ROCK (Rho-associated kinase), a family of serine/threonine kinases, is an important downstream target of Rho-GTPase and plays an important role in Rho-mediated signaling. Two isoforms of ROCK have been identified: ROCK1 and ROCK2. ROCK is composed of N-terminal catalytic, coiled-coil, and C-terminal PH (pleckstrin homology) domains. The C-terminus of ROCK negatively regulates its kinase activity. ROCK1 is cleaved by caspase-3 at a conserved DETD1113/G sequence resulting in loss of its C-terminal inhibitory domain. ROCK2 is directly cleaved by granzyme B (grB). Cleavage activates ROCK2 and leads to phosphorylation of myosin light chain (MLC) and inhibition of myosin phosphatase. This phosphorylation may account for the mechanism by which Rho regulates cytokinesis, cell motility, cell membrane blebbing during apoptosis, and smooth muscle contraction.
Ron is a member of the Met protooncogene family of receptor tyrosine kinases, which also includes Stk, c-Met, and c-Sea. The functional Ron is a heterodimer composed of a 40 kDa α chain and a 150 kDa β chain. Ron is initially synthesized in the cells as a single-chain, pro Ron precursor that is cleaved into the two active chains. The α chain is completely extracellular, whereas the β chain traverses the cell membrane and contains the intracellular tyrosine kinase and regulatory elements. Ron mediates multiple signaling cascades that involve cell motility, adhesion, proliferation, and apoptosis.The signaling pathways activated downstream of Ron include the ras/mitogen-activated protein kinase (MAPK), phosphatidyl inositol-3 kinase (PI3K)/Akt, and focal adhesion kinase (FAK) pathways. Ron activation can also significantly increase c-Src activity, a signaling intermediate involved in cell cycle progression, motility, angiogenesis and survival. The function of Ron has been shown to be important for embryological development as well as implicated in the progression and metastasis of tumors.
Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions.,PTM:Phosphorylated in a cell-cycle-dependent manner (from the S phase until mitosis). Phosphorylated by ATR upon DNA damage, which promotes its translocation to nuclear foci. Can be phosphorylated in vitro by PRKDC/DNA-PK in the presence of Ku and DNA, and by CDC2.,subcellular location:Also present in PML nuclear bodies. Redistributes to discrete nuclear foci upon DNA damage.,subunit:Heterotrimer of 70, 32 and 14 kDa chains. The DNA-binding activity may reside exclusively on the 70 kDa subunit. Binds to SERTAD3/RBT1. Interacts with TIPIN.
RPA70 also named as HSSB, REPA1, RF-A, RP-A, p70, is a component of a heterotrimeric complex, composed of 70, 32/30 and 14 kDa subunits, collectively known as RPA. RPA is a single stranded DNA binding protein, whose DNA binding activity is believed to reside entirely in the 70 kDa subunit. The complex is required for almost all aspects of cellular DNA metabolism such as DNA replication, recombination, cell cycle and DNA damage checkpoints, and all major types of DNA repair including nucleotide excision, base excision, mismatch and double-strand break repairs.
This gene encodes the largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The product of this gene contains a carboxy terminal domain composed of heptapeptide repeats that are essential for polymerase activity. These repeats contain serine and threonine residues that are phosphorylated in actively transcribing RNA polymerase. In addition, this subunit, in combination with several other polymerase subunits, forms the DNA binding domain of the polymerase, a groove in which the DNA template is transcribed into RNA.
RPL26L1 is a protein that shares high sequence similarity with ribosomal protein L26.
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