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:NUMB

Protein Summary

Gene summary

Gene name: NUMB
ASpdb.0 ID: 8650
	Gene
Gene symbol	NUMB
Gene ID	8650
Gene name	NUMB endocytic adaptor protein
Synonyms	C14orf41\|S171\|c14_5527
Cytomap	14q24.2-q24.3
Type of gene	protein-coding
Description	protein numb homologh-Numbnumb homolog
Modification date	20240407
UniProtAcc	P49757

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

Partner	Gene	GO ID	GO term	PubMed ID
Gene	NUMB	GO:0030136	clathrin-coated vesicle	19581412

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
P49757-1	P49757-1_5njk_A.pdb	5NJK	X-ray	3.13	A	25	171

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
P49757	NUMB	P49757-1	P49757-2	651	603	366	413	Deletion	none	none	365	365
P49757	NUMB	P49757-1	P49757-3	651	640	68	78	Deletion	none	none	67	67
P49757	NUMB	P49757-1	P49757-4	651	592	68	78	Deletion	none	none	67	67
P49757	NUMB	P49757-1	P49757-4	651	592	366	413	Deletion	none	none	354	354
P49757	NUMB	P49757-1	P49757-5	651	505	219	316	Deletion	none	none	218	218
P49757	NUMB	P49757-1	P49757-5	651	505	366	413	Deletion	none	none	267	267
P49757	NUMB	P49757-1	P49757-6	651	494	68	78	Deletion	none	none	67	67
P49757	NUMB	P49757-1	P49757-6	651	494	219	316	Deletion	none	none	207	207
P49757	NUMB	P49757-1	P49757-6	651	494	366	413	Deletion	none	none	256	256
P49757	NUMB	P49757-1	P49757-7	651	456	219	316	Deletion	none	none	218	218
P49757	NUMB	P49757-1	P49757-7	651	456	317	365	Deletion	none	none	218	218
P49757	NUMB	P49757-1	P49757-7	651	456	366	413	Deletion	none	none	218	218
P49757	NUMB	P49757-1	P49757-8	651	445	68	78	Deletion	none	none	67	67
P49757	NUMB	P49757-1	P49757-8	651	445	219	316	Deletion	none	none	207	207
P49757	NUMB	P49757-1	P49757-8	651	445	317	365	Deletion	none	none	207	207
P49757	NUMB	P49757-1	P49757-8	651	445	366	413	Deletion	none	none	207	207
P49757	NUMB	P49757-1	P49757-9	651	349	1	254	Deletion	none	none	0	0
P49757	NUMB	P49757-1	P49757-9	651	349	366	413	Deletion	none	none	111	111

Multiple sequence alignment of our canonical and alternatively spliced NUMB

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

UniProt-id	ENSG	ENST	ENSP
P49757-1	ENSG00000133961.21	ENST00000355058.7	ENSP00000347169.3
P49757-1	ENSG00000133961.21	ENST00000555238.6	ENSP00000451300.1
P49757-2	ENSG00000133961.21	ENST00000356296.8	ENSP00000348644.4
P49757-2	ENSG00000133961.21	ENST00000535282.5	ENSP00000441258.2
P49757-2	ENSG00000133961.21	ENST00000555394.5	ENSP00000451625.1
P49757-3	ENSG00000133961.21	ENST00000359560.7	ENSP00000352563.3
P49757-3	ENSG00000133961.21	ENST00000557597.5	ENSP00000451117.1
P49757-4	ENSG00000133961.21	ENST00000554546.5	ENSP00000452416.1
P49757-5	ENSG00000133961.21	ENST00000560335.5	ENSP00000453209.1
P49757-6	ENSG00000133961.21	ENST00000555738.6	ENSP00000452069.2
P49757-7	ENSG00000133961.21	ENST00000544991.7	ENSP00000446001.3
P49757-7	ENSG00000133961.21	ENST00000559312.5	ENSP00000452888.1
P49757-8	ENSG00000133961.21	ENST00000554521.6	ENSP00000450817.2

UniProt-id	NM ID	NP ID
P49757-1	NM_001005743.1	NP_001005743.1
P49757-2	NM_001005744.1	NP_001005744.1
P49757-2	NM_001320114.1	NP_001307043.1
P49757-3	NM_003744.5	NP_003735.3
P49757-4	NM_001005745.1	NP_001005745.1

Amino acid sequences of our canonical and alternatively spliced NUMB

accession_id	Protein sequence
P49757-1	MNKLRQSFRRKKDVYVPEASRPHQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKAERKFFKGFFGKTGKKAVKAVLWV SADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKREKECGVTA TFDASRTTFTREGSFRVTTATEQAEREEIMKQMQDAKKAETDKIVVGSSVAPGNTAPSPSSPTSPTSDATTSLEMNNPHAIPRRHAPIEQ LARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDFPIKNAVPEVEGEAESISSLCSQITNAFSTPEDPFSSAPMTKPVTVVAPQ SPTFQANGTDSAFHVLAKPAHTALAPVAMPVRETNPWAHAPDAANKEIAATCSGTEWGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKS VRAQQPQASAAPLQPVLQPPPPTAISQPASPFQGNAFLTSQPVPVGVVPALQPAFVPAQSYPVANGMPYPAPNVPVVGITPSQMVANVFG TAGHPQAAHPHQSPSLVRQQTFPHYEASSATTSPFFKPPAQHLNGSAAFNGVDDGRLASADRHTEVPTGTCPVDPFEAQWAALENKSKQR
P49757-2	MNKLRQSFRRKKDVYVPEASRPHQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKAERKFFKGFFGKTGKKAVKAVLWV SADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKREKECGVTA TFDASRTTFTREGSFRVTTATEQAEREEIMKQMQDAKKAETDKIVVGSSVAPGNTAPSPSSPTSPTSDATTSLEMNNPHAIPRRHAPIEQ LARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDFPIKNAVPEVEGEAESISSLCSQITNAFSTPEDPFSSAPMTKPVTVVAPQ SPTFQGTEWGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAISQPASPFQGNAFLTSQPVPVGVV PALQPAFVPAQSYPVANGMPYPAPNVPVVGITPSQMVANVFGTAGHPQAAHPHQSPSLVRQQTFPHYEASSATTSPFFKPPAQHLNGSAA
P49757-3	MNKLRQSFRRKKDVYVPEASRPHQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKATGKKAVKAVLWVSADGLRVVDEK TKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKREKECGVTATFDASRTTFTR EGSFRVTTATEQAEREEIMKQMQDAKKAETDKIVVGSSVAPGNTAPSPSSPTSPTSDATTSLEMNNPHAIPRRHAPIEQLARQGSFRGFP ALSQKMSPFKRQLSLRINELPSTMQRKTDFPIKNAVPEVEGEAESISSLCSQITNAFSTPEDPFSSAPMTKPVTVVAPQSPTFQANGTDS AFHVLAKPAHTALAPVAMPVRETNPWAHAPDAANKEIAATCSGTEWGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAA PLQPVLQPPPPTAISQPASPFQGNAFLTSQPVPVGVVPALQPAFVPAQSYPVANGMPYPAPNVPVVGITPSQMVANVFGTAGHPQAAHPH QSPSLVRQQTFPHYEASSATTSPFFKPPAQHLNGSAAFNGVDDGRLASADRHTEVPTGTCPVDPFEAQWAALENKSKQRTNPSPTNPFSS
