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0RT12_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMRPS12
Description28s ribosomal protein s12, mitochondrial precursor (s12mt) (mrp-s12) (mt-rps12).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005761 mitochondrial ribosome (TAS)
0003735 structural constituent of ribosome (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
A five-stranded beta-barrel was first noted as a common structure among four proteins binding single-stranded nucleic acids (staphylococcal nuclease andaspartyl-tRNA synthetase) or oligosaccharides (B subunits of enterotoxin and verotoxin-1).nd has been termed the oligonucleotide/oligosaccharide binding motif.r OB fold. five-stranded beta-sheet coiled to form a closed beta-barrel capped by an alpha helix located between the third and fourth strands . Two ribosomal proteins.17 and S1.re members of this class.nd have different variations of the OB fold theme. Comparisons with other OB fold nucleic acid binding proteins suggest somewhat different mechanisms of nucleic acid recognition in each case .This entry differs from Nucleic acid-binding OB-fold in the classification of the fold: both the NAD+-dependent DNA ligases.NA helicase RecG.nd the phage ssDNA-binding protein gp32 are absent from this classification.ut are found in the Nucleic acid-binding OB-fold.
  IPR012340:Nucleic acid-binding, OB-fold, subgroup
Ribosomes are the particles that catalyze mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain.ituated in the P site as peptidyl-tRNA.s then transferred to aminoacyl-tRNA and the new peptidyl-tRNA.xtended by one residue.s translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites . About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits. Many of ribosomal proteins.articularly those of the large subunit.re composed of a globular.urfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilize its structure. Most of the proteins interact with multiple RNA elements.ften from different domains. In the large subunit.bout 1/3 of the 23S rRNA nucleotides are at least in van der Waals contact with protein.nd L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7.hich initiate assembly of the 16S rRNA.re located at junctions of five and four RNA helices.espectively. In this way proteins serve to organize and stabilize the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based.roteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome.any ribosomal proteins have some function outside the ribosome .Ribosomal protein S12 is one of the proteins from the small ribosomal subunit.In Escherichia coli.12 is known to be involved in the translation initiationstep. It is a very basic protein of 120 to 150 amino-acid residues. S12belongs to a family of ribosomal proteins which are grouped on the basis of sequencesimilarities. This protein is known typically as S12 in bacteria.23 in eukaryotes and as either S12 or S23 in the Archaea .Bacterial S12 molecules contain a conserved aspartic acid residue which undergoes a novel post-translational modification.eta-methylthiolation.o form the corresponding 3-methylthioaspartic acid.
  IPR006032:Ribosomal protein S12/S23
Ribosomes are the particles that catalyze mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain.ituated in the P site as peptidyl-tRNA.s then transferred to aminoacyl-tRNA and the new peptidyl-tRNA.xtended by one residue.s translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites . About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits. Many of ribosomal proteins.articularly those of the large subunit.re composed of a globular.urfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilize its structure. Most of the proteins interact with multiple RNA elements.ften from different domains. In the large subunit.bout 1/3 of the 23S rRNA nucleotides are at least in van der Waals contact with protein.nd L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7.hich initiate assembly of the 16S rRNA.re located at junctions of five and four RNA helices.espectively. In this way proteins serve to organize and stabilize the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based.roteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome.any ribosomal proteins have some function outside the ribosome .Ribosomal protein S12 is one of the proteins from the small ribosomal subunit. In Escherichia coli.12 is known to be involved in the translation initiation step. It is a very basic protein of 120 to 150 amino-acid residues. S12 belongs to a family of ribosomal proteins which are grouped on the basis of sequence similarities. This family consists of ribosomal protein S12 of Bacteria.itochondria.nd chloroplasts.
  IPR005679:Ribosomal protein S12, bacterial and chloroplast form
A five-stranded beta-barrel was first noted as a common structure among four proteins binding single-stranded nucleic acids (staphylococcal nuclease andaspartyl-tRNA synthetase) or oligosaccharides (B subunits of enterotoxin and verotoxin-1).nd has been termed the oligonucleotide/oligosaccharide binding motif.r OB fold. five-stranded beta-sheet coiled to form a closed beta-barrel capped by an alpha helix located between the third and fourth strands . Two ribosomal proteins.17 and S1.re members of this class.nd have different variations of the OB fold theme. Comparisons with other OB fold nucleic acid binding proteins suggest somewhat different mechanisms of nucleic acid recognition in each case .There are many nucleic acid-binding proteins that contain domains with this OB-fold structure.ncluding anticodon-binding tRNA synthetases.NA helicases RecG and RuvA.sDNA-binding proteins (BRCA2.DC13.elomere-end binding proteins).hage ssDNA-binding proteins (gp32.p2.5.pV).old shock proteins.NA ligases.NA-capping enzymes.NA replication initiators and RNA polymerase subunit RBP8 .Please be aware that some of the protein hits may be false positives.
  IPR008994:Nucleic acid-binding, OB-fold
IPR012340:NA-bind_OB_sub 
Evalue:-35.9208183288574 
Location:27-138
SequencesProtein: RT12_HUMAN (138 aa)
mRNA: NM_033362 Y11681
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 98 residues, 44113187-44113478Exon2: 24 residues, 44113755-44113823Exon3: 230 residues, 44114812-44115497Exon4: 2 residues, -Jump to RT12_HUMANExon1: 131 residues, 44113433-44113823Exon2: 230 residues, 44114812-44115497Exon3: 2 residues, -Jump to RT12_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3108 43830166-43913010 ~-83K 18756(ACTN4)(+)Loci: 4387 43953451-43955988 ~-3K 18760(LGALS7)(-)Loci: 3109 43971693-43974232 ~-3K 18761(LGALS7)(+)Loci: 4388 44061041-44082201 ~-21K 18769(SIRT2)(-)Loci: 3110 44082454-44091373 ~-9K 18775(NFKBIB)(+)Loci: 4389 44097746-44113376 ~-16K 18777(SARS2)(-)Loci: 3111 44113187-44115497 ~-2K 18779(MRPS12)(+)Loci: 3112 44308259-44361886 ~-54K 18787(PAK4)(+)Loci: 3107 43616179-43770042 ~-154K 18750(RYR1)(+)Link out to UCSC