ASpdb: an integrative knowledgebase of human protein isoforms from experimental and AI-predicted structures

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	Protein Summary
	AS Summary
	Protein Functional Features
	Gene Isoform Structures and Expression Levels
	Protein Structures
	pLDDT Score Distribution
	Ramachandran Plot of Protein Structures
	Potential Active Site Information
	Protein Structure and Feature Comparision
	Protein-Protein Interaction
	Related Drugs
	Related Diseases
	Clinically Important Variants

Protein:BCL2L11

Protein Summary

Gene summary

Gene name: BCL2L11
ASpdb.0 ID: 10018
	Gene
Gene symbol	BCL2L11
Gene ID	10018
Gene name	BCL2 like 11
Synonyms	BAM\|BIM\|BOD
Cytomap	2q13
Type of gene	protein-coding
Description	bcl-2-like protein 11BCL2-like 11 (apoptosis facilitator)bcl-2 interacting mediator of cell deathbcl-2 interacting protein Bimbcl-2-related ovarian death agonist
Modification date	20240411
UniProtAcc	O43521

Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez

Partner	Gene	GO ID	GO term	PubMed ID
Gene	BCL2L11	GO:0008630	intrinsic apoptotic signaling pathway in response to DNA damage	11546872
Gene	BCL2L11	GO:0031334	positive regulation of protein-containing complex assembly	21041309
Gene	BCL2L11	GO:0034976	response to endoplasmic reticulum stress	22761832
Gene	BCL2L11	GO:0042981	regulation of apoptotic process	18209102
Gene	BCL2L11	GO:2000271	positive regulation of fibroblast apoptotic process	11997495

AS Summary

Information of the canonical protein with experimentally identified structure from PDB (2023).

UniProt Acc	File name	PDB ID	Method	Resolution	Chain	Start	End
O43521-1	O43521-1_6x8o_A.pdb	6X8O	X-ray	1.31	A	141	166

ASpdb's canonical and alternatively spliced isoform information.

accession_id	gene_name	canonical_id	alternative_id	canonical_length	alternative_length	canonical_start	canonical_end	type	originalSEQ	variationSEQ	alternative_start	alternative_end
O43521	BCL2L11	O43521-1	O43521-10	198	135	133	135	Substitution	SMR	NWD	133	135
O43521	BCL2L11	O43521-1	O43521-10	198	135	136	198	Deletion	none	none	135	135
O43521	BCL2L11	O43521-1	O43521-11	198	135	132	135	Substitution	ASMR	GIFE	132	135
O43521	BCL2L11	O43521-1	O43521-11	198	135	136	198	Deletion	none	none	135	135
O43521	BCL2L11	O43521-1	O43521-12	198	198	42	75	Substitution	GNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFAT	VSLCHPGWSALVRSWLTATSNSQVQAVLLPQPPK	42	75
O43521	BCL2L11	O43521-1	O43521-13	198	44	43	44	Substitution	NP	IF	43	44
O43521	BCL2L11	O43521-1	O43521-13	198	44	45	198	Deletion	none	none	44	44
O43521	BCL2L11	O43521-1	O43521-14	198	140	132	140	Substitution	ASMRQAEPA	VREIEEVVV	132	140
O43521	BCL2L11	O43521-1	O43521-14	198	140	141	198	Deletion	none	none	140	140
O43521	BCL2L11	O43521-1	O43521-15	198	75	42	101	Deletion	none	none	41	41
O43521	BCL2L11	O43521-1	O43521-15	198	75	132	135	Substitution	ASMR	GIFE	72	75
O43521	BCL2L11	O43521-1	O43521-15	198	75	136	198	Deletion	none	none	75	75
O43521	BCL2L11	O43521-1	O43521-16	198	80	42	101	Deletion	none	none	41	41
O43521	BCL2L11	O43521-1	O43521-16	198	80	132	140	Substitution	ASMRQAEPA	VREIEEVVV	72	80
O43521	BCL2L11	O43521-1	O43521-16	198	80	141	198	Deletion	none	none	80	80
O43521	BCL2L11	O43521-1	O43521-17	198	112	42	101	Deletion	none	none	41	41
O43521	BCL2L11	O43521-1	O43521-17	198	112	132	198	Substitution	ASMRQAEPADMRPEIWIAQELRRIGDEFNAYYARRVFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH	VVILEDIGDLSLCFGFIFTGLDLYGHHHSQDTEQLNHKDFS	72	112
O43521	BCL2L11	O43521-1	O43521-18	198	103	42	101	Deletion	none	none	41	41
O43521	BCL2L11	O43521-1	O43521-18	198	103	132	166	Deletion	none	none	71	71
O43521	BCL2L11	O43521-1	O43521-19	198	163	132	166	Deletion	none	none	131	131
O43521	BCL2L11	O43521-1	O43521-2	198	138	42	101	Deletion	none	none	41	41
O43521	BCL2L11	O43521-1	O43521-20	198	73	42	166	Deletion	none	none	41	41
O43521	BCL2L11	O43521-1	O43521-3	198	108	42	131	Deletion	none	none	41	41
O43521	BCL2L11	O43521-1	O43521-4	198	169	167	198	Substitution	VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH	LEK	167	169
O43521	BCL2L11	O43521-1	O43521-5	198	109	42	101	Deletion	none	none	41	41
O43521	BCL2L11	O43521-1	O43521-5	198	109	167	198	Substitution	VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH	LEK	107	109
O43521	BCL2L11	O43521-1	O43521-6	198	79	42	131	Deletion	none	none	41	41
O43521	BCL2L11	O43521-1	O43521-6	198	79	167	198	Substitution	VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH	LEK	77	79
O43521	BCL2L11	O43521-1	O43521-7	198	85	42	131	Deletion	none	none	41	41
O43521	BCL2L11	O43521-1	O43521-7	198	85	167	198	Substitution	VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH	LAKLLASST	77	85
O43521	BCL2L11	O43521-1	O43521-8	198	172	167	198	Substitution	VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH	MPLPPD	167	172
O43521	BCL2L11	O43521-1	O43521-9	198	82	42	131	Deletion	none	none	41	41
O43521	BCL2L11	O43521-1	O43521-9	198	82	167	198	Substitution	VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH	MPLPPD	77	82

