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Nuclear Receptor Signaling Atlas
A research resource for the nuclear receptor signaling community
PGC-1β
Overview
Synonyms
4631412G21Rik ; ERR ligand 1 ; ERRL1 ; LOC711027 ; PERC ; PGC-1(beta) ; PGC-1-beta ; PGC-1-related estrogen receptor alpha coactivator ; PGC-1beta ; PGC-1beta/ERRL1 ; PGC-1β ; PGC1B ; PGC1beta ; PPAR gamma coactivator-1beta protein ; PPAR-gamma coactivator 1-beta ; PPARGC-1-beta ; PPARGC1B ; Perc ; Ppargc1b ; peroxisome proliferative activated receptor, gamma, coactivator 1 beta ; peroxisome proliferator-activated receptor gamma coactivator 1 beta ; peroxisome proliferator-activated receptor gamma coactivator 1-beta ; peroxisome proliferator-activated receptor gamma coactivator 1beta-2a
NURSA Name
PPAR-γ coactivator 1 β
NURSA Symbol
PGC-1β
Description
PGC-1β is a protein related to the cold-inducible coactivator PGC-1 α, and has been shown to coactivate several members of the nuclear receptor superfamily of transcription factors. Like PGC1-α, it is highly expressed in brown fat and heart and induced in the liver during fasting, indicating a potential role in hepatic gluconeogenesis. PGC-1β is detectable at elevated levels in heart and skeletal muscle, with lower levels in brain, kidney, liver, adrenal gland, ovary, intestine, and white adipose tissue. Dysregulation of the PGC-1β gene has been associated with metabolic disorders and cancer. PGC-1β has been shown by null deletion in mice to be required for normal growth, puberty, female reproductive function and mammary gland development.
Original References:
Kressler D, Schreiber SN, Knutti D, Kralli A, (2002) The PGC-1-related protein PERC is a selective coactivator of estrogen receptor alpha. J. Biol. Chem. 21 13918-25 View Abstract | View Pubmed
Lin J, Puigserver P, Donovan J, Tarr P, Spiegelman BM, (2002) Peroxisome proliferator-activated receptor gamma coactivator 1beta (PGC-1beta ), a novel PGC-1-related transcription coactivator associated with host cell factor. J. Biol. Chem. 21 1645-8 View Abstract | View Pubmed
Human
Gene
RNA
Protein
GO Terms
Crystal Structures
Post-Translational Modifications
Protein-Protein Interactions
Targeting miRNAs
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Last updated: January 31, 2014