Studijama koimunoprecipitacije na mišjima Shcbp1 i Shc, Schmandt et al. (1999) pokazali su da se Shcbp1 povezuje s izoformama p52 i p46 Shc. Studije padavina pokazale su da je povezanost Shcbp1 i Shc posredovana preko SH2 domena Shc i da je ta interakcija neovisna od fosforilacije tirozina.[8]
2-hibridnim skriningom kvačeve biblioteka mišjih T-ćelija i embrionskecDNK s p52 SHC (SHC1) kao sondom, Schmandt et al. (1999) klonirali su Shcbp1, koji su nazvali Pal. Izvedeni mišji protein od 668 aminokiselina ima predviđenu molekulskuu masu od 75 kD i sadrži 23 ostatka tirozina, od kojih se nekoliko nalazi u motivima dobrog konsenzusa za domene SH2. Izolirali su ljudski SHCBP1, koji dijeli 78,2% aminokiselinskog identiteta sa svojim mišjim homologom. Northern blot analizom mišjih tkiva otkrivena je snažna ekspresija u sjemenicima i niža ekspresija u slezeni, plućima i srcu. Ekspresija iRNK Shcbp1 uočena je u mišićima u svim fazama razvoja embriona, a ekspresija iRNK Shcbp1 i proteina ograničena je na tkiva koja sadrže aktivno dijeleće ćelije i proliferirajuće ćelije u kulturi
^Schmandt, R., Liu, S. K., McGlade, C. J. Cloning and characterization of mPAL, a novel Shc SH2 domain-binding protein expressed in proliferating cells. Oncogene 18: 1867-1879, 1999. [ PubMed: 10086341
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