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Protein

Interleukin-12 subunit beta

Gene

IL12B

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

Functioni

Cytokine that can act as a growth factor for activated T and NK cells, enhance the lytic activity of NK/lymphokine-activated killer cells, and stimulate the production of IFN-gamma by resting PBMC.1 Publication
Associates with IL23A 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.1 Publication

GO - Molecular functioni

  • cytokine receptor activity Source: InterPro
  • identical protein binding Source: IntAct
  • interleukin-12 alpha subunit binding Source: AgBase
  • interleukin-12 receptor binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  • cell cycle arrest Source: BHF-UCL
  • cell migration Source: UniProtKB
  • cellular response to interferon-gamma Source: Ensembl
  • cellular response to lipopolysaccharide Source: Ensembl
  • defense response to Gram-negative bacterium Source: BHF-UCL
  • defense response to protozoan Source: Ensembl
  • defense response to virus Source: Ensembl
  • interferon-gamma biosynthetic process Source: UniProtKB
  • natural killer cell activation Source: UniProtKB
  • natural killer cell activation involved in immune response Source: Ensembl
  • negative regulation of growth of symbiont in host Source: Ensembl
  • negative regulation of inflammatory response to antigenic stimulus Source: Ensembl
  • negative regulation of interleukin-10 production Source: BHF-UCL
  • negative regulation of interleukin-17 production Source: BHF-UCL
  • negative regulation of smooth muscle cell proliferation Source: BHF-UCL
  • positive regulation of activated T cell proliferation Source: UniProtKB
  • positive regulation of activation of JAK2 kinase activity Source: BHF-UCL
  • positive regulation of cell adhesion Source: UniProtKB
  • 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 biosynthetic process Source: UniProtKB
  • positive regulation of interferon-gamma production Source: UniProtKB
  • 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 lymphocyte proliferation Source: UniProtKB
  • positive regulation of memory T cell differentiation Source: BHF-UCL
  • positive regulation of mononuclear cell proliferation Source: AgBase
  • positive regulation of natural killer cell activation Source: UniProtKB
  • positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target Source: UniProtKB
  • positive regulation of natural killer cell proliferation Source: BHF-UCL
  • 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 smooth muscle cell apoptotic process 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 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 cytokine biosynthetic process Source: UniProtKB
  • regulation of tyrosine phosphorylation of Stat1 protein Source: BHF-UCL
  • response to UV-B Source: UniProtKB
  • sensory perception of pain Source: Ensembl
  • sexual reproduction Source: BHF-UCL
  • T-helper 1 type immune response Source: UniProtKB
  • T-helper cell differentiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-12 subunit beta
Short name:
IL-12B
Alternative name(s):
Cytotoxic lymphocyte maturation factor 40 kDa subunit
Short name:
CLMF p40
IL-12 subunit p40
NK cell stimulatory factor chain 2
Short name:
NKSF2
Gene namesi
Name:IL12B
Synonyms:NKSF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:5970. IL12B.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: Ensembl
  • extracellular space Source: UniProtKB
  • interleukin-12 complex Source: UniProtKB
  • interleukin-23 complex Source: BHF-UCL
  • membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Immunodeficiency 29 (IMD29)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of Mendelian susceptibility to mycobacterial disease, a rare condition caused by impairment of interferon-gamma mediated immunity. It is characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. Clinical outcome severity depends on the degree of impairment of interferon-gamma mediated immunity. Some patients die of overwhelming mycobacterial disease with lepromatous-like lesions in early childhood, whereas others develop, later in life, disseminated but curable infections with tuberculoid granulomas. IMD29 is characterized by undetectable IL12B secretion from leukocytes. Affected individuals generally present with BCG disease after vaccination in childhood, and at least half also have Salmonella infection. Disease phenotype is relatively mild, and patients have a good prognosis.

