RACK1

Plasma proteins, Ribosomal proteins, Transporters

Intracellular

Cell type enhanced (Extravillous trophoblasts, Breast myoepithelial cells, Breast glandular cells, Exocrine glandular cells, Cytotrophoblasts, Syncytiotrophoblasts)

Low immune cell specificity

Low cell line specificity

Monomer; also forms homodimers and homooligomers (PubMed:20529362, PubMed:15140893). Interacts with CPNE3 (PubMed:20010870). May interact with ABCB4 (PubMed:19674157). Component of the small (40S) ribosomal subunit (By similarity). Interacts with the 80S ribosome (PubMed:23636399). Binds SLC9A3R1. Forms a ternary complex with TRIM63 and PRKCE. Interacts with HABP4, KRT1 and OTUB1. Interacts with SRC (via SH2 domain); the interaction is enhanced by tyrosine phosphorylation of RACK1. Recruited in a circadian manner into a nuclear complex which also includes BMAL1 and PRKCA. Interacts with AR. Interacts with IGF1R but not with INSR. Interacts with ADAM12. Interacts with CLEC1B (via N-terminal region) and with HIF1A; the interaction promotes their degradation. Interacts with RHOA; this enhances RHOA activation and promotes cell migration. Interacts with CHRM2; the interaction regulates CHRM2 internalization. Interacts with TRPM6 (via kinase domain). Interacts with PTK2/FAK1; required for PTK2/FAK1 phosphorylation and dephosphorylation. Interacts with FLT1. Interacts with TBXA2R isoform 2. Interacts with HRAS. Interacts with LARP4B. Interacts with LARP4 (PubMed:21098120). Interacts with PKD2L1. (Microbial infection) Interacts with Y. pseudotuberculosis yopK. (Microbial infection) Interacts with Y. pseudotuberculosis yopK. Interacts with a number of viral proteins including Epstein-Barr virus BZLF1 and HIV-1 Nef; interaction with Nef increases Nef phosphorylation by PKC.

Developmental protein, Ribonucleoprotein, Ribosomal protein