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Interleukin-12 subunit beta (IL-12B) (Cytotoxic lymphocyte maturation factor 40 kDa subunit) (CLMF p40) (IL-12 subunit p40) (NK cell stimulatory factor chain 2) (NKSF2)

 IL12B_HUMAN             Reviewed;         328 AA.
P29460;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
22-APR-2020, entry version 219.
RecName: Full=Interleukin-12 subunit beta;
Short=IL-12B;
AltName: Full=Cytotoxic lymphocyte maturation factor 40 kDa subunit;
Short=CLMF p40;
AltName: Full=IL-12 subunit p40;
AltName: Full=NK cell stimulatory factor chain 2;
Short=NKSF2;
Flags: Precursor;
Name=IL12B; Synonyms=NKSF2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1674604; DOI=10.1073/pnas.88.10.4143;
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.;
"Coexpression of two distinct genes is required to generate secreted
bioactive cytotoxic lymphocyte maturation factor.";
Proc. Natl. Acad. Sci. U.S.A. 88:4143-4147(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1673147;
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.;
"Cloning of cDNA for natural killer cell stimulatory factor, a
heterodimeric cytokine with multiple biologic effects on T and natural
killer cells.";
J. Immunol. 146:3074-3081(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11197695; DOI=10.1038/sj.gene.6363720;
Huang D., Cancilla M.R., Morahan G.;
"Complete primary structure, chromosomal localization, and definition of
polymorphisms of the gene encoding the human interleukin 12 p40 subunit.";
Genes Immun. 1:515-520(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Hongyuan J., Meiyun Z.;
"Cloning and sequence analysis of IL-12 cDNA from Chinese.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-33 AND PHE-298.
SeattleSNPs variation discovery resource;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 23-45.
PubMed=2204066; DOI=10.1073/pnas.87.17.6808;
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.;
"Purification to homogeneity and partial characterization of cytotoxic
lymphocyte maturation factor from human B-lymphoblastoid cells.";
Proc. Natl. Acad. Sci. U.S.A. 87:6808-6812(1990).
[8]
SIMILARITY TO IL-6 RECEPTOR.
PubMed=2070420; DOI=10.1016/0092-8674(91)90131-h;
Gearing D.P., Cosman D.;
"Homology of the p40 subunit of natural killer cell stimulatory factor
(NKSF) with the extracellular domain of the interleukin-6 receptor.";
Cell 66:9-10(1991).
[9]
SUBUNIT.
PubMed=7836910; DOI=10.1084/jem.181.2.537;
D'Andrea A., Ma X., Aste-Amezaga M., Paganin C., Trinchieri G.;
"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.";
J. Exp. Med. 181:537-546(1995).
[10]
GLYCOSYLATION AT TRP-319.
PubMed=10207176; DOI=10.1093/glycob/9.5.435;
Doucey M.A., Hess D., Blommers M.J., Hofsteenge J.;
"Recombinant human interleukin-12 is the second example of a C-mannosylated
protein.";
Glycobiology 9:435-441(1999).
[11]
INVOLVEMENT IN IMD29.
PubMed=9854038; DOI=10.1172/jci4950;
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.;
"Inherited interleukin 12 deficiency in a child with bacille Calmette-
Guerin and Salmonella enteritidis disseminated infection.";
J. Clin. Invest. 102:2035-2040(1998).
[12]
FUNCTION, AND INTERACTION WITH IL23A.
PubMed=11114383; DOI=10.1016/s1074-7613(00)00070-4;
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.;
"Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with
biological activities similar as well as distinct from IL-12.";
Immunity 13:715-725(2000).
[13]
INVOLVEMENT IN IMD29.
PubMed=11753820; DOI=10.1086/338625;
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.;
"Inherited interleukin-12 deficiency: IL12B genotype and clinical phenotype
of 13 patients from six kindreds.";
Am. J. Hum. Genet. 70:336-348(2002).
[14]
ASSOCIATION WITH PSORIASIS.
PubMed=17587057; DOI=10.1007/s00439-007-0397-0;
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.;
"Sequence variants in the genes for the interleukin-23 receptor (IL23R) and
its ligand (IL12B) confer protection against psoriasis.";
Hum. Genet. 122:201-206(2007).
[15]
ASSOCIATION WITH PSORIASIS.
PubMed=18800148; DOI=10.1038/jid.2008.233;
Huffmeier U., Lascorz J., Bohm B., Lohmann J., Wendler J., Mossner R.,
Reich K., Traupe H., Kurrat W., Burkhardt H., Reis A.;
"Genetic variants of the IL-23R pathway: association with psoriatic
arthritis and psoriasis vulgaris, but no specific risk factor for
arthritis.";
J. Invest. Dermatol. 129:355-358(2009).
[16]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-328 ALONE AND IN COMPLEX WITH
IL12A, GLYCOSYLATION AT ASN-222, AND DISULFIDE BONDS.
PubMed=10899108; DOI=10.1093/emboj/19.14.3530;
Yoon C., Johnston S.C., Tang J., Stahl M., Tobin J.F., Somers W.S.;
"Charged residues dominate a unique interlocking topography in the
heterodimeric cytokine interleukin-12.";
EMBO J. 19:3530-3541(2000).
[17]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 23-328 IN COMPLEX WITH IL23A AND
ANTIBODY.
PubMed=18708069; DOI=10.1016/j.jmb.2008.08.001;
Beyer B.M., Ingram R., Ramanathan L., Reichert P., Le H.V., Madison V.,
Orth P.;
"Crystal structures of the pro-inflammatory cytokine interleukin-23 and its
complex with a high-affinity neutralizing antibody.";
J. Mol. Biol. 382:942-955(2008).
[18]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-328 IN COMPLEX WITH IL23A, AND
SUBUNIT.
PubMed=18680750; DOI=10.1016/j.jmb.2008.07.051;
Lupardus P.J., Garcia K.C.;
"The structure of interleukin-23 reveals the molecular basis of p40 subunit
sharing with interleukin-12.";
J. Mol. Biol. 382:931-941(2008).
-!- 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.
{ECO:0000269|PubMed:11114383}.
-!- FUNCTION: 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.
{ECO:0000269|PubMed:11114383}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:10899108, ECO:0000269|PubMed:18680750,
ECO:0000269|PubMed:18708069, ECO:0000269|PubMed:7836910}.
-!- INTERACTION:
P29460; P29460; NbExp=2; IntAct=EBI-1029614, EBI-1029614;
P29460; P29459: IL12A; NbExp=2; IntAct=EBI-1029614, EBI-1029636;
P29460; Q9NPF7: IL23A; NbExp=6; IntAct=EBI-1029614, EBI-2481154;
P29460; Q9EQ14: Il23a; Xeno; NbExp=2; IntAct=EBI-1029614, EBI-2481329;
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: Known to be C-mannosylated in the recombinant protein; it is not
yet known for sure if the wild-type protein is also modified.
-!- DISEASE: Immunodeficiency 29 (IMD29) [MIM:614890]: A form of Mendelian
susceptibility to mycobacterial disease, a rare condition caused by
impairment of interferon-gamma mediated immunity. It is characterized
by predisposition to illness caused by moderately virulent
mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine,
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. Clinical outcome severity depends on the
degree of impairment of interferon-gamma mediated immunity. 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. IMD29
is characterized by undetectable IL12B secretion from leukocytes.
Affected individuals generally present with BCG disease after
vaccination in childhood, and at least half also have Salmonella
infection. Disease phenotype is relatively mild, and patients have a
good prognosis. {ECO:0000269|PubMed:11753820,
ECO:0000269|PubMed:9854038}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: 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.
-!- SIMILARITY: Belongs to the IL-12B family. {ECO:0000305}.
-!- WEB RESOURCE: Name=IL12Bbase; Note=IL12B mutation db;
URL="http://structure.bmc.lu.se/idbase/IL12Bbase/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il12b/";
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EMBL; M65272; AAA35695.1; -; mRNA.
EMBL; M65290; AAA59938.1; -; mRNA.
EMBL; AY008847; AAG32620.1; -; Genomic_DNA.
EMBL; AF180563; AAD56386.1; -; mRNA.
EMBL; AF512686; AAM34792.1; -; Genomic_DNA.
EMBL; BC067498; AAH67498.1; -; mRNA.
EMBL; BC067499; AAH67499.1; -; mRNA.
EMBL; BC067500; AAH67500.1; -; mRNA.
EMBL; BC067501; AAH67501.1; -; mRNA.
EMBL; BC067502; AAH67502.1; -; mRNA.
EMBL; BC074723; AAH74723.1; -; mRNA.
CCDS; CCDS4346.1; -.
PIR; A38957; A38957.
RefSeq; NP_002178.2; NM_002187.2.
PDB; 1F42; X-ray; 2.50 A; A=23-328.
PDB; 1F45; X-ray; 2.80 A; A=23-328.
PDB; 3D85; X-ray; 1.90 A; D=23-328.
PDB; 3D87; X-ray; 2.90 A; B/D=23-328.
PDB; 3DUH; X-ray; 2.30 A; A/B=23-328.
PDB; 3HMX; X-ray; 3.00 A; A=23-328.
PDB; 3QWR; X-ray; 3.25 A; A=23-328.
PDB; 4GRW; X-ray; 2.55 A; B/D=1-328.
PDB; 5MJ3; X-ray; 1.74 A; A=23-328.
PDB; 5MJ4; X-ray; 3.40 A; A=23-328.
PDB; 5MXA; X-ray; 2.50 A; A=1-328.
PDB; 5MZV; X-ray; 2.80 A; A=1-328.
PDB; 5NJD; X-ray; 3.90 A; A/C/E/G/I/K=1-328.
PDBsum; 1F42; -.
PDBsum; 1F45; -.
PDBsum; 3D85; -.
PDBsum; 3D87; -.
PDBsum; 3DUH; -.
PDBsum; 3HMX; -.
PDBsum; 3QWR; -.
PDBsum; 4GRW; -.
PDBsum; 5MJ3; -.
PDBsum; 5MJ4; -.
PDBsum; 5MXA; -.
PDBsum; 5MZV; -.
PDBsum; 5NJD; -.
SMR; P29460; -.
BioGrid; 109807; 3.
ComplexPortal; CPX-3290; Interleukin-23 complex.
ComplexPortal; CPX-381; Interleukin-12 complex.
ComplexPortal; CPX-382; Interleukin-12-receptor complex.
ComplexPortal; CPX-383; Interleukin-23-receptor complex.
CORUM; P29460; -.
DIP; DIP-3774N; -.
ELM; P29460; -.
IntAct; P29460; 5.
STRING; 9606.ENSP00000231228; -.
ChEMBL; CHEMBL3580484; -.
DrugBank; DB02763; 5-Mercapto-2-Nitro-Benzoic Acid.
DrugBank; DB05459; Briakinumab.
DrugBank; DB05848; humanized SMART Anti-IL-12 Antibody.
DrugBank; DB14762; Risankizumab.
DrugBank; DB06083; Tapinarof.
DrugBank; DB14004; Tildrakizumab.
DrugBank; DB05679; Ustekinumab.
DrugCentral; P29460; -.
GlyConnect; 296; -.
iPTMnet; P29460; -.
PhosphoSitePlus; P29460; -.
UniCarbKB; P29460; -.
BioMuta; IL12B; -.
DMDM; 266320; -.
MassIVE; P29460; -.
PaxDb; P29460; -.
PeptideAtlas; P29460; -.
PRIDE; P29460; -.
ProteomicsDB; 54570; -.
ABCD; P29460; -.
Antibodypedia; 16629; 920 antibodies.
DNASU; 3593; -.
Ensembl; ENST00000231228; ENSP00000231228; ENSG00000113302.
GeneID; 3593; -.
KEGG; hsa:3593; -.
UCSC; uc003lxr.2; human.
CTD; 3593; -.
DisGeNET; 3593; -.
GeneCards; IL12B; -.
HGNC; HGNC:5970; IL12B.
HPA; ENSG00000113302; Tissue enhanced (lymphoid).
MalaCards; IL12B; -.
MIM; 161561; gene.
MIM; 612599; phenotype.
MIM; 614890; phenotype.
neXtProt; NX_P29460; -.
OpenTargets; ENSG00000113302; -.
Orphanet; 319558; Mendelian susceptibility to mycobacterial diseases due to complete IL12B deficiency.
Orphanet; 3287; Takayasu arteritis.
PharmGKB; PA29785; -.
eggNOG; ENOG410IF5K; Eukaryota.
eggNOG; ENOG410YWXR; LUCA.
GeneTree; ENSGT00390000012630; -.
HOGENOM; CLU_071206_1_0_1; -.
InParanoid; P29460; -.
KO; K05425; -.
OMA; AVHKLKY; -.
OrthoDB; 1179405at2759; -.
PhylomeDB; P29460; -.
TreeFam; TF334829; -.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-9020591; Interleukin-12 signaling.
Reactome; R-HSA-9020933; Interleukin-23 signaling.
SIGNOR; P29460; -.
EvolutionaryTrace; P29460; -.
GeneWiki; Interleukin-12_subunit_beta; -.
GenomeRNAi; 3593; -.
Pharos; P29460; Tclin.
PRO; PR:P29460; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; P29460; protein.
Bgee; ENSG00000113302; Expressed in female gonad and 17 other tissues.
Genevisible; P29460; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:UniProtKB.
GO; GO:0043514; C:interleukin-12 complex; IDA:UniProtKB.
GO; GO:0070743; C:interleukin-23 complex; IDA:BHF-UCL.
GO; GO:0031906; C:late endosome lumen; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042164; F:interleukin-12 alpha subunit binding; IPI:AgBase.
GO; GO:0005143; F:interleukin-12 receptor binding; TAS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; IDA:BHF-UCL.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:BHF-UCL.
GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
GO; GO:0042095; P:interferon-gamma biosynthetic process; TAS:UniProtKB.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0038155; P:interleukin-23-mediated signaling pathway; TAS:Reactome.
GO; GO:0030101; P:natural killer cell activation; IDA:UniProtKB.
GO; GO:0002323; P:natural killer cell activation involved in immune response; IEA:Ensembl.
GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:BHF-UCL.
GO; GO:0032700; P:negative regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:UniProtKB.
GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; IDA:BHF-UCL.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:BHF-UCL.
GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IDA:BHF-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0045078; P:positive regulation of interferon-gamma biosynthetic process; TAS:UniProtKB.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:BHF-UCL.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:BHF-UCL.
GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0050671; P:positive regulation of lymphocyte proliferation; IDA:UniProtKB.
GO; GO:0043382; P:positive regulation of memory T cell differentiation; ISS:BHF-UCL.
GO; GO:0032946; P:positive regulation of mononuclear cell proliferation; IMP:AgBase.
GO; GO:0032816; P:positive regulation of natural killer cell activation; IDA:UniProtKB.
GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IDA:UniProtKB.
GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IDA:BHF-UCL.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; TAS:BHF-UCL.
GO; GO:0051135; P:positive regulation of NK T cell activation; IDA:BHF-UCL.
GO; GO:0051142; P:positive regulation of NK T cell proliferation; IDA:BHF-UCL.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:BHF-UCL.
GO; GO:0034393; P:positive regulation of smooth muscle cell apoptotic process; IDA:BHF-UCL.
GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISS:BHF-UCL.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:BHF-UCL.
GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IDA:BHF-UCL.
GO; GO:2000330; P:positive regulation of T-helper 17 cell lineage commitment; ISS:BHF-UCL.
GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; ISS:BHF-UCL.
GO; GO:0034105; P:positive regulation of tissue remodeling; IC:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
GO; GO:0042035; P:regulation of cytokine biosynthetic process; TAS:UniProtKB.
GO; GO:0042509; P:regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
GO; GO:0010224; P:response to UV-B; IDA:UniProtKB.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
GO; GO:0019953; P:sexual reproduction; TAS:BHF-UCL.
GO; GO:0035744; P:T-helper 1 cell cytokine production; IEA:Ensembl.
GO; GO:0042088; P:T-helper 1 type immune response; TAS:UniProtKB.
GO; GO:0042093; P:T-helper cell differentiation; IDA:UniProtKB.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR003530; Hematopoietin_rcpt_L_F3_CS.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR015528; IL-12_beta.
InterPro; IPR019482; IL-12_beta_cen-dom.
PANTHER; PTHR23036:SF156; PTHR23036:SF156; 1.
Pfam; PF10420; IL12p40_C; 1.
PIRSF; PIRSF038007; IL_12_beta; 1.
PRINTS; PR01928; INTRLEUKN12B.
SMART; SM00408; IGc2; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 1.
PROSITE; PS01354; HEMATOPO_REC_L_F3; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Cytokine; Direct protein sequencing; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Polymorphism; Reference proteome;
Secreted; Signal.
