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:IL23R

Protein Summary

Gene summary

Gene name: IL23R
ASpdb.0 ID: 149233
	Gene
Gene symbol	IL23R
Gene ID	149233
Gene name	interleukin 23 receptor
Synonyms	PSORS7
Cytomap	1p31.3
Type of gene	protein-coding
Description	interleukin-23 receptorIL-23 receptor
Modification date	20240403
UniProtAcc	Q5VWK5

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

Partner	Gene	GO ID	GO term	PubMed ID
Gene	IL23R	GO:0002230	positive regulation of defense response to virus by host	12421946
Gene	IL23R	GO:0002827	positive regulation of T-helper 1 type immune response	15114670
Gene	IL23R	GO:0032496	response to lipopolysaccharide	12023369
Gene	IL23R	GO:0032729	positive regulation of type II interferon production	11114383
Gene	IL23R	GO:0032735	positive regulation of interleukin-12 production	20027291
Gene	IL23R	GO:0034341	response to type II interferon	12023369
Gene	IL23R	GO:0042020	interleukin-23 receptor activity	12023369
Gene	IL23R	GO:0043235	receptor complex	23382219
Gene	IL23R	GO:0072536	interleukin-23 receptor complex	12023369

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
Q5VWK5-1	Q5VWK5-1_5mzv_C.pdb	5MZV	X-ray	2.8	C	24	316

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
Q5VWK5	IL23R	Q5VWK5-1	Q5VWK5-2	629	375	1	254	Deletion	none	none	0	0
Q5VWK5	IL23R	Q5VWK5-1	Q5VWK5-3	629	356	349	356	Substitution	DNRGDIGL	GLKEGSYC	349	356
Q5VWK5	IL23R	Q5VWK5-1	Q5VWK5-3	629	356	357	629	Deletion	none	none	356	356
Q5VWK5	IL23R	Q5VWK5-1	Q5VWK5-4	629	174	165	174	Substitution	LETEEEQQYL	DTFCSRHFQG	165	174
Q5VWK5	IL23R	Q5VWK5-1	Q5VWK5-4	629	174	175	629	Deletion	none	none	174	174
Q5VWK5	IL23R	Q5VWK5-1	Q5VWK5-5	629	264	1	365	Deletion	none	none	0	0
Q5VWK5	IL23R	Q5VWK5-1	Q5VWK5-5	629	264	366	383	Substitution	MLSILSLIGIFNRSFRTG	MEFWANSCFHLYRAPYFW	1	18
Q5VWK5	IL23R	Q5VWK5-1	Q5VWK5-6	629	374	1	255	Deletion	none	none	0	0
Q5VWK5	IL23R	Q5VWK5-1	Q5VWK5-6	629	374	256	266	Substitution	RYKATTNQTWN	MILRPYQPCGT	1	11
Q5VWK5	IL23R	Q5VWK5-1	Q5VWK5-7	629	227	1	402	Deletion	none	none	0	0

Multiple sequence alignment of our canonical and alternatively spliced IL23R

Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of IL23R

UniProt-id	ENSG	ENST	ENSP
Q5VWK5-1	ENSG00000162594.17	ENST00000347310.10	ENSP00000321345.5
Q5VWK5-3	ENSG00000162594.17	ENST00000697150.1	ENSP00000513139.1
Q5VWK5-3	ENSG00000162594.17	ENST00000697151.1	ENSP00000513140.1
Q5VWK5-4	ENSG00000162594.17	ENST00000697149.1	ENSP00000513138.1
Q5VWK5-4	ENSG00000162594.17	ENST00000697153.1	ENSP00000513142.1
Q5VWK5-4	ENSG00000162594.17	ENST00000697223.1	ENSP00000513190.1
Q5VWK5-4	ENSG00000162594.17	ENST00000697224.1	ENSP00000513191.1
Q5VWK5-6	ENSG00000162594.17	ENST00000425614.3	ENSP00000387640.2

UniProt-id	NM ID	NP ID
Q5VWK5-1	NM_144701.2	NP_653302.2
Q5VWK5-1	XM_011540790.2	XP_011539092.1
Q5VWK5-1	XM_011540791.2	XP_011539093.1

Amino acid sequences of our canonical and alternatively spliced IL23R

accession_id	Protein sequence
Q5VWK5-1	MNQVTIQWDAVIALYILFSWCHGGITNINCSGHIWVEPATIFKMGMNISIYCQAAIKNCQPRKLHFYKNGIKERFQITRINKTTARLWYK NFLEPHASMYCTAECPKHFQETLICGKDISSGYPPDIPDEVTCVIYEYSGNMTCTWNAGKLTYIDTKYVVHVKSLETEEEQQYLTSSYIN ISTDSLQGGKKYLVWVQAANALGMEESKQLQIHLDDIVIPSAAVISRAETINATVPKTIIYWDSQTTIEKVSCEMRYKATTNQTWNVKEF DTNFTYVQQSEFYLEPNIKYVFQVRCQETGKRYWQPWSSLFFHKTPETVPQVTSKAFQHDTWNSGLTVASISTGHLTSDNRGDIGLLLGM IVFAVMLSILSLIGIFNRSFRTGIKRRILLLIPKWLYEDIPNMKNSNVVKMLQENSELMNNNSSEQVLYVDPMITEIKEIFIPEHKPTDY KKENTGPLETRDYPQNSLFDNTTVVYIPDLNTGYKPQISNFLPEGSHLSNNNEITSLTLKPPVDSLDSGNNPRLQKHPNFAFSVSSVNSL
Q5VWK5-2	MRYKATTNQTWNVKEFDTNFTYVQQSEFYLEPNIKYVFQVRCQETGKRYWQPWSSLFFHKTPETVPQVTSKAFQHDTWNSGLTVASISTG HLTSDNRGDIGLLLGMIVFAVMLSILSLIGIFNRSFRTGIKRRILLLIPKWLYEDIPNMKNSNVVKMLQENSELMNNNSSEQVLYVDPMI TEIKEIFIPEHKPTDYKKENTGPLETRDYPQNSLFDNTTVVYIPDLNTGYKPQISNFLPEGSHLSNNNEITSLTLKPPVDSLDSGNNPRL QKHPNFAFSVSSVNSLSNTIFLGELSLILNQGECSSPDIQNSVEEETTMLLENDSPSETIPEQTLLPDEFVSCLGIVNEELPSINTYFPQ
Q5VWK5-3	MNQVTIQWDAVIALYILFSWCHGGITNINCSGHIWVEPATIFKMGMNISIYCQAAIKNCQPRKLHFYKNGIKERFQITRINKTTARLWYK NFLEPHASMYCTAECPKHFQETLICGKDISSGYPPDIPDEVTCVIYEYSGNMTCTWNAGKLTYIDTKYVVHVKSLETEEEQQYLTSSYIN ISTDSLQGGKKYLVWVQAANALGMEESKQLQIHLDDIVIPSAAVISRAETINATVPKTIIYWDSQTTIEKVSCEMRYKATTNQTWNVKEF
Q5VWK5-4	MNQVTIQWDAVIALYILFSWCHGGITNINCSGHIWVEPATIFKMGMNISIYCQAAIKNCQPRKLHFYKNGIKERFQITRINKTTARLWYK
Q5VWK5-5	MEFWANSCFHLYRAPYFWIKRRILLLIPKWLYEDIPNMKNSNVVKMLQENSELMNNNSSEQVLYVDPMITEIKEIFIPEHKPTDYKKENT GPLETRDYPQNSLFDNTTVVYIPDLNTGYKPQISNFLPEGSHLSNNNEITSLTLKPPVDSLDSGNNPRLQKHPNFAFSVSSVNSLSNTIF
Q5VWK5-6	MILRPYQPCGTVKEFDTNFTYVQQSEFYLEPNIKYVFQVRCQETGKRYWQPWSSLFFHKTPETVPQVTSKAFQHDTWNSGLTVASISTGH LTSDNRGDIGLLLGMIVFAVMLSILSLIGIFNRSFRTGIKRRILLLIPKWLYEDIPNMKNSNVVKMLQENSELMNNNSSEQVLYVDPMIT EIKEIFIPEHKPTDYKKENTGPLETRDYPQNSLFDNTTVVYIPDLNTGYKPQISNFLPEGSHLSNNNEITSLTLKPPVDSLDSGNNPRLQ KHPNFAFSVSSVNSLSNTIFLGELSLILNQGECSSPDIQNSVEEETTMLLENDSPSETIPEQTLLPDEFVSCLGIVNEELPSINTYFPQN
Q5VWK5-7	MKNSNVVKMLQENSELMNNNSSEQVLYVDPMITEIKEIFIPEHKPTDYKKENTGPLETRDYPQNSLFDNTTVVYIPDLNTGYKPQISNFL PEGSHLSNNNEITSLTLKPPVDSLDSGNNPRLQKHPNFAFSVSSVNSLSNTIFLGELSLILNQGECSSPDIQNSVEEETTMLLENDSPSE

Protein Functional Features

Main function of this protein. (from UniProt)

IL23R (go to UniProt):Q5VWK5

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
Q5VWK5	Topological domain	24	355	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=1;End=254
Q5VWK5	Topological domain	24	355	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=349;End=356
Q5VWK5	Topological domain	24	355	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=165;End=174
Q5VWK5	Topological domain	24	355	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=175;End=629
Q5VWK5	Topological domain	24	355	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=1;End=365
Q5VWK5	Topological domain	24	355	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=1;End=255
Q5VWK5	Topological domain	24	355	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=256;End=266
Q5VWK5	Topological domain	24	355	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=1;End=402
Q5VWK5	Transmembrane	356	376	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=349;End=356
Q5VWK5	Transmembrane	356	376	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=357;End=629
Q5VWK5	Transmembrane	356	376	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=175;End=629
Q5VWK5	Transmembrane	356	376	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=1;End=365
Q5VWK5	Transmembrane	356	376	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=366;End=383
Q5VWK5	Transmembrane	356	376	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=1;End=402
Q5VWK5	Topological domain	377	629	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=357;End=629
Q5VWK5	Topological domain	377	629	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=175;End=629
Q5VWK5	Topological domain	377	629	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=366;End=383
Q5VWK5	Topological domain	377	629	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=1;End=402
Q5VWK5	Domain	127	217	Note=Fibronectin type-III 1;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00316	Type=Deletion;Start=1;End=254
Q5VWK5	Domain	127	217	Note=Fibronectin type-III 1;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00316	Type=Substitution;Start=165;End=174
Q5VWK5	Domain	127	217	Note=Fibronectin type-III 1;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00316	Type=Deletion;Start=175;End=629
Q5VWK5	Domain	127	217	Note=Fibronectin type-III 1;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00316	Type=Deletion;Start=1;End=365
Q5VWK5	Domain	127	217	Note=Fibronectin type-III 1;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00316	Type=Deletion;Start=1;End=255
Q5VWK5	Domain	127	217	Note=Fibronectin type-III 1;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00316	Type=Deletion;Start=1;End=402
Q5VWK5	Domain	219	318	Note=Fibronectin type-III 2;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00316	Type=Deletion;Start=1;End=254
Q5VWK5	Domain	219	318	Note=Fibronectin type-III 2;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00316	Type=Deletion;Start=175;End=629
Q5VWK5	Domain	219	318	Note=Fibronectin type-III 2;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00316	Type=Deletion;Start=1;End=365
Q5VWK5	Domain	219	318	Note=Fibronectin type-III 2;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00316	Type=Deletion;Start=1;End=255
Q5VWK5	Domain	219	318	Note=Fibronectin type-III 2;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00316	Type=Substitution;Start=256;End=266
Q5VWK5	Domain	219	318	Note=Fibronectin type-III 2;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00316	Type=Deletion;Start=1;End=402

Gene Isoform Structures and Expression Levels for IL23R

Gene structures of our canonical and alternative spliced genes of IL23R
* 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 Q5VWK5-1

3D view using mol* of Q5VWK5-2

3D view using mol* of Q5VWK5-3

3D view using mol* of Q5VWK5-4

3D view using mol* of Q5VWK5-5

3D view using mol* of Q5VWK5-6

3D view using mol* of Q5VWK5-7

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 Q5VWK5-1

pLDDT distribution across the protein length of Q5VWK5-2

pLDDT distribution across the protein length of Q5VWK5-3

pLDDT distribution across the protein length of Q5VWK5-4

pLDDT distribution across the protein length of Q5VWK5-5

pLDDT distribution across the protein length of Q5VWK5-6

pLDDT distribution across the protein length of Q5VWK5-7

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 Q5VWK5-1

Ramachandran plot of Q5VWK5-2

Ramachandran plot of Q5VWK5-5

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
Q5VWK5-1	1.024	230	1.079	549.829	0.544	0.665	0.896	0.991	0.798	1.242	1.415	38,39,41,42,43,46,124,154,155,157,159,172,173,174, 197,199,200,201,202,203,204,205,475,476,477,478,47 9,480,481,483,484,485,486,488
Q5VWK5-2	1.044	367	1.089	652.729	0.475	0.708	0.965	1.27	0.848	1.498	0.735	1,13,15,16,17,18,20,22,23,24,25,26,38,39,40,41,42, 43,44,45,46,47,49,50,51,52,53,54,55,57,356,357,358 ,359,360,362,363,364,367
Q5VWK5-3	0.69	45	0.621	81.634	0.605	0.595	0.865	0.139	1.124	0.124	0.817	230,232,233,234,235,236,286,315,316,318,319,320,32 1
Q5VWK5-4	0.505	12	0.393	41.16	0.733	0.668	0.933	0.13	1.022	0.127	0.613	61,63,64,77,78,79,85
Q5VWK5-5	0.763	59	0.717	185.22	0.663	0.598	0.818	0.163	1.116	0.146	0.986	111,113,114,115,116,117,118,119,120,242,244,245,24 7,250
Q5VWK5-6	0.985	313	1.019	927.472	0.607	0.651	0.874	0.626	0.955	0.655	0.866	1,3,4,5,7,9,10,11,12,13,14,15,16,17,18,19,20,21,22 ,23,24,25,26,27,28,29,30,35,37,41,42,43,44,45,46,4 8,49,50,56,290,291,292,293,294,295,296,297,298,299 ,300,301,302,303,333,335,339,340,342,343,345,346,3 47
Q5VWK5-7	0.681	37	0.624	84.721	0.57	0.646	0.919	0.33	1.029	0.321	2.254	132,133,134,135,136,137,139,141,142,143,146,147

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 Q5VWK5-1_Q5VWK5-1_5mzv_C.pdb

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

3D view using mol* of Q5VWK5-1_5mzv_C_Q5VWK5-2.pdb

3D view using mol* of Q5VWK5-1_5mzv_C_Q5VWK5-3.pdb

3D view using mol* of Q5VWK5-1_5mzv_C_Q5VWK5-4.pdb

3D view using mol* of Q5VWK5-1_5mzv_C_Q5VWK5-5.pdb

3D view using mol* of Q5VWK5-1_5mzv_C_Q5VWK5-6.pdb

3D view using mol* of Q5VWK5-1_5mzv_C_Q5VWK5-7.pdb

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

3D view using mol* of Q5VWK5-1_Q5VWK5-2.pdb

3D view using mol* of Q5VWK5-1_Q5VWK5-3.pdb

3D view using mol* of Q5VWK5-1_Q5VWK5-4.pdb

3D view using mol* of Q5VWK5-1_Q5VWK5-5.pdb

3D view using mol* of Q5VWK5-1_Q5VWK5-6.pdb

3D view using mol* of Q5VWK5-1_Q5VWK5-7.pdb

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

./stats/secondary_structure/figure/Q5VWK5-1_vs_Q5VWK5-2.png

./stats/secondary_structure/figure/Q5VWK5-1_vs_Q5VWK5-3.png

./stats/secondary_structure/figure/Q5VWK5-1_vs_Q5VWK5-4.png

./stats/secondary_structure/figure/Q5VWK5-1_vs_Q5VWK5-5.png

./stats/secondary_structure/figure/Q5VWK5-1_vs_Q5VWK5-6.png

./stats/secondary_structure/figure/Q5VWK5-1_vs_Q5VWK5-7.png

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

./stats/relative_asa/Q5VWK5-1_vs_Q5VWK5-2.png

./stats/relative_asa/Q5VWK5-1_vs_Q5VWK5-3.png

./stats/relative_asa/Q5VWK5-1_vs_Q5VWK5-4.png

./stats/relative_asa/Q5VWK5-1_vs_Q5VWK5-5.png

./stats/relative_asa/Q5VWK5-1_vs_Q5VWK5-6.png

./stats/relative_asa/Q5VWK5-1_vs_Q5VWK5-7.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 IL23R

Drugs targeting this gene/protein.
(DrugBank)

UniProt accession

Gene name

DrugBank ID

Drug name

Drug group

Actions

Related Diseases to IL23R

Previous studies relating to the alternative splicing of IL23R and disease information from the MeSH term (PubMed)