See also OMIM:614890
Psoriasis 11 (PSORS11)

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionA common, chronic inflammatory disease of the skin with multifactorial etiology. It is characterized by red, scaly plaques usually found on the scalp, elbows and knees. These lesions are caused by abnormal keratinocyte proliferation and infiltration of inflammatory cells into the dermis and epidermis.

See also OMIM:612599

Organism-specific databases

MIMi612599. phenotype.
614890. phenotype.
Orphaneti319558. Mendelian susceptibility to mycobacterial diseases due to complete IL12B deficiency.
3287. Takayasu arteritis.
PharmGKBiPA29785.

Chemistry

DrugBankiDB05679. Ustekinumab.

Polymorphism and mutation databases

BioMutaiIL12B.
DMDMi266320.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 328306Interleukin-12 subunit betaPRO_0000010930Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 90PROSITE-ProRule annotation1 Publication
Disulfide bondi131 ↔ 142PROSITE-ProRule annotation1 Publication
Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi170 ↔ 193PROSITE-ProRule annotation1 Publication
Disulfide bondi199 – 199Interchain (with C-96 in IL12A)PROSITE-ProRule annotation1 Publication
Glycosylationi222 – 2221N-linked (GlcNAc...)1 Publication
Disulfide bondi300 ↔ 327PROSITE-ProRule annotation1 Publication
Glycosylationi319 – 3191C-linked (Man)CAR_000187

Post-translational modificationi

Known to be C-mannosylated in the recombinant protein; it is not yet known for sure if the wild-type protein is also modified.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP29460.
PRIDEiP29460.

PTM databases

PhosphoSiteiP29460.
UniCarbKBiP29460.

Miscellaneous databases

PMAP-CutDBP29460.

Expressioni

Gene expression databases

BgeeiP29460.
CleanExiHS_IL12B.
GenevisibleiP29460. HS.

Organism-specific databases

HPAiHPA040970.

Interactioni

Subunit structurei

Heterodimer with IL12A; disulfide-linked. The heterodimer is known as interleukin IL-12. Heterodimer with IL23A; disulfide-linked. The heterodimer is known as interleukin IL-23. Also secreted as a monomer.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1029614,EBI-1029614
IL12AP294592EBI-1029614,EBI-1029636
IL23AQ9NPF73EBI-1029614,EBI-2481154
Il23aQ9EQ142EBI-1029614,EBI-2481329From a different organism.

Protein-protein interaction databases

BioGridi109807. 2 interactions.
DIPiDIP-3774N.
IntActiP29460. 4 interactions.
STRINGi9606.ENSP00000231228.

Structurei

Secondary structure

1
328
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 274Combined sources
Beta strandi30 – 367Combined sources
Beta strandi44 – 496Combined sources
Beta strandi51 – 533Combined sources
Beta strandi59 – 624Combined sources
Beta strandi70 – 7910Combined sources
Helixi82 – 843Combined sources
Beta strandi86 – 927Combined sources
Beta strandi95 – 10814Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi122 – 1265Combined sources
Beta strandi130 – 14718Combined sources
Beta strandi150 – 16011Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi166 – 1705Combined sources
Beta strandi174 – 19522Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi208 – 2169Combined sources
Beta strandi219 – 2279Combined sources
Helixi229 – 2324Combined sources
Beta strandi239 – 2457Combined sources
Beta strandi249 – 2579Combined sources
Beta strandi260 – 2623Combined sources
Turni266 – 2683Combined sources
Beta strandi271 – 2788Combined sources
Beta strandi287 – 29913Combined sources
Beta strandi305 – 31511Combined sources
Beta strandi323 – 3264Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F42X-ray2.50A23-328[»]
1F45X-ray2.80A23-328[»]
3D85X-ray1.90D23-328[»]
3D87X-ray2.90B/D23-328[»]
3DUHX-ray2.30A/B23-328[»]
3HMXX-ray3.00A23-328[»]
3QWRX-ray3.25A23-328[»]
4GRWX-ray2.55B/D1-328[»]
4OE8X-ray1.74A1-328[»]
4OG9X-ray3.39A1-328[»]
ProteinModelPortaliP29460.
SMRiP29460. Positions 23-328.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29460.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 10684Ig-like C2-typeAdd
BLAST
Domaini237 – 32892Fibronectin type-IIIPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Signal

