[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA). DOI=10.1073/pnas.83.14.5214; PubMed=3523487 [NCBI, ExPASy, EBI, Israel, Japan] Tsujimoto Y., Croce C.M.; "Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma."; Proc. Natl. Acad. Sci. U.S.A. 83:5214-5218(1986).
[2]	SEQUENCE REVISION TO 96; 110 AND 237. DOI=10.1093/nar/20.16.4187; PubMed=1508712 [NCBI, ExPASy, EBI, Israel, Japan] Eguchi Y., Ewert D.L., Tsujimoto Y.; "Isolation and characterization of the chicken bcl-2 gene: expression in a variety of tissues including lymphoid and neuronal organs in adult and embryo."; Nucleic Acids Res. 20:4187-4192(1992).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA). DOI=10.1016/0092-8674(86)90362-4; PubMed=2875799 [NCBI, ExPASy, EBI, Israel, Japan] Cleary M.L., Smith S.D., Sklar J.; "Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocation."; Cell 47:19-28(1986).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND VARIANT SER-7. PubMed=2834197 [NCBI, ExPASy, EBI, Israel, Japan] Seto M., Jaeger U., Hockett R.D., Graninger W., Bennett S., Goldman P., Korsmeyer S.J.; "Alternative promoters and exons, somatic mutation and deregulation of the Bcl-2-Ig fusion gene in lymphoma."; EMBO J. 7:123-131(1988).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT SER-7. PubMed=3285301 [NCBI, ExPASy, EBI, Israel, Japan] Hua C., Zorn S., Jensen J.P., Coupland R.W., Ko H.S., Wright J.J., Bakhshi A.; "Consequences of the t(14;18) chromosomal translocation in follicular lymphoma: deregulated expression of a chimeric and mutated BCL-2 gene."; Oncogene Res. 2:263-275(1988).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-43. NIEHS SNPs program; Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA). TISSUE=Testis; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[8]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131 (ISOFORM ALPHA), AND VARIANTS NON-HODGKIN LYMPHOMA SER-59 AND ILE-93. PubMed=1339299 [NCBI, ExPASy, EBI, Israel, Japan] Tanaka S., Louie D.C., Kant J.A., Reed J.C.; "Frequent incidence of somatic mutations in translocated BCL2 oncogenes of non-Hodgkin's lymphomas."; Blood 79:229-237(1992).
[9]	SUBCELLULAR LOCATION. DOI=10.1038/348334a0; PubMed=2250705 [NCBI, ExPASy, EBI, Israel, Japan] Hockenbery D., Nunez G., Milliman C., Schreiber R.D., Korsmeyer S.J.; "Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death."; Nature 348:334-336(1990).
[10]	MUTAGENESIS. DOI=10.1038/369321a0; PubMed=8183370 [NCBI, ExPASy, EBI, Israel, Japan] Yin X.-M., Oltvai Z.N., Korsmeyer S.J.; "BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax."; Nature 369:321-323(1994).
[11]	CLEAVAGE BY CASPASES, AND MUTAGENESIS. DOI=10.1126/science.278.5345.1966; PubMed=9395403 [NCBI, ExPASy, EBI, Israel, Japan] Cheng E.H.-Y., Kirsch D.G., Clem R.J., Ravi R., Kastan M.B., Bedi A., Ueno K., Hardwick J.M.; "Conversion of Bcl-2 to a Bax-like death effector by caspases."; Science 278:1966-1968(1997).
[12]	INTERACTION WITH TP53BP2. PubMed=8668206 [NCBI, ExPASy, EBI, Israel, Japan] Naumovski L., Cleary M.L.; "The p53-binding protein 53BP2 also interacts with Bcl2 and impedes cell cycle progression at G2/M."; Mol. Cell. Biol. 16:3884-3892(1996).
[13]	REVIEW ON PHOSPHORYLATION. DOI=10.1038/sj/leu/2402090; PubMed=11368354 [NCBI, ExPASy, EBI, Israel, Japan] Ruvolo P.P., Deng X., May W.S.; "Phosphorylation of Bcl2 and regulation of apoptosis."; Leukemia 15:515-522(2001).
[14]	PHOSPHORYLATION BY ASK1/JNK1. PubMed=10567572 [NCBI, ExPASy, EBI, Israel, Japan] Yamamoto K., Ichijo H., Korsmeyer S.J.; "BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M."; Mol. Cell. Biol. 19:8469-8478(1999).
[15]	INTERACTION WITH BBC3 AND BCL2L1. DOI=10.1016/S1097-2765(01)00213-1; PubMed=11463391 [NCBI, ExPASy, EBI, Israel, Japan] Yu J., Zhang L., Hwang P.M., Kinzler K.W., Vogelstein B.; "PUMA induces the rapid apoptosis of colorectal cancer cells."; Mol. Cell 7:673-682(2001).
[16]	INTERACTION WITH BNIPL. DOI=10.1016/S0006-291X(03)01387-1; PubMed=12901880 [NCBI, ExPASy, EBI, Israel, Japan] Qin W., Hu J., Guo M., Xu J., Li J., Yao G., Zhou X., Jiang H., Zhang P., Shen L., Wan D., Gu J.; "BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis."; Biochem. Biophys. Res. Commun. 308:379-385(2003).
[17]	INTERACTION WITH FKBP8. DOI=10.1016/j.febslet.2005.01.053; PubMed=15733859 [NCBI, ExPASy, EBI, Israel, Japan] Kang C.B., Tai J., Chia J., Yoon H.S.; "The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38)."; FEBS Lett. 579:1469-1476(2005).
[18]	INTERACTION WITH MRPL41. DOI=10.1002/jcb.20292; PubMed=15547950 [NCBI, ExPASy, EBI, Israel, Japan] Chintharlapalli S.R., Jasti M., Malladi S., Parsa K.V.L., Ballestero R.P., Gonzalez-Garcia M.; "BMRP is a Bcl-2 binding protein that induces apoptosis."; J. Cell. Biochem. 94:611-626(2005).
[19]	INTERACTION WITH FKBP8. DOI=10.1074/jbc.M606181200; PubMed=17090549 [NCBI, ExPASy, EBI, Israel, Japan] Portier B.P., Taglialatela G.; "Bcl-2 localized at the nuclear compartment induces apoptosis after transient overexpression."; J. Biol. Chem. 281:40493-40502(2006).
[20]	STRUCTURE BY NMR OF 1-207. DOI=10.1073/pnas.041619798; PubMed=11248023 [NCBI, ExPASy, EBI, Israel, Japan] Petros A.M., Medek A., Nettesheim D.G., Kim D.H., Yoon H.S., Swift K., Matayoshi E.D., Oltersdorf T., Fesik S.W.; "Solution structure of the antiapoptotic protein bcl-2."; Proc. Natl. Acad. Sci. U.S.A. 98:3012-3017(2001).
[21]	STRUCTURE BY NMR OF 45-207. DOI=10.1038/nature03579; PubMed=15902208 [NCBI, ExPASy, EBI, Israel, Japan] Oltersdorf T., Elmore S.W., Shoemaker A.R., Armstrong R.C., Augeri D.J., Belli B.A., Bruncko M., Deckwerth T.L., Dinges J., Hajduk P.J., Joseph M.K., Kitada S., Korsmeyer S.J., Kunzer A.R., Letai A., Li C., Mitten M.J., Nettesheim D.G., Ng S.-C., Nimmer P.M., O'Connor J.M., Oleksijew A., Petros A.M., Reed J.C., Shen W., Tahir S.K., Thompson C.B., Tomaselli K.J., Wang B., Wendt M.D., Zhang H., Fesik S.W., Rosenberg S.H.; "An inhibitor of Bcl-2 family proteins induces regression of solid tumours."; Nature 435:677-681(2005).
[22]	STRUCTURE BY NMR OF 44-207. DOI=10.1021/jm061152t; PubMed=17256834 [NCBI, ExPASy, EBI, Israel, Japan] Bruncko M., Oost T.K., Belli B.A., Ding H., Joseph M.K., Kunzer A., Martineau D., McClellan W.J., Mitten M., Ng S.-C., Nimmer P.M., Oltersdorf T., Park C.-M., Petros A.M., Shoemaker A.R., Song X., Wang X., Wendt M.D., Zhang H., Fesik S.W., Rosenberg S.H., Elmore S.W.; "Studies leading to potent, dual inhibitors of Bcl-2 and Bcl-xL."; J. Med. Chem. 50:641-662(2007).

Comments

FUNCTION: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1).
SUBUNIT: Forms homodimers, and heterodimers with BAX, BAD, BAK and Bcl-X(L). Heterodimerization with BAX requires intact BH1 and BH2 motifs, and is necessary for anti-apoptotic activity (By similarity). Also interacts with APAF1, RAF-1, TP53BP2, BBC3, BCL2L1, MRPL41 and BNIPL. Binding to FKBP8 seems to target BCL2 to the mitochondria and probably interferes with the binding of BCL2 to its targets.
INTERACTION:
Self; NbExp=2; IntAct=EBI-77694, EBI-77694;
Q92934:BAD; NbExp=3; IntAct=EBI-77694, EBI-700771;
Q61337:Bad (xeno); NbExp=3; IntAct=EBI-77694, EBI-400328;
Q16611:BAK1; NbExp=1; IntAct=EBI-77694, EBI-519866;
Q07812:BAX; NbExp=2; IntAct=EBI-77694, EBI-516580;
Q07813:Bax (xeno); NbExp=1; IntAct=EBI-77694, EBI-700711;
Q9BXH1:BBC3; NbExp=3; IntAct=EBI-77694, EBI-519884;
Q9BXH1-1:BBC3; NbExp=1; IntAct=EBI-77694, EBI-519891;
Q9BXH1-2:BBC3; NbExp=1; IntAct=EBI-77694, EBI-519896;
P51572:BCAP31; NbExp=2; IntAct=EBI-77694, EBI-77683;
Q07817-1:BCL2L1; NbExp=1; IntAct=EBI-77694, EBI-287195;
O43521:BCL2L11; NbExp=2; IntAct=EBI-77694, EBI-526406;
O43521-1:BCL2L11; NbExp=1; IntAct=EBI-77694, EBI-526416;
O43521-2:BCL2L11; NbExp=2; IntAct=EBI-77694, EBI-526420;
O54918:Bcl2l11 (xeno); NbExp=1; IntAct=EBI-77694, EBI-526067;
P55957:BID; NbExp=3; IntAct=EBI-77694, EBI-519672;
Q13323:BIK; NbExp=2; IntAct=EBI-77694, EBI-700794;
Q91ZE9:Bmf (xeno); NbExp=2; IntAct=EBI-77694, EBI-708032;
O60238:BNIP3L; NbExp=1; IntAct=EBI-77694, EBI-849893;
Q9C000:NLRP1; NbExp=5; IntAct=EBI-77694, EBI-1220518;
P22736:NR4A1; NbExp=3; IntAct=EBI-77694, EBI-721550;
P62136:PPP1CA; NbExp=1; IntAct=EBI-77694, EBI-357253;
P62140:PPP1CB; NbExp=1; IntAct=EBI-77694, EBI-352350;
P36873-1:PPP1CC; NbExp=1; IntAct=EBI-77694, EBI-356289;
O15304:SIVA1; NbExp=1; IntAct=EBI-77694, EBI-520756;
Q9H2V7:SPNS1; NbExp=1; IntAct=EBI-77694, EBI-1386527;
SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein.
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name Alpha

Isoform ID P10415-1

This is the isoform sequence displayed in this entry.

