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:BIN1

Protein Summary

Gene summary

Gene name: BIN1
ASpdb.0 ID: 274
	Gene
Gene symbol	BIN1
Gene ID	274
Gene name	bridging integrator 1
Synonyms	AMPH2\|AMPHL\|CNM2\|SH3P9
Cytomap	2q14.3
Type of gene	protein-coding
Description	myc box-dependent-interacting protein 1amphiphysin 2amphiphysin IIamphiphysin-like proteinbox dependant MYC interacting protein 1box-dependent myc-interacting protein 1
Modification date	20240305
UniProtAcc	O00499

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

Partner	Gene	GO ID	GO term	PubMed ID
Gene	BIN1	GO:0000122	negative regulation of transcription by RNA polymerase II	10412034
Gene	BIN1	GO:0005634	nucleus	8782822\|25051234
Gene	BIN1	GO:0005737	cytoplasm	25051234
Gene	BIN1	GO:0005829	cytosol	-
Gene	BIN1	GO:0005856	cytoskeleton	25051234
Gene	BIN1	GO:0010564	regulation of cell cycle process	8782822
Gene	BIN1	GO:0016020	membrane	16530520\|25051234
Gene	BIN1	GO:0030424	axon	23399914
Gene	BIN1	GO:0033292	T-tubule organization	24755653
Gene	BIN1	GO:0043065	positive regulation of apoptotic process	16530520
Gene	BIN1	GO:0051015	actin filament binding	26506308

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
O00499-1	O00499-1_2fic_B.pdb	2FIC	X-ray	1.99	B	40	271

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
O00499	BIN1	O00499-1	O00499-10	593	424	174	204	Deletion	none	none	173	173
O00499	BIN1	O00499-1	O00499-10	593	424	285	285	Substitution	P	PRKKSKLFSRLRRKKN	254	269
O00499	BIN1	O00499-1	O00499-10	593	424	335	487	Deletion	none	none	318	318
O00499	BIN1	O00499-1	O00499-11	593	497	174	204	Deletion	none	none	173	173
O00499	BIN1	O00499-1	O00499-11	593	497	285	285	Substitution	P	PRKKSKLFSRLRRKKN	254	269
O00499	BIN1	O00499-1	O00499-11	593	497	378	457	Deletion	none	none	361	361
O00499	BIN1	O00499-1	O00499-2	593	518	174	204	Deletion	none	none	173	173
O00499	BIN1	O00499-1	O00499-2	593	518	378	421	Deletion	none	none	346	346
O00499	BIN1	O00499-1	O00499-3	593	506	335	421	Deletion	none	none	334	334
O00499	BIN1	O00499-1	O00499-4	593	475	174	204	Deletion	none	none	173	173
O00499	BIN1	O00499-1	O00499-4	593	475	335	421	Deletion	none	none	303	303
O00499	BIN1	O00499-1	O00499-5	593	550	335	377	Deletion	none	none	334	334
O00499	BIN1	O00499-1	O00499-6	593	482	174	204	Deletion	none	none	173	173
O00499	BIN1	O00499-1	O00499-6	593	482	378	457	Deletion	none	none	346	346
O00499	BIN1	O00499-1	O00499-7	593	439	174	204	Deletion	none	none	173	173
O00499	BIN1	O00499-1	O00499-7	593	439	335	457	Deletion	none	none	303	303
O00499	BIN1	O00499-1	O00499-8	593	454	174	204	Deletion	none	none	173	173
O00499	BIN1	O00499-1	O00499-8	593	454	285	285	Substitution	P	PRKKSKLFSRLRRKKN	254	269
O00499	BIN1	O00499-1	O00499-8	593	454	335	457	Deletion	none	none	318	318
O00499	BIN1	O00499-1	O00499-9	593	409	174	204	Deletion	none	none	173	173
O00499	BIN1	O00499-1	O00499-9	593	409	335	487	Deletion	none	none	303	303

Multiple sequence alignment of our canonical and alternatively spliced BIN1

Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of BIN1

UniProt-id	ENSG	ENST	ENSP
O00499-1	ENSG00000136717.15	ENST00000316724.10	ENSP00000316779.5
O00499-10	ENSG00000136717.15	ENST00000376113.6	ENSP00000365281.2
O00499-11	ENSG00000136717.15	ENST00000259238.8	ENSP00000259238.4
O00499-2	ENSG00000136717.15	ENST00000346226.7	ENSP00000315411.3
O00499-3	ENSG00000136717.15	ENST00000351659.7	ENSP00000315388.3
O00499-4	ENSG00000136717.15	ENST00000393041.7	ENSP00000376761.3
O00499-5	ENSG00000136717.15	ENST00000357970.7	ENSP00000350654.3
O00499-6	ENSG00000136717.15	ENST00000393040.7	ENSP00000376760.3
O00499-7	ENSG00000136717.15	ENST00000409400.1	ENSP00000386797.1
O00499-8	ENSG00000136717.15	ENST00000352848.8	ENSP00000315284.4
O00499-9	ENSG00000136717.15	ENST00000348750.8	ENSP00000259237.5

UniProt-id	NM ID	NP ID
O00499-1	NM_139343.2	NP_647593.1
O00499-10	NM_001320632.1	NP_001307561.1
O00499-11	NM_139346.2	NP_647596.1
O00499-2	NM_139347.2	NP_647597.1
O00499-3	NM_139345.2	NP_647595.1
O00499-4	NM_139349.2	NP_647599.1
O00499-5	NM_139344.2	NP_647594.1
O00499-6	NM_139348.2	NP_647598.1
O00499-7	NM_139350.2	NP_647600.1
O00499-8	NM_004305.3	NP_004296.1
O00499-9	NM_139351.2	NP_647601.1

Amino acid sequences of our canonical and alternatively spliced BIN1

accession_id	Protein sequence
O00499-1	MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVY EPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEK AAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGL EKQHGSNTFTVKAQPSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQLRKGPPVPPPPKHTPSKEVKQEQILS LFEDTFVPEISVTTPSQFEAPGPFSEQASLLDLDFDPLPPVTSPVKAPTPSGQSIPWDLWEPTESPAGSLPSGEPSAAEGTFAVSWPSQT AEPGPAQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPAVVVETFPATVNGTVEGGSGAGRLDLPPGFMFKVQAQHDYTATDTDELQ
O00499-10	MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVY EPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKAEEELIK AQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGLEKQHGSNTFTVKAQPRKKSKLFSRLRRKKNS DNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQSSLPAVVVETFPATVNGTVEGGSGAGRLDLPPGFMFKVQAQH
O00499-11	MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVY EPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKAEEELIK AQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGLEKQHGSNTFTVKAQPRKKSKLFSRLRRKKNS DNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQLRKGPPVPPPPKHTPSKEVKQEQILSLFEDTFVPEISVTTPS QPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPAVVVETFPATVNGTVEGGSGAGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDV
O00499-2	MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVY EPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKAEEELIK AQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPD GSPAATPEIRVNHEPEPAGGATPGATLPKSPSQLRKGPPVPPPPKHTPSKEVKQEQILSLFEDTFVPEISVTTPSQPTESPAGSLPSGEP SAAEGTFAVSWPSQTAEPGPAQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPAVVVETFPATVNGTVEGGSGAGRLDLPPGFMFKV
O00499-3	MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVY EPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEK AAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGL EKQHGSNTFTVKAQPSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQPTESPAGSLPSGEPSAAEGTFAVSWP SQTAEPGPAQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPAVVVETFPATVNGTVEGGSGAGRLDLPPGFMFKVQAQHDYTATDTD
O00499-4	MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVY EPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKAEEELIK AQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPD GSPAATPEIRVNHEPEPAGGATPGATLPKSPSQPTESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPAQPAEASEVAGGTQPAAGAQEPG ETAASEAASSSLPAVVVETFPATVNGTVEGGSGAGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKE
O00499-5	MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVY EPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEK AAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGL EKQHGSNTFTVKAQPSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQFEAPGPFSEQASLLDLDFDPLPPVTS PVKAPTPSGQSIPWDLWEPTESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPAQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPAV VVETFPATVNGTVEGGSGAGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGV
O00499-6	MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVY EPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKAEEELIK AQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPD GSPAATPEIRVNHEPEPAGGATPGATLPKSPSQLRKGPPVPPPPKHTPSKEVKQEQILSLFEDTFVPEISVTTPSQPAEASEVAGGTQPA AGAQEPGETAASEAASSSLPAVVVETFPATVNGTVEGGSGAGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEG
O00499-7	MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVY EPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKAEEELIK AQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPD GSPAATPEIRVNHEPEPAGGATPGATLPKSPSQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPAVVVETFPATVNGTVEGGSGAGR
O00499-8	MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVY EPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKAEEELIK AQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGLEKQHGSNTFTVKAQPRKKSKLFSRLRRKKNS DNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPAVVVETFP ATVNGTVEGGSGAGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFT
O00499-9	MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVY EPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKAEEELIK AQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPD GSPAATPEIRVNHEPEPAGGATPGATLPKSPSQSSLPAVVVETFPATVNGTVEGGSGAGRLDLPPGFMFKVQAQHDYTATDTDELQLKAG

Protein Functional Features

Main function of this protein. (from UniProt)

BIN1 (go to UniProt):O00499

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
O00499	Domain	29	276	Note=BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00361	Type=Deletion;Start=174;End=204
O00499	Domain	29	276	Note=BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00361	Type=Deletion;Start=174;End=204
O00499	Domain	29	276	Note=BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00361	Type=Deletion;Start=174;End=204
O00499	Domain	29	276	Note=BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00361	Type=Deletion;Start=174;End=204
O00499	Domain	29	276	Note=BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00361	Type=Deletion;Start=174;End=204
O00499	Domain	29	276	Note=BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00361	Type=Deletion;Start=174;End=204
O00499	Domain	29	276	Note=BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00361	Type=Deletion;Start=174;End=204
O00499	Domain	29	276	Note=BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00361	Type=Deletion;Start=174;End=204
O00499	Region	280	354	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=285;End=285
O00499	Region	280	354	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=335;End=487
O00499	Region	280	354	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=285;End=285
O00499	Region	280	354	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=335;End=421
O00499	Region	280	354	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=335;End=421
O00499	Region	280	354	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=335;End=377
O00499	Region	280	354	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=335;End=457
O00499	Region	280	354	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=285;End=285
O00499	Region	280	354	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=335;End=457
O00499	Region	280	354	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=335;End=487
O00499	Region	378	421	Note=Clathrin-binding	Type=Deletion;Start=335;End=487
O00499	Region	378	421	Note=Clathrin-binding	Type=Deletion;Start=378;End=457
O00499	Region	378	421	Note=Clathrin-binding	Type=Deletion;Start=378;End=421
O00499	Region	378	421	Note=Clathrin-binding	Type=Deletion;Start=335;End=421
O00499	Region	378	421	Note=Clathrin-binding	Type=Deletion;Start=335;End=421
O00499	Region	378	421	Note=Clathrin-binding	Type=Deletion;Start=378;End=457
O00499	Region	378	421	Note=Clathrin-binding	Type=Deletion;Start=335;End=457
O00499	Region	378	421	Note=Clathrin-binding	Type=Deletion;Start=335;End=457
O00499	Region	378	421	Note=Clathrin-binding	Type=Deletion;Start=335;End=487
O00499	Region	400	488	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=335;End=487
O00499	Region	400	488	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=378;End=457
O00499	Region	400	488	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=378;End=421
O00499	Region	400	488	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=335;End=421
O00499	Region	400	488	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=335;End=421
O00499	Region	400	488	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=378;End=457
O00499	Region	400	488	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=335;End=457
O00499	Region	400	488	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=335;End=457
O00499	Region	400	488	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=335;End=487
O00499	Coiled coil	193	267	Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=174;End=204
O00499	Coiled coil	193	267	Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=174;End=204
O00499	Coiled coil	193	267	Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=174;End=204
O00499	Coiled coil	193	267	Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=174;End=204
O00499	Coiled coil	193	267	Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=174;End=204
O00499	Coiled coil	193	267	Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=174;End=204
O00499	Coiled coil	193	267	Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=174;End=204
O00499	Coiled coil	193	267	Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=174;End=204

Gene Isoform Structures and Expression Levels for BIN1

Gene structures of our canonical and alternative spliced genes of BIN1
* 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 O00499-1

