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0TTC14_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTTC14
DescriptionTetratricopeptide repeat protein 14 (tpr repeat protein 14).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The tetratrico peptide repeat (TPR) is a structural motif present in a wide range of proteins . It mediates proteinprotein interactions and the assembly of multiprotein complexes . The TPR motif consists of 316 tandem-repeats of 34 amino acids residues.lthough individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms.anging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes.uch as cell cycle regulation.ranscriptional control.itochondrial and peroxisomal protein transport.eurogenesis and protein folding. The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helixturnhelix arrangement.ith adjacent TPR motifs packing in a parallel fashion.esulting in a spiral of repeating anti-parallel alpha-helices . The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24° within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A.nd the other surface presents residues from both helices A and B.
  IPR001440:Tetratricopeptide TPR_1
This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by . See: .
  IPR013105:Tetratricopeptide TPR_2
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 .The S1 domain was originally identified in ribosomal protein S1 but is found in a large number of RNA-associated proteins. The structure of the S1 RNA-binding domain from the Escherichia coli polynucleotide phosphorylase has been determined using NMR methods and consists of a five-stranded antiparallel beta barrel. Conserved residues on one face of the barrel and adjacent loops form the putative RNA-binding site . The structure of the S1 domain is very similar to that of cold shock proteins. This suggests that they may both be derived from an ancient nucleic acid-binding protein .
  IPR003029:RNA binding S1
The tetratrico peptide repeat region (TPR) is a structural motif present in a wide range of proteins . It mediates proteinprotein interactions and the assembly of multiprotein complexes . The TPR motif consists of 316 tandem-repeats of 34 amino acids residues.lthough individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms.anging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes.uch as cell cycle regulation.ranscriptional control.itochondrial and peroxisomal protein transport.eurogenesis and protein folding. The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helixturnhelix arrangement.ith adjacent TPR motifs packing in a parallel fashion.esulting in a spiral of repeating anti-parallel alpha-helices . The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24° within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A.nd the other surface presents residues from both helices A and B.
  IPR013026:Tetratricopeptide region
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
This domain consists of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed superhelix.here the repeats that make up this structure are arranged about a common axis . These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. This topology has been found with a number of repeats and domains.ncluding the tetratricopeptide repeat (TPR) (found in kinesin light chains.NAP regulatory proteins.lathrin heavy chains and bacterial aspartyl-phosphate phosphatases).nd the pentatricopeptide repeat (PPR) (RNA-processing proteins). The TRP is likely to be an ancient repeat.ince it is found in eukaryotes.acteria and archaea.hereas the PPR repeat is found predominantly in higher plants. The superhelix formed from these repeats can bind ligands at a number of different regions.nd has the ability to acquire multiple functional roles .
  IPR011990:Tetratricopeptide-like helical
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
IPR001440:TPR_1 
Evalue:-4.95860719680786 
Location:341-374IPR013105:TPR_2 
Evalue:-3.10790538787842 
Location:307-340IPR001440:TPR_1 
Evalue:-1.13076829910278 
Location:382-415IPR003029:S1 
Evalue:-0.886056647693163 
Location:124-208
SequencesProtein: TTC14_HUMAN (770 aa)
mRNA: NM_133462
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 84 residues, 181802653-181802904Exon2: 43 residues, 181803372-181803497Exon3: 68 residues, 181803605-181803805Exon4: 30 residues, 181804706-181804791Exon5: 45 residues, 181804959-181805089Exon6: 54 residues, 181805333-181805489Exon7: 26 residues, 181806247-181806319Exon8: 42 residues, 181806734-181806854Exon9: 43 residues, 181806962-181807085Exon10: 41 residues, 181808129-181808247Exon11: 38 residues, 181809182-181809292Exon12: 449 residues, 181810111-181811453Exon13: 2 residues, -Jump to TTC14_HUMAN  
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