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MAP3K12-BINDING INHIBITORY PROTEIN; MBIP

MAP3K12-BINDING INHIBITORY PROTEIN; MBIP

Alternative titles; symbolsMUK-BINDING INHIBITORY PROTEINHGNC Approved Gene Symbol: MBIPCytogenetic location: 14q13.3 Genomic coordinates (GRCh38): 14:36,298...

Alternative titles; symbols

  • MUK-BINDING INHIBITORY PROTEIN

HGNC Approved Gene Symbol: MBIP

Cytogenetic location: 14q13.3 Genomic coordinates (GRCh38): 14:36,298,557-36,320,675 (from NCBI)

▼ Cloning and Expression
Using a partial sequence of MAP3K12 (600447) as bait in a yeast 2-hybrid screen of a brain cDNA library, followed by screening a kidney cDNA library, Fukuyama et al. (2000) cloned MBIP. The deduced protein contains 344 amino acids. The C-terminal half has 2 leucine zipper-like motifs, which are predicted to form short amphipathic alpha helices, separated by a basic nuclear localization sequence. Northern blot analysis detected a 1.8-kb MBIP transcript in all tissues examined, with relatively high expression in heart and lung. MBIP localized in several nuclear patch-like structures following overexpression in COS-1 cells.

Thorwarth et al. (2014) found expression of the Mbip gene in embryonic mouse thyroid, lung, and forebrain. The expression pattern was similar to that of Nkx2-1 (600635).

▼ Mapping
The International Radiation Hybrid Mapping Consortium mapped the MBIP gene to chromosome 14 (STS-W55968).

Thorwarth et al. (2014) stated that the MBIP gene is adjacent to the NKX2-1 gene (600635) on chromosome 14q13.

▼ Gene Function
By yeast 2-hybrid and immunoprecipitation analyses, Fukuyama et al. (2000) confirmed that the C-terminal half of MBIP interacts with a leucine-zipper-like motif of MAP3K12. When MBIP and MAP3K12 were coexpressed in COS-1 cells, the nuclear localization of MBIP was mostly abolished and cytoplasmic localization was apparent, likely due to MAP3K12 masking the MBIP nuclear localization signal. Binding also inhibited the ability of MAP3K12 to induce JNK (see MAPK8; 601158) activation. Among several JNK-activating pathways tested, the pathway induced by osmotic shock was the most sensitive to MBIP.

Using mass spectrometry, Wang et al. (2008) identified MBIP as a subunit of the ADA2A (TADA2A; 602276)-containing (ATAC) histone acetyltransferase complex in HeLa cells.

Tags: 14q13.3

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