B2L10_HUMAN
ID B2L10_HUMAN Reviewed; 204 AA.
AC Q9HD36; Q3SX80; Q52LQ9; Q8TCS9;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Bcl-2-like protein 10 {ECO:0000312|HGNC:HGNC:993};
DE Short=Bcl2-L-10 {ECO:0000303|PubMed:11689480};
DE AltName: Full=Anti-apoptotic protein Boo {ECO:0000250|UniProtKB:Q9Z0F3};
DE AltName: Full=Anti-apoptotic protein NrH {ECO:0000303|PubMed:11593390};
DE AltName: Full=Apoptosis regulator Bcl-B {ECO:0000303|PubMed:11278245};
GN Name=BCL2L10 {ECO:0000303|PubMed:17532299};
GN Synonyms=BCL-B {ECO:0000303|PubMed:22498477},
GN BCLB {ECO:0000303|PubMed:22233804}, BOO {ECO:0000312|HGNC:HGNC:993},
GN DIVA {ECO:0000312|HGNC:HGNC:993};
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], AND FUNCTION.
RC TISSUE=Ovary;
RX PubMed=11689480; DOI=10.1093/hmg/10.21.2329;
RA Zhang H., Holzgreve W., De Geyter C.;
RT "Bcl2-L-10, a novel anti-apoptotic member of the Bcl-2 family, blocks
RT apoptosis in the mitochondria death pathway but not in the death receptor
RT pathway.";
RL Hum. Mol. Genet. 10:2329-2339(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH BAX; BCL2 AND
RP BCL2L1.
RC TISSUE=Liver;
RX PubMed=11278245; DOI=10.1074/jbc.c000871200;
RA Ke N., Godzik A., Reed J.C.;
RT "Bcl-B, a novel Bcl-2 family member that differentially binds and regulates
RT Bax and Bak.";
RL J. Biol. Chem. 276:12481-12484(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-204, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH BCL2L1.
RX PubMed=11593390; DOI=10.1038/sj.onc.1204740;
RA Aouacheria A., Arnaud E., Venet S., Lalle P., Gouy M., Rigal D., Gillet G.;
RT "NrH, a human homologue of Nr-13 associates with Bcl-Xs and is an inhibitor
RT of apoptosis.";
RL Oncogene 20:5846-5855(2001).
RN [6]
RP INTERACTION WITH NME2, AND MUTAGENESIS OF 178-PHE--LEU-191.
RX PubMed=17532299; DOI=10.1016/j.bbrc.2007.05.090;
RA Kang Y., Lee D.C., Han J., Yoon S., Won M., Yeom J.H., Seong M.J., Ko J.J.,
RA Lee K.A., Lee K., Bae J.;
RT "NM23-H2 involves in negative regulation of Diva and Bcl2L10 in apoptosis
RT signaling.";
RL Biochem. Biophys. Res. Commun. 359:76-82(2007).
RN [7]
RP INTERACTION WITH HIP1R AND CASP9.
RX PubMed=19255499; DOI=10.1159/000204088;
RA Kim J.H., Yoon S., Won M., Sim S.H., Ko J.J., Han S., Lee K.A., Lee K.,
RA Bae J.;
RT "HIP1R interacts with a member of Bcl-2 family, BCL2L10, and induces BAK-
RT dependent cell death.";
RL Cell. Physiol. Biochem. 23:43-52(2009).
RN [8]
RP COFACTOR, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 118-TRP--ASP-133;
RP GLU-131 AND ASP-133.
RX PubMed=21705382; DOI=10.1093/molbev/msr152;
RA Guillemin Y., Cornut-Thibaut A., Gillet G., Penin F., Aouacheria A.;
RT "Characterization of unique signature sequences in the divergent maternal
RT protein Bcl2l10.";
RL Mol. Biol. Evol. 28:3271-3283(2011).
RN [9]
RP INTERACTION WITH BECN1 AND BCL2L11, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF GLY-95.
RX PubMed=22498477; DOI=10.4161/auto.19084;
RA Robert G., Gastaldi C., Puissant A., Hamouda A., Jacquel A., Dufies M.,
RA Belhacene N., Colosetti P., Reed J.C., Auberger P., Luciano F.;
RT "The anti-apoptotic Bcl-B protein inhibits BECN1-dependent autophagic cell
RT death.";
RL Autophagy 8:637-649(2012).
RN [10]
RP INTERACTION WITH UBQLN1, SUBCELLULAR LOCATION, AND UBIQUITINATED.
RX PubMed=22233804; DOI=10.1073/pnas.1119167109;
RA Beverly L.J., Lockwood W.W., Shah P.P., Erdjument-Bromage H., Varmus H.;
RT "Ubiquitination, localization, and stability of an anti-apoptotic BCL2-like
RT protein, BCL2L10/BCLb, are regulated by Ubiquilin1.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E119-E126(2012).