P49757-4	MNKLRQSFRRKKDVYVPEASRPHQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKATGKKAVKAVLWVSADGLRVVDEK TKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKREKECGVTATFDASRTTFTR EGSFRVTTATEQAEREEIMKQMQDAKKAETDKIVVGSSVAPGNTAPSPSSPTSPTSDATTSLEMNNPHAIPRRHAPIEQLARQGSFRGFP ALSQKMSPFKRQLSLRINELPSTMQRKTDFPIKNAVPEVEGEAESISSLCSQITNAFSTPEDPFSSAPMTKPVTVVAPQSPTFQGTEWGQ SSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAISQPASPFQGNAFLTSQPVPVGVVPALQPAFVPAQ SYPVANGMPYPAPNVPVVGITPSQMVANVFGTAGHPQAAHPHQSPSLVRQQTFPHYEASSATTSPFFKPPAQHLNGSAAFNGVDDGRLAS
P49757-5	MNKLRQSFRRKKDVYVPEASRPHQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKAERKFFKGFFGKTGKKAVKAVLWV SADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKREKECGVTA TFDASRTTFTREGSFRVTTATEQAEREEIMKQMQDAKKVPEVEGEAESISSLCSQITNAFSTPEDPFSSAPMTKPVTVVAPQSPTFQGTE WGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAISQPASPFQGNAFLTSQPVPVGVVPALQPAFV PAQSYPVANGMPYPAPNVPVVGITPSQMVANVFGTAGHPQAAHPHQSPSLVRQQTFPHYEASSATTSPFFKPPAQHLNGSAAFNGVDDGR
P49757-6	MNKLRQSFRRKKDVYVPEASRPHQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKATGKKAVKAVLWVSADGLRVVDEK TKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKREKECGVTATFDASRTTFTR EGSFRVTTATEQAEREEIMKQMQDAKKVPEVEGEAESISSLCSQITNAFSTPEDPFSSAPMTKPVTVVAPQSPTFQGTEWGQSSGAASPG LFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAISQPASPFQGNAFLTSQPVPVGVVPALQPAFVPAQSYPVANGM PYPAPNVPVVGITPSQMVANVFGTAGHPQAAHPHQSPSLVRQQTFPHYEASSATTSPFFKPPAQHLNGSAAFNGVDDGRLASADRHTEVP
P49757-7	MNKLRQSFRRKKDVYVPEASRPHQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKAERKFFKGFFGKTGKKAVKAVLWV SADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKREKECGVTA TFDASRTTFTREGSFRVTTATEQAEREEIMKQMQDAKKGTEWGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQP VLQPPPPTAISQPASPFQGNAFLTSQPVPVGVVPALQPAFVPAQSYPVANGMPYPAPNVPVVGITPSQMVANVFGTAGHPQAAHPHQSPS LVRQQTFPHYEASSATTSPFFKPPAQHLNGSAAFNGVDDGRLASADRHTEVPTGTCPVDPFEAQWAALENKSKQRTNPSPTNPFSSDLQK
P49757-8	MNKLRQSFRRKKDVYVPEASRPHQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKATGKKAVKAVLWVSADGLRVVDEK TKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKREKECGVTATFDASRTTFTR EGSFRVTTATEQAEREEIMKQMQDAKKGTEWGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAIS QPASPFQGNAFLTSQPVPVGVVPALQPAFVPAQSYPVANGMPYPAPNVPVVGITPSQMVANVFGTAGHPQAAHPHQSPSLVRQQTFPHYE
P49757-9	MNNPHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDFPIKNAVPEVEGEAESISSLCSQITNAFSTPEDP FSSAPMTKPVTVVAPQSPTFQGTEWGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAISQPASPF QGNAFLTSQPVPVGVVPALQPAFVPAQSYPVANGMPYPAPNVPVVGITPSQMVANVFGTAGHPQAAHPHQSPSLVRQQTFPHYEASSATT

Protein Functional Features

Main function of this protein. (from UniProt)

