Pparg coactivator 1 alpha

PPARG coactivator 1 alpha is a protein that in humans is encoded by the PPARGC1A gene.

PPARGC1A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1XB7, 3B1M, 3CS8, 3D24, 3U9Q, 3V9T, 3V9V, 4QJR, 4QK4
Identifiers
Aliases	PPARGC1A, LEM6, PGC-1(alpha), PGC-1v, PGC1, PGC1A, PPARGC1, PGC-1alpha, PPARG coactivator 1 alpha, PGC-1α
External IDs	OMIM: 604517 MGI: 1342774 HomoloGene: 7485 GeneCards: PPARGC1A
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5|5 C1 Start 51,611,592 bp End 51,725,068 bp
RNA expression pattern Bgee Human Mouse (ortholog) n/a Top expressed in atrioventricular valve retinal pigment epithelium lateral geniculate nucleus medial vestibular nucleus dorsal tegmental nucleus substantia nigra ciliary body pontine nuclei barrel cortex globus pallidus BioGPS More reference expression data
Gene ontology Molecular function promoter-specific chromatin binding transcription factor binding chromatin binding protein binding nuclear receptor binding nucleic acid binding DNA binding sequence-specific DNA binding transcription coactivator activity alpha-tubulin binding transcription coregulator activity androgen receptor binding nuclear receptor coactivator activity RNA binding chromatin DNA binding ubiquitin protein ligase binding signaling receptor binding estrogen receptor binding peroxisome proliferator activated receptor binding Cellular component cytoplasm cytosol cytosolic ribosome nucleus RNA polymerase II, core complex apical dendrite neuronal cell body PML body nucleoplasm intracellular membrane-bounded organelle Biological process negative regulation of neuron apoptotic process response to dietary excess negative regulation of glycolytic process response to fructose cellular response to interleukin-6 rhythmic process cellular response to resveratrol response to thyroid hormone cellular response to fructose stimulus cellular response to ionomycin adaptive thermogenesis response to ischemia circadian rhythm fatty acid oxidation response to metformin cellular response to caffeine response to electrical stimulus involved in regulation of muscle adaptation temperature homeostasis cellular response to hypoxia cellular response to glucose stimulus positive regulation of fatty acid oxidation cellular response to transforming growth factor beta stimulus positive regulation of progesterone biosynthetic process regulation of transcription, DNA-templated cellular response to follicle-stimulating hormone stimulus androgen metabolic process response to reactive oxygen species positive regulation of mitochondrial DNA metabolic process digestion response to leucine response to norepinephrine response to epinephrine transcription, DNA-templated negative regulation of mitochondrial fission positive regulation of transcription, DNA-templated positive regulation of glomerular visceral epithelial cell apoptotic process response to nutrient levels RNA splicing skeletal muscle atrophy cellular respiration negative regulation of signaling receptor activity positive regulation of gluconeogenesis transcription initiation from RNA polymerase II promoter cellular response to potassium ion negative regulation of neuron death negative regulation of protein phosphorylation positive regulation of cellular respiration mRNA processing protein stabilization mitochondrion organization positive regulation of DNA-binding transcription factor activity response to electrical stimulus circadian regulation of gene expression cerebellum development positive regulation of ATP biosynthetic process regulation of NMDA receptor activity galactose metabolic process positive regulation of muscle tissue development regulation of circadian rhythm flavone metabolic process adipose tissue development respiratory electron transport chain positive regulation of cellular metabolic process response to muscle activity cellular response to nitrite positive regulation of smooth muscle cell proliferation gluconeogenesis androgen receptor signaling pathway negative regulation of smooth muscle cell proliferation response to hypoxia response to organic cyclic compound cellular glucose homeostasis cellular response to tumor necrosis factor cellular response to estradiol stimulus human ageing negative regulation of smooth muscle cell migration response to activity positive regulation of histone acetylation cellular response to fatty acid autophagy of mitochondrion cellular response to thyroid hormone stimulus response to methionine response to starvation response to cold cellular response to oxidative stress forebrain development cellular response to lipopolysaccharide positive regulation of transcription by RNA polymerase II positive regulation of mitochondrion organization brown fat cell differentiation protein-containing complex assembly energy homeostasis positive regulation of gene expression positive regulation of cold-induced thermogenesis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10891 19017 Ensembl ENSG00000109819 ENSMUSG00000029167 UniProt Q9UBK2 O70343 RefSeq (mRNA) NM_013261 NM_001330751 NM_001330752 NM_001330753 NM_008904 RefSeq (protein) NP_001317680 NP_001317681 NP_001317682 NP_037393 NP_001341754 NP_001341755 NP_001341756 NP_001341757 NP_032930 NP_001389916 NP_001389917 NP_001389918 NP_001389919 NP_001389920 Location (UCSC) n/a Chr 5: 51.61 – 51.73 Mb PubMed search
Wikidata
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Function

The protein encoded by this gene is a transcriptional coactivator that regulates the genes involved in energy metabolism. This protein interacts with PPARgamma, which permits the interaction of this protein with multiple transcription factors. This protein can interact with, and regulate the activities of, cAMP response element binding protein (CREB) and nuclear respiratory factors (NRFs). It provides a direct link between external physiological stimuli and the regulation of mitochondrial biogenesis, and is a major factor that regulates muscle fiber type determination. This protein may be also involved in controlling blood pressure, regulating cellular cholesterol homoeostasis, and the development of obesity.

Further reading

• Hasstedt SJ, Ren QF, Teng K, Elbein SC (February 2001). "Effect of the peroxisome proliferator-activated receptor-gamma 2 pro(12)ala variant on obesity, glucose homeostasis, and blood pressure in members of familial type 2 diabetic kindreds". J. Clin. Endocrinol. Metab. 86 (2): 536–41. doi:10.1210/jcem.86.2.7205. PMID 11158005.
• Andersson U, Scarpulla RC (June 2001). "Pgc-1-related coactivator, a novel, serum-inducible coactivator of nuclear respiratory factor 1-dependent transcription in mammalian cells". Mol. Cell. Biol. 21 (11): 3738–49. doi:10.1128/MCB.21.11.3738-3749.2001. PMC 87014. PMID 11340167.
• Ek J, Andersen G, Urhammer SA, Gaede PH, Drivsholm T, Borch-Johnsen K, Hansen T, Pedersen O (December 2001). "Mutation analysis of peroxisome proliferator-activated receptor-gamma coactivator-1 (PGC-1) and relationships of identified amino acid polymorphisms to Type II diabetes mellitus". Diabetologia. 44 (12): 2220–6. doi:10.1007/s001250100032. PMID 11793024.
• Oberkofler H, Esterbauer H, Linnemayr V, Strosberg AD, Krempler F, Patsch W (May 2002). "Peroxisome proliferator-activated receptor (PPAR) gamma coactivator-1 recruitment regulates PPAR subtype specificity". J. Biol. Chem. 277 (19): 16750–7. doi:10.1074/jbc.M200475200. PMID 11875072.
• Esterbauer H, Oberkofler H, Linnemayr V, Iglseder B, Hedegger M, Wolfsgruber P, Paulweber B, Fastner G, Krempler F, Patsch W (April 2002). "Peroxisome proliferator-activated receptor-gamma coactivator-1 gene locus: associations with obesity indices in middle-aged women". Diabetes. 51 (4): 1281–6. doi:10.2337/diabetes.51.4.1281. PMID 11916956.
• Fu M, Zhang J, Lin Y, Zhu X, Ehrengruber MU, Chen YE (July 2002). "Early growth response factor-1 is a critical transcriptional mediator of peroxisome proliferator-activated receptor-gamma 1 gene expression in human aortic smooth muscle cells". J. Biol. Chem. 277 (30): 26808–14. doi:10.1074/jbc.M203748200. PMID 12011097.
• Lacquemant C, Chikri M, Boutin P, Samson C, Froguel P (April 2002). "No association between the G482S polymorphism of the proliferator-activated receptor-gamma coactivator-1 (PGC-1) gene and Type II diabetes in French Caucasians". Diabetologia. 45 (4): 602–3, author reply 604. doi:10.1007/s00125-002-0783-z. PMID 12032643.
• Hara K, Tobe K, Okada T, Kadowaki H, Akanuma Y, Ito C, Kimura S, Kadowaki T (May 2002). "A genetic variation in the PGC-1 gene could confer insulin resistance and susceptibility to Type II diabetes". Diabetologia. 45 (5): 740–3. doi:10.1007/s00125-002-0803-z. PMID 12107756.
• Hara K, Tobe K, Okada T, Kadowaki H, Akanuma Y, Ito C, Kimura S, Kadowaki T (May 2002). "A genetic variation in the PGC-1 gene could confer insulin resistance and susceptibility to Type II diabetes". Diabetologia. 45 (5): 740–3. doi:10.1007/s00125-002-0803-z. PMID 12107756.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.