3D view using mol* of O00499-10

3D view using mol* of O00499-11

3D view using mol* of O00499-2

3D view using mol* of O00499-3

3D view using mol* of O00499-4

3D view using mol* of O00499-5

3D view using mol* of O00499-6

3D view using mol* of O00499-7

3D view using mol* of O00499-8

3D view using mol* of O00499-9

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 O00499-1

pLDDT distribution across the protein length of O00499-10

pLDDT distribution across the protein length of O00499-11

pLDDT distribution across the protein length of O00499-2

pLDDT distribution across the protein length of O00499-3

pLDDT distribution across the protein length of O00499-4

pLDDT distribution across the protein length of O00499-5

pLDDT distribution across the protein length of O00499-6

pLDDT distribution across the protein length of O00499-7

pLDDT distribution across the protein length of O00499-8

pLDDT distribution across the protein length of O00499-9

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 O00499-1

Ramachandran plot of O00499-3

Ramachandran plot of O00499-5

Ramachandran plot of O00499-6

Ramachandran plot of O00499-7

Ramachandran plot of O00499-8

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
O00499-1	1.002	77	1.056	220.549	0.469	0.707	1.002	1.852	0.591	3.133	3.61	160,163,164,167,168,171,172,175,179,191,194,195,19 7,198,201,202
O00499-10	1.009	302	0.999	884.254	0.555	0.712	0.915	0.517	1.129	0.458	0.928	13,16,17,20,21,23,24,26,27,30,55,59,62,127,130,131 ,133,134,135,137,138,142,145,146,149,152,153,155,1 56,159,160,170,173,174,177,180,181,184,365,367,368 ,369,370,371,381,382,383,384,385,388,389,390,391,3 93,395,408,409,410,412,413,414
O00499-11	1.008	458	1.02	1570.94	0.575	0.71	0.885	0.407	1.062	0.383	1.105	16,17,19,20,21,23,24,26,27,28,29,30,31,35,36,37,38 ,39,40,41,44,45,48,51,52,55,62,127,130,133,134,135 ,137,138,140,141,142,143,144,145,146,147,148,149,1 52,153,155,156,158,159,177,180,181,184,331,332,333 ,334,335,336,337,338,339,342,343,346,439,440,441,4 42,443,456,457,458,460,461,462,463,464,466,468,482 ,483,485,486,487
O00499-2	1.027	357	1.013	1084.909	0.519	0.738	0.96	0.562	1.134	0.495	0.895	17,19,20,21,23,24,26,27,30,39,40,41,42,44,45,48,51 ,52,55,59,62,127,130,133,134,135,137,138,140,141,1 42,143,144,145,146,147,148,149,152,153,155,156,159 ,174,177,180,181,184,460,461,462,463,464,477,478,4 79,481,482,483,484,485,487,489,503,505,506,507,508
O00499-3	0.999	330	1.009	1102.059	0.588	0.696	0.877	0.429	1.068	0.402	0.962	17,19,20,21,23,24,26,27,28,30,38,39,40,41,44,45,48 ,51,52,55,131,133,134,135,137,138,139,140,141,142, 143,144,145,146,147,148,149,152,153,155,156,159,20 8,211,212,215,216,447,448,449,450,451,452,453,465, 466,467,469,470,471,472,473,475,477,480,491,492,49 4,495,496
O00499-4	1.008	371	1	1129.156	0.573	0.709	0.89	0.414	1.121	0.369	1.021	17,19,20,21,22,23,24,26,27,28,30,31,38,39,40,41,44 ,45,48,131,134,135,137,138,139,140,141,142,143,144 ,145,146,147,148,149,151,152,153,155,156,159,174,1 77,180,181,401,402,416,417,418,419,420,421,422,432 ,433,434,435,436,438,439,440,441,442,444,446,459,4 60,463,464,465
O00499-5	1.011	247	1.032	953.197	0.595	0.71	0.911	0.476	1.026	0.464	0.908	13,14,16,17,19,20,21,23,24,26,27,134,135,137,138,1 39,141,142,145,146,149,152,153,155,156,205,208,211 ,212,215,492,493,494,495,496,497,509,510,511,514,5 15,516,517,519,521,535,536,538,539,540
O00499-6	0.997	448	1.018	1570.254	0.61	0.689	0.836	0.375	1.028	0.364	1.276	17,20,21,23,24,26,27,28,30,31,32,34,35,36,37,38,39 ,40,41,44,45,48,51,52,55,62,130,131,133,134,135,13 7,138,139,140,141,142,143,144,145,146,147,148,149, 152,153,155,156,158,159,160,162,170,173,174,177,18 0,181,184,185,314,317,318,319,320,321,322,324,327, 424,425,426,427,428,429,439,440,441,442,443,445,44 6,447,448,449,451,453,467,468,470,471,472
O00499-7	1.024	258	1.012	788.214	0.566	0.734	0.909	0.47	1.129	0.416	0.846	17,20,24,28,31,32,38,39,40,41,44,45,48,51,52,55,59 ,62,127,130,133,134,135,137,138,140,141,142,143,14 4,145,146,147,148,188,379,382,383,384,385,386,396, 397,398,399,400,402,403,404,405,408,410,424,425,42 6,427,428,429
O00499-8	1.017	366	1.041	1159.34	0.582	0.712	0.886	0.579	1.001	0.578	1.01	17,19,20,21,23,24,26,27,28,30,31,32,38,39,40,41,44 ,45,48,51,52,55,59,62,63,66,127,130,133,134,135,13 7,138,139,140,141,142,143,144,145,146,147,148,149, 152,153,155,156,173,174,177,180,181,397,398,399,40 0,401,413,414,415,417,418,419,420,423,425,439,440, 441,442,443,444
O00499-9	1.029	180	0.985	527.534	0.537	0.742	0.939	0.408	1.228	0.333	1.115	21,24,55,59,62,66,127,130,131,133,134,135,137,138, 140,141,142,145,146,352,353,354,355,368,369,370,37 3,374,375,378,380,394,395,397,398,399