NUMB (go to UniProt):P49757

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
P49757	Domain	33	193	Note=PID;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00148	Type=Deletion;Start=68;End=78
P49757	Domain	33	193	Note=PID;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00148	Type=Deletion;Start=68;End=78
P49757	Domain	33	193	Note=PID;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00148	Type=Deletion;Start=68;End=78
P49757	Domain	33	193	Note=PID;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00148	Type=Deletion;Start=68;End=78
P49757	Domain	33	193	Note=PID;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00148	Type=Deletion;Start=1;End=254
P49757	Region	228	257	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=219;End=316
P49757	Region	228	257	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=219;End=316
P49757	Region	228	257	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=219;End=316
P49757	Region	228	257	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=219;End=316
P49757	Region	228	257	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=254
P49757	Compositional bias	231	257	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=219;End=316
P49757	Compositional bias	231	257	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=219;End=316
P49757	Compositional bias	231	257	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=219;End=316
P49757	Compositional bias	231	257	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=219;End=316
P49757	Compositional bias	231	257	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=254

Gene Isoform Structures and Expression Levels for NUMB

Gene structures of our canonical and alternative spliced genes of NUMB
* 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 P49757-1

3D view using mol* of P49757-2

3D view using mol* of P49757-3

3D view using mol* of P49757-4

3D view using mol* of P49757-5

3D view using mol* of P49757-6

3D view using mol* of P49757-7

3D view using mol* of P49757-8

3D view using mol* of P49757-9

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 P49757-1

pLDDT distribution across the protein length of P49757-2

pLDDT distribution across the protein length of P49757-3

pLDDT distribution across the protein length of P49757-4

pLDDT distribution across the protein length of P49757-5

pLDDT distribution across the protein length of P49757-6

pLDDT distribution across the protein length of P49757-7

pLDDT distribution across the protein length of P49757-8

pLDDT distribution across the protein length of P49757-9

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 P49757-1

Ramachandran plot of P49757-3

Ramachandran plot of P49757-6

Ramachandran plot of P49757-7

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
P49757-1	0.861	67	0.91	216.776	0.763	0.566	0.701	0.696	0.611	1.14	2.52	17,19,20,25,29,33,119,120,121,124,150,151,152,153, 155,156,160,163,164,167,528,529,530,531,534
P49757-2	0.805	65	0.797	141.659	0.545	0.605	0.87	0.43	0.993	0.433	1.16	173,176,177,178,179,180,189,478,479,480,481,482,48 3,486
P49757-3	1.08	226	1.157	544.341	0.519	0.696	0.919	1.326	0.615	2.154	1.441	25,29,32,33,53,55,100,101,102,103,104,105,106,107, 108,121,128,141,142,144,145,148,149,151,152,153,15 4,155,156,157,158,159,520,521,523,524,527,528
P49757-4	0.692	40	0.695	54.194	0.649	0.538	0.801	0.692	0.682	1.014	0.712	168,169,170,171,178,469,470,471,472,475
P49757-5	1.006	155	1.084	534.394	0.67	0.595	0.767	0.715	0.653	1.096	1.599	35,53,89,91,92,93,94,96,108,110,111,112,113,114,11 5,116,117,118,119,155,159,162,165,166,168,169,172, 386,388,389,390,392,393
P49757-6	0.778	43	0.81	113.533	0.669	0.582	0.806	1.355	0.478	2.832	3.863	286,290,293,294,297,377,378,380,381
P49757-7	1.079	92	1.152	382.788	0.618	0.724	0.864	1.265	0.565	2.239	2.411	111,112,114,115,116,117,155,156,159,160,162,163,16 5,166,169,336,337,339,340,343,344
P49757-8	1.04	170	1.099	510.384	0.628	0.674	0.875	1.069	0.752	1.422	1.609	15,17,18,19,25,29,33,106,107,108,109,110,112,113,1 15,139,140,141,144,145,148,149,152,153,155,156,157 ,159,318,319,320,321,322,323,324,326,327,328,329,3 31,332,333
P49757-9	0.66	34	0.675	57.967	0.73	0.498	0.766	0.655	0.526	1.246	0.55	208,209,210,211,213,214,215,216,217

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 P49757-1_P49757-1_5njk_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 P49757-1_5njk_A_P49757-2.pdb

3D view using mol* of P49757-1_5njk_A_P49757-3.pdb

3D view using mol* of P49757-1_5njk_A_P49757-4.pdb

3D view using mol* of P49757-1_5njk_A_P49757-5.pdb

3D view using mol* of P49757-1_5njk_A_P49757-6.pdb

3D view using mol* of P49757-1_5njk_A_P49757-7.pdb

3D view using mol* of P49757-1_5njk_A_P49757-8.pdb

3D view using mol* of P49757-1_5njk_A_P49757-9.pdb

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

3D view using mol* of P49757-1_P49757-2.pdb

3D view using mol* of P49757-1_P49757-3.pdb

3D view using mol* of P49757-1_P49757-4.pdb

3D view using mol* of P49757-1_P49757-5.pdb

3D view using mol* of P49757-1_P49757-6.pdb

3D view using mol* of P49757-1_P49757-7.pdb

3D view using mol* of P49757-1_P49757-8.pdb

3D view using mol* of P49757-1_P49757-9.pdb

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

./stats/secondary_structure/figure/P49757-1_vs_P49757-2.png

./stats/secondary_structure/figure/P49757-1_vs_P49757-3.png

./stats/secondary_structure/figure/P49757-1_vs_P49757-4.png

./stats/secondary_structure/figure/P49757-1_vs_P49757-5.png

./stats/secondary_structure/figure/P49757-1_vs_P49757-6.png

./stats/secondary_structure/figure/P49757-1_vs_P49757-7.png

./stats/secondary_structure/figure/P49757-1_vs_P49757-8.png

./stats/secondary_structure/figure/P49757-1_vs_P49757-9.png

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

./stats/relative_asa/P49757-1_vs_P49757-2.png

./stats/relative_asa/P49757-1_vs_P49757-3.png

./stats/relative_asa/P49757-1_vs_P49757-4.png

./stats/relative_asa/P49757-1_vs_P49757-5.png

./stats/relative_asa/P49757-1_vs_P49757-6.png

./stats/relative_asa/P49757-1_vs_P49757-7.png

./stats/relative_asa/P49757-1_vs_P49757-8.png

./stats/relative_asa/P49757-1_vs_P49757-9.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 NUMB

Drugs targeting this gene/protein.
(DrugBank)

