TRNT1

Protein-coding gene in the species Homo sapiens
TRNT1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1OU5, 4X4W

Identifiers
AliasesTRNT1, CCA1, MtCCA, CGI-47, SIFD, tRNA nucleotidyl transferase 1, RPEM
External IDsOMIM: 612907; MGI: 1917297; HomoloGene: 9333; GeneCards: TRNT1; OMA:TRNT1 - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for TRNT1
Genomic location for TRNT1
Band3p26.2Start3,126,916 bp[1]
End3,150,879 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for TRNT1
Genomic location for TRNT1
Band6|6 E1Start106,746,081 bp[2]
End106,759,435 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • endothelial cell

  • secondary oocyte

  • gonad

  • Achilles tendon

  • parietal pleura

  • epithelium of colon

  • pancreatic epithelial cell

  • cartilage tissue

  • metanephros

  • testicle
Top expressed in
  • spermatocyte

  • zygote

  • spermatid

  • genital tubercle

  • secondary oocyte

  • tail of embryo

  • yolk sac

  • ventricular zone

  • embryo

  • atrioventricular valve
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • CTP:3'-cytidine-tRNA cytidylyltransferase activity
  • transferase activity
  • nucleotide binding
  • tRNA binding
  • nucleotidyltransferase activity
  • ATP binding
  • CTP:tRNA cytidylyltransferase activity
  • RNA binding
  • 5'-3' RNA polymerase activity
  • ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity
Cellular component
  • mitochondrial matrix
  • intracellular anatomical structure
  • mitochondrion
  • nucleoplasm
Biological process
  • RNA processing
  • tRNA 3'-terminal CCA addition
  • tRNA processing
  • tRNA 3'-end processing
  • mitochondrial tRNA 3'-end processing
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

51095

70047

Ensembl

ENSG00000072756

ENSMUSG00000013736

UniProt

Q96Q11

Q8K1J6

RefSeq (mRNA)

NM_001302946
NM_016000
NM_182916

NM_001242358
NM_001242360
NM_027296

RefSeq (protein)

NP_001289875
NP_886552
NP_001354250
NP_001354251
NP_001354252

NP_001229287
NP_001229289
NP_081572

Location (UCSC)Chr 3: 3.13 – 3.15 MbChr 6: 106.75 – 106.76 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

tRNA-nucleotidyltransferase 1, is an enzyme that in humans is encoded by the TRNT1 gene.[5][6][7] This enzyme adds the nucleotide sequence CCA to the 3' end of tRNA, using ATP and CTP as substrates. The sequence creates the binding site for an amino acid.[8]


References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000072756 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000013736 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W (Aug 2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics". Genome Res. 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876. PMID 10810093.
  6. ^ Nagaike T, Suzuki T, Tomari Y, Takemoto-Hori C, Negayama F, Watanabe K, Ueda T (Oct 2001). "Identification and characterization of mammalian mitochondrial tRNA nucleotidyltransferases". J Biol Chem. 276 (43): 40041–9. doi:10.1074/jbc.M106202200. PMID 11504732.
  7. ^ "Entrez Gene: TRNT1 tRNA nucleotidyl transferase, CCA-adding, 1".
  8. ^ Lizano E, Scheibe M, Rammelt C, Betat H, Mörl M (May 2008). "A comparative analysis of CCA-adding enzymes from human and E. coli: differences in CCA addition and tRNA 3'-end repair". Biochimie. 90 (5): 762–72. doi:10.1016/j.biochi.2007.12.007. PMID 18226598.

Further reading

  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
  • Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
  • Reichert AS, Thurlow DL, Mörl M (2002). "A eubacterial origin for the human tRNA nucleotidyltransferase?". Biol. Chem. 382 (10): 1431–8. CiteSeerX 10.1.1.657.1235. doi:10.1515/BC.2001.176. PMID 11727826. S2CID 230616.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Augustin MA, Reichert AS, Betat H, et al. (2003). "Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization". J. Mol. Biol. 328 (5): 985–94. doi:10.1016/S0022-2836(03)00381-4. PMID 12729736.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
  • Lizano E, Schuster J, Müller M, et al. (2007). "A splice variant of the human CCA-adding enzyme with modified activity". J. Mol. Biol. 366 (4): 1258–65. doi:10.1016/j.jmb.2006.12.016. PMID 17204286.
  • v
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  • 1ou5: Crystal structure of human CCA-adding enzyme
    1ou5: Crystal structure of human CCA-adding enzyme
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Transferases: phosphorus-containing groups (EC 2.7)
2.7.1-2.7.4:
phosphotransferase/kinase
(PO4)
2.7.1: OH acceptor
2.7.2: COOH acceptor
2.7.3: N acceptor
2.7.4: PO4 acceptor
2.7.6: diphosphotransferase
(P2O7)
2.7.7: nucleotidyltransferase
(PO4-nucleoside)
Polymerase
DNA polymerase
DNA-directed DNA polymerase
I/A
γ
θ
ν
T7
Taq
II/B
α
δ
ε
ζ
Pfu
III/C
IV/X
β
λ
μ
TDT
V/Y
η
ι
κ
RNA-directed DNA polymerase
Reverse transcriptase
Telomerase
RNA polymerase
Phosphorolytic
3' to 5' exoribonuclease
Nucleotidyltransferase
Guanylyltransferase
Other
2.7.8: miscellaneous
Phosphatidyltransferases
Glycosyl-1-phosphotransferase
2.7.10-2.7.13: protein kinase
(PO4; protein acceptor)
2.7.10: protein-tyrosine
2.7.11: protein-serine/threonine
  • see serine/threonine-specific protein kinases
2.7.12: protein-dual-specificity
  • see serine/threonine-specific protein kinases
2.7.13: protein-histidine


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