Ignet

Gene Information

Gene symbol: NCOA2

Gene name: nuclear receptor coactivator 2

HGNC ID: 7669

Synonyms: TIF2, GRIP1, NCoA-2, KAT13C, bHLHe75

Related Genes

#	Gene Symbol	Number of hits
1	CARM1	1 hits
2	CREB1	1 hits
3	CREBBP	1 hits
4	EP300	1 hits
5	ESR1	1 hits
6	FGR	1 hits
7	H2BFS	1 hits
8	HEATR6	1 hits
9	HNF1A	1 hits
10	HNF4A	1 hits
11	IGF1	1 hits
12	INS	1 hits
13	MED1	1 hits
14	MYBBP1A	1 hits
15	NCOA1	1 hits
16	NCOA3	1 hits
17	NCOR1	1 hits
18	NCOR2	1 hits
19	NR0B1	1 hits
20	NR3C1	1 hits
21	NR5A1	1 hits
22	PAG1	1 hits
23	PPARA	1 hits
24	RORA	1 hits
25	RXRA	1 hits
26	SRA1	1 hits
27	TAF9	1 hits
28	TTLL5	1 hits
29	UCP3	1 hits

Related Sentences

#	PMID	Sentence
1	9812974	SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4.
2	9812974	In this study, we show that SRC-1 and GRIP1, which act as coactivators for various nuclear receptors, associate with HNF4 in vivo and enhance its transactivation potential.
3	9812974	The AF-2 domain of HNF4 is required for this interaction and for the potentiation of transcriptional activity by these coactivators. p300 can also serve as a coactivator with HNF4, and it synergizes with SRC-1 to further augment the activity of HNF4.
4	9812974	HNF4 is also a key regulator of the expression of hepatocyte nuclear factor-1 (HNF1).
5	9812974	The overexpression of SRC-1 or GRIP1 enhances expression from a HNF1 gene promoter-reporter in HepG2 hepatoma cells, and this requires an intact HNF4-binding site in the HNF1 gene promoter.
6	9812974	Type 1 maturity onset diabetes of young (MODY), which is characterized by abnormal glucose-mediated insulin secretion, is caused by mutations of the HNF4 gene.
7	9812974	A mutation of the HNF4-binding site in the HNF1 gene promoter has also been associated with MODY.
8	9812974	Thus, HNF4 is involved in the regulation of glucose homeostasis at several levels and along with the SRC-1, GRIP1, and p300 may play an important role in the pathophysiology of non-insulin-dependent diabetes mellitus.
9	9812974	SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4.
10	9812974	In this study, we show that SRC-1 and GRIP1, which act as coactivators for various nuclear receptors, associate with HNF4 in vivo and enhance its transactivation potential.
11	9812974	The AF-2 domain of HNF4 is required for this interaction and for the potentiation of transcriptional activity by these coactivators. p300 can also serve as a coactivator with HNF4, and it synergizes with SRC-1 to further augment the activity of HNF4.
12	9812974	HNF4 is also a key regulator of the expression of hepatocyte nuclear factor-1 (HNF1).
13	9812974	The overexpression of SRC-1 or GRIP1 enhances expression from a HNF1 gene promoter-reporter in HepG2 hepatoma cells, and this requires an intact HNF4-binding site in the HNF1 gene promoter.
14	9812974	Type 1 maturity onset diabetes of young (MODY), which is characterized by abnormal glucose-mediated insulin secretion, is caused by mutations of the HNF4 gene.
15	9812974	A mutation of the HNF4-binding site in the HNF1 gene promoter has also been associated with MODY.
16	9812974	Thus, HNF4 is involved in the regulation of glucose homeostasis at several levels and along with the SRC-1, GRIP1, and p300 may play an important role in the pathophysiology of non-insulin-dependent diabetes mellitus.
17	9812974	SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4.
18	9812974	In this study, we show that SRC-1 and GRIP1, which act as coactivators for various nuclear receptors, associate with HNF4 in vivo and enhance its transactivation potential.
19	9812974	The AF-2 domain of HNF4 is required for this interaction and for the potentiation of transcriptional activity by these coactivators. p300 can also serve as a coactivator with HNF4, and it synergizes with SRC-1 to further augment the activity of HNF4.
20	9812974	HNF4 is also a key regulator of the expression of hepatocyte nuclear factor-1 (HNF1).
21	9812974	The overexpression of SRC-1 or GRIP1 enhances expression from a HNF1 gene promoter-reporter in HepG2 hepatoma cells, and this requires an intact HNF4-binding site in the HNF1 gene promoter.
22	9812974	Type 1 maturity onset diabetes of young (MODY), which is characterized by abnormal glucose-mediated insulin secretion, is caused by mutations of the HNF4 gene.
