IndraLab

Statements

KMT2C binds BAP1.
4 | 4 21
KMT2C binds BAP1. 10 / 26
4 | 4 18
sparser
"Cancer-associated MLL3 PHD mutations disrupt the interaction between MLL3 and BAP1 and correlate with poor patient survival."
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biogrid
No evidence text available
29785026
sparser
"For instance, the BAP1 H2A deubiquitinase recruits H3K4 monomethylase MLL3 to monomethylate gene enhancers, while disruption of the interaction between BAP1 and MLL3 contributes to the pathogenesis of multiple cancers [ xref ]."
31747960
sparser
"MLL3 COMPASS uniquely associates with the BAP1 complex."
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sparser
"Western blotting analysis confirmed an interaction between the BAP1 complex and the MLL3-NTD ( xref )."
29785026
sparser
"To investigate if the endogenous MLL3 also interacts with BAP1, we immunoprecipitated MLL3, MLL4, SET1A, and SET1B components of the COMPASS family from HEK293T cells using antibodies specific to each methyltransferase ( xref ; xref )."
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sparser
"The interaction between BAP1 and MLL3 was also confirmed in other two additional cell lines ( xref )."
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reach
"Recently identified missense mutations within the PHD fingers 1-3 have been shown to disrupt the interaction between KMT2C and BAP1 leading to reduced recruitment of KMT2C to gene enhancers 1."
30665945
sparser
"In addition, a mutation hotspot within the PHD cluster of the KMT2C gene was described, the mutations of which disrupted the interaction of KMT2C with the BAP1 (BRCA1 associated protein-1) tumor suppressor, resulting in poor patient survival in many types of cancer (liver, lung, bladder, and breast)."
33302406
sparser
"This unique domain could mediate the association of BAP1 (a histone deubiquitinase) with MLL3, but not with, other SET1/MLL family of KMTs, including MLL4."
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BAP1 binds KMT2C and KDM6A. 2 / 2
| 2
sparser
"Mutations within the MLL3 PHD domains abolish the interaction between the BAP1 tumor suppressor complex and MLL3-UTX, which leads to attenuation of enhancer activity."
30753822
sparser
"We found that cancer hotspot mutations in the MLL3 amino terminal PHD repeats disrupt its association with the BAP1 complex and result in reduced MLL3 and UTX recruitment to enhancers misregulating the epigenetic chromatin state at these loci."
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KMT2C binds BAP1 and PDC. 1 / 1
| 1
sparser
"Our data suggest that MLL3 PHD-BAP1 interactions have a crucial function that is disrupted in cancer and implicate BAP1 as a previously uncharacterized regulator of MLL3 COMPASS function."
29785026
KMT2C activates BAP1.
| 1
KMT2C activates BAP1. 1 / 1
| 1
reach
"Although the structure-function activities for the majority of these PHD fingers remain unknown, the sixth PHD (PHD6) finger of MLL4 and the homologous seventh PHD (PHD7) finger of MLL3 were identified as readers of acetylated lysine 16 of histone H4 , and the second and third PHD (PHD2/3) fingers of MLL3 were shown to mediate association of MLL3 with the histone H2A deubiquitinase and tumor suppressor BAP1 (BRCA-1 associated protein 1) ."
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