J Biol Chem 2003,
PMID: 12963728
Cai, Yong; Jin, Jingji; Tomomori-Sato, Chieri; Sato, Shigeo; Sorokina, Irina; Parmely, Tari J; Conaway, Ronald C; Conaway, Joan Weliky
The mammalian ATM/PI 3-kinase-related TRRAP protein was previously found to be a component of a multi-protein histone acetyltransferase (HAT) complex containing the HAT TIP60. In this report, we identify a previously uncharacterized protein encoded by the FLJ10914 ORF, which we designate MRGBP, as a new component of the TRRAP/TIP60 HAT complex. In addition, through purification of MRGBP and its associated proteins from HeLa cell nuclear extracts, we identify the thyroid receptor coactivating protein (TRCp120), DMAP1, and the related MRG15 and MRGX proteins as MRGBP-associating proteins, and we present biochemical evidence that they are previously unrecognized components of the TRRAP/TIP60 HAT complex. Taken together, our findings shed new light on the structure and function of the mammalian TRRAP/TIP60 histone acetyltransferase complex.
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Text Mining Data
Dashed line = No text mining data
Manually curated Databases
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IRef Biogrid Interaction:
MRGBP
—
ING1
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
MRGBP
—
TRRAP
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
MRGBP
—
EPC1
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
MRGBP
—
KAT5
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
HSPA4
—
MRGBP
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
MRGBP
—
MEAF6
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
MRGBP
—
BRD8
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
MRGBP
—
MORF4L1
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
RUVBL1
—
MRGBP
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
MRGBP
—
YEATS4
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
MRGBP
—
ACTL6A
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
MRGBP
—
MORF4L2
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
MRGBP
—
DMAP1
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
RSL1D1
—
MRGBP
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
MRGBP
—
RUVBL2
(physical association, affinity chromatography technology)
-
MIPS CORUM NuA4/Tip60 HAT complex:
NuA4/Tip60 HAT complex complex (ACTL6A-BRD8-MEAF6-DMAP1-EP400-EPC1-KAT5-ING3-MORF4L1-MORF4L2-MRGBP-RUVBL1-RUVBL2-TRRAP-YEATS4)
-
IRef Corum Interaction:
Complex of 16 proteins
(association, affinity chromatography technology)
-
IRef Hprd Interaction:
MRGBP
—
ING1
(in vitro)
-
IRef Hprd Interaction:
MRGBP
—
TRRAP
(in vitro)
-
IRef Hprd Interaction:
BRD8
—
TRRAP
(in vivo)
-
IRef Hprd Interaction:
BRD8
—
TRRAP
(in vitro)
-
IRef Hprd Interaction:
Complex of 325 proteins
(in vivo)
-
IRef Hprd Interaction:
MRGBP
—
MEAF6
(in vitro)
-
IRef Hprd Interaction:
BRD8
—
MRGBP
(in vitro)
-
IRef Hprd Interaction:
MRGBP
—
MORF4L1
(in vitro)
-
IRef Hprd Interaction:
RUVBL1
—
MRGBP
(in vitro)
-
IRef Hprd Interaction:
MRGBP
—
YEATS4
(in vitro)
-
IRef Hprd Interaction:
MRGBP
—
ACTL6A
(in vitro)
-
IRef Hprd Interaction:
MRGBP
—
MORF4L2
(in vitro)
-
IRef Hprd Interaction:
MRGBP
—
DMAP1
(in vitro)
-
IRef Hprd Interaction:
MRGBP
—
TUBB
(in vitro)
-
IRef Hprd Interaction:
MRGBP
—
ACTB
(in vitro)
-
IRef Intact Interaction:
Complex of 18 proteins
(association, anti tag coimmunoprecipitation)
-
IRef Intact Interaction:
Complex of MRGBP-TRRAP-DMAP1-KAT5-KAT5-TRRAP-MRGBP-DMAP1
(physical association, biochemical)
-
IRef Intact Interaction:
Complex of MRGBP-EP400-MORF4L2-MORF4L1-BRD8-TRRAP
(physical association, biochemical)
-
IRef Intact Interaction:
Complex of 11 proteins
(physical association, molecular sieving)
In total, 200 gene pairs are associated to this article in curated databases