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P29460

- IL12B_HUMAN

UniProt

P29460 - IL12B_HUMAN

Protein

Interleukin-12 subunit beta

Gene

IL12B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    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

    1. cytokine receptor activity Source: InterPro
    2. identical protein binding Source: IntAct
    3. interleukin-12 alpha subunit binding Source: AgBase
    4. interleukin-12 receptor binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein heterodimerization activity Source: UniProtKB

    GO - Biological processi

    1. cell cycle arrest Source: BHF-UCL
    2. cell migration Source: UniProtKB
    3. cellular response to interferon-gamma Source: Ensembl
    4. cellular response to lipopolysaccharide Source: Ensembl
    5. defense response to Gram-negative bacterium Source: BHF-UCL
    6. defense response to protozoan Source: Ensembl
    7. defense response to virus Source: Ensembl
    8. interferon-gamma biosynthetic process Source: UniProtKB
    9. natural killer cell activation Source: UniProtKB
    10. natural killer cell activation involved in immune response Source: Ensembl
    11. negative regulation of growth of symbiont in host Source: Ensembl
    12. negative regulation of inflammatory response to antigenic stimulus Source: Ensembl
    13. negative regulation of interleukin-10 production Source: BHF-UCL
    14. negative regulation of interleukin-17 production Source: BHF-UCL
    15. negative regulation of smooth muscle cell proliferation Source: BHF-UCL
    16. positive regulation of activated T cell proliferation Source: UniProtKB
    17. positive regulation of activation of JAK2 kinase activity Source: BHF-UCL
    18. positive regulation of cell adhesion Source: UniProtKB
    19. positive regulation of defense response to virus by host Source: BHF-UCL
    20. positive regulation of granulocyte macrophage colony-stimulating factor production Source: BHF-UCL
    21. positive regulation of inflammatory response Source: BHF-UCL
    22. positive regulation of interferon-gamma biosynthetic process Source: UniProtKB
    23. positive regulation of interferon-gamma production Source: UniProtKB
    24. positive regulation of interleukin-10 production Source: BHF-UCL
    25. positive regulation of interleukin-12 production Source: BHF-UCL
    26. positive regulation of interleukin-17 production Source: BHF-UCL
    27. positive regulation of lymphocyte proliferation Source: UniProtKB
    28. positive regulation of memory T cell differentiation Source: BHF-UCL
    29. positive regulation of mononuclear cell proliferation Source: AgBase
    30. positive regulation of natural killer cell activation Source: UniProtKB
    31. positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target Source: UniProtKB
    32. positive regulation of natural killer cell proliferation Source: BHF-UCL
    33. positive regulation of NF-kappaB import into nucleus Source: BHF-UCL
    34. positive regulation of NK T cell activation Source: BHF-UCL
    35. positive regulation of NK T cell proliferation Source: BHF-UCL
    36. positive regulation of osteoclast differentiation Source: BHF-UCL
    37. positive regulation of smooth muscle cell apoptotic process Source: BHF-UCL
    38. positive regulation of T cell mediated cytotoxicity Source: BHF-UCL
    39. positive regulation of T cell proliferation Source: BHF-UCL
    40. positive regulation of T-helper 17 cell lineage commitment Source: BHF-UCL
    41. positive regulation of T-helper 17 type immune response Source: BHF-UCL
    42. positive regulation of T-helper 1 type immune response Source: BHF-UCL
    43. positive regulation of tissue remodeling Source: BHF-UCL
    44. positive regulation of tumor necrosis factor production Source: BHF-UCL
    45. positive regulation of tyrosine phosphorylation of Stat3 protein Source: BHF-UCL
    46. positive regulation of tyrosine phosphorylation of Stat4 protein Source: BHF-UCL
    47. positive regulation of tyrosine phosphorylation of Stat5 protein Source: BHF-UCL
    48. regulation of cytokine biosynthetic process Source: UniProtKB
    49. regulation of tyrosine phosphorylation of Stat1 protein Source: BHF-UCL
    50. response to UV-B Source: UniProtKB
    51. sensory perception of pain Source: Ensembl
    52. sexual reproduction Source: BHF-UCL
    53. T-helper 1 type immune response Source: UniProtKB
    54. T-helper cell differentiation Source: UniProtKB

    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: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:5970. IL12B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. extracellular space Source: UniProtKB
    3. interleukin-12 complex Source: UniProtKB
    4. interleukin-23 complex Source: BHF-UCL
    5. membrane Source: InterPro

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Mendelian susceptibility to mycobacterial disease (MSMD) [MIM:209950]: This rare condition confers predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine and 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. The pathogenic mechanism underlying MSMD is the impairment of interferon-gamma mediated immunity, whose severity determines the clinical outcome. 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. MSMD is a genetically heterogeneous disease with autosomal recessive, autosomal dominant or X-linked inheritance.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Psoriasis 11 (PSORS11) [MIM:612599]: A 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.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi209950. phenotype.
    612599. phenotype.
    Orphaneti319558. Mendelian susceptibility to mycobacterial diseases due to complete IL12B deficiency.
    3287. Takayasu arteritis.
    PharmGKBiPA29785.

    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 ↔ 901 PublicationPROSITE-ProRule annotation
    Disulfide bondi131 ↔ 1421 PublicationPROSITE-ProRule annotation
    Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi170 ↔ 1931 PublicationPROSITE-ProRule annotation
    Disulfide bondi199 – 199Interchain (with C-96 in IL12A)1 PublicationPROSITE-ProRule annotation
    Glycosylationi222 – 2221N-linked (GlcNAc...)1 Publication
    Disulfide bondi300 ↔ 3271 PublicationPROSITE-ProRule annotation
    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

    ArrayExpressiP29460.
    BgeeiP29460.
    CleanExiHS_IL12B.
    GenevestigatoriP29460.

    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 – 274
    Beta strandi30 – 367
    Beta strandi44 – 496
    Beta strandi51 – 533
    Beta strandi59 – 624
    Beta strandi70 – 7910
    Helixi82 – 843
    Beta strandi86 – 927
    Beta strandi95 – 10814
    Beta strandi116 – 1183
    Beta strandi122 – 1265
    Beta strandi130 – 14718
    Beta strandi150 – 16011
    Beta strandi162 – 1643
    Beta strandi166 – 1705
    Beta strandi174 – 1807
    Beta strandi182 – 1843
    Beta strandi185 – 19511
    Beta strandi200 – 2023
    Beta strandi208 – 2169
    Beta strandi219 – 2279
    Helixi229 – 2324
    Beta strandi239 – 2457
    Beta strandi247 – 2493
    Beta strandi252 – 2576
    Beta strandi260 – 2623
    Turni266 – 2683
    Beta strandi271 – 2788
    Beta strandi288 – 29811
    Beta strandi305 – 31511
    Beta strandi323 – 3264

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    HOGENOMiHOG000113027.
    HOVERGENiHBG052094.
    InParanoidiP29460.
    KOiK05425.
    OMAiWSTPHSY.
    OrthoDBiEOG7TBC2K.
    PhylomeDBiP29460.
    TreeFamiTF334829.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    InterProiIPR003961. Fibronectin_type3.
    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

    MCHQQLVISW FSLVFLASPL VAIWELKKDV YVVELDWYPD APGEMVVLTC    50
    DTPEEDGITW TLDQSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGEVLSHS 100
    LLLLHKKEDG IWSTDILKDQ KEPKNKTFLR CEAKNYSGRF TCWWLTTIST 150
    DLTFSVKSSR GSSDPQGVTC GAATLSAERV RGDNKEYEYS VECQEDSACP 200
    AAEESLPIEV MVDAVHKLKY ENYTSSFFIR DIIKPDPPKN LQLKPLKNSR 250
    QVEVSWEYPD TWSTPHSYFS LTFCVQVQGK SKREKKDRVF TDKTSATVIC 300
    RKNASISVRA QDRYYSSSWS EWASVPCS 328
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi266320.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    IL12Bbase

    IL12B mutation db

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS4346.1.
    PIRi A38957.
    RefSeqi NP_002178.2. NM_002187.2.
    UniGenei Hs.674.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F42 X-ray 2.50 A 23-328 [» ]
    1F45 X-ray 2.80 A 23-328 [» ]
    3D85 X-ray 1.90 D 23-328 [» ]
    3D87 X-ray 2.90 B/D 23-328 [» ]
    3DUH X-ray 2.30 A/B 23-328 [» ]
    3HMX X-ray 3.00 A 23-328 [» ]
    3QWR X-ray 3.25 A 23-328 [» ]
    4GRW X-ray 2.55 B/D 1-328 [» ]
    ProteinModelPortali P29460.
    SMRi P29460. Positions 23-328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109807. 2 interactions.
    DIPi DIP-3774N.
    IntActi P29460. 4 interactions.
    STRINGi 9606.ENSP00000231228.

    Chemistry

    ChEMBLi CHEMBL2364153.

    PTM databases

    PhosphoSitei P29460.
    UniCarbKBi P29460.

    Polymorphism databases

    DMDMi 266320.

    Proteomic databases

    PaxDbi P29460.
    PRIDEi P29460.

    Protocols and materials databases

    DNASUi 3593.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000231228 ; ENSP00000231228 ; ENSG00000113302 .
    GeneIDi 3593.
    KEGGi hsa:3593.
    UCSCi uc003lxr.1. human.

    Organism-specific databases

    CTDi 3593.
    GeneCardsi GC05M158741.
    HGNCi HGNC:5970. IL12B.
    HPAi HPA040970.
    MIMi 161561. gene.
    209950. phenotype.
    612599. phenotype.
    neXtProti NX_P29460.
    Orphaneti 319558. Mendelian susceptibility to mycobacterial diseases due to complete IL12B deficiency.
    3287. Takayasu arteritis.
    PharmGKBi PA29785.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45642.
    HOGENOMi HOG000113027.
    HOVERGENi HBG052094.
    InParanoidi P29460.
    KOi K05425.
    OMAi WSTPHSY.
    OrthoDBi EOG7TBC2K.
    PhylomeDBi P29460.
    TreeFami TF334829.

    Miscellaneous databases

    EvolutionaryTracei P29460.
    GeneWikii Interleukin-12_subunit_beta.
    GenomeRNAii 3593.
    NextBioi 14039.
    PMAP-CutDB P29460.
    PROi P29460.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29460.
    Bgeei P29460.
    CleanExi HS_IL12B.
    Genevestigatori P29460.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    InterProi IPR003961. Fibronectin_type3.
    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 ]
    PANTHERi PTHR11321. PTHR11321. 1 hit.
    Pfami PF10420. IL12p40_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038007. IL_12_beta. 1 hit.
    PRINTSi PR01928. INTRLEUKN12B.
    SMARTi SM00408. IGc2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 2 hits.
    PROSITEi PS50853. FN3. 1 hit.
    PS01354. HEMATOPO_REC_L_F3. 1 hit.
    PS50835. IG_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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 MENDELIAN SUSCEPTIBILITY TO MYCOBACTERIAL DISEASE.
    12. Cited for: FUNCTION, INTERACTION WITH IL23A.
    13. Cited for: INVOLVEMENT IN MENDELIAN SUSCEPTIBILITY TO MYCOBACTERIAL DISEASE.
    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: October 1, 2014
    This is version 171 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