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 O00499-1_O00499-1_2fic_B.pdb

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

3D view using mol* of O00499-1_2fic_B_O00499-10.pdb

3D view using mol* of O00499-1_2fic_B_O00499-11.pdb

3D view using mol* of O00499-1_2fic_B_O00499-2.pdb

3D view using mol* of O00499-1_2fic_B_O00499-3.pdb

3D view using mol* of O00499-1_2fic_B_O00499-4.pdb

3D view using mol* of O00499-1_2fic_B_O00499-5.pdb

3D view using mol* of O00499-1_2fic_B_O00499-6.pdb

3D view using mol* of O00499-1_2fic_B_O00499-7.pdb

3D view using mol* of O00499-1_2fic_B_O00499-8.pdb

3D view using mol* of O00499-1_2fic_B_O00499-9.pdb

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

3D view using mol* of O00499-1_O00499-10.pdb

3D view using mol* of O00499-1_O00499-11.pdb

3D view using mol* of O00499-1_O00499-2.pdb

3D view using mol* of O00499-1_O00499-3.pdb

3D view using mol* of O00499-1_O00499-4.pdb

3D view using mol* of O00499-1_O00499-5.pdb

3D view using mol* of O00499-1_O00499-6.pdb

3D view using mol* of O00499-1_O00499-7.pdb

3D view using mol* of O00499-1_O00499-8.pdb

3D view using mol* of O00499-1_O00499-9.pdb

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

./stats/secondary_structure/figure/O00499-1_vs_O00499-10.png

./stats/secondary_structure/figure/O00499-1_vs_O00499-11.png

./stats/secondary_structure/figure/O00499-1_vs_O00499-2.png

./stats/secondary_structure/figure/O00499-1_vs_O00499-3.png

./stats/secondary_structure/figure/O00499-1_vs_O00499-4.png

./stats/secondary_structure/figure/O00499-1_vs_O00499-5.png

./stats/secondary_structure/figure/O00499-1_vs_O00499-6.png

./stats/secondary_structure/figure/O00499-1_vs_O00499-7.png

./stats/secondary_structure/figure/O00499-1_vs_O00499-8.png

./stats/secondary_structure/figure/O00499-1_vs_O00499-9.png

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

./stats/relative_asa/O00499-1_vs_O00499-10.png

./stats/relative_asa/O00499-1_vs_O00499-11.png

./stats/relative_asa/O00499-1_vs_O00499-2.png

./stats/relative_asa/O00499-1_vs_O00499-3.png

./stats/relative_asa/O00499-1_vs_O00499-4.png

./stats/relative_asa/O00499-1_vs_O00499-5.png

./stats/relative_asa/O00499-1_vs_O00499-6.png

./stats/relative_asa/O00499-1_vs_O00499-7.png

./stats/relative_asa/O00499-1_vs_O00499-8.png

./stats/relative_asa/O00499-1_vs_O00499-9.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 BIN1

