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Reviewed, UniProtKB/Swiss-Prot P29459 (IL12A_HUMAN)

Last modified June 16, 2009. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Interleukin-12 subunit alpha
      Short name=IL-12A
Alternative name(s):
    IL-12 subunit p35
    Cytotoxic lymphocyte maturation factor 35 kDa subunit
      Short name=CLMF p35
    NK cell stimulatory factor chain 1
      Short name=NKSF1
Gene names
Name: IL12A
Synonyms: NKSF1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length219 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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.

Subunit structure

Heterodimer with IL12B; disulfide-linked. The heterodimer is known as interleukin IL-12. Ref.7

Subcellular location

Secreted.

Sequence similarities

Belongs to the IL-6 superfamily.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionCytokine
Growth factor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcell cycle arrest

Inferred from direct assay. Source: UniProtKB

cell migration

Inferred from direct assay. Source: UniProtKB

defense response to Gram-positive bacterium

Inferred from expression pattern. Source: UniProtKB

immune response

Traceable author statement. Source: UniProtKB

negative regulation of smooth muscle cell proliferation

Inferred from direct assay. Source: UniProtKB

positive regulation of T cell mediated cytotoxicity Ref.2 Ref.5

Inferred from direct assay. Source: UniProtKB

positive regulation of cell adhesion

Inferred from direct assay. Source: UniProtKB

positive regulation of interferon-gamma production Ref.2

Inferred from direct assay. Source: UniProtKB

positive regulation of natural killer cell activation Ref.2

Inferred from direct assay. Source: UniProtKB

positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target

Inferred from direct assay. Source: UniProtKB

positive regulation of smooth muscle cell apoptosis

Inferred from direct assay. Source: UniProtKB

positive regulation of tyrosine phosphorylation of Stat4 protein

Inferred from direct assay. Source: UniProtKB

response to UV-B

Inferred from direct assay. Source: UniProtKB

response to lipopolysaccharide

Inferred from direct assay. Source: UniProtKB

   Cellular componentinterleukin-12 complex Ref.2 Ref.5

Inferred from direct assay. Source: UniProtKB

   Molecular functioncytokine activity Ref.1 Ref.2

Inferred from electronic annotation. Source: UniProtKB-KW

interleukin-12 receptor binding Ref.2

Non-traceable author statement. Source: UniProtKB

interleukin-27 binding

Inferred from physical interaction. Source: UniProtKB

protein heterodimerization activity Ref.2

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IL12BP294601EBI-1029636,EBI-1029614

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.5
Chain23 – 219197Interleukin-12 subunit alpha
PRO_0000015604

Amino acid modifications

Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation1071N-linked (GlcNAc...) Potential
Disulfide bond64 ↔ 196 Ref.7
Disulfide bond85 ↔ 123 Ref.7
Disulfide bond96Interchain (with C-199 in IL12B) Ref.7

Experimental info

Sequence conflict2131M → T in AAA35694. Ref.2

Secondary structure

.............. 219
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29459-1 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 7C658AB7716112B2

FASTA21924,874
        10         20         30         40         50         60 
MCPARSLLLV ATLVLLDHLS LARNLPVATP DPGMFPCLHH SQNLLRAVSN MLQKARQTLE 

        70         80         90        100        110        120 
FYPCTSEEID HEDITKDKTS TVEACLPLEL TKNESCLNSR ETSFITNGSC LASRKTSFMM 

       130        140        150        160        170        180 
ALCLSSIYED LKMYQVEFKT MNAKLLMDPK RQIFLDQNML AVIDELMQAL NFNSETVPQK 

       190        200        210 
SSLEEPDFYK TKIKLCILLH AFRIRAVTID RVMSYLNAS 

« Hide

References

« Hide 'large scale' references
[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: 1673147] [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: 1674604] [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. expand/collapse author list , 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: 16641997] [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: 2204066] [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: 1374259] [Abstract]
Cited for: SIMILARITY TO IL-6.
[7]"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: 10899108] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-219, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

Wikipedia

Interleukin-12 entry

SeattleSNPs

Cross-references

Sequence databases

M65291 mRNA. Translation: AAA59937.1. Different initiation.
M65271 mRNA. Translation: AAA35694.1.
AF404773 Genomic DNA. Translation: AAK84425.1.
AC010370 Genomic DNA. No translation available.
IPIIPI00182737.
RefSeqNP_000873.2.
UniGeneHs.673

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1F45X-ray2.80B23-219[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:3772N.
IntActP29459. 1 interaction.

Proteomic databases

PRIDEP29459.

Genome annotation databases

EnsemblENSG00000168811. Homo sapiens. [Contig view]
GeneID3592.
KEGGhsa:3592.

Organism-specific databases

GeneCardsGC03P161189.
H-InvDBHIX0030715.
HGNCHGNC:5969. IL12A.
HPAHPA001886.
MIM161560. gene.
PharmGKBPA29784.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP29459.

Enzyme and pathway databases

Pathway_Interaction_DBil12_2pathway. IL12-mediated signaling events.
il27pathway. IL27-mediated signaling events.

Gene expression databases

ArrayExpressP29459.
BgeeP29459.
CleanExHS_IL12A.

Family and domain databases

InterProIPR012351. 4_helix_cytokine_core.
IPR004281. IL12.
[Graphical view]
Gene3DG3DSA:1.20.1250.10. 4_helix_cytokine_core. 1 hit.
PANTHERPTHR10523. IL12. 1 hit.
PfamPF03039. IL12. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio14035.
SOURCESearch...

Entry information

Entry nameIL12A_HUMAN
AccessionPrimary (citable) accession number: P29459
Secondary accession number(s): Q96QZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2002
Last modified: June 16, 2009
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents