RPLP1 (ribosomal protein large P1) is part of the 60S ribosomal subunit and functions in regulating elongation translation factors, and its expression is regulated by the estrogen target gene, c-Myc. RPLP1 has two alternatively spliced transcript variants that encode different proteins, with variant 1 coding for a protein of ~12-kDa molecular weight and variant 2 coding for an ~8.4-kDa protein, and the variant 1-transcribed protein appears as the major isoform. RPLP1 is proposed to play a role in diseases associated with cell proliferation and cell survival.
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal phosphoprotein that is a component of the 60S subunit. The protein, which is a functional equivalent of the E. coli L7/L12 ribosomal protein, belongs to the L12P family of ribosomal proteins. It plays an important role in the elongation step of protein synthesis. Unlike most ribosomal proteins, which are basic, the encoded protein is acidic. Its C-terminal end is nearly identical to the C-terminal ends of the ribosomal phosphoproteins P0 and P2. The P1 protein can interact with P0 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Two alternatively spliced transcript variants that encode different proteins have been observed. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
40S Ribosomal Protein S19 (RPS19) is a ribosomal protein that Belongs to the ribosomal protein S19e family. RPS19 is located in the nucleoli, and higher level expression is seen in colon carcinoma tissue than normal colon tissue. It required for pre-rRNA processing and maturation of 40S ribosomal subunits. RPS19 plays a role in many biological processes, such as endocrine pancreas development, erythrocyte differentiation, mRNA metabolic process. Defects in RPS19 are the cause of Diamond-Blackfan anemia type 1 (DBA1), which is a form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy.
40S ribosomal protein S7(RPS7) belongs to the S7E family of ribosomal proteins. It is phosphorylated by NEK6 during post-translational modification. RPS7 is located in the cytoplasm, binds IPO9 with high affinity. it also can interacts with NEK6. As is required for rRNA maturation and typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. The unnormal expression of RPS7 may cause Diamond-Blackfan anemia 8.
Ribonucleoside reductase subunit M2B, also known as RRM2B or p53R2, is an enzyme belonging to the iron-dependent ribonucleotide reductase (RNR) enzyme family which is essential for DNA synthesis. Ribonucleotide reductase (RNR) is an enzyme that catalyzes the formation of deoxyribonucleotides from ribonucleotides and plays a critical role in regulating the total rate of DNA synthesis so that DNA to cell mass is maintained at a constant ratio during cell division and DNA repair. RRM2B is a phosphorylated protein. It is hypothesized that RRM2B activity can be regulated at the posttranslational level in response to DNA damage. RRM2B has previously been shown to be essential for the maintenance of mtDNA copy number and its candidacy for tumor suppression has been evaluated in several mutational analyses of different cancer types. However, the contribution of RRM2B to the DNA damage response has been questioned because its transcriptional induction upon DNA damage is not rapid enough for prompt DNA repair. Instead, ATM-mediated phosphorylation has been suggested to regulate the DNA repair activity of RRM2B posttranslationally. In addition, a defect in RRM2B can induce a mild muscle disease of adult onset through disturbance of mitochondrial homeostasis but that this defect does not appear to be oncogenic.
Ribosomal protein S6 kinase alpha-2, also known as 90 kDa ribosomal protein S6 kinase 2, MAP kinase-activated protein kinase 1c, MAPK-activated protein kinase 1c, Ribosomal S6 kinase 3, RSK-3, RPS6KA2 and MAPKAPK1C, is a nucleus protein which belongs to theprotein kinase superfamily, AGC Ser/Thr protein kinase family and S6 kinase subfamily. RPS6KA2 / RSK-3 is expressed in many tissues. Highest expression is in lung and skeletal muscle. The expression of RPS6KA2 reduced proliferation, caused G1 arrest, increased apoptosis, reduced levels of phosphorylated extracellular signal-regulated kinase and altered other cell cycle proteins. RPS6KA2 / RSK-3 contains oneAGC-kinase C-terminal domain and twoprotein kinase domains. It forms a complex with either ERK1 or ERK2 in quiescent cells. It transiently dissociates following mitogenic stimulation. RPS6KA2 / RSK-3 is a serine/threonine kinase that may play a role in mediating the growth-factor and stress induced activation of the transcription factor CREB. RPS6KA1, RPS6KA2, RPS6KB1, RPS6KB2, and PDK1 are involved in several pathways central to the carcinogenic process, including regulation of cell growth, insulin, and inflammation.
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