true2002-09-192024-01-24179B2L10_HUMANBcl2-L-10, a novel anti-apoptotic member of the Bcl-2 family, blocks apoptosis in the mitochondria death pathway but not in the death receptor pathway.Zhang H.Holzgreve W.De Geyter C.doi:10.1093/hmg/10.21.23292001Hum. Mol. Genet.102329-2339NUCLEOTIDE SEQUENCE [MRNA]FUNCTIONOvaryBcl-B, a novel Bcl-2 family member that differentially binds and regulates Bax and Bak.Ke N.Godzik A.Reed J.C.doi:10.1074/jbc.c0008712002001J. Biol. Chem.27612481-12484NUCLEOTIDE SEQUENCE [MRNA]FUNCTIONINTERACTION WITH BAX; BCL2 AND BCL2L1LiverAnalysis of the DNA sequence and duplication history of human chromosome 15.Zody M.C.Garber M.Sharpe T.Young S.K.Rowen L.O'Neill K.Whittaker C.A.Kamal M.Chang J.L.Cuomo C.A.Dewar K.FitzGerald M.G.Kodira C.D.Madan A.Qin S.Yang X.Abbasi N.Abouelleil A.Arachchi H.M.Baradarani L.Birditt B.Bloom S.Bloom T.Borowsky M.L.Burke J.Butler J.Cook A.DeArellano K.DeCaprio D.Dorris L. IIIDors M.Eichler E.E.Engels R.Fahey J.Fleetwood P.Friedman C.Gearin G.Hall J.L.Hensley G.Johnson E.Jones C.Kamat A.Kaur A.Locke D.P.Madan A.'Munson G.Jaffe D.B.Lui A.Macdonald P.Mauceli E.Naylor J.W.Nesbitt R.Nicol R.O'Leary S.B.Ratcliffe A.Rounsley S.She X.Sneddon K.M.B.Stewart S.Sougnez C.Stone S.M.Topham K.Vincent D.Wang S.Zimmer A.R.Birren B.W.Hood L.Lander E.S.Nusbaum C.doi:10.1038/nature046012006Nature440671-675NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project Teamdoi:10.1101/gr.25965042004Genome Res.142121-2127NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]BrainNrH, a human homologue of Nr-13 associates with Bcl-Xs and is an inhibitor of apoptosis.Aouacheria A.Arnaud E.Venet S.Lalle P.Gouy M.Rigal D.Gillet G.doi:10.1038/sj.onc.12047402001Oncogene205846-5855NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-204SUBCELLULAR LOCATIONTISSUE SPECIFICITYINTERACTION WITH BCL2L1NM23-H2 involves in negative regulation of Diva and Bcl2L10 in apoptosis signaling.Kang Y.Lee D.C.Han J.Yoon S.Won M.Yeom J.H.Seong M.J.Ko J.J.Lee K.A.Lee K.Bae J.doi:10.1016/j.bbrc.2007.05.0902007Biochem. Biophys. Res. Commun.35976-82INTERACTION WITH NME2MUTAGENESIS OF 178-PHE--LEU-191HIP1R interacts with a member of Bcl-2 family, BCL2L10, and induces BAK-dependent cell death.Kim J.H.Yoon S.Won M.Sim S.H.Ko J.J.Han S.Lee K.A.Lee K.Bae J.doi:10.1159/0002040882009Cell. Physiol. Biochem.2343-52INTERACTION WITH HIP1R AND CASP9Characterization of unique signature sequences in the divergent maternal protein Bcl2l10.Guillemin Y.Cornut-Thibaut A.Gillet G.Penin F.Aouacheria A.doi:10.1093/molbev/msr1522011Mol. Biol. Evol.283271-3283COFACTORSUBCELLULAR LOCATIONMUTAGENESIS OF 118-TRP--ASP-133; GLU-131 AND ASP-133The anti-apoptotic Bcl-B protein inhibits BECN1-dependent autophagic cell death.Robert G.Gastaldi C.Puissant A.Hamouda A.Jacquel A.Dufies M.Belhacene N.Colosetti P.Reed J.C.Auberger P.Luciano F.doi:10.4161/auto.190842012Autophagy8637-649INTERACTION WITH BECN1 AND BCL2L11SUBCELLULAR LOCATIONMUTAGENESIS OF GLY-95Ubiquitination, localization, and stability of an anti-apoptotic BCL2-like protein, BCL2L10/BCLb, are regulated by Ubiquilin1.Beverly L.J.Lockwood W.W.Shah P.P.Erdjument-Bromage H.Varmus H.doi:10.1073/pnas.11191671092012Proc. Natl. Acad. Sci. U.S.A.109E119-E126INTERACTION WITH UBQLN1SUBCELLULAR LOCATIONUBIQUITINATEDPolyubiquitination and proteasomal turnover controls the anti-apoptotic activity of Bcl-B.van de Kooij B.Rooswinkel R.W.Kok F.Herrebout M.de Vries E.Paauwe M.Janssen G.M.van Veelen P.A.Borst J.doi:10.1038/onc.2013.992013Oncogene325439-5448INTERACTION WITH BCL2L11; BIK AND PMAIP1SUBCELLULAR LOCATIONUBIQUITINATED AT LYS-119; LYS-120 AND LYS-128MUTAGENESIS OF LYS-119; LYS-120 AND LYS-128IRBIT controls apoptosis by interacting with the Bcl-2 homolog, Bcl2l10, and by promoting ER-mitochondria contact.Bonneau B.Ando H.Kawaai K.Hirose M.Takahashi-Iwanaga H.Mikoshiba K.doi:10.7554/elife.198962016Elife5e19896FUNCTIONINTERACTION WITH AHCYL1; ITPR1; ITPR2 AND ITPR3SUBCELLULAR LOCATIONUBQLN4 is an ATM substrate that stabilizes the anti-apoptotic proteins BCL2A1 and BCL2L10 in mesothelioma.Liu F.Pan R.Ding H.Gu L.Yang Y.Li C.Xu Y.Hu R.Chen H.Zhang X.Nie Y.doi:10.1002/1878-0261.130582021Mol. Oncol.153738-3752INTERACTION WITH UBQLN4The restricted binding repertoire of Bcl-B leaves Bim