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Cloning and characterization of MUPP1, a novel PDZ domain protein
Author(s) -
Ullmer Christoph,
Schmuck Karin,
Figge Andrea,
Lübbert Hermann
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00141-0
Subject(s) - pdz domain , complementary dna , cloning (programming) , gene , biology , domain (mathematical analysis) , scaffold protein , protein domain , microbiology and biotechnology , genetics , computational biology , signal transduction , computer science , mathematical analysis , mathematics , programming language
Using the yeast two‐hybrid system we isolated a cDNA clone encoding a novel protein interacting with the C‐terminal domain of the 5‐HT 2C receptor. The protein, named MUPP1 (multi‐PDZ‐domain protein), contains thirteen PDZ domains and no obvious catalytic domain; it is related to hINADL and a putative C. elegans polypeptide referred to as C52A11.4 containing six or ten PDZ domains, respectively. Domains highly similar to those of MUPP1 are arrayed in the same order in all three proteins. The MUPP1 gene is localized on human chromosome 9p24‐p22. Transcripts encoding MUPP1 are abundant in the brain as well as in several peripheral organs.

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