Multiple sequence alignment of our canonical and alternatively spliced BCL2L11

Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of BCL2L11

UniProt-id	ENSG	ENST	ENSP
O43521-1	ENSG00000153094.25	ENST00000393256.8	ENSP00000376943.2
O43521-10	ENSG00000153094.25	ENST00000431217.1	ENSP00000394640.1
O43521-14	ENSG00000153094.25	ENST00000436733.5	ENSP00000403727.1
O43521-16	ENSG00000153094.25	ENST00000415458.5	ENSP00000393781.1
O43521-17	ENSG00000153094.25	ENST00000405953.6	ENSP00000384641.1
O43521-2	ENSG00000153094.25	ENST00000308659.12	ENSP00000309226.8
O43521-7	ENSG00000153094.25	ENST00000439718.1	ENSP00000411137.1
O43521-8	ENSG00000153094.25	ENST00000437029.5	ENSP00000412892.1
O43521-9	ENSG00000153094.25	ENST00000452231.5	ENSP00000391292.1

UniProt-id	NM ID	NP ID
O43521-1	NM_138621.4	NP_619527.1
O43521-10	NM_138624.3	NP_619530.1
O43521-11	NM_138626.3	NP_619532.1
O43521-14	NM_001204109.1	NP_001191038.1
O43521-15	NM_001204111.1	NP_001191040.1
O43521-16	NM_001204112.1	NP_001191041.1
O43521-17	NM_207002.3	NP_996885.1
O43521-2	NM_006538.4	NP_006529.1
O43521-3	NM_001204106.1	NP_001191035.1
O43521-3	XM_005263559.2	XP_005263616.1
O43521-4	NM_138622.3	NP_619528.1
O43521-5	NM_138623.3	NP_619529.1
O43521-6	NM_207003.2	NP_996886.1
O43521-7	NM_001204107.1	NP_001191036.1
O43521-8	NM_001204108.1	NP_001191037.1
O43521-9	NM_001204110.1	NP_001191039.1

