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Protein Page:
IL4 (human)

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; Secreted, signal peptide; Cytokine; Cell cycle regulation; Motility/polarity/chemotaxis
Cellular Component: extracellular space; external side of plasma membrane
Molecular Function: protein binding; growth factor activity; cytokine activity; interleukin-4 receptor binding
Biological Process: regulation of isotype switching; negative regulation of osteoclast differentiation; positive regulation of isotype switching to IgG isotypes; positive regulation of transcription, DNA-dependent; regulation of proton transport; female pregnancy; chemotaxis; positive regulation of activated T cell proliferation; response to organic cyclic substance; 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; connective tissue growth factor biosynthetic process; positive regulation of B cell proliferation; positive regulation of T cell proliferation; positive regulation of interleukin-13 production; negative regulation of macrophage activation; response to nutrient; response to drug; cholesterol metabolic process; negative regulation of chronic inflammatory response; regulation of immune response; T-helper 2 type immune response; regulation of phosphorylation; negative regulation of nitric oxide biosynthetic process; negative regulation of acute inflammatory response; defense response to protozoan; T-helper 1 cell lineage commitment; response to ethanol; positive regulation of chemokine biosynthetic process; positive regulation of T cell differentiation; innate immune response in mucosa; positive regulation of tyrosine phosphorylation of Stat5 protein; B cell differentiation; response to cytokine stimulus; cellular defense response; positive regulation of transcription factor activity; positive regulation of transcription from RNA polymerase II promoter; immune response; T-helper 2 cell differentiation; negative regulation of transcription, DNA-dependent; negative regulation of apoptosis
Reference #:  P05112 (UniProtKB)
Alt. Names/Synonyms: B cell growth factor 1; B cell stimulatory factor 1; B-cell stimulatory factor 1; BCGF-1; BCGF1; BSF1; IL-4; interleukin 4
Gene Symbols: IL4
Molecular weight: 17,492 Da
Basal Isoelectric point: 9.17  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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.


       human

 
0 1 T68-p KNTTEKEtFCRAATV
  mouse

 
L67 KNTTESELVCRASKV
  rat

 
L67 RNTTENELICRASRV
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