UniProt accession

Gene name

DrugBank ID

Drug name

Drug group

Actions

Related Diseases to NUMB

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

Gene	PMID	Title	Abstract	MeSH ID	MeSH term
NUMB	25889998	Insight into the role of alternative splicing within the RBM10v1 exon 10 tandem donor site.	RBM10 is an RNA binding protein involved in the regulation of transcription, alternative splicing and message stabilization. Mutations in RBM10, which maps to the X chromosome, are associated with TARP syndrome, lung and pancreatic cancers. Two predominant isoforms of RBM10 exist, RBM10v1 and RBM10v2. Both variants have alternate isoforms that differ by one valine residue, at amino acid 354 (RBM10v1) or 277 (RBM10v2). It was recently observed that a novel point mutation at amino acid 354 of RBM10v1, replacing valine with glutamic acid, correlated with preferential expression of an exon 11 inclusion variant of the proliferation regulatory protein NUMB, which is upregulated in lung cancer.	D008175	Lung Neoplasms
NUMB	25889998	Insight into the role of alternative splicing within the RBM10v1 exon 10 tandem donor site.	RBM10 is an RNA binding protein involved in the regulation of transcription, alternative splicing and message stabilization. Mutations in RBM10, which maps to the X chromosome, are associated with TARP syndrome, lung and pancreatic cancers. Two predominant isoforms of RBM10 exist, RBM10v1 and RBM10v2. Both variants have alternate isoforms that differ by one valine residue, at amino acid 354 (RBM10v1) or 277 (RBM10v2). It was recently observed that a novel point mutation at amino acid 354 of RBM10v1, replacing valine with glutamic acid, correlated with preferential expression of an exon 11 inclusion variant of the proliferation regulatory protein NUMB, which is upregulated in lung cancer.	D055752	Small Cell Lung Carcinoma
NUMB	26058814	Alternative splicing of the cell fate determinant Numb in hepatocellular carcinoma.	The cell fate determinant Numb is aberrantly expressed in cancer. Numb is alternatively spliced, with one isoform containing a long proline-rich region (PRR(L) ) compared to the other with a short PRR (PRR(S) ). Recently, PRR(L) was reported to enhance proliferation of breast and lung cancer cells. However, the importance of Numb alternative splicing in hepatocellular carcinoma (HCC) remains unexplored. We report here that Numb PRR(L) expression is increased in HCC and associated with early recurrence and reduced overall survival after surgery. In a panel of HCC cell lines, PRR(L) generally promotes and PRR(S) suppresses proliferation, migration, invasion, and colony formation. Knockdown of PRR(S) leads to increased Akt phosphorylation and c-Myc expression, and Akt inhibition or c-Myc silencing dampens the proliferative impact of Numb PRR(S) knockdown. In the cell models explored in this study, alternative splicing of Numb PRR isoforms is coordinately regulated by the splicing factor RNA-binding Fox domain containing 2 (RbFox2) and the kinase serine/arginine protein-specific kinase 2 (SRPK2). Knockdown of the former causes accumulation of PRR(L) , while SRPK2 knockdown causes accumulation of PRR(S) . The subcellular location of SRPK2 is regulated by the molecular chaperone heat shock protein 90, and heat shock protein 90 inhibition or knockdown phenocopies SRPK2 knockdown in promoting accumulation of Numb PRR(S) . Finally, HCC cell lines that predominantly express PRR(L) are differentially sensitive to heat shock protein 90 inhibition.	D006528	Carcinoma, Hepatocellular
NUMB	26058814	Alternative splicing of the cell fate determinant Numb in hepatocellular carcinoma.	The cell fate determinant Numb is aberrantly expressed in cancer. Numb is alternatively spliced, with one isoform containing a long proline-rich region (PRR(L) ) compared to the other with a short PRR (PRR(S) ). Recently, PRR(L) was reported to enhance proliferation of breast and lung cancer cells. However, the importance of Numb alternative splicing in hepatocellular carcinoma (HCC) remains unexplored. We report here that Numb PRR(L) expression is increased in HCC and associated with early recurrence and reduced overall survival after surgery. In a panel of HCC cell lines, PRR(L) generally promotes and PRR(S) suppresses proliferation, migration, invasion, and colony formation. Knockdown of PRR(S) leads to increased Akt phosphorylation and c-Myc expression, and Akt inhibition or c-Myc silencing dampens the proliferative impact of Numb PRR(S) knockdown. In the cell models explored in this study, alternative splicing of Numb PRR isoforms is coordinately regulated by the splicing factor RNA-binding Fox domain containing 2 (RbFox2) and the kinase serine/arginine protein-specific kinase 2 (SRPK2). Knockdown of the former causes accumulation of PRR(L) , while SRPK2 knockdown causes accumulation of PRR(S) . The subcellular location of SRPK2 is regulated by the molecular chaperone heat shock protein 90, and heat shock protein 90 inhibition or knockdown phenocopies SRPK2 knockdown in promoting accumulation of Numb PRR(S) . Finally, HCC cell lines that predominantly express PRR(L) are differentially sensitive to heat shock protein 90 inhibition.	D008113	Liver Neoplasms

Clinically important variants in NUMB

(ClinVar, 04/20/2024)

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