RN [11]
RP INTERACTION WITH BCL2L11; BIK AND PMAIP1, SUBCELLULAR LOCATION,
RP UBIQUITINATED AT LYS-119; LYS-120 AND LYS-128, AND MUTAGENESIS OF LYS-119;
RP LYS-120 AND LYS-128.
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).
RN [12]
RP FUNCTION, INTERACTION WITH AHCYL1; ITPR1; ITPR2 AND ITPR3, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27995898; DOI=10.7554/elife.19896;
RA Bonneau B., Ando H., Kawaai K., Hirose M., Takahashi-Iwanaga H.,
RA Mikoshiba K.;
RT "IRBIT controls apoptosis by interacting with the Bcl-2 homolog, Bcl2l10,
RT and by promoting ER-mitochondria contact.";
RL Elife 5:e19896-e19896(2016).
RN [13]
RP INTERACTION WITH UBQLN4.
RX PubMed=34245648; DOI=10.1002/1878-0261.13058;
RA Liu F., Pan R., Ding H., Gu L., Yang Y., Li C., Xu Y., Hu R., Chen H.,
RA Zhang X., Nie Y.;
RT "UBQLN4 is an ATM substrate that stabilizes the anti-apoptotic proteins
RT BCL2A1 and BCL2L10 in mesothelioma.";
RL Mol. Oncol. 15:3738-3752(2021).
RN [14] {ECO:0007744|PDB:4B4S}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-177 IN COMPLEX WITH BCL2L11,
RP AND INTERACTION WITH BCL2L11; BIK AND BAX.
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).
CC -!- FUNCTION: Promotes cell survival by suppressing apoptosis induced by
CC BAX but not BAK (PubMed:11689480, PubMed:11278245). Increases binding
CC of AHCYL1/IRBIT to ITPR1 (PubMed:27995898). Reduces ITPR1-mediated
CC calcium release from the endoplasmic reticulum cooperatively with
CC AHCYL1/IRBIT under normal cellular conditions (PubMed:27995898). Under
CC apoptotic stress conditions, dissociates from ITPR1 and is displaced
CC from mitochondria-associated endoplasmic reticulum membranes, leading
CC to increased Ca(2+) transfer to mitochondria which promotes apoptosis
CC (PubMed:27995898). Required for the correct formation of the
CC microtubule organizing center during oocyte cell division, potentially
CC via regulation of protein abundance and localization of other
CC microtubule organizing center components such as AURKA and TPX2 (By
CC similarity). {ECO:0000250|UniProtKB:Q9Z0F3,
CC ECO:0000269|PubMed:11278245, ECO:0000269|PubMed:11689480,
CC ECO:0000269|PubMed:27995898}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:21705382};
CC -!- SUBUNIT: Interacts with BAX (PubMed:11278245, PubMed:23235460).
CC Interacts with BCL2 and BCL2L1/BCLX (PubMed:11278245, PubMed:11593390).
CC Interacts with APAF1 (By similarity). Interacts with ITPR1, ITPR2 and
CC ITPR3; the interaction with ITPR1 is increased in the presence of
CC AHCLY1 (PubMed:27995898). Interacts with AHCYL1 (PubMed:27995898).
CC Interacts with HIP1R (via ENTH and I/LWEQ domains) (PubMed:19255499).
CC Interacts with CASP9 (PubMed:19255499). Interacts with BCL2L11/BIM
CC (PubMed:22498477, PubMed:23563182, PubMed:23235460). Interacts with BIK
CC (PubMed:23563182, PubMed:23235460). Interacts with UBQLN4
CC (PubMed:34245648). Interacts with NME2/NM23-H2 (PubMed:17532299).
CC Interacts with PMAIP1/NOXA (PubMed:23563182). Interacts with TPX2 (By
CC similarity). Interacts with UBQLN1; in the cytoplasm (PubMed:22233804).
CC Interacts (via BH1 domain) with BECN1 (PubMed:22498477).
CC {ECO:0000250|UniProtKB:Q9Z0F3, ECO:0000269|PubMed:11278245,
CC ECO:0000269|PubMed:11593390, ECO:0000269|PubMed:17532299,
CC ECO:0000269|PubMed:19255499, ECO:0000269|PubMed:22233804,
CC ECO:0000269|PubMed:22498477, ECO:0000269|PubMed:23235460,
CC ECO:0000269|PubMed:23563182, ECO:0000269|PubMed:27995898,
CC ECO:0000269|PubMed:34245648}.
CC -!- INTERACTION:
CC Q9HD36; O43865: AHCYL1; NbExp=4; IntAct=EBI-2126349, EBI-2371423;
CC Q9HD36; Q07812: BAX; NbExp=2; IntAct=EBI-2126349, EBI-516580;
CC Q9HD36; O43521: BCL2L11; NbExp=10; IntAct=EBI-2126349, EBI-526406;
CC Q9HD36; O43521-1: BCL2L11; NbExp=2; IntAct=EBI-2126349, EBI-526416;
CC Q9HD36; Q13323: BIK; NbExp=8; IntAct=EBI-2126349, EBI-700794;
CC Q9HD36; Q96LC9: BMF; NbExp=3; IntAct=EBI-2126349, EBI-3919268;
CC Q9HD36; Q14643: ITPR1; NbExp=7; IntAct=EBI-2126349, EBI-465548;
CC Q9HD36; Q99735: MGST2; NbExp=3; IntAct=EBI-2126349, EBI-11324706;
CC Q9HD36; Q5PRF9: SAMD4B; NbExp=3; IntAct=EBI-2126349, EBI-1047489;
CC Q9HD36; Q86VY9: TMEM200A; NbExp=3; IntAct=EBI-2126349, EBI-11732844;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11593390,
CC ECO:0000269|PubMed:21705382, ECO:0000269|PubMed:22233804,
CC ECO:0000269|PubMed:22498477, ECO:0000269|PubMed:23563182}. Nucleus
CC membrane {ECO:0000269|PubMed:11593390}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:22498477, ECO:0000269|PubMed:27995898}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9Z0F3}. Note=Localizes to
CC mitochondria-associated endoplasmic reticulum membranes (MAMs)
CC (PubMed:27995898). Localization to MAMs is greatly reduced under
CC apoptotic stress conditions (PubMed:27995898).
CC {ECO:0000269|PubMed:27995898}.
CC -!- TISSUE SPECIFICITY: Widely expressed in adult tissues. Preferentially
CC expressed in lung, liver and kidney. {ECO:0000269|PubMed:11593390}.
CC -!- PTM: Monoubiquitinated by UBQLN1; results in stabilization of BCL2L10
CC protein abundance and in relocalization from mitochondria to cytoplasm.
CC {ECO:0000269|PubMed:22233804}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC {ECO:0000305|PubMed:11593390}.
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DR EMBL; AF285092; AAG00503.1; -; mRNA.
DR EMBL; AF326964; AAK48715.1; -; mRNA.
DR EMBL; AC023906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093826; AAH93826.1; -; mRNA.
DR EMBL; BC093828; AAH93828.1; -; mRNA.
DR EMBL; BC104442; AAI04443.1; -; mRNA.
DR EMBL; BC104443; AAI04444.1; -; mRNA.
DR EMBL; AJ458330; CAD30221.1; -; Genomic_DNA.
DR CCDS; CCDS10148.1; -.
DR RefSeq; NP_001293097.1; NM_001306168.1.
DR RefSeq; NP_065129.1; NM_020396.3.
DR PDB; 4B4S; X-ray; 1.90 A; A=12-177.
DR PDBsum; 4B4S; -.
DR AlphaFoldDB; Q9HD36; -.
DR SMR; Q9HD36; -.
DR BioGRID; 115334; 19.
DR IntAct; Q9HD36; 13.
DR MINT; Q9HD36; -.
DR STRING; 9606.ENSP00000260442; -.
DR ChEMBL; CHEMBL5988; -.
DR iPTMnet; Q9HD36; -.
DR PhosphoSitePlus; Q9HD36; -.
DR BioMuta; BCL2L10; -.
DR DMDM; 23396469; -.
DR MassIVE; Q9HD36; -.
DR PaxDb; Q9HD36; -.
DR PeptideAtlas; Q9HD36; -.
DR PRIDE; Q9HD36; -.
DR Antibodypedia; 24926; 240 antibodies from 36 providers.
DR DNASU; 10017; -.
DR Ensembl; ENST00000260442.3; ENSP00000260442.3; ENSG00000137875.4.
DR GeneID; 10017; -.
DR KEGG; hsa:10017; -.
DR MANE-Select; ENST00000260442.3; ENSP00000260442.3; NM_020396.4; NP_065129.1.
DR UCSC; uc002abq.4; human.
DR CTD; 10017; -.
DR DisGeNET; 10017; -.
DR GeneCards; BCL2L10; -.
DR HGNC; HGNC:993; BCL2L10.
DR HPA; ENSG00000137875; Tissue enhanced (liver, skin).
DR MIM; 606910; gene.
DR neXtProt; NX_Q9HD36; -.
DR OpenTargets; ENSG00000137875; -.
DR PharmGKB; PA25304; -.
DR VEuPathDB; HostDB:ENSG00000137875; -.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT01050000244872; -.
DR HOGENOM; CLU_122207_0_0_1; -.
DR InParanoid; Q9HD36; -.
DR OMA; GRKMSCG; -.
DR OrthoDB; 1193942at2759; -.
DR PhylomeDB; Q9HD36; -.
DR TreeFam; TF334762; -.
DR PathwayCommons; Q9HD36; -.
DR SignaLink; Q9HD36; -.
DR BioGRID-ORCS; 10017; 11 hits in 1070 CRISPR screens.
DR GeneWiki; BCL2L10; -.
DR GenomeRNAi; 10017; -.
DR Pharos; Q9HD36; Tchem.
DR PRO; PR:Q9HD36; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9HD36; protein.
DR Bgee; ENSG00000137875; Expressed in right lobe of liver and 79 other tissues.
DR ExpressionAtlas; Q9HD36; baseline and differential.
DR Genevisible; Q9HD36; HS.
DR GO; GO:0005829; C:cytosol; IDA:HGNC-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IMP:UniProtKB.
DR GO; GO:0089720; F:caspase binding; IPI:ParkinsonsUK-UCL.
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:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR GO; GO:0007292; P:female gamete generation; TAS:ProtInc.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR GO; GO:0031023; P:microtubule organizing center organization; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:HGNC-UCL.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR CDD; cd06845; Bcl-2_like; 1.
DR DisProt; DP02676; -.
DR Gene3D; 1.10.437.10; -; 1.
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 PANTHER; PTHR11256; PTHR11256; 1.
DR Pfam; PF00452; Bcl-2; 1.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW Isopeptide bond; Membrane; Mitochondrion; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..204
FT /note="Bcl-2-like protein 10"
FT /id="PRO_0000143068"
FT TRANSMEM 183..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 118..133
FT /note="Required for Ca(2+) binding"
FT /evidence="ECO:0000269|PubMed:21705382"
FT MOTIF 86..105
FT /note="BH1"
FT MOTIF 156..167
FT /note="BH2"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23563182"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23563182"
FT CROSSLNK 128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23563182"
FT VARIANT 21
FT /note="L -> R (in dbSNP:rs2231292)"
FT /id="VAR_047113"
FT MUTAGEN 95
FT /note="G->A: Reduces interaction with BECN1 and BCL2L11."
FT /evidence="ECO:0000269|PubMed:22498477"
FT MUTAGEN 118..133
FT /note="Missing: Abolishes Ca(2+) binding."
FT /evidence="ECO:0000269|PubMed:21705382"
FT MUTAGEN 119
FT /note="K->R: Abolishes ubiquitination. No effect on
FT localization to the mitochondria. No effect on interaction
FT with BCL2L11, BIK, BBC3 or PMAIP1."
FT /evidence="ECO:0000269|PubMed:23563182"
FT MUTAGEN 120
FT /note="K->R: Abolishes ubiquitination. No effect on
FT localization to the mitochondria. No effect on interaction
FT with BCL2L11, BIK, BBC3 or PMAIP1."
FT /evidence="ECO:0000269|PubMed:23563182"
FT MUTAGEN 128
FT /note="K->R: Abolishes ubiquitination. No effect on
FT localization to the mitochondria. No effect on interaction
FT with BCL2L11, BIK, BBC3 or PMAIP1."
FT /evidence="ECO:0000269|PubMed:23563182"
FT MUTAGEN 131
FT /note="E->R: Abolishes Ca(2+) binding; when associated with
FT N-133."
FT /evidence="ECO:0000269|PubMed:21705382"
FT MUTAGEN 133
FT /note="D->N: Abolishes Ca(2+) binding; when associated with
FT R-131."
FT /evidence="ECO:0000269|PubMed:21705382"
FT MUTAGEN 178..191
FT /note="Missing: Abolishes interaction with NME2."
FT /evidence="ECO:0000269|PubMed:17532299"
FT CONFLICT 52
FT /note="A -> V (in Ref. 4; AAI04444)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="R -> W (in Ref. 4; AAI04444)"
FT /evidence="ECO:0000305"
FT HELIX 14..30
FT /evidence="ECO:0007829|PDB:4B4S"
FT HELIX 44..59
FT /evidence="ECO:0007829|PDB:4B4S"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:4B4S"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:4B4S"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:4B4S"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:4B4S"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:4B4S"
FT HELIX 133..151
FT /evidence="ECO:0007829|PDB:4B4S"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:4B4S"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:4B4S"
SQ SEQUENCE 204 AA; 23204 MW; 4B46B2DC472475CB CRC64;
MVDQLRERTT MADPLRERTE LLLADYLGYC AREPGTPEPA PSTPEAAVLR SAAARLRQIH
RSFFSAYLGY PGNRFELVAL MADSVLSDSP GPTWGRVVTL VTFAGTLLER GPLVTARWKK
WGFQPRLKEQ EGDVARDCQR LVALLSSRLM GQHRAWLQAQ GGWDGFCHFF RTPFPLAFWR
KQLVQAFLSC LLTTAFIYLW TRLL