Name Beta

Isoform ID P10415-2

Features which should be applied to build the isoform sequence: VSP_000512.
TISSUE SPECIFICITY: Expressed in a variety of tissues.
DOMAIN: The BH4 motif is required for anti-apoptotic activity and for interaction with RAF-1.
PTM: Phosphorylation/dephosphorylation on Ser-70 regulates anti-apoptotic activity. Growth factor-stimulated phosphorylation on Ser-70 by PKC is required for the anti-apoptosis activity and occurs during the G2/M phase of the cell cycle. In the absence of growth factors, BCL2 appears to be phosphorylated by other protein kinases such as ERKs and stress-activated kinases. Dephosphorylated by protein phosphatase 2A (PP2A) (By similarity).
PTM: Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity, causes the release of cytochrome c into the cytosol promoting further caspase activity.
DISEASE: A chromosomal aberration involving BCL2 may be a cause of follicular lymphoma (FL) [MIM:151430]; also known as type II chronic lymphatic leukemia. Translocation t(14;18)(q32;q21) with immunoglobulin gene regions. BCL2 mutations found in non-Hodgkin lymphomas carrying the chromosomal translocation could be attributed to the Ig somatic hypermutation mechanism resulting in nucleotide transitions.
SIMILARITY: Belongs to the Bcl-2 family.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/BCL2ID49.html";.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/bcl2/";.
WEB RESOURCE: Name=Wikipedia; Note=Bcl-2 entry; URL="http://en.wikipedia.org/wiki/Bcl-2";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M13994; AAA51813.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M13995; AAA51814.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M14745; AAA35591.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X06487; CAA29778.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY220759; AAO26045.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027258; AAH27258.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S72602; AAD14111.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00020961; -.
IPI00217817; -.

PIR

B29409; TVHUB1.
C37332; TVHUA1.

RefSeq

NP_000624.2; -.

UniGene

Hs.150749

3D structure databases

PDB

1G5M; NMR; -; A=1-207.	[ExPASy / RCSB / EBI]
1GJH; NMR; -; A=1-207.	[ExPASy / RCSB / EBI]
1YSW; NMR; -; A=3-207.	[ExPASy / RCSB / EBI]
2O21; NMR; -; A=3-207.	[ExPASy / RCSB / EBI]
2O22; NMR; -; A=3-207.	[ExPASy / RCSB / EBI]
2O2F; NMR; -; A=8-204.	[ExPASy / RCSB / EBI]
2W3L; X-ray; 2.10 A; A/B=9-206.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1G5M; -.
1GJH; -.
1YSW; -.
2O21; -.
2O22; -.
2O2F; -.
2W3L; -.

DisProt

DP00297; -.

ModBase

P10415.

Protein-protein interaction databases

DIP

DIP:1043N; -.

IntAct

P10415; 32.

PTM databases

PhosphoSite

P10415; -.

Enzyme and pathway databases

Pathway_Interaction_DB

caspase_pathway; Caspase cascade in apoptosis.
ceramidepathway; Ceramide signaling pathway.
epopathway; EPO signaling pathway.
faspathway; FAS signaling pathway (CD95).
hivnefpathway; HIV-1 Nef: Negative effector of Fas and TNF-alpha.
il2_pi3kpathway; IL2 signaling events mediated by PI3K.
il2_stat5pathway; IL2 signaling events mediated by STAT5.
il2_1pathway; IL2-mediated signaling events.
nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
rxr_vdr_pathway; RXR and RAR hetrodimerization with other nuclear receptor.
kitpathway; Signaling events mediated by Stem cell factor receptor (c-Kit).

Reactome

REACT_578; Apoptosis.

Organism-specific databases

GC18M058941; -.

HIX0014496; -.

HGNC:990; BCL2.

CAB000003; -.

151430; gene+phenotype. [NCBI / EBI]

Orphanet

545; Follicular lymphoma.

PharmGKB

PA25302; -.

Gene expression databases

P10415; -.

P10415; -.