Amino acid sequences of our canonical and alternatively spliced BCL2L11

accession_id	Protein sequence
O43521-1	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQGNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFATRSPLFIFMRRSSLLS RSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASMRQAEPADMRPEIWIAQELRRIGDEFNAYYARRVFLNNYQAAEDHPR
O43521-10	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQGNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFATRSPLFIFMRRSSLLS
O43521-11	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQGNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFATRSPLFIFMRRSSLLS
O43521-12	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQVSLCHPGWSALVRSWLTATSNSQVQAVLLPQPPKRSPLFIFMRRSSLLS RSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASMRQAEPADMRPEIWIAQELRRIGDEFNAYYARRVFLNNYQAAEDHPR
O43521-13
O43521-14	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQGNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFATRSPLFIFMRRSSLLS
O43521-15
O43521-16
O43521-17	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMVVILEDIGDLSLCFGFIFT
O43521-18	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMVFLNNYQAAEDHPRMVILR
O43521-19	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQGNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFATRSPLFIFMRRSSLLS
O43521-2	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASMRQAEPADMRPEIWIAQ
O43521-20
O43521-3	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQASMRQAEPADMRPEIWIAQELRRIGDEFNAYYARRVFLNNYQAAEDHPR
O43521-4	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQGNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFATRSPLFIFMRRSSLLS
O43521-5	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASMRQAEPADMRPEIWIAQ
O43521-6
O43521-7
O43521-8	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQGNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFATRSPLFIFMRRSSLLS
O43521-9

Protein Functional Features

Main function of this protein. (from UniProt)

BCL2L11 (go to UniProt):O43521

Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at
download page
* Minus value of BPloci means that the break pointn is located before the CDS.

- Retained protein feature among the 13 regional features.

Accession_id	Subsection	Start	End	Funcitonal feature	Splicing information
O43521	Region	1	72	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=42;End=75
O43521	Region	1	72	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=43;End=44
O43521	Region	1	72	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=45;End=198
O43521	Region	1	72	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=42;End=101
O43521	Region	1	72	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=42;End=101
O43521	Region	1	72	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=42;End=101
O43521	Region	1	72	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=42;End=101
O43521	Region	1	72	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=42;End=101
O43521	Region	1	72	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=42;End=166
O43521	Region	1	72	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=42;End=131
O43521	Region	1	72	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=42;End=101
O43521	Region	1	72	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=42;End=131
O43521	Region	1	72	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=42;End=131
O43521	Region	1	72	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=42;End=131
O43521	Motif	148	162	Note=BH3	Type=Deletion;Start=136;End=198
O43521	Motif	148	162	Note=BH3	Type=Deletion;Start=136;End=198
O43521	Motif	148	162	Note=BH3	Type=Deletion;Start=45;End=198
O43521	Motif	148	162	Note=BH3	Type=Deletion;Start=141;End=198
O43521	Motif	148	162	Note=BH3	Type=Deletion;Start=136;End=198
O43521	Motif	148	162	Note=BH3	Type=Deletion;Start=141;End=198
O43521	Motif	148	162	Note=BH3	Type=Substitution;Start=132;End=198
O43521	Motif	148	162	Note=BH3	Type=Deletion;Start=132;End=166
O43521	Motif	148	162	Note=BH3	Type=Deletion;Start=132;End=166
O43521	Motif	148	162	Note=BH3	Type=Deletion;Start=42;End=166

Gene Isoform Structures and Expression Levels for BCL2L11

Gene structures of our canonical and alternative spliced genes of BCL2L11
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.

Expression levels of gene isoforms across GTEx.

Expression levels of gene isoforms across TCGA.

Protein Structures

PDB and CIF files of the predicted protein structures
* Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format.

3D view using mol* of O43521-1

3D view using mol* of O43521-10

3D view using mol* of O43521-11

3D view using mol* of O43521-12

3D view using mol* of O43521-13

3D view using mol* of O43521-14

3D view using mol* of O43521-15

3D view using mol* of O43521-16

3D view using mol* of O43521-17

3D view using mol* of O43521-18

3D view using mol* of O43521-19

3D view using mol* of O43521-2

3D view using mol* of O43521-20

3D view using mol* of O43521-3

3D view using mol* of O43521-4

3D view using mol* of O43521-5

3D view using mol* of O43521-6

3D view using mol* of O43521-7

3D view using mol* of O43521-8

3D view using mol* of O43521-9

pLDDT Score Distribution

pLDDT score distribution of the predicted protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.

pLDDT distribution across the protein length of O43521-1

pLDDT distribution across the protein length of O43521-10

pLDDT distribution across the protein length of O43521-12

pLDDT distribution across the protein length of O43521-13

pLDDT distribution across the protein length of O43521-14

pLDDT distribution across the protein length of O43521-15

pLDDT distribution across the protein length of O43521-16

pLDDT distribution across the protein length of O43521-17

pLDDT distribution across the protein length of O43521-18

pLDDT distribution across the protein length of O43521-19

pLDDT distribution across the protein length of O43521-2

pLDDT distribution across the protein length of O43521-20

pLDDT distribution across the protein length of O43521-3

pLDDT distribution across the protein length of O43521-4

pLDDT distribution across the protein length of O43521-5

pLDDT distribution across the protein length of O43521-6

pLDDT distribution across the protein length of O43521-7

pLDDT distribution across the protein length of O43521-8

pLDDT distribution across the protein length of O43521-9

Ramachandran Plot of Protein Structures

Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide.

Ramachandran plot of O43521-1

Ramachandran plot of O43521-11

Ramachandran plot of O43521-15

Ramachandran plot of O43521-16

Ramachandran plot of O43521-17

Ramachandran plot of O43521-18

Ramachandran plot of O43521-2

Ramachandran plot of O43521-20

Ramachandran plot of O43521-3

Ramachandran plot of O43521-4

Potential Active Site Information

The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite.

UniProt-id	Site score	Size	D score	Volume	Exposure	Enclosure	Contact	Phobic	Philic	Balance	Don/Acc	Residues
O43521-1	0.925	80	0.935	153.664	0.375	0.677	1	0.857	0.956	0.896	0.835	131,134,135,138,139,140,142,144,147,148
O43521-10	0.543	10	0.475	33.957	0.73	0.653	0.947	1.494	0.655	2.281	1.107	75,80,81,84,85
O43521-12	0.512	23	0.465	53.165	0.838	0.482	0.656	0.142	0.843	0.169	1.349	109,110,111,112,114,117,118,121
O43521-13	0.444	2	0.424	3.087	0.857	0.534	0.847	2.299	0.09	25.478	0.203	25,34,36
O43521-14	0.509	12	0.456	26.754	0.707	0.565	0.847	1.083	0.639	1.696	0.541	70,75,80,81,84,85
O43521-15	0.47	13	0.273	46.305	0.776	0.607	0.965	0.147	1.319	0.111	1.078	50,51,52,54,57,58,61,65
O43521-16	0.457	13	0.164	30.184	0.745	0.587	0.945	0	1.617	0	0.569	49,50,51,54,56,57,58
O43521-17	0.818	39	0.876	98.098	0.683	0.602	0.785	2.066	0.222	9.325	2.243	60,63,64,67,91,94,95,98,99
O43521-18	0.478	14	0.267	50.421	0.736	0.603	1.028	0.029	1.371	0.021	0.96	50,51,52,54,57,58,61
O43521-19	0.58	30	0.547	62.083	0.781	0.504	0.629	0.331	0.827	0.4	1.501	134,137,138,140,141,143,144,146,147,150
O43521-2	0.508	18	0.437	62.426	0.8	0.552	0.709	0.094	0.899	0.104	7.2	75,78,79,80,82,83,84,87,88
O43521-20	0.427	10	0.271	19.551	0.643	0.591	1.012	0.278	1.168	0.238	0.267	67,68,71
O43521-3	0.403	6	0.363	18.865	0.906	0.46	0.45	0.329	0.44	0.748	3.494	57,60,61,64
O43521-4	0.748	57	0.771	82.32	0.682	0.501	0.709	0.411	0.733	0.56	0.735	107,108,109,110,111,112,114,117,118,120,121,124
O43521-5	0.447	15	0.349	39.102	0.8	0.543	0.756	0.023	1.043	0.022	16.715	78,79,82,83,84,87
O43521-6	0.513	10	0.443	71.687	0.841	0.619	0.761	0.546	0.692	0.789	4.721	48,57,60,61
O43521-7	0.592	19	0.561	65.856	0.768	0.581	0.705	0.442	0.606	0.73	6.667	49,57,60,61,64
O43521-8	0.597	34	0.567	75.117	0.79	0.501	0.677	0.214	0.863	0.248	1.113	108,109,110,111,112,114,117,118,120,121,124
O43521-9	0.52	11	0.469	85.407	0.838	0.585	0.696	0.597	0.595	1.004	7.173	48,49,57,60,61,64

Protein Structure and Feature Comparision

Protein Structure Comparision Using Template Modeling Scores (TM-score).

Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green)

3D view using mol* of O43521-1_O43521-1_6x8o_A.pdb

Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green)

3D view using mol* of O43521-1_6x8o_A_O43521-10.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-11.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-12.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-13.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-14.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-15.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-16.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-17.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-18.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-19.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-2.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-20.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-3.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-4.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-5.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-6.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-7.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-8.pdb

3D view using mol* of O43521-1_6x8o_A_O43521-9.pdb

Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green)

3D view using mol* of O43521-1_O43521-10.pdb

3D view using mol* of O43521-1_O43521-11.pdb

3D view using mol* of O43521-1_O43521-12.pdb

3D view using mol* of O43521-1_O43521-13.pdb

3D view using mol* of O43521-1_O43521-14.pdb

3D view using mol* of O43521-1_O43521-15.pdb

3D view using mol* of O43521-1_O43521-16.pdb

3D view using mol* of O43521-1_O43521-17.pdb

3D view using mol* of O43521-1_O43521-18.pdb

3D view using mol* of O43521-1_O43521-19.pdb

3D view using mol* of O43521-1_O43521-2.pdb

3D view using mol* of O43521-1_O43521-20.pdb

3D view using mol* of O43521-1_O43521-3.pdb

3D view using mol* of O43521-1_O43521-4.pdb

3D view using mol* of O43521-1_O43521-5.pdb

3D view using mol* of O43521-1_O43521-6.pdb

3D view using mol* of O43521-1_O43521-7.pdb

3D view using mol* of O43521-1_O43521-8.pdb

3D view using mol* of O43521-1_O43521-9.pdb

Protein Feature Comparison of the protein sequendary structures among the protiens.

./stats/secondary_structure/figure/O43521-1_vs_O43521-10.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-11.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-12.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-13.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-14.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-15.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-16.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-17.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-18.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-19.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-2.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-20.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-3.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-4.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-5.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-6.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-7.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-8.png

./stats/secondary_structure/figure/O43521-1_vs_O43521-9.png

Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens.

./stats/relative_asa/O43521-1_vs_O43521-10.png

./stats/relative_asa/O43521-1_vs_O43521-11.png

./stats/relative_asa/O43521-1_vs_O43521-12.png

./stats/relative_asa/O43521-1_vs_O43521-13.png

./stats/relative_asa/O43521-1_vs_O43521-14.png

./stats/relative_asa/O43521-1_vs_O43521-15.png

./stats/relative_asa/O43521-1_vs_O43521-16.png

./stats/relative_asa/O43521-1_vs_O43521-17.png

./stats/relative_asa/O43521-1_vs_O43521-18.png

./stats/relative_asa/O43521-1_vs_O43521-19.png

./stats/relative_asa/O43521-1_vs_O43521-2.png

./stats/relative_asa/O43521-1_vs_O43521-20.png

./stats/relative_asa/O43521-1_vs_O43521-3.png

./stats/relative_asa/O43521-1_vs_O43521-4.png

./stats/relative_asa/O43521-1_vs_O43521-5.png

./stats/relative_asa/O43521-1_vs_O43521-6.png

./stats/relative_asa/O43521-1_vs_O43521-7.png

./stats/relative_asa/O43521-1_vs_O43521-8.png

./stats/relative_asa/O43521-1_vs_O43521-9.png

Protein-Protein Interaction

Interactors from UniProt.

Accession_id

Subsection

Start

End

Funcitonal feature

Splicing information

Interactors from STRING.

