K02945 RP-S1; small subunit ribosomal protein S1 K02967 RP-S2; small subunit ribosomal protein S2 K02982 RP-S3; small subunit ribosomal protein S3 K02986 RP-S4; small subunit ribosomal protein S4 K02988 RP-S5; small subunit ribosomal protein S5 K02990 RP-S6; small subunit ribosomal protein S6 K02992 RP-S7; small subunit ribosomal protein S7 K02994 RP-S8; small subunit ribosomal protein S8 K02996 RP-S9; small subunit ribosomal protein S9 K02946 RP-S10; small subunit ribosomal protein S10 K02948 RP-S11; small subunit ribosomal protein S11 K02950 RP-S12; small subunit ribosomal protein S12 K02952 RP-S13; small subunit ribosomal protein S13 K02954 RP-S14; small subunit ribosomal protein S14 K02956 RP-S15; small subunit ribosomal protein S15 K02959 RP-S16; small subunit ribosomal protein S16 K02961 RP-S17; small subunit ribosomal protein S17 K02963 RP-S18; small subunit ribosomal protein S18 K02965 RP-S19; small subunit ribosomal protein S19 K02968 RP-S20; small subunit ribosomal protein S20 K02970 ...
K02945 RP-S1; small subunit ribosomal protein S1 K02967 RP-S2; small subunit ribosomal protein S2 K02982 RP-S3; small subunit ribosomal protein S3 K02986 RP-S4; small subunit ribosomal protein S4 K02988 RP-S5; small subunit ribosomal protein S5 K02990 RP-S6; small subunit ribosomal protein S6 K02992 RP-S7; small subunit ribosomal protein S7 K02994 RP-S8; small subunit ribosomal protein S8 K02996 RP-S9; small subunit ribosomal protein S9 K02946 RP-S10; small subunit ribosomal protein S10 K02948 RP-S11; small subunit ribosomal protein S11 K02950 RP-S12; small subunit ribosomal protein S12 K02952 RP-S13; small subunit ribosomal protein S13 K02954 RP-S14; small subunit ribosomal protein S14 K02954 RP-S14; small subunit ribosomal protein S14 K02956 RP-S15; small subunit ribosomal protein S15 K02959 RP-S16; small subunit ribosomal protein S16 K02961 RP-S17; small subunit ribosomal protein S17 K02963 RP-S18; small subunit ribosomal protein S18 K02965 RP-S19; small subunit ribosomal protein S19 K02968 ...
16S ribosomal RNA, 30S ribosomal protein S2, 30S ribosomal protein S3, 30S ribosomal protein S4, 30S ribosomal protein S5, 30S ribosomal protein S6, 30S ribosomal protein S7, 30S ribosomal protein S8, 30S ribosomal protein S9, 30S ribosomal protein S10, 30S ribosomal protein S11, 30S ribosomal protein S12, 30S ribosomal protein S13, 30S ribosomal protein S14, 30S ribosomal protein S15, 30S ribosomal protein S16, 30S ribosomal protein S17, 30S ribosomal protein S18, 30S ribosomal protein S19, 30S ribosomal protein S20, 30S ribosomal protein Thx, RNA (5-R(*AP*AP*AP*AP*AP*GP*GP*AP*AP*AP*UP*A*AP*AP*AP*AP*UP*GP*CP*AP*GP*UP*UP*CP*AP*AP*UP*CP*UP*A)-3), tRNA-Gln, tRNA-Met, tRNA-Gln, capreomycin IA, 50S ribosomal protein L27, 50S ribosomal protein L28, 50S ribosomal protein L29, 50S ribosomal protein L30, 50S ribosomal protein L31, 50S ribosomal protein L32, 50S ribosomal protein L33, 50S ribosomal protein L34, 50S ribosomal protein L35, 50S ribosomal protein L36, 23S ribosomal RNA, 5S ribosomal RNA, ...
