Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bcl-2-like protein 1

Gene

BCL2L1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.
Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F1F0 activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785).1 Publication
Isoform Bcl-X(S) promotes apoptosis.

GO - Molecular functioni

  • BH3 domain binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: GO_Central
  • protein homodimerization activity Source: GO_Central
  • protein kinase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis, Endocytosis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000171552-MONOMER.
ReactomeiR-HSA-111453. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
R-HSA-844455. The NLRP1 inflammasome.
SIGNORiQ07817.

Protein family/group databases

TCDBi1.A.21.1.1. the bcl-2 (bcl-2) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Bcl-2-like protein 1
Short name:
Bcl2-L-1
Alternative name(s):
Apoptosis regulator Bcl-X
Gene namesi
Name:BCL2L1
Synonyms:BCL2L, BCLX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:992. BCL2L1.

Subcellular locationi

Isoform Bcl-X(L) :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei210 – 226HelicalSequence analysisAdd BLAST17

GO - Cellular componenti

  • Bcl-2 family protein complex Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial inner membrane Source: UniProtKB-SubCell
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrial outer membrane Source: UniProtKB
  • mitochondrion Source: HGNC
  • nuclear membrane Source: UniProtKB-SubCell
  • synaptic vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion outer membrane, Nucleus, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi49S → A: Less stable at G2 checkpoint after DNA damage. 1 Publication1
Mutagenesisi61D → A: No cleavage by caspase-1 nor by caspase-3. 1 Publication1
Mutagenesisi131 – 133FRD → VRA: No heterodimerization with BAX. 1 Publication3
Mutagenesisi135 – 137VNW → AIL: Loss of anti-apoptotic activity. 1 Publication3
Mutagenesisi138 – 140GRI → ELN: Loss of anti-apoptotic activity. 1 Publication3
Mutagenesisi138G → A: No heterodimerization with BAX. 1 Publication1
Mutagenesisi145 – 147SFG → YCC: Decreases interaction with DNM1L, no effect on endocytosis enhancement. 1 Publication3
Mutagenesisi148G → E: No heterodimerization with BAX. 1 Publication1
Mutagenesisi156D → A: No effect on caspase-1 cleavage. 1 Publication1
Mutagenesisi176D → A: No effect on caspase-1 cleavage. 1 Publication1
Mutagenesisi188 – 191WDTF → SVTC: Abolishes interaction with DNM1L and endocytosis enhancement. 1 Publication4
Mutagenesisi188 – 189WD → GA: Reduces anti-apoptotic activity by about half. 1 Publication2
Mutagenesisi189D → A: No effect on caspase-1 cleavage. 1 Publication1

Organism-specific databases

DisGeNETi598.
OpenTargetsiENSG00000171552.
PharmGKBiPA76.

Chemistry databases

ChEMBLiCHEMBL4625.
GuidetoPHARMACOLOGYi2845.

Polymorphism and mutation databases

BioMutaiBCL2L1.
DMDMi728955.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001430621 – 233Bcl-2-like protein 1Add BLAST233

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei49Phosphoserine; by PLK31 Publication1
Modified residuei62Phosphoserine; by CDK11 Publication1

Post-translational modificationi

Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity.1 Publication
Phosphorylated on Ser-62 by CDK1. This phosphorylation is partial in normal mitotic cells, but complete in G2-arrested cells upon DNA-damage, thus promoting subsequent apoptosis probably by triggering caspases-mediated proteolysis. Phosphorylated by PLK3, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Phosphorylation at Ser-49 appears during the S phase and G2, disappears rapidly in early mitosis during prometaphase, metaphase and early anaphase, and re-appears during telophase and cytokinesis.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei61 – 62Cleavage; by caspase-12

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ07817.
MaxQBiQ07817.
PaxDbiQ07817.
PeptideAtlasiQ07817.
PRIDEiQ07817.
TopDownProteomicsiQ07817-1. [Q07817-1]
Q07817-2. [Q07817-2]

PTM databases

iPTMnetiQ07817.
PhosphoSitePlusiQ07817.

Miscellaneous databases

PMAP-CutDBQ07817.

Expressioni

Tissue specificityi

Bcl-X(S) is expressed at high levels in cells that undergo a high rate of turnover, such as developing lymphocytes. In contrast, Bcl-X(L) is found in tissues containing long-lived postmitotic cells, such as adult brain.

