| First Author | Kotaka M | Year | 1999 |
| Journal | J Cell Biochem | Volume | 72 |
| Issue | 2 | Pages | 279-85 |
| PubMed ID | 10022510 | Mgi Jnum | J:52171 |
| Mgi Id | MGI:1328525 | Doi | 10.1002/(sici)1097-4644(19990201)72:2<279::aid-jcb12>3.0.co;2-7 |
| Citation | Kotaka M, et al. (1999) Characterization of the human 36-kDa carboxyl terminal LIM domain protein (hCLIM1). J Cell Biochem 72(2):279-85 |
| abstractText | We characterized a human cDNA clone encoding a 36-kDa carboxyl terminal LIM domain protein with a PDZ domain at the amino terminal. This full-length cDNA clone has a predicted open reading frame (ORF) of 329 amino-acid residues. The ORF of this cDNA encodes the human homolog of rat CLP36, and the putative protein is named human 36-kDa carboxyl terminal LIM domain protein (hCLIM1, nomenclature approved by the HUGO/GDB Nomenclature Committee). The hCLIM1 probe was used to hybridize with poly(A)+ RNA of various human tissues. Strong signals were detected in heart and skeletal muscle; moderate signals were detected in spleen, small intestine, colon, placenta, and lung; weaker levels were detected in liver, thymus, kidney, prostate, and pancreas; and no observable signals were detected in brain, testis, ovary, and peripheral blood leukocytes. The hCLIM1 gene was studied by fluorescence in situ hybridization (FISH), somatic cell hybrid analysis, and radiation hybrid mapping, and it is located at the human chromosome 10q26. |