Gene name

Interactors

Related Drugs to BCL2L11

Drugs targeting this gene/protein.
(DrugBank)

UniProt accession

Gene name

DrugBank ID

Drug name

Drug group

Actions

Related Diseases to BCL2L11

Previous studies relating to the alternative splicing of BCL2L11 and disease information from the MeSH term (PubMed)

Gene	PMID	Title	Abstract	MeSH ID	MeSH term
BCL2L11	23737756	GLIS3, a susceptibility gene for type 1 and type 2 diabetes, modulates pancreatic beta cell apoptosis via regulation of a splice variant of the BH3-only protein Bim.	Mutations in human Gli-similar (GLIS) 3 protein cause neonatal diabetes. The GLIS3 gene region has also been identified as a susceptibility risk locus for both type 1 and type 2 diabetes. GLIS3 plays a role in the generation of pancreatic beta cells and in insulin gene expression, but there is no information on the role of this gene on beta cell viability and/or susceptibility to immune- and metabolic-induced stress. GLIS3 knockdown (KD) in INS-1E cells, primary FACS-purified rat beta cells, and human islet cells decreased expression of MafA, Ins2, and Glut2 and inhibited glucose oxidation and insulin secretion, confirming the role of this transcription factor for the beta cell differentiated phenotype. GLIS3 KD increased beta cell apoptosis basally and sensitized the cells to death induced by pro-inflammatory cytokines (interleukin 1Î² + interferon-Î³) or palmitate, agents that may contribute to beta cell loss in respectively type 1 and 2 diabetes. The increased cell death was due to activation of the intrinsic (mitochondrial) pathway of apoptosis, as indicated by cytochrome c release to the cytosol, Bax translocation to the mitochondria and activation of caspases 9 and 3. Analysis of the pathways implicated in beta cell apoptosis following GLIS3 KD indicated modulation of alternative splicing of the pro-apoptotic BH3-only protein Bim, favouring expression of the pro-death variant BimS via inhibition of the splicing factor SRp55. KD of Bim abrogated the pro-apoptotic effect of GLIS3 loss of function alone or in combination with cytokines or palmitate. The present data suggest that altered expression of the candidate gene GLIS3 may contribute to both type 1 and 2 type diabetes by favouring beta cell apoptosis. This is mediated by alternative splicing of the pro-apoptotic protein Bim and exacerbated formation of the most pro-apoptotic variant BimS.	D003922	Diabetes Mellitus, Type 1
BCL2L11	23737756	GLIS3, a susceptibility gene for type 1 and type 2 diabetes, modulates pancreatic beta cell apoptosis via regulation of a splice variant of the BH3-only protein Bim.	Mutations in human Gli-similar (GLIS) 3 protein cause neonatal diabetes. The GLIS3 gene region has also been identified as a susceptibility risk locus for both type 1 and type 2 diabetes. GLIS3 plays a role in the generation of pancreatic beta cells and in insulin gene expression, but there is no information on the role of this gene on beta cell viability and/or susceptibility to immune- and metabolic-induced stress. GLIS3 knockdown (KD) in INS-1E cells, primary FACS-purified rat beta cells, and human islet cells decreased expression of MafA, Ins2, and Glut2 and inhibited glucose oxidation and insulin secretion, confirming the role of this transcription factor for the beta cell differentiated phenotype. GLIS3 KD increased beta cell apoptosis basally and sensitized the cells to death induced by pro-inflammatory cytokines (interleukin 1Î² + interferon-Î³) or palmitate, agents that may contribute to beta cell loss in respectively type 1 and 2 diabetes. The increased cell death was due to activation of the intrinsic (mitochondrial) pathway of apoptosis, as indicated by cytochrome c release to the cytosol, Bax translocation to the mitochondria and activation of caspases 9 and 3. Analysis of the pathways implicated in beta cell apoptosis following GLIS3 KD indicated modulation of alternative splicing of the pro-apoptotic BH3-only protein Bim, favouring expression of the pro-death variant BimS via inhibition of the splicing factor SRp55. KD of Bim abrogated the pro-apoptotic effect of GLIS3 loss of function alone or in combination with cytokines or palmitate. The present data suggest that altered expression of the candidate gene GLIS3 may contribute to both type 1 and 2 type diabetes by favouring beta cell apoptosis. This is mediated by alternative splicing of the pro-apoptotic protein Bim and exacerbated formation of the most pro-apoptotic variant BimS.	D003924	Diabetes Mellitus, Type 2

Clinically important variants in BCL2L11

(ClinVar, 04/20/2024)

accession_id

uniprot_id

gene_name

Type

Variant

Clinical_significance