Gene expression databases

BgeeiENSG00000171552.
CleanExiHS_BCL2L1.
ExpressionAtlasiQ07817. baseline and differential.
GenevisibleiQ07817. HS.

Organism-specific databases

HPAiCAB000105.
CAB072801.
CAB072802.
HPA035734.

Interactioni

Subunit structurei

Homodimer. Isoform Bcl-X(L) forms heterodimers with BAX, BAK or BCL2. Heterodimerization with BAX does not seem to be required for anti-apoptotic activity. Interacts with BCL2L11. Interacts with BAD. Interacts (isoform Bcl-X(L)) with SIVA1 (isoform 1); the interaction inhibits the anti-apoptotic activity. Interacts with BECN1 and PGAM5. Isoform Bcl-X(L) interacts with IKZF3. Interacts with HEBP2. Isoform Bcl-X(L) interacts with BOP/C22orf29. Interacts with p53/TP53 and BBC3; interaction with BBC3 disrupts the interaction with p53/TP53. Isoform Bcl-X(L) interacts with DNM1L and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may form a complex in synaptic vesicles that also contains clathrin and MFF. Interacts with ATP5A and ATP5B; the interactions mediate the association of isoform Bcl-X(L) with the mitochondrial membrane ATP synthase F1F0 ATP synthase. Interacts with VDAC1 (PubMed:25296756). Isoform Bcl-X(L) interacts (via the loop between motifs BH4 and BH3) with NLRP1 (via LRR repeats), but not with NLRP2, NLRP3, NLRP4, PYCARD, nor MEFV (PubMed:17418785). Interacts with BCL2L11 (via BH3) (PubMed:27013495).14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-78035,EBI-78035
BADQ929347EBI-78035,EBI-700771
BadQ613372EBI-287195,EBI-400328From a different organism.
BAK1Q1661112EBI-287195,EBI-519866
BAXQ0781213EBI-287195,EBI-516580
BBC3Q9BXH17EBI-287195,EBI-519884
Bbc3Q99ML13EBI-287195,EBI-727801From a different organism.
BCL2L11O4352110EBI-287195,EBI-526406
BCL2L11O43521-12EBI-287195,EBI-526416
BECN1Q144575EBI-287195,EBI-949378
BIDP559576EBI-287195,EBI-519672
BIKQ133239EBI-78035,EBI-700794
BMFQ96LC97EBI-78035,EBI-3919268
BOPQ7L3V23EBI-287195,EBI-10697720
ced-4P30429-22EBI-78035,EBI-536271From a different organism.
CLUP10909-46EBI-287195,EBI-4322678
CYCSP999992EBI-78035,EBI-446479
HRKO001983EBI-287195,EBI-701322
NLRP1Q9C0009EBI-78035,EBI-1220518
SIVA1O153042EBI-287195,EBI-520756
SIVA1O15304-15EBI-287195,EBI-520766
SPNS1Q9H2V73EBI-78035,EBI-1386527
TP53P0463718EBI-287195,EBI-366083
Tp53P023403EBI-287195,EBI-474016From a different organism.
TP53BP2Q136254EBI-287195,EBI-77642
VRK2Q86Y07-12EBI-287195,EBI-1207633

GO - Molecular functioni

  • BH3 domain binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: GO_Central
  • protein homodimerization activity Source: GO_Central
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107070. 94 interactors.
DIPiDIP-30916N.
IntActiQ07817. 66 interactors.
MINTiMINT-89538.
STRINGi9606.ENSP00000302564.

Chemistry databases

BindingDBiQ07817.

Structurei

Secondary structure

1233
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 18Combined sources16
Turni19 – 21Combined sources3
Helixi24 – 26Combined sources3
Beta strandi29 – 36Combined sources8
Beta strandi38 – 41Combined sources4
Turni42 – 44Combined sources3
Beta strandi50 – 53Combined sources4
Beta strandi56 – 59Combined sources4
Turni65 – 68Combined sources4
Turni70 – 73Combined sources4
Beta strandi82 – 84Combined sources3
Helixi85 – 101Combined sources17
Helixi102 – 104Combined sources3
Helixi108 – 111Combined sources4
Turni112 – 114Combined sources3
Turni116 – 118Combined sources3
Helixi120 – 130Combined sources11
Turni131 – 133Combined sources3
Helixi137 – 156Combined sources20
Helixi162 – 177Combined sources16
Helixi179 – 184Combined sources6
Turni185 – 187Combined sources3
Helixi188 – 198Combined sources11
Helixi199 – 205Combined sources7
Beta strandi206 – 208Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BXLNMR-A1-209[»]
1G5JNMR-A1-209[»]
1LXLNMR-A1-209[»]
1MAZX-ray2.20A1-209[»]
1R2DX-ray1.95A1-211[»]
1R2EX-ray2.10A1-211[»]
1R2GX-ray2.70A1-211[»]
1R2HX-ray2.20A1-211[»]
1R2IX-ray2.00A1-211[»]
1YSGNMR-A1-209[»]
1YSINMR-A1-209[»]
1YSNNMR-A1-209[»]
2B48X-ray3.45A1-211[»]
2LP8NMR-A1-209[»]
2LPCNMR-A1-209[»]
2M03NMR-A1-209[»]
2M04NMR-A1-209[»]
2ME8NMR-A1-209[»]
2ME9NMR-A1-209[»]
2MEJNMR-A1-209[»]
2O1YNMR-A1-209[»]
2O2MNMR-A2-20[»]
A83-196[»]
2O2NNMR-A2-20[»]
A83-196[»]
2P1LX-ray2.50A/C/E/G1-209[»]
2PONNMR-B1-196[»]
2YJ1X-ray2.24A/C1-209[»]
2YQ6X-ray1.80A1-209[»]
2YQ7X-ray1.90A1-209[»]
2YXJX-ray2.20A/B1-209[»]
3CVAX-ray2.70X1-211[»]
3FDLX-ray1.78A1-209[»]
3FDMX-ray2.26A/B/C1-209[»]
3INQX-ray2.00A/B1-209[»]
3IO8X-ray2.30A/C1-209[»]
3PL7X-ray2.61A/B1-209[»]
3QKDX-ray2.02A/B1-209[»]
3R85X-ray1.95A/B/C/D1-197[»]
3SP7X-ray1.40A1-209[»]
3SPFX-ray1.70A1-209[»]
3WIZX-ray2.45A/B1-209[»]
3ZK6X-ray2.48A/B1-209[»]
3ZLNX-ray2.29A1-209[»]
3ZLOX-ray2.60A1-209[»]
3ZLRX-ray2.03A/B1-209[»]
4A1UX-ray1.54A1-209[»]
4A1WX-ray2.50A/B/C/D1-209[»]
4AQ3X-ray2.40A/B/C/D/E/F29-44[»]
4BPKX-ray1.76A/B1-209[»]
4C52X-ray2.05A/B1-209[»]
4C5DX-ray2.30A/B1-209[»]
4CINX-ray2.69A/B1-209[»]
C/D79-102[»]
4EHRX-ray2.09A1-209[»]
4HNJX-ray2.90A/B1-209[»]
4IEHX-ray2.10A29-44[»]
4PPIX-ray2.85A1-209[»]
4QVEX-ray2.05A1-209[»]
4QVFX-ray1.53A1-209[»]
4QVXX-ray2.10A/B1-23[»]
A/B83-209[»]
4TUHX-ray1.80A/B/C/D/E/F/G/H1-209[»]
4Z9VX-ray2.10A/B1-208[»]
5AGWX-ray2.69A/B29-44[»]
5AGXX-ray2.24A/B29-44[»]
5C3GX-ray2.45A83-209[»]
5FMJX-ray2.43A1-209[»]
5FMKX-ray1.73A1-209[»]
DisProtiDP00298.
ProteinModelPortaliQ07817.
SMRiQ07817.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07817.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi4 – 24BH4Add BLAST21
Motifi86 – 100BH3Add BLAST15
Motifi129 – 148BH1Add BLAST20
Motifi180 – 195BH2Add BLAST16

Domaini

The BH4 motif is required for anti-apoptotic activity. The BH1 and BH2 motifs are required for both heterodimerization with other Bcl-2 family members and for repression of cell death.
The loop between motifs BH4 and BH3 is required for the interaction with NLRP1.1 Publication

Sequence similaritiesi

Belongs to the Bcl-2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4728. Eukaryota.
ENOG41123S0. LUCA.
GeneTreeiENSGT00530000062935.
HOGENOMiHOG000056452.
InParanoidiQ07817.
KOiK04570.
OMAiNGSPSWH.
OrthoDBiEOG091G0OCU.
PhylomeDBiQ07817.
TreeFamiTF315834.

