PDCD4 Recombinant Rabbit Monoclonal Antibody [JA80-83] (ET1704-70)

UNIPROT #

Q53EL6

PROTEIN NAME

PDCD4

SYNONYMS

Death up-regulated gene protein antibody;Dug antibody;H731 antibody;Ma3 antibody;MGC33046 antibody;MGC33047 antibody;Neoplastic transformation inhibitor antibody;Neoplastic transformation inhibitor protein antibody;Nuclear antigen H731 antibody;Nuclear antigen H731 like antibody;Nuclear antigen H731 like protein antibody;Nuclear antigen H731-like antibody;PDCD 4 antibody;Pdcd4 antibody;PDCD4_HUMAN antibody;Programmed cell death 4 antibody;programmed cell death 4 (neoplastic transformation inhibitor) antibody;Programmed cell death protein 4 antibody;Protein 197/15a antibody;Protein MA-3 antibody;Tis antibody;Topoisomerase-inhibitor suppressed protein antibody

SEQUENCE SIMILARITIES

Belongs to the PDCD4 family.

TISSUE SPECIFICITY

Up-regulated in proliferative cells. Highly expressed in epithelial cells of the mammary gland. Reduced expression in lung cancer and colon carcinoma.

POST-TRANSLATIONAL MODIFICATION

Polyubiquitinated, leading to its proteasomal degradation. Rapidly degraded in response to mitogens. Phosphorylation of the phosphodegron promotes interaction with BTRC and proteasomal degradation.; Phosphorylated at Ser-67 by RPS6KB1 in response to mitogens; phosphorylation promotes proteasomal degradation of PDCD4.

SUBCELLULAR LOCATION

Nucleus. Cytoplasm.

FUNCTION

The transformation suppressor gene Pdcd-4 (programmed cell death gene 4) inhibits the tumor-promoter mediated transformation of mouse keratinocytes and is a potential tumor suppressor gene in the development of human lung cancer. Biochemical analysis suggests that the Pdcd-4 protein is involved in protein translation as well as in nuclear events. Pdcd-4 directly interacts with the RNA helicase eIF4A and inhibits protein synthesis by interfering with the assembly of the cap-dependent translation initiation complex. Pdcd-4 also suppresses the transactivation of AP-1 responsive promoters by c-Jun, suggesting that the transformation-suppressor activity of Pdcd-4 might be due, at least in part, to the inhibition of c-Jun activity. In addition to affecting c-Jun phosphorylation, Pdcd-4 blocks the recruitment of the co-activator p300 by c-Jun.