Drugs targeting this gene/protein.
(DrugBank)

UniProt accession

Gene name

DrugBank ID

Drug name

Drug group

Actions

Related Diseases to BIN1

Previous studies relating to the alternative splicing of BIN1 and disease information from the MeSH term (PubMed)

Gene	PMID	Title	Abstract	MeSH ID	MeSH term
BIN1	21623381	Misregulated alternative splicing of BIN1 is associated with T tubule alterations and muscle weakness in myotonic dystrophy.	Myotonic dystrophy is the most common muscular dystrophy in adults and the first recognized example of an RNA-mediated disease. Congenital myotonic dystrophy (CDM1) and myotonic dystrophy of type 1 (DM1) or of type 2 (DM2) are caused by the expression of mutant RNAs containing expanded CUG or CCUG repeats, respectively. These mutant RNAs sequester the splicing regulator Muscleblind-like-1 (MBNL1), resulting in specific misregulation of the alternative splicing of other pre-mRNAs. We found that alternative splicing of the bridging integrator-1 (BIN1) pre-mRNA is altered in skeletal muscle samples of people with CDM1, DM1 and DM2. BIN1 is involved in tubular invaginations of membranes and is required for the biogenesis of muscle T tubules, which are specialized skeletal muscle membrane structures essential for excitation-contraction coupling. Mutations in the BIN1 gene cause centronuclear myopathy, which shares some histopathological features with myotonic dystrophy. We found that MBNL1 binds the BIN1 pre-mRNA and regulates its alternative splicing. BIN1 missplicing results in expression of an inactive form of BIN1 lacking phosphatidylinositol 5-phosphate-binding and membrane-tubulating activities. Consistent with a defect of BIN1, muscle T tubules are altered in people with myotonic dystrophy, and membrane structures are restored upon expression of the normal splicing form of BIN1 in muscle cells of such individuals. Finally, reproducing BIN1 splicing alteration in mice is sufficient to promote T tubule alterations and muscle weakness, a predominant feature of myotonic dystrophy.	D018908	Muscle Weakness
BIN1	21623381	Misregulated alternative splicing of BIN1 is associated with T tubule alterations and muscle weakness in myotonic dystrophy.	Myotonic dystrophy is the most common muscular dystrophy in adults and the first recognized example of an RNA-mediated disease. Congenital myotonic dystrophy (CDM1) and myotonic dystrophy of type 1 (DM1) or of type 2 (DM2) are caused by the expression of mutant RNAs containing expanded CUG or CCUG repeats, respectively. These mutant RNAs sequester the splicing regulator Muscleblind-like-1 (MBNL1), resulting in specific misregulation of the alternative splicing of other pre-mRNAs. We found that alternative splicing of the bridging integrator-1 (BIN1) pre-mRNA is altered in skeletal muscle samples of people with CDM1, DM1 and DM2. BIN1 is involved in tubular invaginations of membranes and is required for the biogenesis of muscle T tubules, which are specialized skeletal muscle membrane structures essential for excitation-contraction coupling. Mutations in the BIN1 gene cause centronuclear myopathy, which shares some histopathological features with myotonic dystrophy. We found that MBNL1 binds the BIN1 pre-mRNA and regulates its alternative splicing. BIN1 missplicing results in expression of an inactive form of BIN1 lacking phosphatidylinositol 5-phosphate-binding and membrane-tubulating activities. Consistent with a defect of BIN1, muscle T tubules are altered in people with myotonic dystrophy, and membrane structures are restored upon expression of the normal splicing form of BIN1 in muscle cells of such individuals. Finally, reproducing BIN1 splicing alteration in mice is sufficient to promote T tubule alterations and muscle weakness, a predominant feature of myotonic dystrophy.	D009223	Myotonic Dystrophy

Clinically important variants in BIN1

(ClinVar, 04/20/2024)

accession_id

uniprot_id

gene_name

Type

Variant

Clinical_significance