| First Author | Yamao T | Year | 1997 |
| Journal | Biochem Biophys Res Commun | Volume | 231 |
| Issue | 1 | Pages | 61-7 |
| PubMed ID | 9070220 | Mgi Jnum | J:38263 |
| Mgi Id | MGI:85640 | Doi | 10.1006/bbrc.1996.6047 |
| Citation | Yamao T, et al. (1997) Mouse and human SHPS-1: molecular cloning of cDNAs and chromosomal localization of genes. Biochem Biophys Res Commun 231(1):61-7 |
| abstractText | SHPS-1 (SHP substrate-1) is a glycosylated receptor-like protein with three immunoglobulin-like domains in its extracellular region and four YXX(L/V/I) motifs, potential tyrosine phosphorylation and SRC homology 2 (SH2) domain binding sites, in its cytoplasmic region, Various mitogens and cell adhesion induce tyrosine phosphorylation of SHPS- 1 and its subsequent association with SHP-2, an SH2 domain- containing protein tyrosine phosphatase, suggesting that SHPS-1 plays a role in cell signaling in response to both growth factors and cell adhesion. The mouse and human cDNAs encoding SHPS-1 have now been isolated. The deduced amino acid sequences of rat, human, and mouse SHPS-1 show identities of 65 to 81 %. In addition to the SH2 domain binding sites, a proline-rich putative SH3 domain binding site was detected in the cytoplasmic region of SHPS-1. Northern blot analysis revealed that human SHPS-1 mRNA is most abundant in brain and that the mouse mRNA is present in embryos as early as day 7. Fluorescence in situ hybridization localized the SHPS-1 gene to human chromosome 20p13 and the F3 band of mouse chromosome 2, Furthermore, interspecific backcross analysis placed the mouse SHPS-1 locus 5.0 centimorgans distal and 1.4 centimorgans proximal to the microsatellite markers D2Mit63 and D2Mit19, respectively, in a region associated with the mutations coloboma (Cm), lethal milk (lm), and well-haarig (we). (C) 1997 Academic Press. |