as the universal BH3-only prosurvival Bcl-2 protein antagonist.Rautureau G.J.Yabal M.Yang H.Huang D.C.Kvansakul M.Hinds M.G.doi:10.1038/cddis.2012.1782012Cell Death Dis.3e443X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-177 IN COMPLEX WITH BCL2L11INTERACTION WITH BCL2L11; BIK AND BAX1.90A=12-1772013266 antibodies from 36 providershumanBCL2L10Tissue enhanced (liver, skin)geneEukaryota13 hits in 1149 CRISPR screensTchemProteinExpressed in right lobe of liver and 80 other cell types or tissuesbaseline and differentialBcl-2_likeBlc2-likeBcl-2-like_sfBcl-2_BH1-3Bcl-2_famBcl2-likeBcl2_BH1_motif_CSBcl2_BH2_motif_CSBCL-2 RELATEDBCL-2-LIKE PROTEIN 10Bcl-2BCLBcl-2 inhibitors of programmed cell deathBCL2_FAMILYBH1BH2HSBcl-2-like protein 10Bcl2-L-10Anti-apoptotic protein BooAnti-apoptotic protein NrHApoptosis regulator Bcl-BBCL2L10BCL-BBCLBBOODIVAPromotes cell survival by suppressing apoptosis induced by BAX but not BAK (PubMed:11689480, PubMed:11278245). Increases binding of AHCYL1/IRBIT to ITPR1 (PubMed:27995898). Reduces ITPR1-mediated calcium release from the endoplasmic reticulum cooperatively with AHCYL1/IRBIT under normal cellular conditions (PubMed:27995898). Under apoptotic stress conditions, dissociates from ITPR1 and is displaced from mitochondria-associated endoplasmic reticulum membranes, leading to increased Ca(2+) transfer to mitochondria which promotes apoptosis (PubMed:27995898). Required for the correct formation of the microtubule organizing center during oocyte cell division, potentially via regulation of protein abundance and localization of other microtubule organizing center components such as AURKA and TPX2 (By similarity).Interacts with BAX (PubMed:11278245, PubMed:23235460). Interacts with BCL2 and BCL2L1/BCLX (PubMed:11278245, PubMed:11593390). Interacts with APAF1 (By similarity). Interacts with ITPR1, ITPR2 and ITPR3; the interaction with ITPR1 is increased in the presence of AHCLY1 (PubMed:27995898). Interacts with AHCYL1 (PubMed:27995898). Interacts with HIP1R (via ENTH and I/LWEQ domains) (PubMed:19255499). Interacts with CASP9 (PubMed:19255499). Interacts with BCL2L11/BIM (PubMed:22498477, PubMed:23563182, PubMed:23235460). Interacts with BIK (PubMed:23563182, PubMed:23235460). Interacts with UBQLN4 (PubMed:34245648). Interacts with NME2/NM23-H2 (PubMed:17532299). Interacts with PMAIP1/NOXA (PubMed:23563182). Interacts with TPX2 (By similarity). Interacts with UBQLN1; in the cytoplasm (PubMed:22233804). Interacts (via BH1 domain) with BECN1 (PubMed:22498477).Localizes to mitochondria-associated endoplasmic reticulum membranes (MAMs) (PubMed:27995898). Localization to MAMs is greatly reduced under apoptotic stress conditions (PubMed:27995898).Widely expressed in adult tissues. Preferentially expressed in lung, liver and kidney.Monoubiquitinated by UBQLN1; results in stabilization of BCL2L10 protein abundance and in relocalization from mitochondria to cytoplasm.Belongs to the Bcl-2 family.It is uncertain whether Met-1 or Met-11 is the initiator.Bcl-2-like protein 10232041204Helical183200Required for Ca(2+) binding118133BH186105BH2156167Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)128R21Reduces interaction with BECN1 and BCL2L11.A95Abolishes Ca(2+) binding.Abolishes ubiquitination. No effect on localization to the mitochondria. No effect on interaction with BCL2L11, BIK, BBC3 or PMAIP1.RAbolishes ubiquitination. No effect on localization to the mitochondria. No effect on interaction with BCL2L11, BIK, BBC3 or PMAIP1.RAbolishes ubiquitination. No effect on localization to the mitochondria. No effect on interaction with BCL2L11, BIK, BBC3 or PMAIP1.RAbolishes Ca(2+) binding; when associated with N-133.R131Abolishes Ca(2+) binding; when associated with R-131.NAbolishes interaction with NME2.178191V52W551430445961656669748794108112115151154159162170false4false2false10false2false8false3false7false3false3false3AHCYL1BAXBCL2L11BCL2L11BIKBMFITPR1MGST2SAMD4BTMEM200A2019-05-08323204e85dcfa0013906ae8427a5b561e2aa8fMVDQLRERTTMADPLRERTELLLADYLGYCAREPGTPEPAPSTPEAAVLRSAAARLRQIHRSFFSAYLGYPGNRFELVALMADSVLSDSPGPTWGRVVTLVTFAGTLLERGPLVTARWKKWGFQPRLKEQEGDVARDCQRLVALLSSRLMGQHRAWLQAQGGWDGFCHFFRTPFPLAFWRKQLVQAFLSCLLTTAFIYLWTRLLtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue