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Protein

Interleukin-23 subunit alpha

Gene

IL23A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Associates with IL12B to form the IL-23 interleukin, a heterodimeric cytokine which functions in innate and adaptive immunity. IL-23 may constitute with IL-17 an acute response to infection in peripheral tissues. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R, activates the Jak-Stat signaling cascade, stimulates memory rather than naive T-cells and promotes production of proinflammatory cytokines. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis.3 Publications

GO - Biological processi

  • defense response to Gram-negative bacterium Source: BHF-UCL
  • defense response to virus Source: UniProtKB-KW
  • inflammatory response Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
  • negative regulation of interleukin-10 production Source: BHF-UCL
  • positive regulation of activated T cell proliferation Source: BHF-UCL
  • positive regulation of activation of JAK2 kinase activity Source: BHF-UCL
  • positive regulation of defense response to virus by host Source: BHF-UCL
  • positive regulation of granulocyte macrophage colony-stimulating factor production Source: BHF-UCL
  • positive regulation of inflammatory response Source: BHF-UCL
  • positive regulation of interferon-gamma production Source: BHF-UCL
  • positive regulation of interleukin-10 production Source: BHF-UCL
  • positive regulation of interleukin-12 production Source: BHF-UCL
  • positive regulation of interleukin-17 production Source: BHF-UCL
  • positive regulation of memory T cell differentiation Source: BHF-UCL
  • positive regulation of natural killer cell activation Source: BHF-UCL
  • positive regulation of natural killer cell proliferation Source: BHF-UCL
  • positive regulation of neutrophil chemotaxis Source: Ensembl
  • positive regulation of NF-kappaB import into nucleus Source: BHF-UCL
  • positive regulation of NK T cell activation Source: BHF-UCL
  • positive regulation of NK T cell proliferation Source: BHF-UCL
  • positive regulation of osteoclast differentiation Source: BHF-UCL
  • positive regulation of T cell mediated cytotoxicity Source: BHF-UCL
  • positive regulation of T cell proliferation Source: BHF-UCL
  • positive regulation of T-helper 17 cell lineage commitment Source: BHF-UCL
  • positive regulation of T-helper 17 type immune response Source: BHF-UCL
  • positive regulation of T-helper 1 type immune response Source: BHF-UCL
  • positive regulation of tissue remodeling Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • positive regulation of tumor necrosis factor production Source: BHF-UCL
  • positive regulation of tyrosine phosphorylation of Stat3 protein Source: BHF-UCL
  • positive regulation of tyrosine phosphorylation of Stat4 protein Source: BHF-UCL
  • positive regulation of tyrosine phosphorylation of Stat5 protein Source: BHF-UCL
  • regulation of tyrosine phosphorylation of Stat1 protein Source: BHF-UCL
  • T cell proliferation Source: Ensembl
  • tissue remodeling Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Antiviral defense, Immunity, Inflammatory response, Innate immunity, Tissue remodeling

Enzyme and pathway databases

SignaLinkiQ9NPF7.

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-23 subunit alpha
Short name:
IL-23 subunit alpha
Short name:
IL-23-A
Alternative name(s):
Interleukin-23 subunit p19
Short name:
IL-23p19
Gene namesi
Name:IL23A
Synonyms:SGRF
ORF Names:UNQ2498/PRO5798
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:15488. IL23A.

Subcellular locationi

GO - Cellular componenti

  • interleukin-23 complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29824.

Polymorphism and mutation databases

BioMutaiIL23A.
DMDMi74761641.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 189170Interleukin-23 subunit alphaPRO_0000259488Add
BLAST

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ9NPF7.
PRIDEiQ9NPF7.

Expressioni

Tissue specificityi

Secreted by activated dendritic and phagocytic cells and keratinocytes. Also expressed by dermal Langerhans cells (at protein level).2 Publications

Developmental stagei

Expressed by newborns dendritic cells.1 Publication

Inductioni

Up-regulated by a wide array of pathogens and pathogen-products together with self-signals for danger or injury. Up-regulated in psoriatic dermal tissues, in dendritic cells of multiple sclerosis patients and in tumors.7 Publications

Gene expression databases

BgeeiQ9NPF7.
CleanExiHS_IL23A.
GenevisibleiQ9NPF7. HS.

Organism-specific databases

HPAiHPA001554.

Interactioni

Subunit structurei

Heterodimer with IL12B; disulfide-linked. The heterodimer is known as interleukin IL-23.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
IL12BP294603EBI-2481154,EBI-1029614
PEX19P408553EBI-2481154,EBI-594747

Protein-protein interaction databases

BioGridi119611. 7 interactions.
IntActiQ9NPF7. 2 interactions.
STRINGi9606.ENSP00000228534.

Structurei

Secondary structure

1
189
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 4617Combined sources
Turni49 – 513Combined sources
Helixi61 – 633Combined sources
Helixi73 – 753Combined sources
Helixi79 – 857Combined sources
Helixi87 – 10418Combined sources
Helixi107 – 1104Combined sources
Beta strandi111 – 1133Combined sources
Helixi120 – 13516Combined sources
Beta strandi136 – 1383Combined sources
Helixi155 – 18632Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D85X-ray1.90C20-189[»]
3D87X-ray2.90A/C20-189[»]
3DUHX-ray2.30C/D20-189[»]
3QWRX-ray3.25B20-189[»]
4GRWX-ray2.55A/C1-189[»]
4OE8X-ray1.74B1-189[»]
4OG9X-ray3.39B1-189[»]
ProteinModelPortaliQ9NPF7.
SMRiQ9NPF7. Positions 27-188.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NPF7.

Family & Domainsi

Sequence similaritiesi

Belongs to the IL-6 superfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG42887.
GeneTreeiENSGT00390000006482.
HOGENOMiHOG000048728.
HOVERGENiHBG081786.
InParanoidiQ9NPF7.
KOiK05426.
OMAiIHQGLVF.
OrthoDBiEOG76HQ32.
PhylomeDBiQ9NPF7.
TreeFamiTF337234.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR010831. IL-23_alpha.
IPR003573. IL-6/IL-23/GCSF/MGF.
[Graphical view]
PANTHERiPTHR15947. PTHR15947. 1 hit.
PfamiPF00489. IL6. 1 hit.
[Graphical view]
SUPFAMiSSF47266. SSF47266. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NPF7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGSRAVMLL LLLPWTAQGR AVPGGSSPAW TQCQQLSQKL CTLAWSAHPL
60 70 80 90 100
VGHMDLREEG DEETTNDVPH IQCGDGCDPQ GLRDNSQFCL QRIHQGLIFY
110 120 130 140 150
EKLLGSDIFT GEPSLLPDSP VGQLHASLLG LSQLLQPEGH HWETQQIPSL
160 170 180
SPSQPWQRLL LRFKILRSLQ AFVAVAARVF AHGAATLSP
Length:189
Mass (Da):20,730
Last modified:October 1, 2000 - v1
Checksum:i51B5C0F188EC1B9F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221G → A in AAG37232 (PubMed:11114383).Curated
Sequence conflicti147 – 1471I → M in AAH66267 (PubMed:15489334).Curated
Sequence conflicti168 – 1681S → N in AAH66267 (PubMed:15489334).Curated
Sequence conflicti173 – 1731V → A in AAH66269 (PubMed:15489334).Curated
Sequence conflicti189 – 1891P → L in AAH66269 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF301620 mRNA. Translation: AAG37232.1.
AB030000 mRNA. Translation: BAA93686.1.
AB030001 Genomic DNA. Translation: BAA93687.1.
AY359083 mRNA. Translation: AAQ89442.1.
BC066267 mRNA. Translation: AAH66267.1.
BC066268 mRNA. Translation: AAH66268.1.
BC066269 mRNA. Translation: AAH66269.1.
BC067511 mRNA. Translation: AAH67511.1.
BC067512 mRNA. Translation: AAH67512.1.
BC067513 mRNA. Translation: AAH67513.1.
CCDSiCCDS8916.1.
RefSeqiNP_057668.1. NM_016584.2.
UniGeneiHs.382212.
Hs.98309.

Genome annotation databases

EnsembliENST00000228534; ENSP00000228534; ENSG00000110944.
GeneIDi51561.
KEGGihsa:51561.
UCSCiuc001sla.3. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF301620 mRNA. Translation: AAG37232.1.
AB030000 mRNA. Translation: BAA93686.1.
AB030001 Genomic DNA. Translation: BAA93687.1.
AY359083 mRNA. Translation: AAQ89442.1.
BC066267 mRNA. Translation: AAH66267.1.
BC066268 mRNA. Translation: AAH66268.1.
BC066269 mRNA. Translation: AAH66269.1.
BC067511 mRNA. Translation: AAH67511.1.
BC067512 mRNA. Translation: AAH67512.1.
BC067513 mRNA. Translation: AAH67513.1.
CCDSiCCDS8916.1.
RefSeqiNP_057668.1. NM_016584.2.
UniGeneiHs.382212.
Hs.98309.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D85X-ray1.90C20-189[»]
3D87X-ray2.90A/C20-189[»]
3DUHX-ray2.30C/D20-189[»]
3QWRX-ray3.25B20-189[»]
4GRWX-ray2.55A/C1-189[»]
4OE8X-ray1.74B1-189[»]
4OG9X-ray3.39B1-189[»]
ProteinModelPortaliQ9NPF7.
SMRiQ9NPF7. Positions 27-188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119611. 7 interactions.
IntActiQ9NPF7. 2 interactions.
STRINGi9606.ENSP00000228534.

Chemistry

ChEMBLiCHEMBL2364154.

Polymorphism and mutation databases

BioMutaiIL23A.
DMDMi74761641.

Proteomic databases

PaxDbiQ9NPF7.
PRIDEiQ9NPF7.

Protocols and materials databases

DNASUi51561.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228534; ENSP00000228534; ENSG00000110944.
GeneIDi51561.
KEGGihsa:51561.
UCSCiuc001sla.3. human.

Organism-specific databases

CTDi51561.
GeneCardsiGC12P056732.
HGNCiHGNC:15488. IL23A.
HPAiHPA001554.
MIMi605580. gene.
neXtProtiNX_Q9NPF7.
PharmGKBiPA29824.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42887.
GeneTreeiENSGT00390000006482.
HOGENOMiHOG000048728.
HOVERGENiHBG081786.
InParanoidiQ9NPF7.
KOiK05426.
OMAiIHQGLVF.
OrthoDBiEOG76HQ32.
PhylomeDBiQ9NPF7.
TreeFamiTF337234.

Enzyme and pathway databases

SignaLinkiQ9NPF7.

Miscellaneous databases

EvolutionaryTraceiQ9NPF7.
GeneWikiiInterleukin_23.
GenomeRNAii51561.
NextBioi55362.
PROiQ9NPF7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NPF7.
CleanExiHS_IL23A.
GenevisibleiQ9NPF7. HS.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR010831. IL-23_alpha.
IPR003573. IL-6/IL-23/GCSF/MGF.
[Graphical view]
PANTHERiPTHR15947. PTHR15947. 1 hit.
PfamiPF00489. IL6. 1 hit.
[Graphical view]
SUPFAMiSSF47266. SSF47266. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH IL12B, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "SGRF; a novel member of the IL-6/G-CSF family."
    Hirata Y., Kosuge Y.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Spleen.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Cited for: FUNCTION, INTERACTION WITH IL12RB1 AND IL23R.
  6. "Regulation of virus-induced IL-12 and IL-23 expression in human macrophages."
    Pirhonen J., Matikainen S., Julkunen I.
    J. Immunol. 169:5673-5678(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  7. "Commensal Gram-negative bacteria prime human dendritic cells for enhanced IL-23 and IL-27 expression and enhanced Th1 development."
    Smits H.H., van Beelen A.J., Hessle C., Westland R., de Jong E., Soeteman E., Wold A., Wierenga E.A., Kapsenberg M.L.
    Eur. J. Immunol. 34:1371-1380(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "Extracellular nucleotide signaling by P2 receptors inhibits IL-12 and enhances IL-23 expression in human dendritic cells: a novel role for the cAMP pathway."
    Schnurr M., Toy T., Shin A., Wagner M., Cebon J., Maraskovsky E.
    Blood 105:1582-1589(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  9. "Bordetella pertussis-infected human monocyte-derived dendritic cells undergo maturation and induce Th1 polarization and interleukin-23 expression."
    Fedele G., Stefanelli P., Spensieri F., Fazio C., Mastrantonio P., Ausiello C.M.
    Infect. Immun. 73:1590-1597(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "Preferential production of the IL-12(p40)/IL-23(p19) heterodimer by dendritic cells from human newborns."
    Vanden Eijnden S., Goriely S., De Wit D., Goldman M., Willems F.
    Eur. J. Immunol. 36:21-26(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  11. "In vitro and in situ expression of IL-23 by keratinocytes in healthy skin and psoriasis lesions: enhanced expression in psoriatic skin."
    Piskin G., Sylva-Steenland R.M.R., Bos J.D., Teunissen M.B.M.
    J. Immunol. 176:1908-1915(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
  12. "IL-23 is increased in dendritic cells in multiple sclerosis and down-regulation of IL-23 by antisense oligos increases dendritic cell IL-10 production."
    Vaknin-Dembinsky A., Balashov K., Weiner H.L.
    J. Immunol. 176:7768-7774(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  13. Cited for: INDUCTION.
  14. "The structure of interleukin-23 reveals the molecular basis of p40 subunit sharing with interleukin-12."
    Lupardus P.J., Garcia K.C.
    J. Mol. Biol. 382:931-941(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 20-189 IN COMPLEX WITH IL12B, SUBUNIT.

Entry informationi

Entry nameiIL23A_HUMAN
AccessioniPrimary (citable) accession number: Q9NPF7
Secondary accession number(s): Q6NZ80, Q6NZ82, Q9H2A5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.