Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as a RNA ligase with broad substrate specificity, and may function toward other RNAs.
Splicing of mammalian precursor transfer RNA (tRNA) molecules involves two enzymatic steps. First, intron removal by the tRNA splicing endonuclease generates separate 5' and 3' exons. In animals, the second step predominantly entails direct exon ligation by an elusive RNA ligase. Using activity-guided purification of tRNA ligase from HeLa cell extracts, we identified HSPC117, a member of the UPF0027 (RtcB) family, as the essential subunit of a tRNA ligase complex. RNA interference-mediated depletion of HSPC117 inhibited maturation of intron-containing pre-tRNA both in vitro and in living cells. The high sequence conservation of HSPC117/RtcB proteins is suggestive of RNA ligase roles of this protein family in various organisms.
Splicing of mammalian precursor transfer RNA (tRNA) molecules involves two enzymatic steps. First, intron removal by the tRNA splicing endonuclease generates separate 5' and 3' exons. In animals, the second step predominantly entails direct exon ligation by an elusive RNA ligase. Using activity-guided purification of tRNA ligase from HeLa cell extracts, we identified HSPC117, a member of the UPF0027 (RtcB) family, as the essential subunit of a tRNA ligase complex. RNA interference-mediated depletion of HSPC117 inhibited maturation of intron-containing pre-tRNA both in vitro and in living cells. The high sequence conservation of HSPC117/RtcB proteins is suggestive of RNA ligase roles of this protein family in various organisms.
Interacting selectively and non-covalently with vinculin, a protein found in muscle, fibroblasts, and epithelial cells that binds actin and appears to mediate attachment of actin filaments to integral proteins of the plasma membrane.
Evidence
1:
Inferred from Physical InteractionUniProtKB
Focal adhesions are specialized attachment and signaling centers that form at sites of cell-matrix contacts. We employed a quantitative mass spectrometry-based method called SILAC to identify and quantify proteins interacting in an attachment-dependent manner with focal adhesion proteins. Subsequent confocal microscopy revealed a previously undescribed structure, which we have termed a spreading initiation center (SIC), existing only in early stages of cell spreading. SICs contain focal adhesion markers, appear to be surrounded by an actin sheath, and, surprisingly, contain numerous RNA binding proteins, ribosomal RNA, and perhaps other RNAs. Interfering with the function of FUS/TLS, hnRNP K, and hnRNP E1 results in increased spreading. Spreading initiation centers are ribonucleoprotein complexes distinct from focal adhesions and demonstrate a role for RNA and RNA binding proteins in the initiation of cell spreading.
Focal adhesions are specialized attachment and signaling centers that form at sites of cell-matrix contacts. We employed a quantitative mass spectrometry-based method called SILAC to identify and quantify proteins interacting in an attachment-dependent manner with focal adhesion proteins. Subsequent confocal microscopy revealed a previously undescribed structure, which we have termed a spreading initiation center (SIC), existing only in early stages of cell spreading. SICs contain focal adhesion markers, appear to be surrounded by an actin sheath, and, surprisingly, contain numerous RNA binding proteins, ribosomal RNA, and perhaps other RNAs. Interfering with the function of FUS/TLS, hnRNP K, and hnRNP E1 results in increased spreading. Spreading initiation centers are ribonucleoprotein complexes distinct from focal adhesions and demonstrate a role for RNA and RNA binding proteins in the initiation of cell spreading.
The process whose specific outcome is the progression of the embryo in the uterus over time, from formation of the zygote in the oviduct, to birth. An example of this process is found in Mus musculus.
The process whose specific outcome is the progression of the placenta over time, from its formation to the mature structure. The placenta is an organ of metabolic interchange between fetus and mother, partly of embryonic origin and partly of maternal origin.
Focal adhesions are specialized attachment and signaling centers that form at sites of cell-matrix contacts. We employed a quantitative mass spectrometry-based method called SILAC to identify and quantify proteins interacting in an attachment-dependent manner with focal adhesion proteins. Subsequent confocal microscopy revealed a previously undescribed structure, which we have termed a spreading initiation center (SIC), existing only in early stages of cell spreading. SICs contain focal adhesion markers, appear to be surrounded by an actin sheath, and, surprisingly, contain numerous RNA binding proteins, ribosomal RNA, and perhaps other RNAs. Interfering with the function of FUS/TLS, hnRNP K, and hnRNP E1 results in increased spreading. Spreading initiation centers are ribonucleoprotein complexes distinct from focal adhesions and demonstrate a role for RNA and RNA binding proteins in the initiation of cell spreading.
Splicing of tRNA substrates via recognition of the folded RNA structure that brings the 5' and 3' splice sites into proximity and cleavage of the RNA at both the 3' and 5' splice sites by an endonucleolytic mechanism, followed by ligation of the exons.
Splicing of mammalian precursor transfer RNA (tRNA) molecules involves two enzymatic steps. First, intron removal by the tRNA splicing endonuclease generates separate 5' and 3' exons. In animals, the second step predominantly entails direct exon ligation by an elusive RNA ligase. Using activity-guided purification of tRNA ligase from HeLa cell extracts, we identified HSPC117, a member of the UPF0027 (RtcB) family, as the essential subunit of a tRNA ligase complex. RNA interference-mediated depletion of HSPC117 inhibited maturation of intron-containing pre-tRNA both in vitro and in living cells. The high sequence conservation of HSPC117/RtcB proteins is suggestive of RNA ligase roles of this protein family in various organisms.
Splicing of mammalian precursor transfer RNA (tRNA) molecules involves two enzymatic steps. First, intron removal by the tRNA splicing endonuclease generates separate 5' and 3' exons. In animals, the second step predominantly entails direct exon ligation by an elusive RNA ligase. Using activity-guided purification of tRNA ligase from HeLa cell extracts, we identified HSPC117, a member of the UPF0027 (RtcB) family, as the essential subunit of a tRNA ligase complex. RNA interference-mediated depletion of HSPC117 inhibited maturation of intron-containing pre-tRNA both in vitro and in living cells. The high sequence conservation of HSPC117/RtcB proteins is suggestive of RNA ligase roles of this protein family in various organisms.
Protein involved in the processing of the primary tRNA transcript to yield a functional tRNA. Transcription of tRNA genes results in a large precursor molecule which may even contain sequences for several tRNA molecules. This primary transcript is subsequently processed by cleavage and by modification of the appropriate bases.
Enzyme that catalyzes the joining of two molecules coupled with the breakdown of a pyrophosphate bond in ATP or a similar triphosphate. Sometimes the terms "synthase", "synthetase" or "carboxylase" are also used for this class of enzymes.
A reference proteome is a set of protein sequences derived from a complete proteome which constitutes a defined standard for a particular user community. Reference proteomes are manually defined according to a number of criteria. They cover the proteomes of well- studied model organisms and other proteomes of interest for biomedical and biotechnological research. Reference proteomes have been selected to provide broad coverage of the tree of life, and constitute a representative cross-section of the taxonomic diversity to be found within UniProtKB.
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