SIGNAL 1..22
/evidence="ECO:0000269|PubMed:2204066"
CHAIN 23..328
/note="Interleukin-12 subunit beta"
/id="PRO_0000010930"
DOMAIN 23..106
/note="Ig-like C2-type"
DOMAIN 237..328
/note="Fibronectin type-III"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
CARBOHYD 135
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 222
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:10899108"
CARBOHYD 319
/note="C-linked (Man) tryptophan"
/evidence="ECO:0000269|PubMed:10207176"
/id="CAR_000187"
DISULFID 50..90
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10899108"
DISULFID 131..142
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10899108"
DISULFID 170..193
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10899108"
DISULFID 199
/note="Interchain (with C-96 in IL12A)"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10899108"
DISULFID 300..327
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10899108"
VARIANT 33
/note="V -> I (in dbSNP:rs3213096)"
/evidence="ECO:0000269|Ref.5"
/id="VAR_020001"
VARIANT 298
/note="V -> F (in dbSNP:rs3213119)"
/evidence="ECO:0000269|Ref.5"
/id="VAR_049170"
CONFLICT 239
/note="K -> N (in Ref. 2; AAA59938)"
/evidence="ECO:0000305"
STRAND 24..27
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 30..36
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 44..49
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 51..53
/evidence="ECO:0000244|PDB:3D85"
STRAND 59..62
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 70..79
/evidence="ECO:0000244|PDB:5MJ3"
HELIX 82..84
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 86..92
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 95..108
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 116..118
/evidence="ECO:0000244|PDB:3D87"
STRAND 122..126
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 130..147
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 150..160
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 162..164
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 166..170
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 174..181
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 184..197
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 200..202
/evidence="ECO:0000244|PDB:3D87"
STRAND 208..216
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 219..227
/evidence="ECO:0000244|PDB:5MJ3"
HELIX 229..232
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 239..245
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 249..257
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 260..262
/evidence="ECO:0000244|PDB:3HMX"
TURN 266..268
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 271..278
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 287..299
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 302..304
/evidence="ECO:0000244|PDB:5MJ4"
STRAND 305..315
/evidence="ECO:0000244|PDB:5MJ3"
STRAND 323..326
/evidence="ECO:0000244|PDB:5MJ3"
SEQUENCE 328 AA; 37169 MW; 118FA801B8F5BB2F CRC64;
MCHQQLVISW FSLVFLASPL VAIWELKKDV YVVELDWYPD APGEMVVLTC DTPEEDGITW
TLDQSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGEVLSHS LLLLHKKEDG IWSTDILKDQ
KEPKNKTFLR CEAKNYSGRF TCWWLTTIST DLTFSVKSSR GSSDPQGVTC GAATLSAERV
RGDNKEYEYS VECQEDSACP AAEESLPIEV MVDAVHKLKY ENYTSSFFIR DIIKPDPPKN
LQLKPLKNSR QVEVSWEYPD TWSTPHSYFS LTFCVQVQGK SKREKKDRVF TDKTSATVIC
RKNASISVRA QDRYYSSSWS EWASVPCS


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WP2292: Chemokine signaling pathway
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Related Genes :
[RPSA LAMBR LAMR1] 40S ribosomal protein SA (37 kDa laminin receptor precursor) (37LRP) (37/67 kDa laminin receptor) (LRP/LR) (67 kDa laminin receptor) (67LR) (Colon carcinoma laminin-binding protein) (Laminin receptor 1) (LamR) (Laminin-binding protein precursor p40) (LBP/p40) (Multidrug resistance-associated protein MGr1-Ag) (NEM/1CHD4) (Small ribosomal subunit protein uS2)
[Rpsa Lamr1 P40-8] 40S ribosomal protein SA (37 kDa laminin receptor precursor) (37LRP) (37 kDa oncofetal antigen) (37/67 kDa laminin receptor) (LRP/LR) (67 kDa laminin receptor) (67LR) (Laminin receptor 1) (LamR) (Laminin-binding protein precursor p40) (LBP/p40) (OFA/iLRP)
[ARHGEF2 KIAA0651 LFP40] Rho guanine nucleotide exchange factor 2 (Guanine nucleotide exchange factor H1) (GEF-H1) (Microtubule-regulated Rho-GEF) (Proliferating cell nucleolar antigen p40)
[PSMD7 MOV34L] 26S proteasome non-ATPase regulatory subunit 7 (26S proteasome regulatory subunit RPN8) (26S proteasome regulatory subunit S12) (Mov34 protein homolog) (Proteasome subunit p40)
[PSMD13] 26S proteasome non-ATPase regulatory subunit 13 (26S proteasome regulatory subunit RPN9) (26S proteasome regulatory subunit S11) (26S proteasome regulatory subunit p40.5)
[IL23A SGRF UNQ2498/PRO5798] Interleukin-23 subunit alpha (IL-23 subunit alpha) (IL-23-A) (Interleukin-23 subunit p19) (IL-23p19)
[EIF3H EIF3S3] Eukaryotic translation initiation factor 3 subunit H (eIF3h) (Eukaryotic translation initiation factor 3 subunit 3) (eIF-3-gamma) (eIF3 p40 subunit)
[Il23a] Interleukin-23 subunit alpha (IL-23 subunit alpha) (IL-23-A) (Interleukin-23 subunit p19) (IL-23p19)
[IL4] Interleukin-4 (IL-4) (B-cell stimulatory factor 1) (BSF-1) (Binetrakin) (Lymphocyte stimulatory factor 1) (Pitrakinra)
[NCF4 SH3PXD4] Neutrophil cytosol factor 4 (NCF-4) (Neutrophil NADPH oxidase factor 4) (SH3 and PX domain-containing protein 4) (p40-phox) (p40phox)
[TP63 KET P63 P73H P73L TP73L] Tumor protein 63 (p63) (Chronic ulcerative stomatitis protein) (CUSP) (Keratinocyte transcription factor KET) (Transformation-related protein 63) (TP63) (Tumor protein p73-like) (p73L) (p40) (p51)
[IL16] Pro-interleukin-16 [Cleaved into: Interleukin-16 (IL-16) (Lymphocyte chemoattractant factor) (LCF)]
[Il12rb2] Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)
[IL12RB2] Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)
[IL2RB IL15RB] Interleukin-2 receptor subunit beta (IL-2 receptor subunit beta) (IL-2R subunit beta) (IL-2RB) (High affinity IL-2 receptor subunit beta) (Interleukin-15 receptor subunit beta) (p70-75) (p75) (CD antigen CD122)
[RPSaA At1g72370 T10D10.16] 40S ribosomal protein Sa-1 (Laminin receptor homolog) (p40)
[IL12RB1 IL12R IL12RB] Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12RB1) (IL-12 receptor beta component) (CD antigen CD212)
[IFNLR1 IL28RA LICR2] Interferon lambda receptor 1 (IFN-lambda receptor 1) (IFN-lambda-R1) (Cytokine receptor class-II member 12) (Cytokine receptor family 2 member 12) (CRF2-12) (Interleukin-28 receptor subunit alpha) (IL-28 receptor subunit alpha) (IL-28R-alpha) (IL-28RA) (Likely interleukin or cytokine receptor 2) (LICR2)
[Il12rb1 Il12rb] Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12 receptor beta component) (CD antigen CD212)
[precore C PreC preC PreC-C preC-C PreC/C precore+core] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[Rpsa LAMR1] 40S ribosomal protein SA (37 kDa laminin receptor precursor) (37LRP) (37/67 kDa laminin receptor) (LRP/LR) (67 kDa laminin receptor) (67LR) (Laminin receptor 1) (LamR) (Laminin-binding protein precursor p40) (LBP/p40)
[Rpsa Lamr1] 40S ribosomal protein SA (37 kDa laminin receptor precursor) (37LRP) (37/67 kDa laminin receptor) (LRP/LR) (67 kDa laminin receptor) (67LR) (Laminin receptor 1) (LamR) (Laminin-binding protein precursor p40) (LBP/p40)
[Il6st] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[IL6ST] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (CDw130) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[Il6st] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[IL10RB CRFB4 D21S58 D21S66] Interleukin-10 receptor subunit beta (IL-10 receptor subunit beta) (IL-10R subunit beta) (IL-10RB) (Cytokine receptor class-II member 4) (Cytokine receptor family 2 member 4) (CRF2-4) (Interleukin-10 receptor subunit 2) (IL-10R subunit 2) (IL-10R2) (CD antigen CDw210b)
[IL18 IGIF IL1F4] Interleukin-18 (IL-18) (Iboctadekin) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[TAF11 TAF40 YML015C YM9571.03C] Transcription initiation factor TFIID subunit 11 (TAFII-40) (TAFII40) (TBP-associated factor 11) (TBP-associated factor 40 kDa) (P40)

Bibliography :