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Protein Page:
IL4 (mouse)

Overview
IL4 Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Genetic variations in IL4 may be a cause of susceptibility to ischemic stroke (ISCHSTR); also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. Belongs to the IL-4/IL-13 family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Secreted, signal peptide; Cytokine; Motility/polarity/chemotaxis; Secreted; Cell cycle regulation
Cellular Component: extracellular space; extracellular region; external side of plasma membrane
Molecular Function: growth factor activity; hematopoietin/interferon-class (D200-domain) cytokine receptor binding; cytokine activity; interleukin-4 receptor binding
Biological Process: negative regulation of osteoclast differentiation; positive regulation of isotype switching to IgG isotypes; positive regulation of transcription, DNA-dependent; regulation of proton transport; microglial cell activation; positive regulation of activated T cell proliferation; positive regulation of interleukin-10 production; positive regulation of isotype switching to IgE isotypes; B cell costimulation; positive regulation of MHC class II biosynthetic process; positive regulation of cell proliferation; positive regulation of B cell proliferation; positive regulation of T cell proliferation; positive regulation of interleukin-13 production; negative regulation of macrophage activation; cholesterol metabolic process; regulation of immune response; negative regulation of chronic inflammatory response; B cell activation; negative regulation of nitric oxide biosynthetic process; negative regulation of acute inflammatory response; defense response to protozoan; positive regulation of peptidyl-tyrosine phosphorylation; T-helper 1 cell lineage commitment; positive regulation of chemokine biosynthetic process; positive regulation of tyrosine phosphorylation of Stat5 protein; innate immune response in mucosa; positive regulation of T cell differentiation; positive regulation of B cell activation; regulation of inflammatory response; immune response; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription factor activity; positive regulation of protein amino acid phosphorylation; T-helper 2 cell differentiation; negative regulation of transcription, DNA-dependent; positive regulation of defense response to virus by host; negative regulation of T cell activation
Reference #:  P07750 (UniProtKB)
Alt. Names/Synonyms: B-cell growth factor 1; B-cell IgG differentiation factor; B-cell stimulatory factor 1; BSF-1; IGG1 induction factor; IL-4; IL4; interleukin 4; Lymphocyte stimulatory factor 1
Gene Symbols: Il4
Molecular weight: 15,834 Da
Basal Isoelectric point: 8.18  Predict pI for various phosphorylation states
Select Structure to View Below

IL4

Protein Structure Not Found.


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Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       mouse

 
0 1 L67 KNTTESELVCRASKV
  human

 
T68-p KNTTEKEtFCRAATV
  rat

 
L67 RNTTENELICRASRV
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