HS_BCL2; -.

ENSG00000171791; Homo sapiens.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005741;	Cellular component: mitochondrial outer membrane (inferred from direct assay from UniProtKB).
GO:0031965;	Cellular component: nuclear membrane (inferred from direct assay from UniProtKB).
GO:0051434;	Molecular function: BH3 domain binding (inferred from physical interaction from UniProtKB).
GO:0002020;	Molecular function: protease binding (inferred from direct assay from UniProtKB).
GO:0046982;	Molecular function: protein heterodimerization activity (inferred from physical interaction from UniProtKB).
GO:0042803;	Molecular function: protein homodimerization activity (inferred from direct assay from UniProtKB).
GO:0008633;	Biological process: activation of pro-apoptotic gene products (inferred from experiment from Reactome).
GO:0006916;	Biological process: anti-apoptosis (inferred from direct assay from UniProtKB).
GO:0070059;	Biological process: apoptosis in response to endoplasmic reticulum stress (inferred from direct assay from MGI).
GO:0042100;	Biological process: B cell proliferation (inferred from direct assay from MGI).
GO:0051607;	Biological process: defense response to virus (inferred from direct assay from UniProtKB).
GO:0007565;	Biological process: female pregnancy (non-traceable author statement from UniProtKB).
GO:0006959;	Biological process: humoral immune response (traceable author statement from UniProtKB).
GO:0032848;	Biological process: negative regulation of cellular pH reduction (inferred from direct assay from UniProtKB).
GO:0051902;	Biological process: negative regulation of mitochondrial depolarization (traceable author statement from UniProtKB).
GO:0043524;	Biological process: negative regulation of neuron apoptosis (inferred from direct assay from MGI).
GO:0051402;	Biological process: neuron apoptosis (traceable author statement from HGNC).
GO:0046902;	Biological process: regulation of mitochondrial membrane permeability (inferred from sequence or structural similarity from HGNC).
GO:0051881;	Biological process: regulation of mitochondrial membrane potential (inferred from sequence or structural similarity from HGNC).
GO:0043497;	Biological process: regulation of protein heterodimerization activity (inferred from direct assay from UniProtKB).
GO:0043496;	Biological process: regulation of protein homodimerization activity (inferred from direct assay from UniProtKB).
GO:0001836;	Biological process: release of cytochrome c from mitochondria (non-traceable author statement from UniProtKB).
GO:0034097;	Biological process: response to cytokine stimulus (inferred from direct assay from MGI).
GO:0042493;	Biological process: response to drug (inferred from direct assay from MGI).
GO:0010039;	Biological process: response to iron ion (inferred from direct assay from UniProtKB).
GO:0035094;	Biological process: response to nicotine (inferred from direct assay from UniProtKB).
GO:0009636;	Biological process: response to toxin (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR013278; Apop_reg_Bcl2.
IPR002475; BCL2_apoptsis.
IPR000712; Bcl2_BH.
IPR003093; Bcl2_BH4.
IPR004725; Bcl2_reg.
Graphical view of domain structure.

Pfam

PF00452; Bcl-2; 1.
PF02180; BH4; 1.
Pfam graphical view of domain structure.

PRINTS

PR01863; APOPREGBCL2.
PR01862; BCL2FAMILY.

SMART

SM00337; BCL; 1.
SM00265; BH4; 1.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00865; bcl-2; 1.

PROSITE

PS50062; BCL2_FAMILY; 1.
PS01080; BH1; 1.
PS01258; BH2; 1.
PS01259; BH3; 1.
PS01260; BH4_1; 1.
PS50063; BH4_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P10415; -.

Genome annotation databases

Ensembl

ENSG00000171791; Homo sapiens. [Contig view]

GeneID

596; -.

KEGG

hsa:596; -.

Phylogenomic databases

HOGENOM

P10415; -.

HOVERGEN

P10415; -.

OMA

P10415; GYEWEAG.

