P29460 (IL12B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	IL12B
Synonyms:	NKSF2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	328 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.12 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. Ref.12
Subunit structure	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. Ref.9 Ref.16 Ref.18
Subcellular location	Secreted.
Post-translational modification	Known to be C-mannosylated in the recombinant protein; it is not yet known for sure if the wild-type protein is also modified.
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.13 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. Ref.11 Ref.13
Sequence similarities	Belongs to the type I cytokine receptor family. Type 3 subfamily. Contains 1 fibronectin type-III domain. Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Signal
Molecular function	Cytokine
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	T-helper 1 type immune response Traceable author statement Ref.2. Source: UniProtKB T-helper cell differentiation Inferred from direct assay Ref.2. Source: UniProtKB cell cycle arrest Inferred from direct assay PubMed 16942485. Source: BHF-UCL cell migration Inferred from direct assay PubMed 7903063. Source: UniProtKB cellular response to interferon-gamma Inferred from electronic annotation. Source: Compara cellular response to lipopolysaccharide Inferred from electronic annotation. Source: Compara cytokine-mediated signaling pathway Inferred from electronic annotation. Source: GOC defense response to Gram-negative bacterium Inferred from direct assay PubMed 15114670PubMed 20027291. Source: BHF-UCL defense response to protozoan Inferred from electronic annotation. Source: Compara defense response to virus Inferred from electronic annotation. Source: Compara interferon-gamma biosynthetic process Traceable author statement Ref.2. Source: UniProtKB natural killer cell activation Inferred from direct assay Ref.2. Source: UniProtKB negative regulation of growth of symbiont in host Inferred from electronic annotation. Source: Compara negative regulation of inflammatory response to antigenic stimulus Inferred from electronic annotation. Source: Compara negative regulation of interleukin-10 production Inferred from mutant phenotype PubMed 16751425. Source: BHF-UCL negative regulation of interleukin-17 production Inferred from direct assay PubMed 16482511. Source: BHF-UCL negative regulation of smooth muscle cell proliferation Inferred from direct assay PubMed 16942485. Source: BHF-UCL positive regulation of NF-kappaB import into nucleus Traceable author statement PubMed 20428758. Source: BHF-UCL positive regulation of NK T cell activation Inferred from direct assay PubMed 19088061. Source: BHF-UCL positive regulation of NK T cell proliferation Inferred from direct assay PubMed 19088061. Source: BHF-UCL positive regulation of T cell mediated cytotoxicity Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of T-helper 1 type immune response Inferred from direct assay PubMed 15114670. Source: BHF-UCL positive regulation of T-helper 17 cell lineage commitment Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of T-helper 17 type immune response Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of activated T cell proliferation Inferred from direct assay Ref.1. Source: UniProtKB positive regulation of activation of JAK2 kinase activity Inferred from direct assay PubMed 12023369. Source: BHF-UCL positive regulation of cell adhesion Inferred from direct assay PubMed 7903063. Source: UniProtKB positive regulation of defense response to virus by host Inferred from direct assay PubMed 12421946. Source: BHF-UCL positive regulation of granulocyte macrophage colony-stimulating factor production Inferred from direct assay PubMed 20027291. Source: BHF-UCL positive regulation of inflammatory response Inferred by curator PubMed 16482511. Source: BHF-UCL positive regulation of interferon-gamma biosynthetic process Traceable author statement Ref.2. Source: UniProtKB positive regulation of interferon-gamma production Inferred from direct assay Ref.1. Source: UniProtKB positive regulation of interleukin-10 production Inferred from direct assay PubMed 15265908. Source: BHF-UCL positive regulation of interleukin-12 production Inferred from direct assay PubMed 20027291. Source: BHF-UCL positive regulation of interleukin-17 production Inferred from direct assay PubMed 16482511PubMed 16751425PubMed 17888176. Source: BHF-UCL positive regulation of memory T cell differentiation Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target Inferred from direct assay PubMed 7903063. Source: UniProtKB positive regulation of natural killer cell proliferation Inferred from direct assay PubMed 19088061. Source: BHF-UCL positive regulation of osteoclast differentiation Inferred from direct assay PubMed 17888176. Source: BHF-UCL positive regulation of smooth muscle cell apoptotic process Inferred from direct assay PubMed 16942485. Source: BHF-UCL positive regulation of tissue remodeling Inferred by curator PubMed 16482511. Source: BHF-UCL positive regulation of tumor necrosis factor production Inferred from mutant phenotype PubMed 16751425. Source: BHF-UCL positive regulation of tyrosine phosphorylation of Stat3 protein Inferred from direct assay PubMed 12023369. Source: BHF-UCL positive regulation of tyrosine phosphorylation of Stat4 protein Inferred from direct assay Ref.12PubMed 12023369PubMed 19088061. Source: BHF-UCL positive regulation of tyrosine phosphorylation of Stat5 protein Inferred from direct assay PubMed 12023369. Source: BHF-UCL regulation of tyrosine phosphorylation of Stat1 protein Inferred from direct assay PubMed 12023369. Source: BHF-UCL response to UV-B Inferred from direct assay PubMed 8992506. Source: UniProtKB sexual reproduction Traceable author statement PubMed 16772281. Source: BHF-UCL
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara interleukin-12 complex Inferred from direct assay Ref.1. Source: UniProtKB interleukin-23 complex Inferred from direct assay Ref.12. Source: BHF-UCL membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	cytokine receptor activity Inferred from electronic annotation. Source: InterPro interleukin-12 receptor binding Traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-1029614,EBI-1029614
IL12A	P29459	2	EBI-1029614,EBI-1029636
Il23a	Q9EQ14	2	EBI-1029614,EBI-2481329	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.7

Chain

23 – 328

306

Interleukin-12 subunit beta

PRO_0000010930

Regions

Domain

23 – 106

84

Ig-like C2-type

Domain

235 – 327

93

Fibronectin type-III

Amino acid modifications

Glycosylation

135

1

N-linked (GlcNAc...) Potential

Glycosylation

222

1

N-linked (GlcNAc...) Ref.16

Glycosylation

319

1

C-linked (Man) Ref.10

CAR_000187

Disulfide bond

50 ↔ 90

Ref.16

Disulfide bond

131 ↔ 142

Ref.16

Disulfide bond

170 ↔ 193

Ref.16

Disulfide bond

199

Interchain (with C-96 in IL12A) Ref.16

Disulfide bond

300 ↔ 327

Ref.16

Natural variations

Natural variant

33

1

V → I. Ref.5
Corresponds to variant rs3213096 [ dbSNP | Ensembl ].

VAR_020001

Natural variant

298

1

V → F. Ref.5
Corresponds to variant rs3213119 [ dbSNP | Ensembl ].

VAR_049170

Experimental info

Sequence conflict

239

1

K → N in AAA59938. Ref.2

Secondary structure

1

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328

Helix Strand Turn

Details...

Beta strand

23 – 27

5

Beta strand

30 – 36

7

Beta strand

44 – 49

6

Beta strand

51 – 53

3

Beta strand

59 – 62

4

Beta strand

70 – 81

12

Helix

82 – 84

3

Beta strand

86 – 92

7

Beta strand

95 – 112

18

Beta strand

116 – 118

3

Beta strand

122 – 126

5

Beta strand

130 – 147

18

Beta strand

150 – 160

11

Beta strand

162 – 164

3

Beta strand

166 – 170

5

Beta strand

174 – 177

4

Beta strand

182 – 184

3

Beta strand

187 – 195

9

Beta strand

200 – 202

3

Beta strand

208 – 216

9

Beta strand

219 – 227

9

Helix

229 – 232

4

Beta strand

239 – 245

7

Beta strand

249 – 257

9

Beta strand

260 – 262

3

Turn

266 – 268

3

Beta strand

271 – 284

14

Beta strand

286 – 299

14

Beta strand

304 – 315

12

Beta strand

323 – 326

4

Sequences

	Sequence		Length	Mass (Da)
	P29460 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 118FA801B8F5BB2F	FASTA	328	37,169
	10 20 30 40 50 60 MCHQQLVISW FSLVFLASPL VAIWELKKDV YVVELDWYPD APGEMVVLTC DTPEEDGITW 70 80 90 100 110 120 TLDQSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGEVLSHS LLLLHKKEDG IWSTDILKDQ 130 140 150 160 170 180 KEPKNKTFLR CEAKNYSGRF TCWWLTTIST DLTFSVKSSR GSSDPQGVTC GAATLSAERV 190 200 210 220 230 240 RGDNKEYEYS VECQEDSACP AAEESLPIEV MVDAVHKLKY ENYTSSFFIR DIIKPDPPKN 250 260 270 280 290 300 LQLKPLKNSR QVEVSWEYPD TWSTPHSYFS LTFCVQVQGK SKREKKDRVF TDKTSATVIC 310 320 RKNASISVRA QDRYYSSSWS EWASVPCS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Inherited interleukin 12 deficiency in a child with bacille Calmette-Guerin and Salmonella enteritidis disseminated infection." Altare F., Lammas D., Revy P., Jouanguy E., Doeffinger R., Lamhamedi-Cherradi S.-E., Drysdale P., Scheel-Toellner D., Girdlestone J., Darbyshire P., Wadhwa M., Dockrell H., Salmon M., Fischer A., Durandy A., Casanova J.-L., Kumararatne D.S. J. Clin. Invest. 102:2035-2040(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MENDELIAN SUSCEPTIBILITY TO MYCOBACTERIAL DISEASE.
[12]	"Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with biological activities similar as well as distinct from IL-12." Oppmann B., Lesley R., Blom B., Timans J.C., Xu Y., Hunte B., Vega F., Yu N., Wang J., Singh K.P., Zonin F., Vaisberg E., Churakova T., Liu M.-R., Gorman D., Wagner J., Zurawski S., Liu Y.-J. , Abrams J.S., Moore K.W., Rennick D.M., de Waal-Malefyt R., Hannum C., Bazan J.F., Kastelein R.A. Immunity 13:715-725(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH IL23A.
[13]	"Inherited interleukin-12 deficiency: IL12B genotype and clinical phenotype of 13 patients from six kindreds." Picard C., Fieschi C., Altare F., Al-Jumaah S., Al-Hajjar S., Feinberg J., Dupuis S., Soudais C., Al-Mohsen I.Z., Genin E., Lammas D., Kumararatne D.S., Leclerc T., Rafii A., Frayha H., Murugasu B., Wah L.B., Sinniah R. , Loubser M., Okamoto E., Al-Ghonaium A., Tufenkeji H., Abel L., Casanova J.-L. Am. J. Hum. Genet. 70:336-348(2002) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

IL12Bbase

IL12B mutation db

GeneReviews

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00021798.

PIR

A38957.

RefSeq

NP_002178.2. NM_002187.2.

UniGene

Hs.674.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P29460.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3774N.

IntAct

P29460. 4 interactions.

STRING

9606.ENSP00000231228.

PTM databases

GlycoSuiteDB

P29460.

PhosphoSite

P29460.

Polymorphism databases

DMDM

266320.

Proteomic databases

PaxDb

P29460.

PRIDE

P29460.

Protocols and materials databases

DNASU

3593.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000231228; ENSP00000231228; ENSG00000113302.

GeneID

3593.

KEGG

hsa:3593.

UCSC

uc003lxr.1. human.

Organism-specific databases

CTD

3593.

GeneCards

GC05M158741.

HGNC

HGNC:5970. IL12B.

HPA

HPA040970.

MIM

161561. gene.
209950. phenotype.
612599. phenotype.

neXtProt

NX_P29460.

Orphanet

748. Mendelian susceptibility to mycobacterial diseases.

PharmGKB

PA29785.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG45642.

HOGENOM

HOG000113027.

HOVERGEN

HBG052094.

InParanoid

P29460.

KO

K05425.

OMA

WSTPHSY.

OrthoDB

EOG4KH2W2.

PhylomeDB

P29460.

Enzyme and pathway databases

Pathway_Interaction_DB

il12_2pathway. IL12-mediated signaling events.
il23pathway. IL23-mediated signaling events.
il27pathway. IL27-mediated signaling events.

Gene expression databases

ArrayExpress

P29460.

Bgee

P29460.

CleanEx

HS_IL12B.

Genevestigator

P29460.

GermOnline

ENSG00000113302. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 3 hits.

InterPro

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. Interleukin-12_bsu_cen-dom.
[Graphical view]

PANTHER

PTHR11321. PTHR11321. 1 hit.

Pfam

PF10420. IL12p40_C. 1 hit.
[Graphical view]

PIRSF

PIRSF038007. IL_12_beta. 1 hit.

PRINTS

PR01928. INTRLEUKN12B.

SMART

SM00408. IGc2. 1 hit.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 2 hits.

PROSITE

PS50853. FN3. 1 hit.
PS01354. HEMATOPO_REC_L_F3. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P29460.

GenomeRNAi

3593.

NextBio

14039.

PMAP-CutDB

P29460.

SOURCE

Search...

Entry information

Entry name

IL12B_HUMAN

Accession

Primary (citable) accession number: P29460

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	May 1, 2013
This is version 157 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.