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Protein Page:
leptin (human)

Overview
leptin May function as part of a signaling pathway that acts to regulate the size of the body fat depot. An increase in the level of LEP may act directly or indirectly on the CNS to inhibit food intake and/or regulate energy expenditure as part of a homeostatic mechanism to maintain constancy of the adipose mass. Defects in LEP may be a cause of obesity (OBESITY). It is a condition characterized by an increase of body weight beyond the limitation of skeletal and physical requirements, as the result of excessive accumulation of body fat. Belongs to the leptin family. Note: This description may include information from UniProtKB.
Protein type: Secreted; Hormone; Secreted, signal peptide; Cell development/differentiation
Chromosomal Location of Human Ortholog: 7q31.3
Cellular Component: cytoplasm; extracellular region; extracellular space
Molecular Function: growth factor activity; hormone activity; peptide hormone receptor binding
Biological Process: adult feeding behavior; angiogenesis; bile acid metabolic process; central nervous system neuron development; cholesterol metabolic process; circadian rhythm; eating behavior; energy reserve metabolic process; fatty acid beta-oxidation; female pregnancy; glucose homeostasis; glucose metabolic process; glycerol biosynthetic process; hormone metabolic process; insulin secretion; intestinal absorption; leptin-mediated signaling pathway; leukocyte tethering or rolling; lipid metabolic process; negative regulation of apoptosis; negative regulation of appetite; negative regulation of autophagy; negative regulation of glucose import; negative regulation of transcription from RNA polymerase II promoter; negative regulation of vasoconstriction; ovulation from ovarian follicle; placenta development; positive regulation of cytokine production; positive regulation of developmental growth; positive regulation of follicle-stimulating hormone secretion; positive regulation of insulin receptor signaling pathway; positive regulation of ion transport; positive regulation of JAK-STAT cascade; positive regulation of luteinizing hormone secretion; positive regulation of MAPKKK cascade; positive regulation of myeloid cell differentiation; positive regulation of phosphoinositide 3-kinase cascade; positive regulation of protein kinase B signaling cascade; positive regulation of T cell proliferation; positive regulation of TOR signaling pathway; positive regulation of tyrosine phosphorylation of Stat3 protein; prostaglandin secretion; regulation of angiogenesis; regulation of blood pressure; regulation of bone remodeling; regulation of cell cycle; regulation of cholesterol absorption; regulation of endothelial cell proliferation; regulation of gluconeogenesis; regulation of insulin secretion; regulation of natural killer cell activation; regulation of natural killer cell mediated cytotoxicity; regulation of natural killer cell proliferation; regulation of nitric-oxide synthase activity; regulation of steroid biosynthetic process; response to activity; response to dietary excess; response to estradiol stimulus; response to ethanol; response to hypoxia; response to insulin stimulus; response to vitamin E; sexual reproduction; T cell differentiation; tyrosine phosphorylation of STAT protein
Disease: Leptin Deficiency
Reference #:  P41159 (UniProtKB)
Gene Symbols: LEP
Molecular weight: 18,641 Da
Basal Isoelectric point: 5.88  Predict pI for various phosphorylation states
CST Pathways:  AMPK Signaling
Select Structure to View Below

leptin

Protein Structure Not Found.
Download PyMol Script
Download ChimeraX Script


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Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: 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.


 HTP 

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


       human

 
0 1 T48‑p RINDISHtQSVSSKQ
  mouse

 
T48 RINDISHTQSVSAKQ
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