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Protein

Interleukin-12 subunit alpha

Gene

IL12A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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.

GO - Molecular functioni

  • cytokine activity Source: UniProtKB-KW
  • growth factor activity Source: UniProtKB-KW
  • interleukin-12 beta subunit binding Source: AgBase
  • interleukin-12 receptor binding Source: UniProtKB
  • interleukin-27 binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  • cell cycle arrest Source: BHF-UCL
  • cell migration Source: UniProtKB
  • cell proliferation Source: Ensembl
  • cellular response to lipopolysaccharide Source: Ensembl
  • cellular response to virus Source: UniProtKB
  • cytokine-mediated signaling pathway Source: Reactome
  • defense response to Gram-positive bacterium Source: UniProtKB
  • defense response to protozoan Source: Ensembl
  • extrinsic apoptotic signaling pathway Source: BHF-UCL
  • immune response Source: UniProtKB
  • interferon-gamma production Source: Ensembl
  • interleukin-12-mediated signaling pathway Source: Reactome
  • interleukin-35-mediated signaling pathway Source: Reactome
  • negative regulation of interleukin-17 production Source: BHF-UCL
  • negative regulation of smooth muscle cell proliferation Source: BHF-UCL
  • positive regulation of cell adhesion Source: UniProtKB
  • positive regulation of dendritic cell chemotaxis Source: UniProtKB
  • positive regulation of interferon-gamma production Source: UniProtKB
  • positive regulation of lymphocyte proliferation Source: UniProtKB
  • 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 Source: UniProtKB
  • positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target Source: UniProtKB
  • positive regulation of NK T cell activation Source: BHF-UCL
  • positive regulation of smooth muscle cell apoptotic process Source: BHF-UCL
  • positive regulation of T cell differentiation Source: Ensembl
  • positive regulation of T cell mediated cytotoxicity Source: UniProtKB
  • positive regulation of T cell proliferation Source: Ensembl
  • positive regulation of tyrosine phosphorylation of STAT protein Source: UniProtKB
  • response to lipopolysaccharide Source: UniProtKB
  • response to UV-B Source: UniProtKB
  • response to virus Source: UniProtKB
  • T-helper 1 cell activation Source: Ensembl
  • T-helper 1 cell cytokine production Source: Ensembl

Keywordsi

Molecular functionCytokine, Growth factor

Enzyme and pathway databases

ReactomeiR-HSA-6783783 Interleukin-10 signaling
R-HSA-6785807 Interleukin-4 and 13 signaling
R-HSA-8984722 Interleukin-35 Signalling
R-HSA-9020591 Interleukin-12 signaling
SignaLinkiP29459
SIGNORiP29459

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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000168811.6
HGNCiHGNC:5969 IL12A
MIMi161560 gene
neXtProtiNX_P29459

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi3592
MalaCardsiIL12A
Orphaneti186 Primary biliary cirrhosis
PharmGKBiPA29784

Chemistry databases

ChEMBLiCHEMBL2364153

Polymorphism and mutation databases

BioMutaiIL12A
DMDMi20141534

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
ChainiPRO_000001560423 – 219Interleukin-12 subunit alphaAdd BLAST197

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi64 ↔ 1961 Publication
Disulfide bondi85 ↔ 1231 Publication
Glycosylationi93N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi96Interchain (with C-199 in IL12B)1 Publication
Glycosylationi107N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP29459
PeptideAtlasiP29459
PRIDEiP29459
ProteomicsDBi54569

PTM databases

iPTMnetiP29459
PhosphoSitePlusiP29459

Expressioni

Inductioni

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

Gene expression databases

BgeeiENSG00000168811
CleanExiHS_IL12A
ExpressionAtlasiP29459 baseline and differential
GenevisibleiP29459 HS

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

GO - Molecular functioni

  • cytokine activity Source: UniProtKB-KW
  • growth factor activity Source: UniProtKB-KW
  • interleukin-12 beta subunit binding Source: AgBase
  • interleukin-12 receptor binding Source: UniProtKB
  • interleukin-27 binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi109806, 7 interactors
ComplexPortaliCPX-381 Interleukin-12 complex
CPX-382 Interleukin-12-receptor complex
CORUMiP29459
DIPiDIP-3772N
IntActiP29459, 3 interactors
STRINGi9606.ENSP00000303231

Structurei

Secondary structure

1219
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 58Combined sources16
Helixi59 – 61Combined sources3
Turni74 – 78Combined sources5
Helixi81 – 84Combined sources4
Helixi88 – 92Combined sources5
Beta strandi107 – 109Combined sources3
Turni114 – 116Combined sources3
Helixi118 – 145Combined sources28
Helixi155 – 169Combined sources15
Helixi190 – 217Combined sources28

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F45X-ray2.80B23-219[»]
3HMXX-ray3.00B23-219[»]
ProteinModelPortaliP29459
SMRiP29459
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29459

Family & Domainsi

Sequence similaritiesi

Belongs to the IL-6 superfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IVIR Eukaryota
ENOG410ZGHJ LUCA
HOVERGENiHBG063691
InParanoidiP29459
KOiK05406
OrthoDBiEOG091G13SK
PhylomeDBiP29459
TreeFamiTF330814

Family and domain databases

InterProiView protein in InterPro
IPR009079 4_helix_cytokine-like_core
IPR004281 IL-12_alpha
PANTHERiPTHR45311 PTHR45311, 1 hit
PfamiView protein in Pfam
PF03039 IL12, 1 hit
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

        10         20         30         40         50
MCPARSLLLV ATLVLLDHLS LARNLPVATP DPGMFPCLHH SQNLLRAVSN
60 70 80 90 100
MLQKARQTLE FYPCTSEEID HEDITKDKTS TVEACLPLEL TKNESCLNSR
110 120 130 140 150
ETSFITNGSC LASRKTSFMM ALCLSSIYED LKMYQVEFKT MNAKLLMDPK
160 170 180 190 200
RQIFLDQNML AVIDELMQAL NFNSETVPQK SSLEEPDFYK TKIKLCILLH
210
AFRIRAVTID RVMSYLNAS
Length:219
Mass (Da):24,874
Last modified:January 23, 2002 - v2
Checksum:i7C658AB7716112B2
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti213M → T in AAA35694 (PubMed:1674604).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
UCSCiuc003fcx.4 human

Similar proteinsi

Entry informationi

Entry nameiIL12A_HUMAN
AccessioniPrimary (citable) accession number: P29459
Secondary accession number(s): Q96QZ1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2002
Last modified: June 20, 2018
This is version 168 of the entry and version 2 of the sequence. See 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

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