GRIP1 [GRP01]

GWB-53B5CD

IgG1Light chain: kappa

Human

Nuclear

10mM Phosphate-buffered saline pH7. 4 containing 0. 2%BSA and 0. 1% sodium azide

Nuclear The steroid hormones thyroid hormone vitamin D and retinoic acid function by activating specific nuclear receptor proteins found inside of target cells. The activated receptors bind to and activate specific genes and the products of these activated genes change cellular activities in specific ways thus constituting the biological response to the hormone. After binding to target genes the activated nuclear receptors require the assistance of proteins called transcriptional coactivators in order to activate the target genes. GRIP 1 is a novel protein that serves as a transcriptional coactivator for steroid and nuclear hormone receptors.

Interacts with EPHA7 EPHB2 KIF5A KIF5B KIF5C GRIA2 GRIA3 GRIPAP1/GRASP1 PPFIA1 PPFIA4 FRAS1 PLCD4 PTPRF and liprins-alpha. Can form homomultimers or heteromultimers with GRIP2. Forms a ternary complex with GRIA2 and CSPG4 (By similarity). Interacts with EFNB1 EFNB3 and the C-terminal tail of PRLHR. Interacts with SLC30A9 (By similarity).

PDZ 6 mediates interaction with the PDZ recognition motif of EFNB1 and EPHB2 and with the C-terminus of PPFIA1 and PPFIA4. PDZ 4 and PDZ 5 mediate interaction with the C-terminus of GRIA2 and GRIA3. PDZ 4 PDZ 5 and PDZ 6 mediate homomultimers. PDZ 7 mediates interaction with PDZ domain of GRASP1. PDZ 7 domain binds CSPG4. PDZ 6 mediates interaction with the C-terminus of liprins-alpha. PDZ 1 PDZ 2 and PDZ 3 mediate interaction with the PDZ-binding motif of FRAS1 (By similarity). PDZ 4 and PDZ 5 mediate interaction with PRLHR.