Other

DrugBank

DB01248; Docetaxel.
DB01073; Fludarabine.
DB01065; Melatonin.
DB01229; Paclitaxel.
DB01367; Rasagiline.

2423; -.

P10415; -.

BCL2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Apoptosis; Chromosomal rearrangement; Disease mutation; Endoplasmic reticulum; Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 239`	`239`	`Apoptosis regulator Bcl-2.`	`PRO_0000143048`
`TRANSMEM`	`212 233`	`22`	`Potential.`
`MOTIF`	`10 30`	`21`	`BH4.`
`MOTIF`	`93 107`	`15`	`BH3.`
`MOTIF`	`136 155`	`20`	`BH1.`
`MOTIF`	`187 202`	`16`	`BH2.`
`SITE`	`34 35`	`2`	`Cleavage; by caspase-3.`
`MOD_RES`	`70 70`		`Phosphoserine; by PKC (By similarity).`
`VAR_SEQ`	`196 239`		`DAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGA` `YLGHK -> VGASGDVS (in isoform Beta).`	`VSP_000512`
`VARIANT`	`7 7`	`1`	`T -> S.`	`VAR_000827`
`VARIANT`	`43 43`	`1`	`A -> T (in dbSNP:rs1800477 [NCBI]).`	`VAR_014716`
`VARIANT`	`59 59`	`1`	`P -> S (in non-Hodgkin lymphoma; somatic mutation).`	`VAR_000828`
`VARIANT`	`93 93`	`1`	`V -> I (in non-Hodgkin lymphoma; somatic mutation).`	`VAR_000829`
`MUTAGEN`	`34 34`		`D->A: Abolishes cleavage by caspase-3.`
`MUTAGEN`	`64 64`		`D->A: No effect on cleavage by caspase-3.`
`MUTAGEN`	`145 145`		`G->A: No heterodimerization with BAX and loss of anti-apoptotic activity.`
`MUTAGEN`	`188 188`		`W->A: No heterodimerization with BAX and loss of anti-apoptotic activity.`
`CONFLICT`	`48 48`		`I -> F (in Ref. 4; CAA29778).`
`CONFLICT`	`59 59`		`P -> T (in Ref. 3; AAA35591).`
`CONFLICT`	`96 96`		`T -> A (in Ref. 8; AAD14111).`
`CONFLICT`	`110 110`		`R -> G (in Ref. 8; AAD14111).`
`CONFLICT`	`117 117`		`S -> R (in Ref. 3; AAA35591).`
`CONFLICT`	`129 129`		`R -> C (in Ref. 4; CAA29778).`
`HELIX`	`52 65`	`14`
`TURN`	`73 75`	`3`
`STRAND`	`88 92`	`5`
`HELIX`	`93 108`	`16`
`STRAND`	`110 112`	`3`
`HELIX`	`114 117`	`4`
`HELIX`	`123 137`	`15`
`HELIX`	`144 163`	`20`
`HELIX`	`167 183`	`17`
`HELIX`	`185 192`	`8`
`HELIX`	`195 202`	`8`

Sequence information

Length: 239 AA [This is the length of the unprocessed precursor]

Molecular weight: 26266 Da [This is the MW of the unprocessed precursor]

CRC64: 3C49F2B714DC9CCB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAHAGRTGYD NREIVMKYIH YKLSQRGYEW DAGDVGAAPP GAAPAPGIFS SQPGHTPHPA 

        70         80         90        100        110        120 
ASRDPVARTS PLQTPAAPGA AAGPALSPVP PVVHLTLRQA GDDFSRRYRR DFAEMSSQLH 

       130        140        150        160        170        180 
LTPFTARGRF ATVVEELFRD GVNWGRIVAF FEFGGVMCVE SVNREMSPLV DNIALWMTEY 

       190        200        210        220        230 
LNRHLHTWIQ DNGGWDAFVE LYGPSMRPLF DFSWLSLKTL LSLALVGACI TLGAYLGHK

P10415 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools