UniProtKB - Q15848 (ADIPO_HUMAN)
Protein
Adiponectin
Gene
ADIPOQ
Organism
Homo sapiens (Human)
Status
Functioni
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.1 Publication
Miscellaneous
Variants Arg-84 and Ser-90 show impaired formation of HMW complexes whereas variants Cys-112 and Thr-164 show impaired secretion of adiponectin in any form.
HMW-complex blood contents are higher in females than in males, are increased in males by castration and decreased again upon subsequent testosterone treatment, which blocks HMW-complex secretion (By similarity). In type 2 diabetic patients, both the ratios of HMW to total adiponectin and the degree of adiponectin glycosylation are significantly decreased as compared with healthy controls.By similarity
Caution
The expected hydroxylation of Lys-33 was not identified, probably due to poor representation of the N-terminal peptide in mass fingerprinting.1 Publication
Activity regulationi
Polymerization and secretion of adiponectin is inhibited by succination of cysteine residues by the Krebs cycle intermediate fumarate, which leads to S-(2-succinyl)cysteine residues.By similarity
GO - Molecular functioni
- cytokine activity Source: BHF-UCL
- hormone activity Source: BHF-UCL
- identical protein binding Source: BHF-UCL
- protein homodimerization activity Source: BHF-UCL
- sialic acid binding Source: UniProtKB
- signaling receptor binding Source: UniProtKB
GO - Biological processi
- brown fat cell differentiation Source: UniProtKB
- cellular response to cAMP Source: Ensembl
- cellular response to drug Source: UniProtKB
- cellular response to epinephrine stimulus Source: Ensembl
- cellular response to insulin stimulus Source: UniProtKB
- circadian rhythm Source: Ensembl
- detection of oxidative stress Source: UniProtKB
- fatty acid beta-oxidation Source: UniProtKB
- fatty acid oxidation Source: UniProtKB
- gene expression Source: Ensembl
- generation of precursor metabolites and energy Source: ProtInc
- glucose homeostasis Source: UniProtKB
- glucose metabolic process Source: UniProtKB
- low-density lipoprotein particle clearance Source: BHF-UCL
- negative regulation of blood pressure Source: UniProtKB
- negative regulation of cell migration Source: UniProtKB
- negative regulation of cold-induced thermogenesis Source: YuBioLab
- negative regulation of DNA biosynthetic process Source: UniProtKB
- negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
- negative regulation of fat cell differentiation Source: BHF-UCL
- negative regulation of gluconeogenesis Source: BHF-UCL
- negative regulation of granulocyte differentiation Source: BHF-UCL
- negative regulation of heterotypic cell-cell adhesion Source: BHF-UCL
- negative regulation of hormone secretion Source: Ensembl
- negative regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
- negative regulation of inflammatory response Source: UniProtKB
- negative regulation of intracellular protein transport Source: UniProtKB
- negative regulation of low-density lipoprotein particle receptor biosynthetic process Source: BHF-UCL
- negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
- negative regulation of macrophage differentiation Source: BHF-UCL
- negative regulation of MAP kinase activity Source: UniProtKB
- negative regulation of metanephric mesenchymal cell migration Source: UniProtKB
- negative regulation of phagocytosis Source: BHF-UCL
- negative regulation of platelet-derived growth factor receptor-alpha signaling pathway Source: UniProtKB
- negative regulation of platelet-derived growth factor receptor signaling pathway Source: UniProtKB
- negative regulation of protein autophosphorylation Source: UniProtKB
- negative regulation of receptor binding Source: UniProtKB
- negative regulation of synaptic transmission Source: UniProtKB
- negative regulation of transcription, DNA-templated Source: UniProtKB
- negative regulation of tumor necrosis factor-mediated signaling pathway Source: BHF-UCL
- negative regulation of tumor necrosis factor production Source: BHF-UCL
- negative regulation of vascular associated smooth muscle cell migration Source: UniProtKB
- negative regulation of vascular smooth muscle cell proliferation Source: UniProtKB
- positive regulation of cAMP-dependent protein kinase activity Source: UniProtKB
- positive regulation of cellular protein metabolic process Source: BHF-UCL
- positive regulation of cholesterol efflux Source: BHF-UCL
- positive regulation of cold-induced thermogenesis Source: YuBioLab
- positive regulation of fatty acid metabolic process Source: BHF-UCL
- positive regulation of glucose import Source: BHF-UCL
- positive regulation of glycogen (starch) synthase activity Source: UniProtKB
- positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
- positive regulation of interleukin-8 production Source: UniProtKB
- positive regulation of metanephric glomerular visceral epithelial cell development Source: UniProtKB
- positive regulation of monocyte chemotactic protein-1 production Source: UniProtKB
- positive regulation of myeloid cell apoptotic process Source: BHF-UCL
- positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
- positive regulation of protein kinase A signaling Source: BHF-UCL
- positive regulation of protein phosphorylation Source: UniProtKB
- positive regulation of renal albumin absorption Source: UniProtKB
- positive regulation of signal transduction Source: BHF-UCL
- protein homooligomerization Source: UniProtKB
- protein localization to plasma membrane Source: UniProtKB
- regulation of fatty acid biosynthetic process Source: Reactome
- regulation of glucose metabolic process Source: UniProtKB
- response to activity Source: Ensembl
- response to bacterium Source: Ensembl
- response to ethanol Source: Ensembl
- response to glucocorticoid Source: Ensembl
- response to glucose Source: BHF-UCL
- response to hypoxia Source: Ensembl
- response to linoleic acid Source: Ensembl
- response to nutrient Source: Ensembl
- response to sucrose Source: Ensembl
- response to tumor necrosis factor Source: BHF-UCL
Keywordsi
| Molecular function | Hormone |
Enzyme and pathway databases
| Reactomei | R-HSA-163680 AMPK inhibits chREBP transcriptional activation activity R-HSA-381340 Transcriptional regulation of white adipocyte differentiation |
| SIGNORi | Q15848 |
Protein family/group databases
| TCDBi | 8.A.94.1.1 the adiponectin (adiponectin) family |
Names & Taxonomyi
| Protein namesi | Recommended name: AdiponectinAlternative name(s): 30 kDa adipocyte complement-related protein Adipocyte complement-related 30 kDa protein Short name: ACRP30 Adipocyte, C1q and collagen domain-containing protein Adipose most abundant gene transcript 1 protein1 Publication Short name: apM-11 Publication Gelatin-binding protein |
| Gene namesi | Name:ADIPOQ Synonyms:ACDC, ACRP30, APM1, GBP282 Publications |
| Organismi | Homo sapiens (Human) |
| Taxonomic identifieri | 9606 [NCBI] |
| Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
| Proteomesi |
|
Organism-specific databases
| HGNCi | HGNC:13633 ADIPOQ |
| MIMi | 605441 gene |
| neXtProti | NX_Q15848 |
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
Extracellular region or secreted
- collagen-containing extracellular matrix Source: BHF-UCL
- extracellular region Source: BHF-UCL
- extracellular space Source: UniProtKB
Other locations
- cell surface Source: BHF-UCL
- collagen trimer Source: UniProtKB-KW
Keywords - Cellular componenti
SecretedPathology & Biotechi
Involvement in diseasei
Adiponectin deficiency (ADPND)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA condition that results in very low concentrations of plasma adiponectin.
Related information in OMIM| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_013274 | 112 | R → C in ADPND; does not assemble into trimers resulting in impaired secretion from the cell. 3 PublicationsCorresponds to variant dbSNP:rs121917815EnsemblClinVar. | 1 |
Diabetes mellitus, non-insulin-dependent (NIDDM)
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.
Related information in OMIMPharmaceutical usei
Adiponectin might be used in the treatment of diabetes type 2 and insulin resistance.
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Mutagenesisi | 20 | T → A: No change in sialylated isoforms. 1 Publication | 1 | |
| Mutagenesisi | 21 | T → A: Some loss of sialylated isoforms. 1 Publication | 1 | |
| Mutagenesisi | 22 | T → A: Abolishes sialylated isoforms. 1 Publication | 1 | |
| Mutagenesisi | 33 | K → R: No effect on formation of HMW multimers. 1 Publication | 1 | |
| Mutagenesisi | 36 | C → S: Impaired formation of MMW and HMW multimers. 2 Publications | 1 | |
| Mutagenesisi | 65 | K → R: Impaired formation of HMW multimers; when associated with R-68. 1 Publication | 1 | |
| Mutagenesisi | 68 | K → R: Impaired formation of HMW multimers; when associated with R-65. 1 Publication | 1 | |
| Mutagenesisi | 77 | K → R: Impaired formation of HMW multimers; when associated with R-101. 1 Publication | 1 | |
| Mutagenesisi | 101 | K → R: Impaired formation of HMW multimers; when associated with R-77. 1 Publication | 1 |
Keywords - Diseasei
Diabetes mellitus, Disease mutation, ObesityOrganism-specific databases
| DisGeNETi | 9370 |
| MalaCardsi | ADIPOQ |
| MIMi | 125853 phenotype 612556 phenotype |
| OpenTargetsi | ENSG00000181092 |
| PharmGKBi | PA134933118 |
Miscellaneous databases
| Pharosi | Q15848 Tbio |
Polymorphism and mutation databases
| BioMutai | ADIPOQ |
| DMDMi | 2493789 |
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Signal peptidei | 1 – 18 | 2 PublicationsAdd BLAST | 18 | |
| ChainiPRO_0000003543 | 19 – 244 | AdiponectinAdd BLAST | 226 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Glycosylationi | 21 | O-linked (GalNAc...) threonine1 Publication | 1 | |
| Glycosylationi | 22 | O-linked (GalNAc...) threonine1 Publication | 1 | |
| Modified residuei | 33 | 5-hydroxylysineBy similarity | 1 | |
| Modified residuei | 36 | S-(2-succinyl)cysteineBy similarity | 1 | |
| Disulfide bondi | 36 | Interchain; in form MMW and form HMW2 Publications | ||
| Modified residuei | 44 | 4-hydroxyproline1 Publication | 1 | |
| Modified residuei | 47 | 4-hydroxyproline1 Publication | 1 | |
| Modified residuei | 53 | 4-hydroxyproline1 Publication | 1 | |
| Modified residuei | 65 | 5-hydroxylysine1 Publication | 1 | |
| Glycosylationi | 65 | O-linked (Gal...) hydroxylysine; partial1 Publication | 1 | |
| Modified residuei | 68 | 5-hydroxylysine1 Publication | 1 | |
| Glycosylationi | 68 | O-linked (Gal...) hydroxylysine; partial1 Publication | 1 | |
| Modified residuei | 71 | 4-hydroxyproline; partial1 Publication | 1 | |
| Modified residuei | 76 | 4-hydroxyproline; partial1 Publication | 1 | |
| Modified residuei | 77 | 5-hydroxylysine1 Publication | 1 | |
| Glycosylationi | 77 | O-linked (Gal...) hydroxylysine; partial1 Publication | 1 | |
| Modified residuei | 91 | 4-hydroxyproline1 Publication | 1 | |
| Modified residuei | 95 | 4-hydroxyproline; partial1 Publication | 1 | |
| Modified residuei | 101 | 5-hydroxylysine1 Publication | 1 | |
| Glycosylationi | 101 | O-linked (Gal...) hydroxylysine; partial1 Publication | 1 |
Post-translational modificationi
HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagen-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin-sensitizing activity of adiponectin in hepatocytes.By similarity
O-glycosylated. Not N-glycosylated. O-linked glycans on hydroxylysines consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Sialylated to varying degrees depending on tissue. Thr-22 appears to be the major site of sialylation. Higher sialylation found in SGBS adipocytes than in HEK fibroblasts. Sialylation is not required neither for heterodimerization nor for secretion. Not sialylated on the glycosylated hydroxylysines. Desialylated forms are rapidly cleared from the circulation.2 Publications
Succination of Cys-36 by the Krebs cycle intermediate fumarate, which leads to S-(2-succinyl)cysteine residues, inhibits polymerization and secretion of adiponectin. Adiponectin is a major target for succination in both adipocytes and adipose tissue of diabetic mammals. It was proposed that succination of proteins is a biomarker of mitochondrial stress and accumulation of Krebs cycle intermediates in adipose tissue in diabetes and that succination of adiponectin may contribute to the decrease in plasma adiponectin in diabetes.By similarity
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sitei | 62 | Not hydroxylated1 Publication | 1 | |
| Sitei | 86 | Not hydroxylated1 Publication | 1 | |
| Sitei | 104 | Not hydroxylated1 Publication | 1 | |
| Sitei | 230 | Not glycosylated1 Publication | 1 |
Keywords - PTMi
Disulfide bond, Glycoprotein, HydroxylationProteomic databases
| CPTACi | non-CPTAC-1057 |
| EPDi | Q15848 |
| jPOSTi | Q15848 |
| MassIVEi | Q15848 |
| PaxDbi | Q15848 |
| PeptideAtlasi | Q15848 |
| PRIDEi | Q15848 |
| ProteomicsDBi | 60791 |
PTM databases
| iPTMneti | Q15848 |
| PhosphoSitePlusi | Q15848 |
Expressioni
Tissue specificityi
Synthesized exclusively by adipocytes and secreted into plasma.1 Publication
Gene expression databases
| Bgeei | ENSG00000181092 Expressed in adipose tissue of abdominal region and 119 other tissues |
| ExpressionAtlasi | Q15848 baseline and differential |
| Genevisiblei | Q15848 HS |
Organism-specific databases
| HPAi | CAB046467 HPA051767 |
Interactioni
Subunit structurei
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 is also modulated by the degree of 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 CTRP9 via the C1q domain (heterotrimeric complex).
By similarityBinary interactionsi
Show more detailsGO - Molecular functioni
- cytokine activity Source: BHF-UCL
- hormone activity Source: BHF-UCL
- identical protein binding Source: BHF-UCL
- protein homodimerization activity Source: BHF-UCL
- signaling receptor binding Source: UniProtKB
Protein-protein interaction databases
| BioGridi | 114771, 22 interactors |
| CORUMi | Q15848 |
| IntActi | Q15848, 55 interactors |
| STRINGi | 9606.ENSP00000389814 |
Miscellaneous databases
| RNActi | Q15848 protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
| SMRi | Q15848 |
| ModBasei | Search... |
| PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Domaini | 42 – 107 | Collagen-likeAdd BLAST | 66 | |
| Domaini | 108 – 244 | C1qPROSITE-ProRule annotationAdd BLAST | 137 |
Domaini
The C1q domain is commonly called the globular domain.
Keywords - Domaini
Collagen, Repeat, SignalPhylogenomic databases
| eggNOGi | ENOG410IHSJ Eukaryota ENOG4111F5K LUCA |
| GeneTreei | ENSGT00940000159828 |
| HOGENOMi | CLU_001074_0_2_1 |
| InParanoidi | Q15848 |
| KOi | K07296 |
| OMAi | NDSTFMG |
| OrthoDBi | 1110472at2759 |
| PhylomeDBi | Q15848 |
| TreeFami | TF329591 |
Family and domain databases
| Gene3Di | 2.60.120.40, 1 hit |
| InterProi | View protein in InterPro IPR001073 C1q_dom IPR008160 Collagen IPR008983 Tumour_necrosis_fac-like_dom |
| Pfami | View protein in Pfam PF00386 C1q, 1 hit PF01391 Collagen, 1 hit |
| PRINTSi | PR00007 COMPLEMNTC1Q |
| SMARTi | View protein in SMART SM00110 C1Q, 1 hit |
| SUPFAMi | SSF49842 SSF49842, 1 hit |
| PROSITEi | View protein in PROSITE PS50871 C1Q, 1 hit |
Sequencei
Sequence statusi: Complete.
Sequence processingi: The displayed sequence is further processed into a mature form.
Q15848-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLLLGAVLLL LALPGHDQET TTQGPGVLLP LPKGACTGWM AGIPGHPGHN
60 70 80 90 100
GAPGRDGRDG TPGEKGEKGD PGLIGPKGDI GETGVPGAEG PRGFPGIQGR
110 120 130 140 150
KGEPGEGAYV YRSAFSVGLE TYVTIPNMPI RFTKIFYNQQ NHYDGSTGKF
160 170 180 190 200
HCNIPGLYYF AYHITVYMKD VKVSLFKKDK AMLFTYDQYQ ENNVDQASGS
210 220 230 240
VLLHLEVGDQ VWLQVYGEGE RNGLYADNDN DSTFTGFLLY HDTN
Polymorphismi
Genetic variations in ADIPOQ influence the variance in adiponectin serum levels and define the adiponectin serum levels quantitative trait locus 1 (ADIPQTL1) [MIMi:612556].
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_013273 | 84 | G → R Does not form high molecular weight multimers. 3 PublicationsCorresponds to variant dbSNP:rs199646033Ensembl. | 1 | |
| Natural variantiVAR_027395 | 90 | G → S Does not form high molecular weight multimers. 2 PublicationsCorresponds to variant dbSNP:rs62625753Ensembl. | 1 | |
| Natural variantiVAR_027396 | 111 | Y → H1 PublicationCorresponds to variant dbSNP:rs17366743Ensembl. | 1 | |
| Natural variantiVAR_013274 | 112 | R → C in ADPND; does not assemble into trimers resulting in impaired secretion from the cell. 3 PublicationsCorresponds to variant dbSNP:rs121917815EnsemblClinVar. | 1 | |
| Natural variantiVAR_013275 | 117 | V → M1 PublicationCorresponds to variant dbSNP:rs747223144Ensembl. | 1 | |
| Natural variantiVAR_013276 | 164 | I → T Associated with low plasma adiponectin concentration and diabetes mellitus type 2; does not assemble into trimers resulting in impaired secretion from the cell. 3 PublicationsCorresponds to variant dbSNP:rs185847354Ensembl. | 1 | |
| Natural variantiVAR_013277 | 221 | R → S2 PublicationsCorresponds to variant dbSNP:rs138773406Ensembl. | 1 | |
| Natural variantiVAR_013278 | 241 | H → P2 PublicationsCorresponds to variant dbSNP:rs141205818Ensembl. | 1 |
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D45371 mRNA Translation: BAA08227.1 AB012165 Genomic DNA Translation: BAA86716.1 AJ131460, AJ131461 Genomic DNA Translation: CAB52413.1 BC054496 mRNA Translation: AAH54496.1 BC096308 mRNA Translation: AAH96308.1 BC096309 mRNA Translation: AAH96309.1 BC096310 mRNA Translation: AAH96310.1 BC096311 mRNA Translation: AAH96311.1 |
| CCDSi | CCDS3284.1 |
| PIRi | JC4708 |
| RefSeqi | NP_001171271.1, NM_001177800.1 NP_004788.1, NM_004797.3 |
Genome annotation databases
| Ensembli | ENST00000320741; ENSP00000320709; ENSG00000181092 ENST00000444204; ENSP00000389814; ENSG00000181092 |
| GeneIDi | 9370 |
| KEGGi | hsa:9370 |
| UCSCi | uc003fra.4 human |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
Cross-referencesi
Web resourcesi
| Wikipedia Adiponectin entry |
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D45371 mRNA Translation: BAA08227.1 AB012165 Genomic DNA Translation: BAA86716.1 AJ131460, AJ131461 Genomic DNA Translation: CAB52413.1 BC054496 mRNA Translation: AAH54496.1 BC096308 mRNA Translation: AAH96308.1 BC096309 mRNA Translation: AAH96309.1 BC096310 mRNA Translation: AAH96310.1 BC096311 mRNA Translation: AAH96311.1 |
| CCDSi | CCDS3284.1 |
| PIRi | JC4708 |
| RefSeqi | NP_001171271.1, NM_001177800.1 NP_004788.1, NM_004797.3 |
3D structure databases
| Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 4DOU | X-ray | 2.00 | A | 104-244 | [»] | |
| SMRi | Q15848 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| BioGridi | 114771, 22 interactors |
| CORUMi | Q15848 |
| IntActi | Q15848, 55 interactors |
| STRINGi | 9606.ENSP00000389814 |
Protein family/group databases
| TCDBi | 8.A.94.1.1 the adiponectin (adiponectin) family |
PTM databases
| iPTMneti | Q15848 |
| PhosphoSitePlusi | Q15848 |
Polymorphism and mutation databases
| BioMutai | ADIPOQ |
| DMDMi | 2493789 |
Proteomic databases
| CPTACi | non-CPTAC-1057 |
| EPDi | Q15848 |
| jPOSTi | Q15848 |
| MassIVEi | Q15848 |
| PaxDbi | Q15848 |
| PeptideAtlasi | Q15848 |
| PRIDEi | Q15848 |
| ProteomicsDBi | 60791 |
Protocols and materials databases
| ABCDi | Q15848 |
Genome annotation databases
| Ensembli | ENST00000320741; ENSP00000320709; ENSG00000181092 ENST00000444204; ENSP00000389814; ENSG00000181092 |
| GeneIDi | 9370 |
| KEGGi | hsa:9370 |
| UCSCi | uc003fra.4 human |
Organism-specific databases
| CTDi | 9370 |
| DisGeNETi | 9370 |
| GeneCardsi | ADIPOQ |
| HGNCi | HGNC:13633 ADIPOQ |
| HPAi | CAB046467 HPA051767 |
| MalaCardsi | ADIPOQ |
| MIMi | 125853 phenotype 605441 gene 612556 phenotype |
| neXtProti | NX_Q15848 |
| OpenTargetsi | ENSG00000181092 |
| PharmGKBi | PA134933118 |
| GenAtlasi | Search... |
Phylogenomic databases
| eggNOGi | ENOG410IHSJ Eukaryota ENOG4111F5K LUCA |
| GeneTreei | ENSGT00940000159828 |
| HOGENOMi | CLU_001074_0_2_1 |
| InParanoidi | Q15848 |
| KOi | K07296 |
| OMAi | NDSTFMG |
| OrthoDBi | 1110472at2759 |
| PhylomeDBi | Q15848 |
| TreeFami | TF329591 |
Enzyme and pathway databases
| Reactomei | R-HSA-163680 AMPK inhibits chREBP transcriptional activation activity R-HSA-381340 Transcriptional regulation of white adipocyte differentiation |
| SIGNORi | Q15848 |
Miscellaneous databases
| GeneWikii | Adiponectin |
| GenomeRNAii | 9370 |
| Pharosi | Q15848 Tbio |
| PROi | PR:Q15848 |
| RNActi | Q15848 protein |
| SOURCEi | Search... |
Gene expression databases
| Bgeei | ENSG00000181092 Expressed in adipose tissue of abdominal region and 119 other tissues |
| ExpressionAtlasi | Q15848 baseline and differential |
| Genevisiblei | Q15848 HS |
Family and domain databases
| Gene3Di | 2.60.120.40, 1 hit |
| InterProi | View protein in InterPro IPR001073 C1q_dom IPR008160 Collagen IPR008983 Tumour_necrosis_fac-like_dom |
| Pfami | View protein in Pfam PF00386 C1q, 1 hit PF01391 Collagen, 1 hit |
| PRINTSi | PR00007 COMPLEMNTC1Q |
| SMARTi | View protein in SMART SM00110 C1Q, 1 hit |
| SUPFAMi | SSF49842 SSF49842, 1 hit |
| PROSITEi | View protein in PROSITE PS50871 C1Q, 1 hit |
| ProtoNeti | Search... |
| MobiDBi | Search... |
Entry informationi
| Entry namei | ADIPO_HUMAN | |
| Accessioni | Q15848Primary (citable) accession number: Q15848 Secondary accession number(s): Q58EX9 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
| Last sequence update: | November 1, 1996 | |
| Last modified: | February 26, 2020 | |
| This is version 202 of the entry and version 1 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Pharmaceutical, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Human chromosome 3
Human chromosome 3: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