23	9812974	A mutation of the HNF4-binding site in the HNF1 gene promoter has also been associated with MODY.
24	9812974	Thus, HNF4 is involved in the regulation of glucose homeostasis at several levels and along with the SRC-1, GRIP1, and p300 may play an important role in the pathophysiology of non-insulin-dependent diabetes mellitus.
25	9812974	SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4.
26	9812974	In this study, we show that SRC-1 and GRIP1, which act as coactivators for various nuclear receptors, associate with HNF4 in vivo and enhance its transactivation potential.
27	9812974	The AF-2 domain of HNF4 is required for this interaction and for the potentiation of transcriptional activity by these coactivators. p300 can also serve as a coactivator with HNF4, and it synergizes with SRC-1 to further augment the activity of HNF4.
28	9812974	HNF4 is also a key regulator of the expression of hepatocyte nuclear factor-1 (HNF1).
29	9812974	The overexpression of SRC-1 or GRIP1 enhances expression from a HNF1 gene promoter-reporter in HepG2 hepatoma cells, and this requires an intact HNF4-binding site in the HNF1 gene promoter.
30	9812974	Type 1 maturity onset diabetes of young (MODY), which is characterized by abnormal glucose-mediated insulin secretion, is caused by mutations of the HNF4 gene.
31	9812974	A mutation of the HNF4-binding site in the HNF1 gene promoter has also been associated with MODY.
32	9812974	Thus, HNF4 is involved in the regulation of glucose homeostasis at several levels and along with the SRC-1, GRIP1, and p300 may play an important role in the pathophysiology of non-insulin-dependent diabetes mellitus.
33	10478845	Coactivators for the orphan nuclear receptor RORalpha.
34	10478845	Several known and putative coactivators were isolated, including glucocorticoid receptor-interacting protein-1 (GRIP-1) and peroxisome proliferator-activated receptor (PPAR)-binding protein (PBP/TRAP220/DRIP205).
35	10478845	These interactions were confirmed in vitro and require the intact activation domain of RORalpha although different requirements for interaction with GRIP-1 and PBP were detected.
36	10478845	Both PBP and GRIP-1 were shown to be present in these complexes.
37	10478845	GRIP-1 functioned as a coactivator for the RORalpha both in yeast and in mammalian cells.
38	10478845	Thus, GRIP-1 is the first proven coactivator for RORalpha.
39	10478845	Coactivators for the orphan nuclear receptor RORalpha.
40	10478845	Several known and putative coactivators were isolated, including glucocorticoid receptor-interacting protein-1 (GRIP-1) and peroxisome proliferator-activated receptor (PPAR)-binding protein (PBP/TRAP220/DRIP205).
41	10478845	These interactions were confirmed in vitro and require the intact activation domain of RORalpha although different requirements for interaction with GRIP-1 and PBP were detected.
42	10478845	Both PBP and GRIP-1 were shown to be present in these complexes.
43	10478845	GRIP-1 functioned as a coactivator for the RORalpha both in yeast and in mammalian cells.
44	10478845	Thus, GRIP-1 is the first proven coactivator for RORalpha.
45	10478845	Coactivators for the orphan nuclear receptor RORalpha.
46	10478845	Several known and putative coactivators were isolated, including glucocorticoid receptor-interacting protein-1 (GRIP-1) and peroxisome proliferator-activated receptor (PPAR)-binding protein (PBP/TRAP220/DRIP205).
47	10478845	These interactions were confirmed in vitro and require the intact activation domain of RORalpha although different requirements for interaction with GRIP-1 and PBP were detected.
48	10478845	Both PBP and GRIP-1 were shown to be present in these complexes.
49	10478845	GRIP-1 functioned as a coactivator for the RORalpha both in yeast and in mammalian cells.
50	10478845	Thus, GRIP-1 is the first proven coactivator for RORalpha.
51	10478845	Coactivators for the orphan nuclear receptor RORalpha.
52	10478845	Several known and putative coactivators were isolated, including glucocorticoid receptor-interacting protein-1 (GRIP-1) and peroxisome proliferator-activated receptor (PPAR)-binding protein (PBP/TRAP220/DRIP205).
53	10478845	These interactions were confirmed in vitro and require the intact activation domain of RORalpha although different requirements for interaction with GRIP-1 and PBP were detected.
54	10478845	Both PBP and GRIP-1 were shown to be present in these complexes.
55	10478845	GRIP-1 functioned as a coactivator for the RORalpha both in yeast and in mammalian cells.
56	10478845	Thus, GRIP-1 is the first proven coactivator for RORalpha.
57	10478845	Coactivators for the orphan nuclear receptor RORalpha.
58	10478845	Several known and putative coactivators were isolated, including glucocorticoid receptor-interacting protein-1 (GRIP-1) and peroxisome proliferator-activated receptor (PPAR)-binding protein (PBP/TRAP220/DRIP205).
59	10478845	These interactions were confirmed in vitro and require the intact activation domain of RORalpha although different requirements for interaction with GRIP-1 and PBP were detected.
60	10478845	Both PBP and GRIP-1 were shown to be present in these complexes.
61	10478845	GRIP-1 functioned as a coactivator for the RORalpha both in yeast and in mammalian cells.
62	10478845	Thus, GRIP-1 is the first proven coactivator for RORalpha.
63	10598585	Candidate factors have been identified by the observation that changes in glucocorticoid induction parameters in CV-1 cells could be reproduced by varying the cellular levels of coactivators [transcriptional intermediary factor 2 (TIF2), steroid receptor coactivator 1 (SRC-1), and amplified in breast cancer 1 (AIB1)], comodulator [CREB-binding protein (CBP)], or corepressor [silencing mediator for retinoid and thyroid-hormone receptors (SMRT)] without concomitant increases in GR.
64	10598585	Significantly, the effects of TIF2 and SMRT were mutually antagonistic.
65	10598585	Candidate factors have been identified by the observation that changes in glucocorticoid induction parameters in CV-1 cells could be reproduced by varying the cellular levels of coactivators [transcriptional intermediary factor 2 (TIF2), steroid receptor coactivator 1 (SRC-1), and amplified in breast cancer 1 (AIB1)], comodulator [CREB-binding protein (CBP)], or corepressor [silencing mediator for retinoid and thyroid-hormone receptors (SMRT)] without concomitant increases in GR.
66	10598585	Significantly, the effects of TIF2 and SMRT were mutually antagonistic.
67	11158332	Furthermore, the corepressors SMRT (silencing mediator for retinoid and thyroid receptors) and NCoR (nuclear receptor corepressor) each suppresses gene induction but NCoR acts opposite to SMRT and, like the coactivator TIF2, reduces the EC(50) and increases the partial agonist activity of antiprogestins.
68	12562779	Protein fragments harboring the LXXLL motifs of the coactivators GRIP1 and SRC1 or TRAP220 interacted predominantly with the TR.retinoid X receptor heterodimeric pair in a ligand-dependent fashion.
69	17116691	STAMP, a novel predicted factor assisting TIF2 actions in glucocorticoid receptor-mediated induction and repression.
70	17116691	The coactivator TIF2 was predicted to interact with an unknown factor to modify both the relative inhibition in glucocorticoid receptor (GR)-mediated gene repression and several parameters of agonists and antisteroids in GR-regulated induction.
71	17116691	STAMP associates with coactivators (TIF2 and SRC-1) and is selective for a subset of the steroid/nuclear receptors including GRs.
72	17116691	Transfected STAMP increases the effects of TIF2 in GR-mediated repression and induction.
73	17116691	STAMP, a novel predicted factor assisting TIF2 actions in glucocorticoid receptor-mediated induction and repression.
74	17116691	The coactivator TIF2 was predicted to interact with an unknown factor to modify both the relative inhibition in glucocorticoid receptor (GR)-mediated gene repression and several parameters of agonists and antisteroids in GR-regulated induction.
75	17116691	STAMP associates with coactivators (TIF2 and SRC-1) and is selective for a subset of the steroid/nuclear receptors including GRs.
76	17116691	Transfected STAMP increases the effects of TIF2 in GR-mediated repression and induction.
77	17116691	STAMP, a novel predicted factor assisting TIF2 actions in glucocorticoid receptor-mediated induction and repression.
78	17116691	The coactivator TIF2 was predicted to interact with an unknown factor to modify both the relative inhibition in glucocorticoid receptor (GR)-mediated gene repression and several parameters of agonists and antisteroids in GR-regulated induction.
79	17116691	STAMP associates with coactivators (TIF2 and SRC-1) and is selective for a subset of the steroid/nuclear receptors including GRs.
80	17116691	Transfected STAMP increases the effects of TIF2 in GR-mediated repression and induction.
81	17116691	STAMP, a novel predicted factor assisting TIF2 actions in glucocorticoid receptor-mediated induction and repression.
82	17116691	The coactivator TIF2 was predicted to interact with an unknown factor to modify both the relative inhibition in glucocorticoid receptor (GR)-mediated gene repression and several parameters of agonists and antisteroids in GR-regulated induction.
83	17116691	STAMP associates with coactivators (TIF2 and SRC-1) and is selective for a subset of the steroid/nuclear receptors including GRs.
84	17116691	Transfected STAMP increases the effects of TIF2 in GR-mediated repression and induction.
85	19188450	Dax-1 and steroid receptor RNA activator (SRA) function as transcriptional coactivators for steroidogenic factor 1 in steroidogenesis.
86	19188450	The atypical orphan nuclear receptor Dax-1 binds to SF-1 and represses SF-1 target genes.
87	19188450	Paradoxically, however, loss-of-function mutations of Dax-1 also cause adrenal hypoplasia, suggesting that Dax-1 may function as an SF-1 coactivator under some circumstances.
88	19188450	Indeed, we found that Dax-1 can function as a dosage-dependent SF-1 coactivator.
89	19188450	Both SF-1 and Dax-1 bind to steroid receptor RNA activator (SRA), a coactivator that functions as an RNA.
90	19188450	The coactivator TIF2 also associates with Dax-1 and synergistically coactivates SF-1 target gene transcription.
91	19188450	Coactivation by Dax-1 is abolished by SRA knockdown.
92	19188450	The expression of the steroidogenic gene products steroidogenic acute regulatory protein (StAR) and melanocortin 2 receptor is reduced in adrenal Y1 cells following the knockdown of endogenous SRA.
93	19188450	Similarly, the knockdown of endogenous Dax-1 downregulates the expression of the steroidogenic gene products CYP11A1 and StAR in both H295R adrenal and MA-10 Leydig cells.
94	19188450	These findings reveal novel functions of SRA and Dax-1 in steroidogenesis and adrenal biology.
95	19707557	Transcriptional activation by steroid hormone receptors is accompanied by changes in histone and non-histone protein post-translational modification (PTM) that result from the enzymatic activity of coactivator and corepressor proteins such as GRIP1 and CARM1.
96	19707557	Promoter interaction of the coactivator CARM1 was disrupted, but the interaction of GRIP1, a p160 coactivator through which CARM1 interacts with a promoter, was intact.
97	19707557	We postulate that iAs effects on CARM1 and GRIP1 may underlie some of its therapeutic effects and as well be associated with its toxic effects.
98	19707557	Transcriptional activation by steroid hormone receptors is accompanied by changes in histone and non-histone protein post-translational modification (PTM) that result from the enzymatic activity of coactivator and corepressor proteins such as GRIP1 and CARM1.
99	19707557	Promoter interaction of the coactivator CARM1 was disrupted, but the interaction of GRIP1, a p160 coactivator through which CARM1 interacts with a promoter, was intact.
100	19707557	We postulate that iAs effects on CARM1 and GRIP1 may underlie some of its therapeutic effects and as well be associated with its toxic effects.
101	19707557	Transcriptional activation by steroid hormone receptors is accompanied by changes in histone and non-histone protein post-translational modification (PTM) that result from the enzymatic activity of coactivator and corepressor proteins such as GRIP1 and CARM1.
102	19707557	Promoter interaction of the coactivator CARM1 was disrupted, but the interaction of GRIP1, a p160 coactivator through which CARM1 interacts with a promoter, was intact.
103	19707557	We postulate that iAs effects on CARM1 and GRIP1 may underlie some of its therapeutic effects and as well be associated with its toxic effects.
104	21035760	The transcriptional coregulators TIF2 and SRC-1 regulate energy homeostasis by modulating mitochondrial respiration in skeletal muscles.
105	21035760	The two p160 transcriptional coregulator family members SRC-1 and TIF2 have important metabolic functions in white and brown adipose tissues as well as in the liver.
106	21035760	Moreover, our results demonstrate that SRC-1 and TIF2 can modulate the expression of the uncoupling protein 3 (UCP3) in an antagonistic manner and that enhanced SRC-1 levels in TIF2-deficient myofibers are critically involved in the metabolic changes of TIF2((i)skm)⁻(/)⁻ mice.
107	21035760	The transcriptional coregulators TIF2 and SRC-1 regulate energy homeostasis by modulating mitochondrial respiration in skeletal muscles.
108	21035760	The two p160 transcriptional coregulator family members SRC-1 and TIF2 have important metabolic functions in white and brown adipose tissues as well as in the liver.
109	21035760	Moreover, our results demonstrate that SRC-1 and TIF2 can modulate the expression of the uncoupling protein 3 (UCP3) in an antagonistic manner and that enhanced SRC-1 levels in TIF2-deficient myofibers are critically involved in the metabolic changes of TIF2((i)skm)⁻(/)⁻ mice.
110	21035760	The transcriptional coregulators TIF2 and SRC-1 regulate energy homeostasis by modulating mitochondrial respiration in skeletal muscles.
111	21035760	The two p160 transcriptional coregulator family members SRC-1 and TIF2 have important metabolic functions in white and brown adipose tissues as well as in the liver.
112	21035760	Moreover, our results demonstrate that SRC-1 and TIF2 can modulate the expression of the uncoupling protein 3 (UCP3) in an antagonistic manner and that enhanced SRC-1 levels in TIF2-deficient myofibers are critically involved in the metabolic changes of TIF2((i)skm)⁻(/)⁻ mice.
113	22859932	The transcriptional coactivators p/CIP and SRC-1 control insulin resistance through IRS1 in obesity models.
114	22859932	Three p160 family members, p/CIP, SRC1, and TIF2, have been identified as transcriptional coactivators for nuclear hormone receptors and other transcription factors in vitro.
115	22859932	In a previous study, we reported initial characterization of the obesity-resistant phenotypes of p/CIP and SRC-1 double knockout (DKO) mice, which exhibit increased energy expenditure, and suggested that nuclear hormone receptor target genes were involved in these phenotypes.
116	22859932	In this study, we demonstrate that p/CIP and SRC1 control insulin signaling in a cell-autonomous manner both in vitro and in vivo.
117	22859932	Genetic deletion of p/CIP and SRC-1 increases glucose uptake and enhances insulin sensitivity in both regular chow- and high fat diet-fed DKO mice despite increased food intake.
118	22859932	Interestingly, we discover that loss of p/CIP and SRC-1 results in resistance to age-related obesity and glucose intolerance.
119	22859932	We show that expression levels of a key insulin signaling component, insulin receptor substrate 1 (IRS1), are significantly increased in two cell lines representing fat and muscle lineages with p/CIP and SRC-1 deletions and in white adipose tissue and skeletal muscle of DKO mice; this may account for increased glucose metabolism and insulin sensitivity.
120	22859932	This is the first evidence that the p160 coactivators control insulin signaling and glucose metabolism through IRS1.
121	22859932	Therefore, our studies indicate that p/CIP and SRC-1 are potential therapeutic targets not only for obesity but also for diabetes.
122	23569420	The cofactors SRC1 and GRIP1 mediate the activity of telmisartan and rosiglitazone and partially determine the difference in their effects.
123	23719562	Insulin-like growth factor 1 mRNA expression in the uterus of streptozotocin-treated diabetic mice.
124	23719562	We aimed to clarify the changes in the estrous cycle and in insulin-like growth factor 1 (IGF1) expression in the uteri of streptozotocin (STZ)-treated diabetic mice, because IGF1 is one of the main growth factors involved in estrogen-induced uterine growth.
125	23719562	Estrogen is known to stimulate Igf1 mRNA expression in the uterus, but estrogen action was abolished in the uteri of STZ-treated diabetic mice. mRNA expressions of estrogen receptor α (ERα) and steroid hormone receptor coactivators (SRC-1/Ncoa1, SRC-2/Ncoa2, SRC-3/Ncoa3 and CBP/p300/Crebbp) were reduced in the uteri of ovariectomized STZ-treated diabetic mice.
126	23719562	Igf1 expression in ovariectomized diabetic female mice was decreased, and decreased responsiveness to estrogen in the uteri of diabetic mice is probably associated with a reduction in ERα and steroid receptor coactivator mRNA expression.