Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Interleukin-12 subunit beta  

UniProtKB / Swiss-Prot ID :  IL12B_HUMAN

Gene Name (Synonyms) : 
IL12B, NKSF2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted. 

Protein 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. Associates with IL23A to form the IL-23 interleukin, an 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 an 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. 

Protein Sequence MCHQQLVISWFSLVFLASPLVAIWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLG...
Predicted Secondary Structure CCCCEEEHHHHHHHHHHHHHHHHHHCCCCEEEEEEEECCCCCCCCEEEECCCCCCCCEEEEECCCCEEEE...
Protein Variant
LocationDescription
33V -> I (in dbSNP:rs3213096). VAR_020001
298V -> F (in dbSNP:rs3213119). VAR_049170
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
162PhosphoserineSSRGSSDPQ
EECCCCCCC
30.38HPRD
Link-
162PhosphoserineSSRGSSDPQ
EECCCCCCC
30.38Phosphositeplus
Link-
162PhosphoserineSSRGSSDPQ
EECCCCCCC
30.38SysPTM
Link-
163PhosphoserineSRGSSDPQG
ECCCCCCCC
57.01HPRD
Link-
163PhosphoserineSRGSSDPQG
ECCCCCCCC
57.01Phosphositeplus
Link-
163PhosphoserineSRGSSDPQG
ECCCCCCCC
57.01SysPTM
Link-
222N-linked (Glc...)LKYENYTSS
CEECCCCEE
42.14OGlycBase
Link
222N-linked (GlcNAc...).LKYENYTSS
CEECCCCEE
42.14UniProtKB
Link
319C-linked (Man)YSSSWSEWA
CCCCCCCCE
11.39OGlycBase
Link
319C-linked (Man).YSSSWSEWA
CCCCCCCCE
11.39UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
IL12A_HUMANphysical interaction
physical interaction
DIP:5741EDIP10779781
7527811
IL12B_HUMANphysical interactionDIP:10909EDIP7527811
IL12A_HUMANdirect interactionEBI-1029655
intact10899108
IL12A_HUMANin vitroHPRD:01194HPRD10899108
IL12B_HUMANin vitroHPRD:01194HPRD7527811
I12R1_HUMANENSP00000231228STRING
IL2_HUMANENSP00000231228STRING
IL23A_HUMANENSP00000231228STRING
IFNG_HUMANENSP00000231228STRING
IL4_HUMANENSP00000231228STRING
IL6_HUMANENSP00000231228STRING
I12R2_HUMANENSP00000231228STRING
INGR2_HUMANENSP00000231228STRING
IL12A_HUMANENSP00000231228STRING
STAT1_HUMANENSP00000231228STRING
STAT1_HUMANENSP00000231228STRING
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Disease Reference
Kegg disease
OMIM disease
614890Immunodeficiency 29 (IMD29)
612599Psoriasis 11 (PSORS11)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
C-linked Glycosylation
ReferencePubMed
"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).
Cited for: GLYCOSYLATION AT TRP-319.
N-linked Glycosylation
ReferencePubMed
"Charged residues dominate a unique interlocking topography in theheterodimeric cytokine interleukin-12.";
Yoon C., Johnston S.C., Tang J., Stahl M., Tobin J.F., Somers W.S.;
EMBO J. 19:3530-3541(2000).
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-328 ALONE AND IN COMPLEXWITH IL12A, GLYCOSYLATION AT ASN-222, AND DISULFIDE BONDS.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures