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|---|---|
| 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 | molecule |
Cross database links:
| DIP: | DIP-328N |
|---|---|
| RefSeq: | NP_001182.1 NP_612815.1 |
| Entrez Gene ID: | 598 |
| Pfam: | PF00452 PF02180 |
| 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
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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 | |
| Structure: | |
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External Searches:
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Analyze:
| Predict TMSs (Predict number of transmembrane segments) | ||||
| FASTA formatted sequence |
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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