60S ribosomal protein L36a is a protein that in humans is encoded by the RPL36A gene. Cytoplasmic ribosomes, 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 protein that is a component of the 60S subunit. The protein, which shares sequence similarity with yeast ribosomal protein L44, belongs to the L44E (L36AE) family of ribosomal proteins. Although this gene has been referred to as ribosomal protein L44 (RPL44), its official name is ribosomal protein L36a (RPL36A). This gene and the human gene officially named ribosomal protein L36a-like (RPL36AL) encode nearly identical proteins; however, they are distinct genes. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. GRCh38: Ensembl release 89: ENSG00000241343 - Ensembl, May ...
Human ribosomal protein L7 has been shown to be involved in the control of translation of distinct mRNAs. In this study we report the existence of an RNA carrying sequences that are complementary (antisense) to the entire coding (sense) region of L7 mRNA. L7 antisense transcripts are not polyadenylated and associate with the large subunit of the ribosome. The antisense sequence is encoded by an intronless gene segment distinct from the active copy of the L7 gene. Upon mitogenic stimulation of lymphocytes and monocytes from mice and humans, complex expression patterns of L7 transcripts are observed.
Cytoplasmic ribosomes, 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 protein that is a component of the 60S subunit. The protein, which shares sequence similarity with yeast ribosomal protein L44, belongs to the L44E (L36AE) family of ribosomal proteins. This gene and the human gene officially named ribosomal protein L36a (RPL36A) encode nearly identical proteins; however, they are distinct genes. Although the name of this gene has been referred to as ribosomal protein L36a (RPL36A), its official name is ribosomal protein L36a-like (RPL36AL). As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. [provided by RefSeq, Jul 2008 ...
60S ribosomal protein L29 is a protein that in humans is encoded by the RPL29 gene. 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 cytoplasmic ribosomal protein that is a component of the 60S subunit. The protein belongs to the L29E family of ribosomal proteins. The protein is also a peripheral membrane protein expressed on the cell surface that directly binds heparin. Although this gene was previously reported to map to 3q29-qter, it is believed that it is located at 3p21.3-p21.2. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. RPL29 has been shown to interact with BLMH. GRCh38: Ensembl release 89: ENSG00000162244 - Ensembl, May 2017 "Human PubMed Reference:". Law PT, Tsui SK, Lam WY, Luk SC, Hwang DM, Liew CC, Lee ...
TY - JOUR. T1 - Nuclear and nucleolar localization of Saccharomyces cerevisiae ribosomal proteins S22 and S25. AU - Timmers, A.C.J.. AU - Stuger, R.. AU - Schaap, P.J.. AU - van t Riet, J.. AU - Raue, H.A.. PY - 1999. Y1 - 1999. U2 - 10.1016/s0014-5793(99)00669-9. DO - 10.1016/s0014-5793(99)00669-9. M3 - Article. VL - 452. SP - 335. EP - 340. JO - FEBS Letters. JF - FEBS Letters. SN - 0014-5793. ER - ...
90-kDa Ribosomal Protein S6 Kinases: A family of ribosomal protein S6 kinases that are structurally distinguished from RIBOSOMAL PROTEIN S6 KINASES, 70-KDA by their apparent molecular size and the fact they contain two functional kinase domains. Although considered RIBOSOMAL PROTEIN S6 KINASES, members of this family are activated via the MAP KINASE SIGNALING SYSTEM and have been shown to act on a diverse array of substrates that are involved in cellular regulation such as RIBOSOMAL PROTEIN S6 and CAMP RESPONSE ELEMENT-BINDING PROTEIN.
By differential hybridization, we identified a number of genes in Saccharomyces cerevisiae that are activated by addition of cyclic AMP (cAMP) to cAMP-depleted cells. A majority, but not all, of these genes encode ribosomal proteins. While expression of these genes is also induced by addition of the appropriate nutrient to cells starved for a nitrogen source or for a sulfur source, the pathway for nutrient activation of ribosomal protein gene transcription is distinct from that of cAMP activation: (i) cAMP-mediated transcriptional activation was blocked by prior addition of an inhibitor of protein synthesis whereas nutrient-mediated activation was not, and (ii) cAMP-mediated induction of expression occurred through transcriptional activation whereas nutrient-mediated induction was predominantly a posttranscriptional response. Transcriptional activation of the ribosomal protein gene RPL16A by cAMP is mediated through a upstream activation sequence element consisting of a pair of RAP1 binding ...
The communication reports the cloning, sequencing, and analysis of the RPS3 gene from yeast, which codes for the ribosomal protein YS3. Sequence analyses of a 2.45 kb DNA fragment revealed an open reading frame with the potential to code for a 240 amino-acid long protein. The first 20 amino acids display a 90% identity to a 20 amino-acid long protein sequence of yeast ribosomal protein S3, that was obtained by protein sequencing of purified yeast ribosomal proteins. The promoter region of the RPS3 gene contains several upstream conserved sequence elements (UASrpg, T-rich region) that usually regulate transcription of ribosomal protein genes. Northern blot experiments demonstrate that this ORF is transcribed into an approximately 900 nt long mRNA. The major start site of transcription is located near position -20. The RPS3 gene is a single copy gene in yeast. Its disruption yields non viable haploid spores of Saccharomyces cerevisiae.
canSAR Domains and Structures of Q0TCF6 | rplF | 50S ribosomal protein L6 - Also known as RL6_ECOL5, rplF. This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. Part of the 50S ribosomal subunit.
Ribosomal Protein S23 antibody LS-C268553 is an APC-conjugated rabbit polyclonal antibody to human Ribosomal Protein S23 (RPS23 ). Validated for ELISA and WB.
Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 39S subunit protein. Sequence analysis identified three transcript variants. Pseudogenes corresponding to this gene are found on chromosomes 6p, 10q, and Xp. [provided by RefSeq, Jul 2008 ...
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To measure 40S ribosome biogenesis, we analyzed either nascent ribosomal proteins or ribosomal RNA (rRNA) in the livers of IFN-α-treated mice that were fasted and then refed for 3 hours in the presence of 35S-methionine or inorganic phosphate-32 (32Pi). Staining of ribosomal proteins (Fig. 2C) or rRNA (Fig. 2D) from livers of fS6/CRE+ and fS6/CRE− mice showed no difference in their steady-state levels. In both fS6/CRE+ and fS6/CRE− mice, increased phosphorylation of S6 was detected, as measured by its decreased mobility in both dimensions of electrophoresis (insets, Fig. 2C) (16). However, no newly synthesized35S-labeled 40S ribosomal proteins (Fig. 2C) nor32P-labeled 18S rRNA (Fig. 2D) were detected in livers of fS6/CRE+ mice. In addition, an rRNA species of 34S accumulated in the livers of fS6/CRE+ mice, most likely representing the 34S precursor of 18S rRNA (17). There was no difference in the production of 60S proteins (Fig. 2C) or 28S rRNA (Fig. 2D) in livers of fS6/CRE+ or ...
Protein synthesis is a highly regulated and energy consuming process, during which a large ribonucleoprotein particle called the ribosome, synthesizes new proteins. The eukaryotic ribosome consists of two unequal subunits called: small and large subunits. Both subunits are composed of ribosomal RNA (rRNA) and ribosomal proteins (r-proteins).. Although rRNAs build the matrix of the ribosome and carries out catalysing of the peptide-bond formation between amino acids, r-proteins also appear to play important structural and functional roles. The primary role of r-proteins is to initiate the correct tertiary fold of rRNA and to organize the overall structure of the ribosome.. In this thesis, I focus on two proteins from the large subunit of the eukaryotic ribosome: r-proteins L5 and L15 from bakers yeast S. cerevisiae. Both r-proteins are essential for ribosome function. Their life cycle is primarily associated with rRNA interactions. As a consequence, the proteins show high sequence homology across ...
Ribosomal protein L4 (RPL4) is a large ribosomal subunit protein that is structurally conserved in all kingdoms of life. This protein is a component of the 90S pre-ribosomal particle that initiates ribosomal assembly on the primary (35S) transcript. Here I show that in vivo repression of Rpl4p synthesis in S. cerevisiae results in severe loss of 60S ribosomal subunits and affects progression of the cell cycle. Analysis of rRNA processing suggests that these effects are associated with a block in the processing of the 27SA3 precursor RNA into 5.8S and 25S rRNA as well as a delay in processing of 35S precursor. More surprisingly, depletion of Rpl4p results in a unique bi-budded phenotype, with multiple cell cycle defects mainly affecting mitotic exit. To further characterize the role of RPL4 in cell cycle progression, I isolated temperature-sensitive L4 mutants. To date I have analyzed one of these mutants. Six hours after a temperature shift of this mutant, cells are uniformly arrested in SG2 ...
Ribosomal protein L4 (RPL4) is a large ribosomal subunit protein that is structurally conserved in all kingdoms of life. This protein is a component of the 90S pre-ribosomal particle that initiates ribosomal assembly on the primary (35S) transcript. Here I show that in vivo repression of Rpl4p synthesis in S. cerevisiae results in severe loss of 60S ribosomal subunits and affects progression of the cell cycle. Analysis of rRNA processing suggests that these effects are associated with a block in the processing of the 27SA3 precursor RNA into 5.8S and 25S rRNA as well as a delay in processing of 35S precursor. More surprisingly, depletion of Rpl4p results in a unique bi-budded phenotype, with multiple cell cycle defects mainly affecting mitotic exit. To further characterize the role of RPL4 in cell cycle progression, I isolated temperature-sensitive L4 mutants. To date I have analyzed one of these mutants. Six hours after a temperature shift of this mutant, cells are uniformly arrested in SG2 ...
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. RPS13 encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S15P family of ribosomal proteins. It is located in the cytoplasm. The protein has been shown to bind to the 5.8S rRNA in rat. The gene product of the E. coli ortholog (ribosomal protein S15) functions at early steps in ribosome assembly. This gene is co-transcribed with two U14 small nucleolar RNA genes, which are located in its third and fifth introns. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
BACKGROUND: Genome-wide assays performed in Arabidopsis and other organisms have revealed that the translation status of mRNAs responds dramatically to different environmental stresses and genetic lesions in the translation apparatus. To identify additional features of the global landscape of translational control, we used microarray analysis of polysomal as well as non-polysomal mRNAs to examine the defects in translation in a poly(A) binding protein mutant, pab2 pab8, as well as in a mutant of a large ribosomal subunit protein, rpl24b/shortvalve1. RESULTS: The mutation of RPL24B stimulated the ribosome occupancy of mRNAs for nuclear encoded ribosomal proteins. Detailed analysis yielded new insights into the translational regulon containing the ribosomal protein mRNAs. First, the ribosome occupancy defects in the rpl24b mutant partially overlapped with those in a previously analyzed initiation factor mutant, eif3h. Second, a group of mRNAs with incomplete coding sequences appeared to be uncoupled from
casSAR Dugability of Q02608 | MRPS16 | 37S ribosomal protein S16, mitochondrial - Also known as RT16_YEAST, MRPS16. Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. Component of the mitochondrial small ribosomal subunit (mt-SSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins.
canSAR Cell Line Evidence of Q5SLP8 | rpsF | 30S ribosomal protein S6 - Also known as RS6_THET8, rpsF. Located on the outer edge of the platform on the body of the 30S subunit. Part of the 30S ribosomal subunit. Forms a tight heterodimer with protein S18. May make transient contacts with protein L2 of the 50S subunit during translation.
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Mitochondria have their own transcriptional and translational apparatus, even though they produce only a handful of proteins, therefore most of the proteins are imported from the cytoplasm. Trancription, translation and protein insertion into the membrane are interconnected: translational activators regulating mitochondrial translation are interacting with mitochondrial RNA polymerase via Nam1p and Sls1p proteins (Bryan et al. Genetics 2002), Puf proteins connect cytoplasmic translation and protein import into mitochondria by direct interaction with Tom20 subunit of the TOM protein import channel (Saint-Georges et al. PLoS ONE 2008 ...
Expression of the Saccharomyces cerevisiae mitochondrial gene coding cytochrome c oxidase subunit III is specifically activated at the level of translation by at least three nuclear genes, PET122, PET494 and PET54. We have shown previously that carboxy-terminal deletions of PET122 are allele-specifically suppressed by mutations in an unlinked nuclear gene, termed PET123, that encodes a small subunit ribosomal protein. Here we describe additional pet122 suppressors generated by mutations in a second gene which we show to be the previously identified nuclear gene MRP1. Like PET123, MRP1 encodes a component of the small subunit of mitochondrial ribosomes. Our mrp1 mutations are allele-specific suppressors of carboxyl-terminal truncations of the PET122 protein and do not bypass the requirement for residual function of PET122. None of our mrp1 mutations has an intrinsic phenotype in an otherwise wild-type background. However, some of the mrp1 mutations cause a non-conditional respiratory-defective ...
60S ribosomal protein L10 is a protein belongs to the L10E family of ribosomal proteins. It is located in the cytoplasm. In vitro studies have shown that the chicken protein can bind to c-Jun and can repress c-Jun-mediated transcriptional activation, but these activities have not been demonstrated in vivo. This gene was initially identified as a candidate for a Wilms tumor suppressor gene, but later studies determined that this gene is not involved in the suppression of Wilms tumor. This gene has been referred to as laminin receptor homolog because a chimeric transcript consisting of sequence from this gene and sequence from the laminin receptor gene was isolated; however, it is not believed that this gene encodes a laminin receptor. Transcript variants utilizing alternative polyA signals exist.
Domain combinations containing the Ribosomal protein L1 superfamily in Saccharomyces cerevisiae YJM789. Domain architectures illustrate each occurrence of the Ribosomal protein L1 superfamily.
Domain combinations containing the Ribosomal protein L1 superfamily in Saccharomyces cerevisiae CLIB324. Domain architectures illustrate each occurrence of the Ribosomal protein L1 superfamily.
Mrps17 (untagged) - Mouse mitochondrial ribosomal protein S17 (Mrps17), nuclear gene encoding mitochondrial protein, (10ug), 10 µg.
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Here we report the novel finding that ribosomal protein genes are routinely deleted across human cancers, particularly in concert with TP53 mutation. Such a finding could lead to new possibilities for cancer therapy in TP53‐mutant patients. Previously, mutation of RPGs (without concurrent TP53 mutation) has primarily been associated with rare ribosomopathies, specific tumor subtypes, and cancer development in zebrafish models.. The analyses in this study are based on a large number of samples from primary samples, belonging to a broad range of different cancer types. The results indicate that RPG deletions are enriched among the samples that have concurrent TP53 mutation. This finding is in accordance with previous studies on ribosomopathies (particularly DBA and the 5q‐syndrome) showing that RPG haploinsufficiency leads to activation of the p53 pathway, most likely through the 5S RNP‐MDM2 pathway. One of the current main hypotheses is that the ribosomal assembly intermediate 5S ...
Here we report the novel finding that ribosomal protein genes are routinely deleted across human cancers, particularly in concert with TP53 mutation. Such a finding could lead to new possibilities for cancer therapy in TP53‐mutant patients. Previously, mutation of RPGs (without concurrent TP53 mutation) has primarily been associated with rare ribosomopathies, specific tumor subtypes, and cancer development in zebrafish models.. The analyses in this study are based on a large number of samples from primary samples, belonging to a broad range of different cancer types. The results indicate that RPG deletions are enriched among the samples that have concurrent TP53 mutation. This finding is in accordance with previous studies on ribosomopathies (particularly DBA and the 5q‐syndrome) showing that RPG haploinsufficiency leads to activation of the p53 pathway, most likely through the 5S RNP‐MDM2 pathway. One of the current main hypotheses is that the ribosomal assembly intermediate 5S ...
The assignment of specific ribosomal functions toindividual ribosomal proteins is difficult due to the enormous cooperativity of the ribosome; however, important roles for distinct ribosomal proteins are becoming evident
TY - JOUR. T1 - Determining efficient helical IMRT modulation factor from the MLC leaf-open time distribution on precision treatment planning system. AU - Boyd, Robert. AU - Jeong, Kyoungkeun. AU - Tome, Wolfgang A.. PY - 2019/5/1. Y1 - 2019/5/1. N2 - Purpose: Since the modulation factor (MF) impacts both plan quality and delivery efficiency in tomotherapy Intensity Modulated Radiation Therapy (IMRT) treatment planning, the purpose of this study was to demonstrate a technique in determining an efficient MF from the Multileaf Collimator (MLC) leaf-open time (LOT) distribution of a tomotherapy treatment delivery plan. Methods: Eight clinical plans of varying complexity were optimized with the highest allowed MF on the Accuracy Precision treatment planning system. Using a central limit theorem argument a range of reduced MFs were then determined from the first two moments of the LOT distribution. A step down approach was used to calculate the reduced-MF plans and plan comparison tools available on ...
GT:ID BAD55678.1 GT:GENE rpmJ GT:PRODUCT putative ribosomal protein L36 GT:DATABASE GIB00210CH01 GT:ORG nfar0 GB:ACCESSION GIB00210CH01 GB:LOCATION 928349..928462 GB:FROM 928349 GB:TO 928462 GB:DIRECTION + GB:GENE rpmJ GB:PRODUCT putative ribosomal protein L36 GB:PROTEIN_ID BAD55678.1 LENGTH 37 SQ:AASEQ MKVQPSVKKICEKCKVIRRHGRVMVICDNLRHKQRQG GT:EXON 1,1-37:0, SW:ID RL36_NOCFA SW:DE RecName: Full=50S ribosomal protein L36; SW:GN Name=rpmJ; OrderedLocusNames=NFA_8330; SW:KW Complete proteome; Ribonucleoprotein; Ribosomal protein. SW:EXACT T SW:FUNC + BL:SWS:NREP 1 BL:SWS:REP 1-,37,RL36_NOCFA,1e-18,100.0,37/37, GO:SWS:NREP 2 GO:SWS GO:0030529,GO:ribonucleoprotein complex,Ribonucleoprotein, GO:SWS GO:0005840,GO:ribosome,Ribosomal protein, PROS 11-,36,PS00828,RIBOSOMAL_L36,PDOC00650, BL:PDB:NREP 1 BL:PDB:REP 1-,37,2hgu8,3e-14,78.4,37/37, RP:PDB:NREP 1 RP:PDB:REP 1-,37,3bbo6,5e-07,67.6,37/38, HM:PFM:NREP 1 HM:PFM:REP 1-,37,PF00444,1.5e-22,70.3,37/38,Ribosomal_L36, HM:SCP:REP ...
TY - JOUR. T1 - Ribosomal protein S3. T2 - A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. AU - Yadavilli, Sridevi. AU - Mayo, Lindsey D.. AU - Higgins, Maureen. AU - Lain, Sonia. AU - Hegde, Vijay. AU - Deutsch, Walter A.. PY - 2009/10/2. Y1 - 2009/10/2. N2 - The p53 protein responds to cellular stress and regulates genes involved in cell cycle, apoptosis, and DNA repair. Under normal conditions, p53 levels are kept low through MDM2-mediated ubiquitination and proteosomal degradation. In search for novel proteins that participate in this regulatory loop, we performed an MDM2 peptide pull-down assay and mass spectrometry to screen for potential interacting partners of MDM2. We identified ribosomal protein S3 (RPS3), whose interaction with MDM2, and notably p53, was further established by His and GST pull-down assays, fluorescence resonance energy transfer and an in situ proximity ligation assay. Additionally, in cells exposed to oxidative stress, p53 ...
90 kDa ribosomal protein S6 kinase 1; HU-1; MAP kinase-activated protein kinase 1a; MAPK-activated protein kinase 1a; MAPKAP kinase 1a; MAPKAPK-1a; MAPKAPK1A; RSK; RSK-1; RSK1; S6K-alpha 1; S6K-alpha-1; dJ590P13.1 (ribosomal protein S6 kinase, 90kD, polypeptide 1); p90-RSK 1; p90RSK1; p90S6K; ribosomal S6 kinase 1; ribosomal protein S6 kinase alpha 1; ribosomal protein S6 kinase alpha-1; ribosomal protein S6 kinase, 90kD, polypeptide 1; ribosomal protein S6 kinase, 90kDa, polypeptide ...
BX251410.RPLM Location/Qualifiers FT CDS 178288..178713 FT /transl_table=11 FT /gene="rplM" FT /locus_tag="TW153" FT /product="50S ribosomal protein L13" FT /note="Similar to Escherichia coli 50s ribosomal protein FT L13 RplM or b3231 or z4589 or ecs4104 or stm3345 or sty3525 FT SWALL:RL13_ECOLI (SWALL:P02410) (142 aa) fasta scores: E(): FT 3.8e-25, 54.33% id in 127 aa, and to Streptomyces FT coelicolor 50s ribosomal protein L13 RplM or SCO4734 or FT SC6G4.12 SWALL:RL13_STRCO (SWALL:Q53874) (147 aa) fasta FT scores: E(): 3e-29, 52.94% id in 136 aa. N-terminus FT truncated relative to homologues." FT /protein_id="CAD66833.1" FT /translation="MSSKQWVLVDAKDMVLGRLATQVAVLLRGKHRPTYEPHLDTGDCV FT IVVNAALIRVTSNKHAKKVFYTHSGYPGGLKKRGFSDVFQKSPERVLEKAVKGMLPKNK FT LGRSVFRNLRVYPGQDHPHAAQKPSVYAPTRVAQVLV" MSSKQWVLVD AKDMVLGRLA TQVAVLLRGK HRPTYEPHLD TGDCVIVVNA ALIRVTSNKH 60 AKKVFYTHSG YPGGLKKRGF SDVFQKSPER VLEKAVKGML PKNKLGRSVF RNLRVYPGQD 120 HPHAAQKPSV YAPTRVAQVL V 141 ...
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Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
We sought to characterize the expression patterns of several X-Y gene pairs in a panel of human somatic tissues and testis in order to evaluate the contribution of sex-linked isoforms to the transcriptome of the male germline. Considering testis-specific expression as a strong indication of a function in spermatogenesis, we then focused on a particularly interesting gene family, Ribosomal Protein S4, presenting five protein coding isoforms with diverse expression patterns, RPS4Y2 being only expressed in testis and prostate. Interestingly, the quantification of transcripts in testis biopsies strongly suggests that RPS4Y2 is more highly expressed during spermatogenesis, although this trend should be confirmed in a larger cohort of patients.. Ribosomes are the site of mRNA translation and protein synthesis and comprise an assembly of a few rRNA molecules and a large number of proteins. Although the major biochemical steps in protein synthesis are carried out by the rRNA, ribosomal proteins (RPs) ...
RPL14 - RPL14 (untagged)-Human ribosomal protein L14 (RPL14), transcript variant 2 available for purchase from OriGene - Your Gene Company.
ID RL40_BOVIN Reviewed; 128 AA. AC P63048; O97577; P02248; P02249; P02250; P62990; P80169; Q01235; AC Q24K23; Q28169; Q28170; Q29120; Q3T0V5; Q3ZCE3; Q862C1; Q862F4; AC Q862M4; Q862T5; Q862X8; Q91887; Q91888; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 10-AUG-2010, sequence version 2. DT 08-MAY-2019, entry version 109. DE RecName: Full=Ubiquitin-60S ribosomal protein L40; DE AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; DE Contains: DE RecName: Full=Ubiquitin; DE Contains: DE RecName: Full=60S ribosomal protein L40; DE AltName: Full=CEP52; DE Flags: Precursor; GN Name=UBA52; Synonyms=UBCEP2; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=12658628; DOI=10.1002/mrd.10292; RA Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., RA Takahashi ...
... , AS16 3835, Q2F963; LOC_Osm1g00500.1, Ribosomal protein small subunit 1.
... , AS16 3832, Q2F981; LOC_Osm1g00310.1, Ribosomal protein small subunit 2.
RL22_THETH] This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome. This extension seems to form part of the wall of the exit tunnel (By similarity). Deleting residues 82 to 84 (the equivalent deletion in E.coli renders cells resistant to erythromycin) would probably cause the tip of the hairpin to penetrate into the tunnel. [RS9_THET8] Part of the top of the head of the 30S subunit. The C-terminal region penetrates the head emerging in the P-site where it contacts tRNA.[HAMAP-Rule:MF_00532_B] [RS20_THET8] One of the primary rRNA ...