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:EPB41

Protein Summary

Gene summary

Gene name: EPB41
ASpdb.0 ID: 2035
	Gene
Gene symbol	EPB41
Gene ID	2035
Gene name	erythrocyte membrane protein band 4.1
Synonyms	4.1R\|EL1\|HE
Cytomap	1p35.3
Type of gene	protein-coding
Description	protein 4.1EPB4.1P4.1band 4.1elliptocytosis 1, RH-linkederythrocyte surface protein band 4.1
Modification date	20240407
UniProtAcc	P11171

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

Partner	Gene	GO ID	GO term	PubMed ID
Gene	EPB41	GO:0005545	1-phosphatidylinositol binding	16669616
Gene	EPB41	GO:0005829	cytosol	-
Gene	EPB41	GO:0005886	plasma membrane	-
Gene	EPB41	GO:0005938	cell cortex	23870127
Gene	EPB41	GO:0016604	nuclear body	-
Gene	EPB41	GO:0030054	cell junction	-
Gene	EPB41	GO:0030863	cortical cytoskeleton	16254212
Gene	EPB41	GO:0032092	positive regulation of protein binding	3693401
Gene	EPB41	GO:0032991	protein-containing complex	16060676
Gene	EPB41	GO:0045171	intercellular bridge	-
Gene	EPB41	GO:0072686	mitotic spindle	-

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
P11171-1	P11171-1_1gg3_A.pdb	1GG3	X-ray	2.8	A	210	488

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
P11171	EPB41	P11171-1	P11171-2	864	831	616	648	Deletion	none	none	615	615
P11171	EPB41	P11171-1	P11171-3	864	641	1	209	Deletion	none	none	0	0
P11171	EPB41	P11171-1	P11171-3	864	641	635	648	Deletion	none	none	425	425
P11171	EPB41	P11171-1	P11171-4	864	588	1	209	Deletion	none	none	0	0
P11171	EPB41	P11171-1	P11171-4	864	588	616	648	Deletion	none	none	406	406
P11171	EPB41	P11171-1	P11171-4	864	588	772	805	Deletion	none	none	529	529
P11171	EPB41	P11171-1	P11171-5	864	775	228	262	Deletion	none	none	227	227
P11171	EPB41	P11171-1	P11171-5	864	775	616	648	Deletion	none	none	580	580
P11171	EPB41	P11171-1	P11171-5	864	775	649	669	Deletion	none	none	580	580
P11171	EPB41	P11171-1	P11171-6	864	566	1	209	Deletion	none	none	0	0
P11171	EPB41	P11171-1	P11171-6	864	566	228	262	Deletion	none	none	18	18
P11171	EPB41	P11171-1	P11171-6	864	566	616	648	Deletion	none	none	371	371
P11171	EPB41	P11171-1	P11171-6	864	566	649	669	Deletion	none	none	371	371
P11171	EPB41	P11171-1	P11171-7	864	720	635	648	Deletion	none	none	634	634
P11171	EPB41	P11171-1	P11171-7	864	720	729	734	Substitution	PPLVKT	VSTLST	715	720
P11171	EPB41	P11171-1	P11171-7	864	720	735	864	Deletion	none	none	720	720

Multiple sequence alignment of our canonical and alternatively spliced EPB41

Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of EPB41

UniProt-id	ENSG	ENST	ENSP
P11171-1	ENSG00000159023.23	ENST00000343067.9	ENSP00000345259.4
P11171-1	ENSG00000159023.23	ENST00000373798.5	ENSP00000362904.1
P11171-4	ENSG00000159023.23	ENST00000373800.7	ENSP00000362906.3
P11171-5	ENSG00000159023.23	ENST00000347529.7	ENSP00000290100.6
P11171-7	ENSG00000159023.23	ENST00000373797.2	ENSP00000362903.1

UniProt-id	NM ID	NP ID
P11171-1	NM_001166005.1	NP_001159477.1
P11171-2	XM_005245764.1	XP_005245821.1
P11171-3	NM_203342.2	NP_976217.1
P11171-4	NM_004437.3	NP_004428.1
P11171-7	NM_001166006.1	NP_001159478.1

Amino acid sequences of our canonical and alternatively spliced EPB41

accession_id	Protein sequence
P11171-1	MTTEKSLVTEAENSQHQQKEEGEEAINSGQQEPQQEESCQTAAEGDNWCEQKLKASNGDTPTHEDLTKNKERTSESRGLSRLFSSFLKRP KSQVSEEEGKEVESDKEKGEGGQKEIEFGTSLDEEIILKAPIAAPEPELKTDPSLDLHSLSSAETQPAQEELREDPDFEIKEGEGLEECS KIEVKEESPQSKAETELKASQKPIRKHRNMHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKE IKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGVDYVSDFKLAPNQT KELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIK IRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTIPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRAS RSLDGAAAVDSADRSPRPTSAPAITQGQVAEGGVLDASAKKTVVPKAQKETVKAEVKKEDEPPEQAEPEPTEAWKVEKTHIEVTVPTSNG DQTQKLAEKTEDLIRMRKKKRERLDGENIYIRHSNLMLEDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNIN GQIPTGEGPPLVKTQTVTISDNANAVKSEIPTKDVPIVHTETKTITYEAAQTDDNSGDLDPGVLLTAQTITSETPSSTTTTQITKTVKGG
P11171-2	MTTEKSLVTEAENSQHQQKEEGEEAINSGQQEPQQEESCQTAAEGDNWCEQKLKASNGDTPTHEDLTKNKERTSESRGLSRLFSSFLKRP KSQVSEEEGKEVESDKEKGEGGQKEIEFGTSLDEEIILKAPIAAPEPELKTDPSLDLHSLSSAETQPAQEELREDPDFEIKEGEGLEECS KIEVKEESPQSKAETELKASQKPIRKHRNMHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKE IKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGVDYVSDFKLAPNQT KELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIK IRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTIPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRAS RSLDGAAAVDSADRSPRPTSAPAITQGQVAEGGVLDASAKKTVVPKAQKETVKAEVKKEDEPPEQAEPEPTEAWKKKRERLDGENIYIRH SNLMLEDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQIPTGEGPPLVKTQTVTISDNANAVKSEIPTK DVPIVHTETKTITYEAAQTDDNSGDLDPGVLLTAQTITSETPSSTTTTQITKTVKGGISETRIEKRIVITGDADIDHDQVLVQAIKEAKE
P11171-3	MHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTED ITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGVDYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLEN AKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKV CVEHHTFFRLTSTDTIPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRASRSLDGAAAVDSADRSPRPTSAPAITQGQV AEGGVLDASAKKTVVPKAQKETVKAEVKKEDEPPEQAEPEPTEAWKVEKTHIEVTVPTSNGDQTQKKRERLDGENIYIRHSNLMLEDLDK SQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQIPTGEGPPLVKTQTVTISDNANAVKSEIPTKDVPIVHTETK TITYEAAQTDDNSGDLDPGVLLTAQTITSETPSSTTTTQITKTVKGGISETRIEKRIVITGDADIDHDQVLVQAIKEAKEQHPDMSVTKV
P11171-4	MHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTED ITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGVDYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLEN AKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKV CVEHHTFFRLTSTDTIPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRASRSLDGAAAVDSADRSPRPTSAPAITQGQV AEGGVLDASAKKTVVPKAQKETVKAEVKKEDEPPEQAEPEPTEAWKKKRERLDGENIYIRHSNLMLEDLDKSQEEIKKHHASISELKKNF MESVPEPRPSEWDKRLSTHSPFRTLNINGQIPTGEGPPLVKTQTVTISDNANAVKSEIPTKDVPIVHTETKTITYEAAQTVKGGISETRI
P11171-5	MTTEKSLVTEAENSQHQQKEEGEEAINSGQQEPQQEESCQTAAEGDNWCEQKLKASNGDTPTHEDLTKNKERTSESRGLSRLFSSFLKRP KSQVSEEEGKEVESDKEKGEGGQKEIEFGTSLDEEIILKAPIAAPEPELKTDPSLDLHSLSSAETQPAQEELREDPDFEIKEGEGLEECS KIEVKEESPQSKAETELKASQKPIRKHRNMHCKVSLLDDTVYECVVETWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYL CLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGVDYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSM YGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHT FFRLTSTDTIPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRASRSLDGAAAVDSADRSPRPTSAPAITQGQVAEGGVL DASAKKTVVPKAQKETVKAEVKKEDEPPEQAEPEPTEAWKDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNI NGQIPTGEGPPLVKTQTVTISDNANAVKSEIPTKDVPIVHTETKTITYEAAQTDDNSGDLDPGVLLTAQTITSETPSSTTTTQITKTVKG
P11171-6	MHCKVSLLDDTVYECVVETWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQ SELGDYDPELHGVDYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYK DKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTIPKSKFLALGSKFRYSGRTQ AQTRQASALIDRPAPHFERTASKRASRSLDGAAAVDSADRSPRPTSAPAITQGQVAEGGVLDASAKKTVVPKAQKETVKAEVKKEDEPPE QAEPEPTEAWKDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQIPTGEGPPLVKTQTVTISDNANAVKS EIPTKDVPIVHTETKTITYEAAQTDDNSGDLDPGVLLTAQTITSETPSSTTTTQITKTVKGGISETRIEKRIVITGDADIDHDQVLVQAI
P11171-7	MTTEKSLVTEAENSQHQQKEEGEEAINSGQQEPQQEESCQTAAEGDNWCEQKLKASNGDTPTHEDLTKNKERTSESRGLSRLFSSFLKRP KSQVSEEEGKEVESDKEKGEGGQKEIEFGTSLDEEIILKAPIAAPEPELKTDPSLDLHSLSSAETQPAQEELREDPDFEIKEGEGLEECS KIEVKEESPQSKAETELKASQKPIRKHRNMHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKE IKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGVDYVSDFKLAPNQT KELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIK IRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTIPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRAS RSLDGAAAVDSADRSPRPTSAPAITQGQVAEGGVLDASAKKTVVPKAQKETVKAEVKKEDEPPEQAEPEPTEAWKVEKTHIEVTVPTSNG DQTQKKRERLDGENIYIRHSNLMLEDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQIPTGEGVSTLST

Protein Functional Features

Main function of this protein. (from UniProt)

EPB41 (go to UniProt):P11171

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
P11171	Domain	210	491	Note=FERM;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00084	Type=Deletion;Start=228;End=262
P11171	Domain	210	491	Note=FERM;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00084	Type=Deletion;Start=228;End=262
P11171	Region	1	122	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Region	1	122	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Region	1	122	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Region	136	170	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Region	136	170	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Region	136	170	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Region	182	202	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Region	182	202	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Region	182	202	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Region	615	713	Note=Spectrin--actin-binding	Type=Deletion;Start=616;End=648
P11171	Region	615	713	Note=Spectrin--actin-binding	Type=Deletion;Start=635;End=648
P11171	Region	615	713	Note=Spectrin--actin-binding	Type=Deletion;Start=616;End=648
P11171	Region	615	713	Note=Spectrin--actin-binding	Type=Deletion;Start=616;End=648
P11171	Region	615	713	Note=Spectrin--actin-binding	Type=Deletion;Start=649;End=669
P11171	Region	615	713	Note=Spectrin--actin-binding	Type=Deletion;Start=616;End=648
P11171	Region	615	713	Note=Spectrin--actin-binding	Type=Deletion;Start=649;End=669
P11171	Region	615	713	Note=Spectrin--actin-binding	Type=Deletion;Start=635;End=648
P11171	Region	714	864	Note=C-terminal (CTD)	Type=Deletion;Start=772;End=805
P11171	Region	714	864	Note=C-terminal (CTD)	Type=Substitution;Start=729;End=734
P11171	Region	714	864	Note=C-terminal (CTD)	Type=Deletion;Start=735;End=864
P11171	Compositional bias	27	45	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Compositional bias	27	45	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Compositional bias	27	45	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Compositional bias	57	77	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Compositional bias	57	77	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Compositional bias	57	77	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Compositional bias	91	122	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Compositional bias	91	122	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209
P11171	Compositional bias	91	122	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=209

Gene Isoform Structures and Expression Levels for EPB41

Gene structures of our canonical and alternative spliced genes of EPB41
* 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 P11171-1

3D view using mol* of P11171-2

3D view using mol* of P11171-3

3D view using mol* of P11171-4

3D view using mol* of P11171-5

3D view using mol* of P11171-6

3D view using mol* of P11171-7

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 P11171-1

pLDDT distribution across the protein length of P11171-2

pLDDT distribution across the protein length of P11171-3

pLDDT distribution across the protein length of P11171-4

pLDDT distribution across the protein length of P11171-5

pLDDT distribution across the protein length of P11171-6

pLDDT distribution across the protein length of P11171-7

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 P11171-1

Ramachandran plot of P11171-2

Ramachandran plot of P11171-5

Ramachandran plot of P11171-7

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
P11171-1	1.059	347	1.094	581.728	0.378	0.743	0.988	1.193	0.895	1.333	0.554	801,802,804,814,815,816,817,818,819,820,821,822,82 3,824,830,833,834,837,838,841,842,844,845,848,849, 850,851,852,853,854,855,856,857,858,859,860
P11171-2	1.057	147	1.092	570.752	0.454	0.742	0.958	1.115	0.898	1.241	0.437	783,784,785,786,787,788,789,797,800,801,804,805,80 8,812,815,816,817,818,819,820,821,822,823,824,825
P11171-3	1.022	64	0.829	105.301	0.347	0.95	1.306	0.923	1.513	0.61	0.442	225,226,228,229,230,231,268,272,275,276,279,280,43 8,439,440,443
P11171-4	1.052	202	1.104	686	0.5	0.703	0.911	0.99	0.789	1.256	0.62	521,523,537,538,539,540,541,542,543,544,545,546,54 7,548,552,554,558,561,562,565,569,572,573,574,575, 576,577,578,579,580,581,582
P11171-5	1.073	146	1.109	420.518	0.528	0.762	1.003	0.931	0.883	1.054	1.543	217,218,219,268,272,275,276,278,279,293,294,297,30 1,302,309,310,311,314,317,318,319,320,351,499,500, 501,502,503,504
P11171-6	1.07	157	0.988	330.995	0.419	0.803	1.143	1.044	1.332	0.784	0.9	161,162,163,165,167,178,180,185,186,187,188,189,19 2,207,208,209,210,211,212,213,217,219,220,221,384, 387,388,390,391,393,394,397,398,399
P11171-7	1.091	115	1.116	287.091	0.385	0.804	1.102	0.911	0.94	0.97	1.446	217,218,219,307,310,311,313,314,328,329,332,336,35 3,354,355,386,534,536,537,538

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 P11171-1_P11171-1_1gg3_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 P11171-1_1gg3_A_P11171-2.pdb

3D view using mol* of P11171-1_1gg3_A_P11171-3.pdb

3D view using mol* of P11171-1_1gg3_A_P11171-4.pdb

3D view using mol* of P11171-1_1gg3_A_P11171-5.pdb

3D view using mol* of P11171-1_1gg3_A_P11171-6.pdb

3D view using mol* of P11171-1_1gg3_A_P11171-7.pdb

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

3D view using mol* of P11171-1_P11171-2.pdb

3D view using mol* of P11171-1_P11171-3.pdb

3D view using mol* of P11171-1_P11171-4.pdb

3D view using mol* of P11171-1_P11171-5.pdb

3D view using mol* of P11171-1_P11171-6.pdb

3D view using mol* of P11171-1_P11171-7.pdb

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

./stats/secondary_structure/figure/P11171-1_vs_P11171-2.png

./stats/secondary_structure/figure/P11171-1_vs_P11171-3.png

./stats/secondary_structure/figure/P11171-1_vs_P11171-4.png

./stats/secondary_structure/figure/P11171-1_vs_P11171-5.png

./stats/secondary_structure/figure/P11171-1_vs_P11171-6.png

./stats/secondary_structure/figure/P11171-1_vs_P11171-7.png

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

./stats/relative_asa/P11171-1_vs_P11171-2.png

./stats/relative_asa/P11171-1_vs_P11171-3.png

./stats/relative_asa/P11171-1_vs_P11171-4.png

./stats/relative_asa/P11171-1_vs_P11171-5.png

./stats/relative_asa/P11171-1_vs_P11171-6.png

./stats/relative_asa/P11171-1_vs_P11171-7.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 EPB41

Drugs targeting this gene/protein.
(DrugBank)

UniProt accession

Gene name

DrugBank ID

Drug name

Drug group

Actions

Related Diseases to EPB41

Previous studies relating to the alternative splicing of EPB41 and disease information from the MeSH term (PubMed)

Gene	PMID	Title	Abstract	MeSH ID	MeSH term
EPB41	3194408	Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells.	Protein 4.1 is a multifunctional structural protein located in the erythrocyte membrane skeleton and in many nonerythroid cells. Molecular characterization of cloned protein 4.1 sequences from human reticulocytes has revealed the existence of multiple transcripts of the protein 4.1 gene that may encode a family of closely related protein isoforms. Several independently isolated cDNAs were sequenced and demonstrated to encode four different protein 4.1 species having identical primary sequences, except for the presence or absence of discrete peptides in the 8-kDa spectrin/actin binding domain (21 amino acids) and near the carboxyl terminus (43 and 34 amino acids). The same four protein 4.1 isoforms were detected when reticulocyte protein 4.1 mRNA sequences were reverse transcribed into cDNA and enzymatically amplified in vitro by using protein 4.1-specific oligonucleotide primers and the polymerase chain reaction. The finding of multiple protein 4.1 isoforms raises the possibility that the many binding functions ascribed to protein 4.1 may reside in distinct structural isoforms. Since only a single protein 4.1 gene appears to be expressed in erythrocytes, it is likely that these isoforms are produced by alternative mRNA splicing from a common protein 4.1 pre-mRNA. Multiple RNA splicing pathways are thus operative in the protein 4.1 gene even within a single cell lineage, human erythroid cells.	D000755	Anemia, Sickle Cell
EPB41	11737230	Reassignment of the EPB4.1 gene to 1p36 and assessment of its involvement in neuroblastomas.	EPB4.1 has been previously mapped to human chromosome 1p33-p34.2. In contradiction to this chromosomal location, we have mapped EPB4.1-1p36 by using fluorescence in situ hybridization and radiation hybrid mapping. In neuroblastomas, deletions of the telomeric end of chromosome 1 (1p36) are the most common genetic aberration.	D002872	Chromosome Deletion
EPB41	11737230	Reassignment of the EPB4.1 gene to 1p36 and assessment of its involvement in neuroblastomas.	EPB4.1 has been previously mapped to human chromosome 1p33-p34.2. In contradiction to this chromosomal location, we have mapped EPB4.1-1p36 by using fluorescence in situ hybridization and radiation hybrid mapping. In neuroblastomas, deletions of the telomeric end of chromosome 1 (1p36) are the most common genetic aberration.	D009447	Neuroblastoma
EPB41	15714879	Protein 4.1R expression in normal and dystrophic skeletal muscle.	4.1R pre-mRNA alternative splicing results in multiple mRNA and protein isoforms that are expressed in virtually all tissues. More specifically, isoforms containing the alternative exon 17a, are exclusively expressed in muscle tissues. In this report, we show that these isoforms are preferentially present in the myoplasm of fast myofibres. 4.1R epitopes are also found at the sarcolemma of both slow and fast myofibres in normal muscle. Interestingly, they are absent from dystrophin-deficient sarcolemma of DMD muscle, and colocalize with partially expressed dystrophin in BMD muscle. We also show that alternative splicing of exons 16 and 17a is regulated during muscle differentiation in an asynchronous fashion, with an early inclusion of exon 16 in forming myotubes, and a late inclusion of exon 17a. Consistently, Western blot analysis led to characterize mainly an approximately 96/98-kDa doublet bearing exons 16-17a-encoding peptide, exclusively occurring in the differentiated muscle.	D009136	Muscular Dystrophies

Clinically important variants in EPB41

(ClinVar, 04/20/2024)

accession_id

uniprot_id

gene_name

Type

Variant

Clinical_significance