Family and domain databases

InterProiIPR013279. Apop_reg_BclX.
IPR002475. Bcl2-like.
IPR004725. Bcl2/BclX.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
IPR003093. Bcl2_BH4.
IPR020731. Bcl2_BH4_motif_CS.
IPR026298. Blc2_fam.
[Graphical view]
PANTHERiPTHR11256. PTHR11256. 1 hit.
PTHR11256:SF12. PTHR11256:SF12. 1 hit.
PfamiPF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]
PRINTSiPR01864. APOPREGBCLX.
PR01862. BCL2FAMILY.
SMARTiSM00265. BH4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00865. bcl-2. 1 hit.
PROSITEiPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01259. BH3. 1 hit.
PS01260. BH4_1. 1 hit.
PS50063. BH4_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Bcl-X(L) (identifier: Q07817-1) [UniParc]FASTAAdd to basket
Also known as: Bcl-xL

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEG TESEMETPSA
60 70 80 90 100
INGNPSWHLA DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR
110 120 130 140 150
YRRAFSDLTS QLHITPGTAY QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL
160 170 180 190 200
CVESVDKEMQ VLVSRIAAWM ATYLNDHLEP WIQENGGWDT FVELYGNNAA
210 220 230
AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK
Length:233
Mass (Da):26,049
Last modified:February 1, 1995 - v1
Checksum:iE09D3CDD851AE9BE
GO
Isoform Bcl-X(S) (identifier: Q07817-2) [UniParc]FASTAAdd to basket
Also known as: Bcl-xS

The sequence of this isoform differs from the canonical sequence as follows:
     126-188: Missing.

Show »
Length:170
Mass (Da):18,894
Checksum:i75D1FC01EC06AD47
GO
Isoform Bcl-X(beta) (identifier: Q07817-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     189-233: DTFVELYGNN...VLLGSLFSRK → VRTKPLVCPF...CWVIVGDVDS

Show »
Length:227
Mass (Da):25,290
Checksum:i1EF621E5D0744E4E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti70G → A in CAA80661 (PubMed:8358789).Curated1
Sequence conflicti168A → V in CAI56777 (PubMed:17974005).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000515126 – 188Missing in isoform Bcl-X(S). CuratedAdd BLAST63
Alternative sequenceiVSP_000516189 – 233DTFVE…LFSRK → VRTKPLVCPFSLASGQRSPT ALLLYLFLLCWVIVGDVDS in isoform Bcl-X(beta). CuratedAdd BLAST45

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z23115 mRNA. Translation: CAA80661.1.
Z23116 mRNA. Translation: CAA80662.1.
U72398 Genomic DNA. Translation: AAB17354.1.
CR936637 mRNA. Translation: CAI56777.1.
BT007208 mRNA. Translation: AAP35872.1.
AL160175, AL117381 Genomic DNA. Translation: CAI12811.1.
AL117381, AL160175 Genomic DNA. Translation: CAI23025.1.
CH471077 Genomic DNA. Translation: EAW76424.1.
CH471077 Genomic DNA. Translation: EAW76425.1.
CH471077 Genomic DNA. Translation: EAW76429.1.
BC019307 mRNA. Translation: AAH19307.1.
CCDSiCCDS13188.1. [Q07817-2]
CCDS13189.1. [Q07817-1]
PIRiB47537.
JE0203.
RefSeqiNP_001182.1. NM_001191.3. [Q07817-2]
NP_001304848.1. NM_001317919.1. [Q07817-1]
NP_001304849.1. NM_001317920.1. [Q07817-1]
NP_001304850.1. NM_001317921.1. [Q07817-1]
NP_001309168.1. NM_001322239.1. [Q07817-1]
NP_001309169.1. NM_001322240.1. [Q07817-1]
NP_001309171.1. NM_001322242.1. [Q07817-1]
NP_612815.1. NM_138578.2. [Q07817-1]
XP_011527266.1. XM_011528964.2. [Q07817-1]
XP_016883482.1. XM_017027993.1. [Q07817-1]
UniGeneiHs.516966.
Hs.732176.