Phylogenomic databases

eggNOGiNOG45642.
GeneTreeiENSGT00390000012630.
HOGENOMiHOG000113027.
HOVERGENiHBG052094.
InParanoidiP29460.
KOiK05425.
OMAiWSTPHSY.
OrthoDBiEOG7TBC2K.
PhylomeDBiP29460.
TreeFamiTF334829.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR003961. FN3_dom.
IPR003530. Hematopoietin_rcpt_L_F3_CS.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
IPR015528. IL-12_beta.
IPR019482. IL-12_beta_cen-dom.
[Graphical view]
PANTHERiPTHR11321. PTHR11321. 1 hit.
PfamiPF10420. IL12p40_C. 1 hit.
[Graphical view]
PIRSFiPIRSF038007. IL_12_beta. 1 hit.
PRINTSiPR01928. INTRLEUKN12B.
SMARTiSM00408. IGc2. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 1 hit.
PS01354. HEMATOPO_REC_L_F3. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P29460-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCHQQLVISW FSLVFLASPL VAIWELKKDV YVVELDWYPD APGEMVVLTC
60 70 80 90 100
DTPEEDGITW TLDQSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGEVLSHS
110 120 130 140 150
LLLLHKKEDG IWSTDILKDQ KEPKNKTFLR CEAKNYSGRF TCWWLTTIST
160 170 180 190 200
DLTFSVKSSR GSSDPQGVTC GAATLSAERV RGDNKEYEYS VECQEDSACP
210 220 230 240 250
AAEESLPIEV MVDAVHKLKY ENYTSSFFIR DIIKPDPPKN LQLKPLKNSR
260 270 280 290 300
QVEVSWEYPD TWSTPHSYFS LTFCVQVQGK SKREKKDRVF TDKTSATVIC
310 320
RKNASISVRA QDRYYSSSWS EWASVPCS
Length:328
Mass (Da):37,169
Last modified:April 1, 1993 - v1
Checksum:i118FA801B8F5BB2F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 2391K → N in AAA59938 (PubMed:1673147).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331V → I.1 Publication
Corresponds to variant rs3213096 [ dbSNP | Ensembl ].
VAR_020001
Natural varianti298 – 2981V → F.1 Publication
Corresponds to variant rs3213119 [ dbSNP | Ensembl ].
VAR_049170

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65272 mRNA. Translation: AAA35695.1.
M65290 mRNA. Translation: AAA59938.1.
AY008847 Genomic DNA. Translation: AAG32620.1.
AF180563 mRNA. Translation: AAD56386.1.
AF512686 Genomic DNA. Translation: AAM34792.1.
BC067498 mRNA. Translation: AAH67498.1.
BC067499 mRNA. Translation: AAH67499.1.
BC067500 mRNA. Translation: AAH67500.1.
BC067501 mRNA. Translation: AAH67501.1.
BC067502 mRNA. Translation: AAH67502.1.
BC074723 mRNA. Translation: AAH74723.1.
CCDSiCCDS4346.1.
PIRiA38957.
RefSeqiNP_002178.2. NM_002187.2.
UniGeneiHs.674.

Genome annotation databases

EnsembliENST00000231228; ENSP00000231228; ENSG00000113302.
GeneIDi3593.
KEGGihsa:3593.
UCSCiuc003lxr.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

IL12Bbase

IL12B mutation db

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65272 mRNA. Translation: AAA35695.1.
M65290 mRNA. Translation: AAA59938.1.
AY008847 Genomic DNA. Translation: AAG32620.1.
AF180563 mRNA. Translation: AAD56386.1.
AF512686 Genomic DNA. Translation: AAM34792.1.
BC067498 mRNA. Translation: AAH67498.1.
BC067499 mRNA. Translation: AAH67499.1.
BC067500 mRNA. Translation: AAH67500.1.
BC067501 mRNA. Translation: AAH67501.1.
BC067502 mRNA. Translation: AAH67502.1.
BC074723 mRNA. Translation: AAH74723.1.
CCDSiCCDS4346.1.
PIRiA38957.
RefSeqiNP_002178.2. NM_002187.2.
UniGeneiHs.674.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F42X-ray2.50A23-328[»]
1F45X-ray2.80A23-328[»]
3D85X-ray1.90D23-328[»]
3D87X-ray2.90B/D23-328[»]
3DUHX-ray2.30A/B23-328[»]
3HMXX-ray3.00A23-328[»]
3QWRX-ray3.25A23-328[»]
4GRWX-ray2.55B/D1-328[»]
4OE8X-ray1.74A1-328[»]
4OG9X-ray3.39A1-328[»]
ProteinModelPortaliP29460.
SMRiP29460. Positions 23-328.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109807. 2 interactions.
DIPiDIP-3774N.
IntActiP29460. 4 interactions.
STRINGi9606.ENSP00000231228.

Chemistry

ChEMBLiCHEMBL2364153.
DrugBankiDB05679. Ustekinumab.

PTM databases

PhosphoSiteiP29460.
UniCarbKBiP29460.

Polymorphism and mutation databases

BioMutaiIL12B.
DMDMi266320.

Proteomic databases

PaxDbiP29460.
PRIDEiP29460.

Protocols and materials databases

DNASUi3593.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000231228; ENSP00000231228; ENSG00000113302.
GeneIDi3593.
KEGGihsa:3593.
UCSCiuc003lxr.1. human.

Organism-specific databases

CTDi3593.
GeneCardsiGC05M158741.
HGNCiHGNC:5970. IL12B.
HPAiHPA040970.
MIMi161561. gene.
612599. phenotype.
614890. phenotype.
neXtProtiNX_P29460.
Orphaneti319558. Mendelian susceptibility to mycobacterial diseases due to complete IL12B deficiency.
3287. Takayasu arteritis.
PharmGKBiPA29785.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG45642.
GeneTreeiENSGT00390000012630.
HOGENOMiHOG000113027.
HOVERGENiHBG052094.
InParanoidiP29460.
KOiK05425.
OMAiWSTPHSY.
OrthoDBiEOG7TBC2K.
PhylomeDBiP29460.
TreeFamiTF334829.

Miscellaneous databases

EvolutionaryTraceiP29460.
GeneWikiiInterleukin-12_subunit_beta.
GenomeRNAii3593.
NextBioi14039.
PMAP-CutDBP29460.
PROiP29460.
SOURCEiSearch...

Gene expression databases

BgeeiP29460.
CleanExiHS_IL12B.
GenevisibleiP29460. HS.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR003961. FN3_dom.
IPR003530. Hematopoietin_rcpt_L_F3_CS.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
IPR015528. IL-12_beta.
IPR019482. IL-12_beta_cen-dom.
[Graphical view]
PANTHERiPTHR11321. PTHR11321. 1 hit.
PfamiPF10420. IL12p40_C. 1 hit.
[Graphical view]
PIRSFiPIRSF038007. IL_12_beta. 1 hit.
PRINTSiPR01928. INTRLEUKN12B.
SMARTiSM00408. IGc2. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 1 hit.
PS01354. HEMATOPO_REC_L_F3. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Coexpression of two distinct genes is required to generate secreted bioactive cytotoxic lymphocyte maturation factor."
    Gubler U., Chua A.O., Schoenhaut D.S., Dwyer C.M., McComas W., Motyka R., Nabavi N., Wolitzky A.G., Quinn P.M., Familletti P.C., Gately M.K.
    Proc. Natl. Acad. Sci. U.S.A. 88:4143-4147(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of cDNA for natural killer cell stimulatory factor, a heterodimeric cytokine with multiple biologic effects on T and natural killer cells."
    Wolf S.F., Temple P.A., Kobayashi M., Young D., Dicig M., Lowe L., Dzialo R., Fitz L., Ferenz C., Hewick R.M., Kelleher K., Herrmann S.H., Clark S.C., Azzoni L., Chan S.H., Trinchieri G., Perussia B.
    J. Immunol. 146:3074-3081(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Complete primary structure, chromosomal localization, and definition of polymorphisms of the gene encoding the human interleukin 12 p40 subunit."
    Huang D., Cancilla M.R., Morahan G.
    Genes Immun. 1:515-520(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Cloning and sequence analysis of IL-12 cDNA from Chinese."
    Hongyuan J., Meiyun Z.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. SeattleSNPs variation discovery resource
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-33 AND PHE-298.
  6. "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].
    Tissue: Brain.
  7. "Purification to homogeneity and partial characterization of cytotoxic lymphocyte maturation factor from human B-lymphoblastoid cells."
    Stern A.S., Podlaski F.J., Hulmes J.D., Pan Y.C.E., Quinn P.M., Wolitzky A.G., Familletti P.C., Stremlo D.L., Truitt T., Chizzonite R., Gately M.K.
    Proc. Natl. Acad. Sci. U.S.A. 87:6808-6812(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-45.
  8. "Homology of the p40 subunit of natural killer cell stimulatory factor (NKSF) with the extracellular domain of the interleukin-6 receptor."
    Gearing D.P., Cosman D.
    Cell 66:9-10(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO IL-6 RECEPTOR.
  9. "Stimulatory and inhibitory effects of interleukin (IL)-4 and IL-13 on the production of cytokines by human peripheral blood mononuclear cells: priming for IL-12 and tumor necrosis factor alpha production."
    D'Andrea A., Ma X., Aste-Amezaga M., Paganin C., Trinchieri G.
    J. Exp. Med. 181:537-546(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  10. "Recombinant human interleukin-12 is the second example of a C-mannosylated protein."
    Doucey M.A., Hess D., Blommers M.J., Hofsteenge J.
    Glycobiology 9:435-441(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT TRP-319.
  11. Cited for: INVOLVEMENT IN IMD29.
  12. Cited for: FUNCTION, INTERACTION WITH IL23A.
  13. Cited for: INVOLVEMENT IN IMD29.
  14. "Sequence variants in the genes for the interleukin-23 receptor (IL23R) and its ligand (IL12B) confer protection against psoriasis."
    Capon F., Di Meglio P., Szaub J., Prescott N.J., Dunster C., Baumber L., Timms K., Gutin A., Abkevic V., Burden A.D., Lanchbury J., Barker J.N., Trembath R.C., Nestle F.O.
    Hum. Genet. 122:201-206(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH PSORIASIS.
  15. "Genetic variants of the IL-23R pathway: association with psoriatic arthritis and psoriasis vulgaris, but no specific risk factor for arthritis."
    Huffmeier U., Lascorz J., Bohm B., Lohmann J., Wendler J., Mossner R., Reich K., Traupe H., Kurrat W., Burkhardt H., Reis A.
    J. Invest. Dermatol. 129:355-358(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH PSORIASIS.
  16. "Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12."
    Yoon C., Johnston S.C., Tang J., Stahl M., Tobin J.F., Somers W.S.
    EMBO J. 19:3530-3541(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-328 ALONE AND IN COMPLEX WITH IL12A, GLYCOSYLATION AT ASN-222, DISULFIDE BONDS.
  17. "Crystal structures of the pro-inflammatory cytokine interleukin-23 and its complex with a high-affinity neutralizing antibody."
    Beyer B.M., Ingram R., Ramanathan L., Reichert P., Le H.V., Madison V., Orth P.
    J. Mol. Biol. 382:942-955(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 23-328 IN COMPLEX WITH IL23A AND ANTIBODY.
  18. "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 23-328 IN COMPLEX WITH IL23A, SUBUNIT.

Entry informationi

Entry nameiIL12B_HUMAN
AccessioniPrimary (citable) accession number: P29460
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: July 22, 2015
This is version 180 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.