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P29459

- IL12A_HUMAN

UniProt

P29459 - IL12A_HUMAN

Protein

Interleukin-12 subunit alpha

Gene

IL12A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (23 Jan 2002)
      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.

    GO - Molecular functioni

    1. interleukin-12 beta subunit binding Source: AgBase
    2. interleukin-12 receptor binding Source: UniProtKB
    3. interleukin-27 binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein heterodimerization activity Source: UniProtKB

    GO - Biological processi

    1. cell cycle arrest Source: BHF-UCL
    2. cell migration Source: UniProtKB
    3. defense response to Gram-positive bacterium Source: UniProtKB
    4. defense response to protozoan Source: Ensembl
    5. extrinsic apoptotic signaling pathway Source: BHF-UCL
    6. immune response Source: UniProtKB
    7. negative regulation of interleukin-17 production Source: BHF-UCL
    8. negative regulation of smooth muscle cell proliferation Source: BHF-UCL
    9. positive regulation of cell adhesion Source: UniProtKB
    10. positive regulation of interferon-gamma production Source: UniProtKB
    11. positive regulation of lymphocyte proliferation Source: UniProtKB
    12. positive regulation of mononuclear cell proliferation Source: AgBase
    13. positive regulation of natural killer cell activation Source: UniProtKB
    14. positive regulation of natural killer cell mediated cytotoxicity Source: UniProtKB
    15. positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target Source: UniProtKB
    16. positive regulation of NK T cell activation Source: BHF-UCL
    17. positive regulation of smooth muscle cell apoptotic process Source: BHF-UCL
    18. positive regulation of T cell differentiation Source: Ensembl
    19. positive regulation of T cell mediated cytotoxicity Source: UniProtKB
    20. positive regulation of T cell proliferation Source: Ensembl
    21. positive regulation of tyrosine phosphorylation of Stat4 protein Source: UniProtKB
    22. response to lipopolysaccharide Source: UniProtKB
    23. response to UV-B Source: UniProtKB
    24. response to virus Source: UniProtKB

    Keywords - Molecular functioni

    Cytokine, Growth factor

    Enzyme and pathway databases

    SignaLinkiP29459.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interleukin-12 subunit alpha
    Short name:
    IL-12A
    Alternative name(s):
    Cytotoxic lymphocyte maturation factor 35 kDa subunit
    Short name:
    CLMF p35
    IL-12 subunit p35
    NK cell stimulatory factor chain 1
    Short name:
    NKSF1
    Gene namesi
    Name:IL12A
    Synonyms:NKSF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:5969. IL12A.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. extracellular space Source: UniProtKB
    3. interleukin-12 complex Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti186. Primary biliary cirrhosis.
    PharmGKBiPA29784.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 219197Interleukin-12 subunit alphaPRO_0000015604Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi64 ↔ 1961 Publication
    Disulfide bondi85 ↔ 1231 Publication
    Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi96 – 96Interchain (with C-199 in IL12B)1 Publication
    Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP29459.
    PRIDEiP29459.

    Expressioni

    Inductioni

    Down-regulated in response to enterovirus 71 (EV71) infection.1 Publication

    Gene expression databases

    ArrayExpressiP29459.
    BgeeiP29459.
    CleanExiHS_IL12A.
    GenevestigatoriP29459.

    Organism-specific databases

    HPAiHPA001886.

    Interactioni

    Subunit structurei

    Heterodimer with IL12B; disulfide-linked. The heterodimer is known as interleukin IL-12.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IL12BP294602EBI-1029636,EBI-1029614

    Protein-protein interaction databases

    BioGridi109806. 1 interaction.
    DIPiDIP-3772N.
    IntActiP29459. 2 interactions.
    STRINGi9606.ENSP00000303231.

    Structurei

    Secondary structure

    1
    219
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi43 – 5816
    Helixi59 – 613
    Turni74 – 785
    Helixi81 – 844
    Helixi88 – 925
    Beta strandi107 – 1093
    Turni114 – 1163
    Helixi118 – 14528
    Helixi155 – 16915
    Helixi190 – 21728

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F45X-ray2.80B23-219[»]
    3HMXX-ray3.00B23-219[»]
    ProteinModelPortaliP29459.
    SMRiP29459. Positions 34-219.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29459.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the IL-6 superfamily.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG47298.
    HOVERGENiHBG063691.
    InParanoidiP29459.
    KOiK05406.
    OrthoDBiEOG7VDXQX.
    PhylomeDBiP29459.
    TreeFamiTF330814.

    Family and domain databases

    Gene3Di1.20.1250.10. 1 hit.
    InterProiIPR009079. 4_helix_cytokine-like_core.
    IPR012351. 4_helix_cytokine_core.
    IPR004281. IL-12_alpha.
    [Graphical view]
    PANTHERiPTHR10523. PTHR10523. 1 hit.
    PfamiPF03039. IL12. 1 hit.
    [Graphical view]
    SUPFAMiSSF47266. SSF47266. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P29459-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCPARSLLLV ATLVLLDHLS LARNLPVATP DPGMFPCLHH SQNLLRAVSN    50
    MLQKARQTLE FYPCTSEEID HEDITKDKTS TVEACLPLEL TKNESCLNSR 100
    ETSFITNGSC LASRKTSFMM ALCLSSIYED LKMYQVEFKT MNAKLLMDPK 150
    RQIFLDQNML AVIDELMQAL NFNSETVPQK SSLEEPDFYK TKIKLCILLH 200
    AFRIRAVTID RVMSYLNAS 219
    Length:219
    Mass (Da):24,874
    Last modified:January 23, 2002 - v2
    Checksum:i7C658AB7716112B2
    GO

    Sequence cautioni

    The sequence AAA59937.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti213 – 2131M → T in AAA35694. (PubMed:1674604)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M65291 mRNA. Translation: AAA59937.1. Different initiation.
    M65271 mRNA. Translation: AAA35694.1.
    AF404773 Genomic DNA. Translation: AAK84425.1.
    AC010370 Genomic DNA. No translation available.
    RefSeqiNP_000873.2. NM_000882.3.
    UniGeneiHs.673.

    Genome annotation databases

    EnsembliENST00000305579; ENSP00000303231; ENSG00000168811.
    GeneIDi3592.
    KEGGihsa:3592.

    Polymorphism databases

    DMDMi20141534.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Interleukin-12 entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M65291 mRNA. Translation: AAA59937.1 . Different initiation.
    M65271 mRNA. Translation: AAA35694.1 .
    AF404773 Genomic DNA. Translation: AAK84425.1 .
    AC010370 Genomic DNA. No translation available.
    RefSeqi NP_000873.2. NM_000882.3.
    UniGenei Hs.673.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F45 X-ray 2.80 B 23-219 [» ]
    3HMX X-ray 3.00 B 23-219 [» ]
    ProteinModelPortali P29459.
    SMRi P29459. Positions 34-219.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109806. 1 interaction.
    DIPi DIP-3772N.
    IntActi P29459. 2 interactions.
    STRINGi 9606.ENSP00000303231.

    Chemistry

    ChEMBLi CHEMBL2364153.

    Polymorphism databases

    DMDMi 20141534.

    Proteomic databases

    PaxDbi P29459.
    PRIDEi P29459.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000305579 ; ENSP00000303231 ; ENSG00000168811 .
    GeneIDi 3592.
    KEGGi hsa:3592.

    Organism-specific databases

    CTDi 3592.
    GeneCardsi GC03P159706.
    HGNCi HGNC:5969. IL12A.
    HPAi HPA001886.
    MIMi 161560. gene.
    neXtProti NX_P29459.
    Orphaneti 186. Primary biliary cirrhosis.
    PharmGKBi PA29784.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47298.
    HOVERGENi HBG063691.
    InParanoidi P29459.
    KOi K05406.
    OrthoDBi EOG7VDXQX.
    PhylomeDBi P29459.
    TreeFami TF330814.

    Enzyme and pathway databases

    SignaLinki P29459.

    Miscellaneous databases

    EvolutionaryTracei P29459.
    GeneWikii IL12A.
    GenomeRNAii 3592.
    NextBioi 14035.
    PROi P29459.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29459.
    Bgeei P29459.
    CleanExi HS_IL12A.
    Genevestigatori P29459.

    Family and domain databases

    Gene3Di 1.20.1250.10. 1 hit.
    InterProi IPR009079. 4_helix_cytokine-like_core.
    IPR012351. 4_helix_cytokine_core.
    IPR004281. IL-12_alpha.
    [Graphical view ]
    PANTHERi PTHR10523. PTHR10523. 1 hit.
    Pfami PF03039. IL12. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47266. SSF47266. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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].
    2. "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].
    3. SeattleSNPs variation discovery resource
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 23-48.
    6. "Sequence similarity between NKSF and the IL-6/G-CSF family."
      Merberg D.M., Wolf S.F., Clark S.C.
      Immunol. Today 13:77-78(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO IL-6.
    7. "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
      Leong W.F., Chow V.T.
      Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "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 (2.8 ANGSTROMS) OF 23-219, DISULFIDE BONDS.

    Entry informationi

    Entry nameiIL12A_HUMAN
    AccessioniPrimary (citable) accession number: P29459
    Secondary accession number(s): Q96QZ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 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 3
      Human chromosome 3: 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