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1.A.21.1.1
Apoptosis regulator Bcl-X(L) of 233 aas.  Also called Bcl2-like protein 1, isoform 1. Membrane insertion of the soluble form has been characterized (Vargas-Uribe et al. 2013).  The cytosolic domain of Bcl-2 forms small pores in the mitochondrial outer membrane (Peng et al. 2009).

Accession Number:Q07817
Protein Name:Bcl-X aka BCL2L1 aka BCL2L
Length:233
Molecular Weight:26049.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Mitochondrion membrane1 / Single-pass membrane protein2 / Cytoplasmic side3
Substrate small molecules

Cross database links:

Genevestigator: Q07817
eggNOG: prNOG07177
HEGENOM: HBG717457
DIP: DIP-328N
RefSeq: NP_001182.1    NP_612815.1   
Entrez Gene ID: 598   
Pfam: PF00452    PF02180   
Drugbank: Drugbank Link   
OMIM: 600039  gene
KEGG: hsa:598   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005741 C:mitochondrial outer membrane
GO:0031965 C:nuclear membrane
GO:0042802 F:identical protein binding
GO:0008634 P:negative regulation of survival gene produc...
GO:0046902 P:regulation of mitochondrial membrane permea...
GO:0051881 P:regulation of mitochondrial membrane potential
GO:0001836 P:release of cytochrome c from mitochondria
GO:0034097 P:response to cytokine stimulus

References (20)

[1] “bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death.”  Boise L.H.et.al.   8358789
[2] “Identification of a human cDNA encoding a novel Bcl-x isoform.”  Ban J.et.al.   9675101
[3] “The full-ORF clone resource of the German cDNA consortium.”  Bechtel S.et.al.   17974005
[4] “The DNA sequence and comparative analysis of human chromosome 20.”  Deloukas P.et.al.   11780052
[5] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[6] “Multiple Bcl-2 family members demonstrate selective dimerizations with Bax.”  Sedlak T.W.et.al.   7644501
[7] “Bax-independent inhibition of apoptosis by Bcl-XL.”  Cheng E.H.-Y.et.al.   8596636
[8] “Modulation of cell death by Bcl-xL through caspase interaction.”  Clem R.J.et.al.   9435230
[9] “Characterization of Bax-sigma, a cell death-inducing isoform of Bax.”  Schmitt E.et.al.   10772918
[10] “PUMA induces the rapid apoptosis of colorectal cancer cells.”  Yu J.et.al.   11463391
[11] “Siva-1 binds to and inhibits BCL-X(L)-mediated protection against UV radiation-induced apoptosis.”  Xue L.et.al.   12011449
[12] “PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the redox-regulated Keap1-dependent ubiquitin ligase complex.”  Lo S.-C.et.al.   17046835
[13] “X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death.”  Muchmore S.W.et.al.   8692274
[14] “Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis.”  Sattler M.et.al.   9020082
[15] “Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies.”  Petros A.M.et.al.   11206074
[16] “Bcl-XL mutations suppress cellular sensitivity to antimycin A.”  Manion M.K.et.al.   14534311
[17] “An inhibitor of Bcl-2 family proteins induces regression of solid tumours.”  Oltersdorf T.et.al.   15902208
[18] “BCL-XL dimerization by three-dimensional domain swapping.”  O'Neill J.W.et.al.   16368107
[19] “Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein.”  Oberstein A.et.al.   17337444
[20] “Studies leading to potent, dual inhibitors of Bcl-2 and Bcl-xL.”  Bruncko M.et.al.   17256834
Structure:
1BXL   1G5J   1LXL   1MAZ   1R2D   1R2E   1R2G   1R2H   1R2I   1YSG   [...more]

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEG TESEMETPSA INGNPSWHLA 
61:	DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY 
121:	QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL CVESVDKEMQ VLVSRIAAWM ATYLNDHLEP 
181:	WIQENGGWDT FVELYGNNAA AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK