTION:
CC Q92843; Q68DC2: ANKS6; NbExp=3; IntAct=EBI-707714, EBI-7054139;
CC Q92843; P02654: APOC1; NbExp=3; IntAct=EBI-707714, EBI-1220105;
CC Q92843; P55056: APOC4; NbExp=3; IntAct=EBI-707714, EBI-18302142;
CC Q92843; P18859: ATP5PF; NbExp=3; IntAct=EBI-707714, EBI-2606700;
CC Q92843; Q92934: BAD; NbExp=7; IntAct=EBI-707714, EBI-700771;
CC Q92843; Q16611: BAK1; NbExp=8; IntAct=EBI-707714, EBI-519866;
CC Q92843; Q07812: BAX; NbExp=5; IntAct=EBI-707714, EBI-516580;
CC Q92843; Q9BXH1: BBC3; NbExp=3; IntAct=EBI-707714, EBI-519884;
CC Q92843; O43521: BCL2L11; NbExp=9; IntAct=EBI-707714, EBI-526406;
CC Q92843; Q92843: BCL2L2; NbExp=3; IntAct=EBI-707714, EBI-707714;
CC Q92843; Q7RTU4: BHLHA9; NbExp=3; IntAct=EBI-707714, EBI-17508719;
CC Q92843; P55957: BID; NbExp=5; IntAct=EBI-707714, EBI-519672;
CC Q92843; Q13323: BIK; NbExp=22; IntAct=EBI-707714, EBI-700794;
CC Q92843; Q96LC9: BMF; NbExp=13; IntAct=EBI-707714, EBI-3919268;
CC Q92843; P0C671: BNIP5; NbExp=3; IntAct=EBI-707714, EBI-12806802;
CC Q92843; Q8IYJ2-2: C10orf67; NbExp=3; IntAct=EBI-707714, EBI-13381098;
CC Q92843; P11912: CD79A; NbExp=3; IntAct=EBI-707714, EBI-7797864;
CC Q92843; Q9H9P2: CHODL; NbExp=3; IntAct=EBI-707714, EBI-17447707;
CC Q92843; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-707714, EBI-7062247;
CC Q92843; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-707714, EBI-1045797;
CC Q92843; O95471: CLDN7; NbExp=3; IntAct=EBI-707714, EBI-740744;
CC Q92843; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-707714, EBI-781551;
CC Q92843; P60508: ERVFRD-1; NbExp=3; IntAct=EBI-707714, EBI-17973325;
CC Q92843; Q969F0: FATE1; NbExp=6; IntAct=EBI-707714, EBI-743099;
CC Q92843; Q92915-2: FGF14; NbExp=3; IntAct=EBI-707714, EBI-12836320;
CC Q92843; P27469: G0S2; NbExp=3; IntAct=EBI-707714, EBI-3939849;
CC Q92843; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-707714, EBI-3917143;
CC Q92843; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-707714, EBI-11955647;
CC Q92843; Q8TED1: GPX8; NbExp=3; IntAct=EBI-707714, EBI-11721746;
CC Q92843; Q8N6L0: KASH5; NbExp=8; IntAct=EBI-707714, EBI-749265;
CC Q92843; P48051: KCNJ6; NbExp=3; IntAct=EBI-707714, EBI-12017638;
CC Q92843; Q7Z4F1: LRP10; NbExp=3; IntAct=EBI-707714, EBI-2830349;
CC Q92843; Q99735: MGST2; NbExp=3; IntAct=EBI-707714, EBI-11324706;
CC Q92843; P15941-11: MUC1; NbExp=3; IntAct=EBI-707714, EBI-17263240;
CC Q92843; Q96RD7: PANX1; NbExp=3; IntAct=EBI-707714, EBI-7037612;
CC Q92843; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-707714, EBI-17589229;
CC Q92843; Q7L3V2: RTL10; NbExp=5; IntAct=EBI-707714, EBI-10697720;
CC Q92843; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-707714, EBI-3920694;
CC Q92843; O95470: SGPL1; NbExp=3; IntAct=EBI-707714, EBI-1046170;
CC Q92843; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-707714, EBI-17295964;
CC Q92843; Q7Z769: SLC35E3; NbExp=3; IntAct=EBI-707714, EBI-13389236;
CC Q92843; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-707714, EBI-12898013;
CC Q92843; Q13433-2: SLC39A6; NbExp=3; IntAct=EBI-707714, EBI-12956703;
CC Q92843; P27105: STOM; NbExp=3; IntAct=EBI-707714, EBI-1211440;
CC Q92843; Q96L08: SUSD3; NbExp=3; IntAct=EBI-707714, EBI-18194029;
CC Q92843; P15884: TCF4; NbExp=3; IntAct=EBI-707714, EBI-533224;
CC Q92843; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-707714, EBI-11523345;
CC Q92843; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-707714, EBI-7238458;
CC Q92843; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-707714, EBI-11724423;
CC Q92843; Q9H3N1: TMX1; NbExp=3; IntAct=EBI-707714, EBI-1051115;
CC Q92843; Q13625: TP53BP2; NbExp=4; IntAct=EBI-707714, EBI-77642;
CC Q92843; Q91ZE9: Bmf; Xeno; NbExp=2; IntAct=EBI-707714, EBI-708032;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:11423909, ECO:0000269|PubMed:12952938}; Peripheral
CC membrane protein {ECO:0000269|PubMed:11423909,
CC ECO:0000269|PubMed:12952938}. Note=Loosely associated with the
CC mitochondrial membrane in healthy cells. During apoptosis, tightly
CC bound to the membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92843-1; Sequence=Displayed;
CC Name=3; Synonyms=BCL2L2-PABPN1;
CC IsoId=Q92843-2; Sequence=VSP_042064;
CC -!- TISSUE SPECIFICITY: Expressed (at protein level) in a wide range of
CC tissues with highest levels in brain, spinal cord, testis, pancreas,
CC heart, spleen and mammary glands. Moderate levels found in thymus,
CC ovary and small intestine. Not detected in salivary gland, muscle or
CC liver. Also expressed in cell lines of myeloid, fibroblast and
CC epithelial origin. Not detected in most lymphoid cell lines.
CC {ECO:0000269|PubMed:11423909}.
CC -!- DOMAIN: The BH4 motif seems to be involved in the anti-apoptotic
CC function.
CC -!- DOMAIN: The BH1 and BH2 motifs form a hydrophobic groove which acts as
CC a docking site for the BH3 domain of some pro-apoptotic proteins. The
CC C-terminal residues of BCL2L2 fold into the BH3-binding cleft and
CC modulate pro-survival activity by regulating ligand access. When BH3
CC domain-containing proteins bind, they displace the C-terminus, allowing
CC its insertion into the membrane and neutralizing the pro-survival
CC activity of BCL2L2.
CC -!- MISCELLANEOUS: [Isoform 3]: Based on a readthrough transcript which may
CC produce a BCL2L2-PABPN1 fusion protein. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA19666.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U59747; AAB09055.1; -; mRNA.
DR EMBL; D87461; BAA19666.2; ALT_INIT; mRNA.
DR EMBL; BT019549; AAV38356.1; -; mRNA.
DR EMBL; AK289519; BAF82208.1; -; mRNA.
DR EMBL; AL049829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66169.1; -; Genomic_DNA.
DR EMBL; BC011637; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC021198; AAH21198.1; -; mRNA.
DR EMBL; BC104789; AAI04790.1; -; mRNA.
DR EMBL; BC113522; AAI13523.1; -; mRNA.
DR CCDS; CCDS9591.1; -. [Q92843-1]
DR RefSeq; NP_001186768.1; NM_001199839.1. [Q92843-1]
DR RefSeq; NP_004041.1; NM_004050.4. [Q92843-1]
DR PDB; 1MK3; NMR; -; A=2-171.
DR PDB; 1O0L; NMR; -; A=1-183.
DR PDB; 1ZY3; NMR; -; A=2-171.
DR PDB; 2Y6W; X-ray; 2.00 A; A/B=1-164.
DR PDB; 4CIM; X-ray; 1.50 A; A/B=1-163, P/Q=38-58.
DR PDBsum; 1MK3; -.
DR PDBsum; 1O0L; -.
DR PDBsum; 1ZY3; -.
DR PDBsum; 2Y6W; -.
DR PDBsum; 4CIM; -.
DR AlphaFoldDB; Q92843; -.
DR SMR; Q92843; -.
DR BioGRID; 107071; 78.
DR ComplexPortal; CPX-309; BIK:BCL-w complex.
DR DIP; DIP-33700N; -.
DR IntAct; Q92843; 62.
DR MINT; Q92843; -.
DR STRING; 9606.ENSP00000250405; -.
DR BindingDB; Q92843; -.
DR ChEMBL; CHEMBL4677; -.
DR DrugBank; DB12340; Navitoclax.
DR DrugCentral; Q92843; -.
DR GuidetoPHARMACOLOGY; 2846; -.
DR TCDB; 1.A.21.1.5; the bcl-2 (bcl-2) family.
DR iPTMnet; Q92843; -.
DR PhosphoSitePlus; Q92843; -.
DR SwissPalm; Q92843; -.
DR BioMuta; BCL2L2-PABPN1; -.
DR DMDM; 296434404; -.
DR EPD; Q92843; -.
DR jPOST; Q92843; -.
DR MassIVE; Q92843; -.
DR MaxQB; Q92843; -.
DR PaxDb; Q92843; -.
DR PeptideAtlas; Q92843; -.
DR PRIDE; Q92843; -.
DR ProteomicsDB; 75535; -. [Q92843-1]
DR ProteomicsDB; 75536; -. [Q92843-2]
DR Antibodypedia; 3670; 436 antibodies from 38 providers.
DR CPTC; Q92843; 3 antibodies.
DR DNASU; 599; -.
DR Ensembl; ENST00000250405.10; ENSP00000250405.6; ENSG00000129473.11. [Q92843-1]
DR Ensembl; ENST00000553781.5; ENSP00000451320.1; ENSG00000258643.6. [Q92843-2]
DR Ensembl; ENST00000556100.3; ENSP00000503091.1; ENSG00000129473.11. [Q92843-1]
DR Ensembl; ENST00000557008.2; ENSP00000452479.1; ENSG00000258643.6. [Q92843-2]
DR Ensembl; ENST00000678311.1; ENSP00000504570.1; ENSG00000129473.11. [Q92843-1]
DR Ensembl; ENST00000679000.1; ENSP00000503368.1; ENSG00000129473.11. [Q92843-1]
DR Ensembl; ENST00000679219.1; ENSP00000503012.1; ENSG00000129473.11. [Q92843-1]
DR GeneID; 599; -.
DR KEGG; hsa:599; -.
DR MANE-Select; ENST00000250405.10; ENSP00000250405.6; NM_004050.5; NP_004041.2.
DR UCSC; uc001wjg.4; human. [Q92843-1]
DR CTD; 599; -.
DR DisGeNET; 599; -.
DR GeneCards; BCL2L2; -.
DR GeneCards; BCL2L2-PABPN1; -.
DR HGNC; HGNC:995; BCL2L2.
DR HGNC; HGNC:42959; BCL2L2-PABPN1.
DR HPA; ENSG00000129473; Low tissue specificity.
DR HPA; ENSG00000258643; Low tissue specificity.
DR MalaCards; BCL2L2-PABPN1; -.
DR MIM; 601931; gene.
DR neXtProt; NX_Q92843; -.
DR OpenTargets; ENSG00000129473; -.
DR OpenTargets; ENSG00000258643; -.
DR PharmGKB; PA25307; -.
DR VEuPathDB; HostDB:ENSG00000129473; -.
DR VEuPathDB; HostDB:ENSG00000258643; -.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT00940000154606; -.
DR GeneTree; ENSGT01050000244953; -.
DR HOGENOM; CLU_834081_0_0_1; -.
DR InParanoid; Q92843; -.
DR OMA; DVARWMT; -.
DR OrthoDB; 1412946at2759; -.
DR PhylomeDB; Q92843; -.
DR TreeFam; TF105907; -.
DR TreeFam; TF315834; -.
DR PathwayCommons; Q92843; -.
DR SignaLink; Q92843; -.
DR SIGNOR; Q92843; -.
DR BioGRID-ORCS; 599; 27 hits in 1053 CRISPR screens.
DR EvolutionaryTrace; Q92843; -.
DR GeneWiki; BCL2L2; -.
DR GenomeRNAi; 599; -.
DR Pharos; Q92843; Tchem.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q92843; protein.
DR Bgee; ENSG00000129473; Expressed in C1 segment of cervical spinal cord and 190 other tissues.
DR ExpressionAtlas; Q92843; baseline and differential.
DR Genevisible; Q92843; HS.
DR GO; GO:0097136; C:Bcl-2 family protein complex; IMP:CAFA.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0051400; F:BH domain binding; IEA:Ensembl.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:1905430; P:cellular response to glycine; IEA:Ensembl.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0035795; P:negative regulation of mitochondrial membrane permeability; IEA:Ensembl.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:ComplexPortal.
DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR GO; GO:0060011; P:Sertoli cell proliferation; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR CDD; cd06845; Bcl-2_like; 1.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR013280; Apop_reg_BclW.
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; IPR003093; Bcl2_BH4.
DR InterPro; IPR020731; Bcl2_BH4_motif_CS.
DR PANTHER; PTHR11256; PTHR11256; 1.
DR PANTHER; PTHR11256:SF51; PTHR11256:SF51; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR Pfam; PF02180; BH4; 1.
DR PRINTS; PR01865; APOPREGBCLW.
DR PRINTS; PR01862; BCL2FAMILY.
DR SMART; SM00337; BCL; 1.
DR SMART; SM00265; BH4; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
DR PROSITE; PS01080; BH1; 1.
DR PROSITE; PS01258; BH2; 1.
DR PROSITE; PS01260; BH4_1; 1.
DR PROSITE; PS50063; BH4_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Membrane;
KW Methylation; Mitochondrion; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..193
FT /note="Bcl-2-like protein 2"
FT /id="PRO_0000143066"
FT MOTIF 9..29
FT /note="BH4"
FT MOTIF 85..104
FT /note="BH1"
FT MOTIF 136..151
FT /note="BH2"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VAR_SEQ 145..193
FT /note="AEFTALYGDGALEEARRLREGNWASVRTVLTGAVALGALVTVGAFFASK ->
FT ELEAIKARVREMEEEAEKLKELQNEVEKQMNMSPPPGNAGPVIMSIEEKMEADARSIYV
FT GNVDYGATAEELEAHFHGCGSVNRVTILCDKFSGHPKGFAYIEFSDKESVRTSLALDES
FT LFRGRQIKVIPKRTNRPGISTTDRGFPRARYRARTTNYNSSRSRFYSGFNSRPRGRVYR
FT GRARATSWYSPY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042064"
FT VARIANT 133
FT /note="Q -> R (in dbSNP:rs910332)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8761287,
FT ECO:0000269|PubMed:9039502, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.6"
FT /id="VAR_048418"
FT HELIX 10..24
FT /evidence="ECO:0007829|PDB:4CIM"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4CIM"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:4CIM"
FT HELIX 41..60
FT /evidence="ECO:0007829|PDB:4CIM"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4CIM"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1O0L"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4CIM"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:4CIM"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:4CIM"
FT HELIX 93..112
FT /evidence="ECO:0007829|PDB:4CIM"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:4CIM"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:4CIM"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:4CIM"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:1MK3"
FT TURN 171..176
FT /evidence="ECO:0007829|PDB:1O0L"
FT MOD_RES Q92843-2:177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES Q92843-2:262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q92843-2:286
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q92843-2:290
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 193 AA; 20746 MW; 3542243A532B1762 CRC64;
MATPASAPDT RALVADFVGY KLRQKGYVCG AGPGEGPAAD PLHQAMRAAG DEFETRFRRT
FSDLAAQLHV TPGSAQQRFT QVSDELFQGG PNWGRLVAFF VFGAALCAES VNKEMEPLVG
QVQEWMVAYL ETQLADWIHS SGGWAEFTAL YGDGALEEAR RLREGNWASV RTVLTGAVAL
GALVTVGAFF ASK
