Cloning and characterization of mouse disabled 2 interacting protein 2, a mouse orthologue of human NOSTRIN

Young Joon Choi, Si Young Cho, Hyung Wook Kim, Jung Ah Kim, Sung Ho Bae, Sung Soo Park

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16 Citations (Scopus)


The mouse disabled 2 interacting protein 2 (mDaIP2) had been obtained through yeast two hybrid system. It consists of 506 amino acids and its calculated molecular weight is 57.7 kDa. The protein contains N-terminal FCH domain and C-terminal SH3 domain. The SH3 domain interacts with the proline rich domain of mDab2 which had been identified to possess a transcriptional activation function. In RA-treated F9 teratocarcinoma cell, the mDaIP2 and mDab2 genes were differentially expressed in a RA-responsive manner and both were detected to localize in cytoplasm and nucleus. Homology search of all NCBI sequences indicated that the amino acid sequence of mDaIP2 shares 82% identity with human NOSTRIN which controls activity, trafficking, and targeting of nitric oxide synthase (eNos). The eNos was not detected in RA-treated F9 cell. These results suggest that mDaIP2 somehow functions in a different fashion from NOSTRIN in F9 cell differentiation and that its function may be concerted with that of mDab2.

Original languageEnglish
Pages (from-to)594-599
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 2005 Jan 21


ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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