Gene	PMID	Title	Abstract	MeSH ID	MeSH term
IL23R	16372191	Identification and expression analysis of alternatively spliced isoforms of human interleukin-23 receptor gene in normal lymphoid cells and selected tumor cells.	Interleukin 23 (IL-23) is a new member of the IL-12 family that plays a critical role in promoting the proliferation of memory T helper 1 cells. The heterodimerized IL-23 receptor is composed of a shared IL-12 receptor beta 1 (IL-12Rbeta1) and an IL-12Rbeta2-related molecule called IL-23R. The standard form of IL-23R is encoded by at least 12 exons. Here, we demonstrate that at least six spliced isoforms of IL-23R (IL-23R1 to 6) can be generated through alternative splicing. The splicing strategies for the IL-23R gene are complicated and most often result in the deletion of exon 7 and/or exon 10. Translation prediction revealed that these spliced variants result in either premature termination to give rise to a diverse form of receptor ectodomain, or a frameshift to generate various lengths of the IL-23R endodomain. Differential expressions of IL-23R spliced variants are observed in natural killer and CD3+ CD4+ T cells. The expressions of these spliced variants are also prevalently and complicatedly regulated in tumor cell lines. Interestingly, only IL-23R2 and/or IL-23R4 variants are predominantly detected in certain human lung carcinomas, but not in their resected normal margin tissues. Thus, our results indicate that the regulation of alternative splicing on the IL-23R gene is complicated, and the preferential expression of certain IL-23R spliced variants may be a contributive factor to the pathogenesis of certain cancers.	D008175	Lung Neoplasms
IL23R	16372191	Identification and expression analysis of alternatively spliced isoforms of human interleukin-23 receptor gene in normal lymphoid cells and selected tumor cells.	Interleukin 23 (IL-23) is a new member of the IL-12 family that plays a critical role in promoting the proliferation of memory T helper 1 cells. The heterodimerized IL-23 receptor is composed of a shared IL-12 receptor beta 1 (IL-12Rbeta1) and an IL-12Rbeta2-related molecule called IL-23R. The standard form of IL-23R is encoded by at least 12 exons. Here, we demonstrate that at least six spliced isoforms of IL-23R (IL-23R1 to 6) can be generated through alternative splicing. The splicing strategies for the IL-23R gene are complicated and most often result in the deletion of exon 7 and/or exon 10. Translation prediction revealed that these spliced variants result in either premature termination to give rise to a diverse form of receptor ectodomain, or a frameshift to generate various lengths of the IL-23R endodomain. Differential expressions of IL-23R spliced variants are observed in natural killer and CD3+ CD4+ T cells. The expressions of these spliced variants are also prevalently and complicatedly regulated in tumor cell lines. Interestingly, only IL-23R2 and/or IL-23R4 variants are predominantly detected in certain human lung carcinomas, but not in their resected normal margin tissues. Thus, our results indicate that the regulation of alternative splicing on the IL-23R gene is complicated, and the preferential expression of certain IL-23R spliced variants may be a contributive factor to the pathogenesis of certain cancers.	D009369	Neoplasms
IL23R	18754016	Identification and characterization of multiple splice forms of the human interleukin-23 receptor alpha chain in mitogen-activated leukocytes.	The signalling of interleukin-23 (IL-23) and its receptor (IL-23R) is a key element in the differentiation of T cells to the Th17 phenotype. Here, we present the identification and characterization of human IL23R splice variants resulting from alternative splicing of the IL23R mRNA, from activated human leukocytes, following the analysis of IL23R cDNA. Twenty-four different IL23R transcripts were observed in this study, which may potentially lead to an alteration in the protein coding region of IL-23R alpha. Consequently, by analysing amino acid sequences deduced from alternatively spliced mRNA sequences, four different putative premature early termination forms of IL-23R alpha: (1) a very short 'IL-23R alpha', (2) an IL-23R alpha containing only the extracellular region, (3) a IL-23R alpha with truncated intracellular domain and (4) in-frame exon-skipping causing changes to the extracellular region of the IL-23R alpha were revealed. These changes may affect the function of IL-23R by altering the ligand-binding interaction, producing a soluble form of the receptor to act as a decoy receptor and/or modify the IL-23/IL-23R signalling, respectively. Taken together, identification of potentially functional splice variants of IL23R underscores the biological diversity of the IL23R gene and will aid in the understanding of the gene's function in normal and pathological conditions.	D003424	Crohn Disease
IL23R	18754016	Identification and characterization of multiple splice forms of the human interleukin-23 receptor alpha chain in mitogen-activated leukocytes.	The signalling of interleukin-23 (IL-23) and its receptor (IL-23R) is a key element in the differentiation of T cells to the Th17 phenotype. Here, we present the identification and characterization of human IL23R splice variants resulting from alternative splicing of the IL23R mRNA, from activated human leukocytes, following the analysis of IL23R cDNA. Twenty-four different IL23R transcripts were observed in this study, which may potentially lead to an alteration in the protein coding region of IL-23R alpha. Consequently, by analysing amino acid sequences deduced from alternatively spliced mRNA sequences, four different putative premature early termination forms of IL-23R alpha: (1) a very short 'IL-23R alpha', (2) an IL-23R alpha containing only the extracellular region, (3) a IL-23R alpha with truncated intracellular domain and (4) in-frame exon-skipping causing changes to the extracellular region of the IL-23R alpha were revealed. These changes may affect the function of IL-23R by altering the ligand-binding interaction, producing a soluble form of the receptor to act as a decoy receptor and/or modify the IL-23/IL-23R signalling, respectively. Taken together, identification of potentially functional splice variants of IL23R underscores the biological diversity of the IL23R gene and will aid in the understanding of the gene's function in normal and pathological conditions.	D020022	Genetic Predisposition to Disease

Clinically important variants in IL23R

(ClinVar, 04/20/2024)

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uniprot_id

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Clinical_significance