Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Protein Page:
adiponectin (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
adiponectin Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW. Homomultimer. Forms trimers, hexamers and 12- to 18-mers. The trimers (low molecular weight complexes / LMW) are assembled via non-covalent interactions of the collagen-like domains in a triple helix and hydrophobic interactions within the globular C1q domain. Several trimers can associate to form disulfide-linked hexamers (middle molecular weight complexes / MMW) and larger complexes (higher molecular weight / HMW). The HMW-complex assembly may rely aditionally on lysine hydroxylation and glycosylation. LMW, MMW and HMW complexes bind to HBEGF, MMW and HMW complexes bind to PDGFB, and HMW complex binds to FGF2. Interacts with CTRP9A via the C1q domain (heterotrimeric complex). Synthesized exclusively by adipocytes and secreted into plasma. Note: This description may include information from UniProtKB.
Protein type: Endoplasmic reticulum; Secreted, signal peptide; Hormone; Secreted
Chromosomal Location of Human Ortholog: 3q27
Cellular Component: cell surface; collagen; endoplasmic reticulum; extracellular region; extracellular space
Molecular Function: cytokine activity; hormone activity; identical protein binding; protein binding; protein homodimerization activity; receptor binding; sialic acid binding
Biological Process: adiponectin-mediated signaling pathway; brown fat cell differentiation; cellular response to insulin stimulus; circadian rhythm; fatty acid beta-oxidation; fatty acid oxidation; generation of precursor metabolites and energy; glucose homeostasis; glucose metabolic process; membrane depolarization; membrane hyperpolarization; negative regulation of blood pressure; negative regulation of cell migration; negative regulation of fat cell differentiation; negative regulation of gluconeogenesis; negative regulation of granulocyte differentiation; negative regulation of heterotypic cell-cell adhesion; negative regulation of hormone secretion; negative regulation of I-kappaB kinase/NF-kappaB cascade; negative regulation of inflammatory response; negative regulation of low-density lipoprotein receptor biosynthetic process; negative regulation of macrophage differentiation; negative regulation of MAP kinase activity; negative regulation of phagocytosis; negative regulation of protein amino acid autophosphorylation; negative regulation of smooth muscle cell migration; negative regulation of smooth muscle cell proliferation; negative regulation of synaptic transmission; negative regulation of transcription, DNA-dependent; negative regulation of tumor necrosis factor production; positive regulation of blood pressure; positive regulation of cellular protein metabolic process; positive regulation of fatty acid metabolic process; positive regulation of glucose import; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of interleukin-8 production; positive regulation of myeloid cell apoptosis; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of protein amino acid phosphorylation; positive regulation of signal transduction; protein homooligomerization; response to activity; response to ethanol; response to glucocorticoid stimulus; response to glucose stimulus; response to hypoxia; response to nutrient; response to sucrose stimulus
Disease: Adiponectin, Serum Level Of, Quantitative Trait Locus 1
Reference #:  Q15848 (UniProtKB)
Alt. Names/Synonyms: 30 kDa adipocyte complement-related protein; ACDC; ACRP30; Adipocyte complement-related 30 kDa protein; Adipocyte, C1q and collagen domain-containing protein; Adiponectin; adiponectin, C1Q and collagen domain containing; ADIPOQ; Adipose most abundant gene transcript 1 protein; APM1; GBP28; Gelatin-binding protein
Gene Symbols: ADIPOQ
Molecular weight: 26,414 Da
Basal Isoelectric point: 5.42  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

adiponectin

Protein Structure Not Found.


STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  Phospho.ELM  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains  
Click here to view other types of protein modifications

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 K180 VSLFKKDKAMLFTYD
  mouse

 
K183 VSLFKKDKAVLFTYD
  rat

 
K180‑ac VSLFKKDkAVLFTYD
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.