Genome annotation databases

EnsembliENST00000307677; ENSP00000302564; ENSG00000171552. [Q07817-1]
ENST00000376055; ENSP00000365223; ENSG00000171552. [Q07817-2]
ENST00000376062; ENSP00000365230; ENSG00000171552. [Q07817-1]
GeneIDi598.
KEGGihsa:598.
UCSCiuc002wwl.4. human. [Q07817-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z23115 mRNA. Translation: CAA80661.1.
Z23116 mRNA. Translation: CAA80662.1.
U72398 Genomic DNA. Translation: AAB17354.1.
CR936637 mRNA. Translation: CAI56777.1.
BT007208 mRNA. Translation: AAP35872.1.
AL160175, AL117381 Genomic DNA. Translation: CAI12811.1.
AL117381, AL160175 Genomic DNA. Translation: CAI23025.1.
CH471077 Genomic DNA. Translation: EAW76424.1.
CH471077 Genomic DNA. Translation: EAW76425.1.
CH471077 Genomic DNA. Translation: EAW76429.1.
BC019307 mRNA. Translation: AAH19307.1.
CCDSiCCDS13188.1. [Q07817-2]
CCDS13189.1. [Q07817-1]
PIRiB47537.
JE0203.
RefSeqiNP_001182.1. NM_001191.3. [Q07817-2]
NP_001304848.1. NM_001317919.1. [Q07817-1]
NP_001304849.1. NM_001317920.1. [Q07817-1]
NP_001304850.1. NM_001317921.1. [Q07817-1]
NP_001309168.1. NM_001322239.1. [Q07817-1]
NP_001309169.1. NM_001322240.1. [Q07817-1]
NP_001309171.1. NM_001322242.1. [Q07817-1]
NP_612815.1. NM_138578.2. [Q07817-1]
XP_011527266.1. XM_011528964.2. [Q07817-1]
XP_016883482.1. XM_017027993.1. [Q07817-1]
UniGeneiHs.516966.
Hs.732176.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BXLNMR-A1-209[»]
1G5JNMR-A1-209[»]
1LXLNMR-A1-209[»]
1MAZX-ray2.20A1-209[»]
1R2DX-ray1.95A1-211[»]
1R2EX-ray2.10A1-211[»]
1R2GX-ray2.70A1-211[»]
1R2HX-ray2.20A1-211[»]
1R2IX-ray2.00A1-211[»]
1YSGNMR-A1-209[»]
1YSINMR-A1-209[»]
1YSNNMR-A1-209[»]
2B48X-ray3.45A1-211[»]
2LP8NMR-A1-209[»]
2LPCNMR-A1-209[»]
2M03NMR-A1-209[»]
2M04NMR-A1-209[»]
2ME8NMR-A1-209[»]
2ME9NMR-A1-209[»]
2MEJNMR-A1-209[»]
2O1YNMR-A1-209[»]
2O2MNMR-A2-20[»]
A83-196[»]
2O2NNMR-A2-20[»]
A83-196[»]
2P1LX-ray2.50A/C/E/G1-209[»]
2PONNMR-B1-196[»]
2YJ1X-ray2.24A/C1-209[»]
2YQ6X-ray1.80A1-209[»]
2YQ7X-ray1.90A1-209[»]
2YXJX-ray2.20A/B1-209[»]
3CVAX-ray2.70X1-211[»]
3FDLX-ray1.78A1-209[»]
3FDMX-ray2.26A/B/C1-209[»]
3INQX-ray2.00A/B1-209[»]
3IO8X-ray2.30A/C1-209[»]
3PL7X-ray2.61A/B1-209[»]
3QKDX-ray2.02A/B1-209[»]
3R85X-ray1.95A/B/C/D1-197[»]
3SP7X-ray1.40A1-209[»]
3SPFX-ray1.70A1-209[»]
3WIZX-ray2.45A/B1-209[»]
3ZK6X-ray2.48A/B1-209[»]
3ZLNX-ray2.29A1-209[»]
3ZLOX-ray2.60A1-209[»]
3ZLRX-ray2.03A/B1-209[»]
4A1UX-ray1.54A1-209[»]
4A1WX-ray2.50A/B/C/D1-209[»]
4AQ3X-ray2.40A/B/C/D/E/F29-44[»]
4BPKX-ray1.76A/B1-209[»]
4C52X-ray2.05A/B1-209[»]
4C5DX-ray2.30A/B1-209[»]
4CINX-ray2.69A/B1-209[»]
C/D79-102[»]
4EHRX-ray2.09A1-209[»]
4HNJX-ray2.90A/B1-209[»]
4IEHX-ray2.10A29-44[»]
4PPIX-ray2.85A1-209[»]
4QVEX-ray2.05A1-209[»]
4QVFX-ray1.53A1-209[»]
4QVXX-ray2.10A/B1-23[»]
A/B83-209[»]
4TUHX-ray1.80A/B/C/D/E/F/G/H1-209[»]
4Z9VX-ray2.10A/B1-208[»]
5AGWX-ray2.69A/B29-44[»]
5AGXX-ray2.24A/B29-44[»]
5C3GX-ray2.45A83-209[»]
5FMJX-ray2.43A1-209[»]
5FMKX-ray1.73A1-209[»]
DisProtiDP00298.
ProteinModelPortaliQ07817.
SMRiQ07817.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107070. 94 interactors.
DIPiDIP-30916N.
IntActiQ07817. 66 interactors.
MINTiMINT-89538.
STRINGi9606.ENSP00000302564.

Chemistry databases

BindingDBiQ07817.
ChEMBLiCHEMBL4625.
GuidetoPHARMACOLOGYi2845.

Protein family/group databases

TCDBi1.A.21.1.1. the bcl-2 (bcl-2) family.

PTM databases

iPTMnetiQ07817.
PhosphoSitePlusiQ07817.

Polymorphism and mutation databases

BioMutaiBCL2L1.
DMDMi728955.

Proteomic databases

EPDiQ07817.
MaxQBiQ07817.
PaxDbiQ07817.
PeptideAtlasiQ07817.
PRIDEiQ07817.
TopDownProteomicsiQ07817-1. [Q07817-1]
Q07817-2. [Q07817-2]

Protocols and materials databases

DNASUi598.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307677; ENSP00000302564; ENSG00000171552. [Q07817-1]
ENST00000376055; ENSP00000365223; ENSG00000171552. [Q07817-2]
ENST00000376062; ENSP00000365230; ENSG00000171552. [Q07817-1]
GeneIDi598.
KEGGihsa:598.
UCSCiuc002wwl.4. human. [Q07817-1]

Organism-specific databases

CTDi598.
DisGeNETi598.
GeneCardsiBCL2L1.
HGNCiHGNC:992. BCL2L1.
HPAiCAB000105.
CAB072801.
CAB072802.
HPA035734.
MIMi600039. gene.
neXtProtiNX_Q07817.
OpenTargetsiENSG00000171552.
PharmGKBiPA76.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4728. Eukaryota.
ENOG41123S0. LUCA.
GeneTreeiENSGT00530000062935.
HOGENOMiHOG000056452.
InParanoidiQ07817.
KOiK04570.
OMAiNGSPSWH.
OrthoDBiEOG091G0OCU.
PhylomeDBiQ07817.
TreeFamiTF315834.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000171552-MONOMER.
ReactomeiR-HSA-111453. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
R-HSA-844455. The NLRP1 inflammasome.
SIGNORiQ07817.

Miscellaneous databases

ChiTaRSiBCL2L1. human.
EvolutionaryTraceiQ07817.
GeneWikiiBCL2-like_1_(gene).
GenomeRNAii598.
PMAP-CutDBQ07817.
PROiQ07817.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000171552.
CleanExiHS_BCL2L1.
ExpressionAtlasiQ07817. baseline and differential.
GenevisibleiQ07817. HS.

Family and domain databases

InterProiIPR013279. Apop_reg_BclX.
IPR002475. Bcl2-like.
IPR004725. Bcl2/BclX.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
IPR003093. Bcl2_BH4.
IPR020731. Bcl2_BH4_motif_CS.
IPR026298. Blc2_fam.
[Graphical view]
PANTHERiPTHR11256. PTHR11256. 1 hit.
PTHR11256:SF12. PTHR11256:SF12. 1 hit.
PfamiPF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]
PRINTSiPR01864. APOPREGBCLX.
PR01862. BCL2FAMILY.
SMARTiSM00265. BH4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00865. bcl-2. 1 hit.
PROSITEiPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01259. BH3. 1 hit.
PS01260. BH4_1. 1 hit.
PS50063. BH4_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiB2CL1_HUMAN
AccessioniPrimary (citable) accession number: Q07817
Secondary accession number(s): E1P5L6
, Q5CZ89, Q5TE65, Q92976
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 201 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.