TRNT1

TRNT1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1OU5, 4X4W

Identifiers

Aliases

TRNT1, CCA1, MtCCA, CGI-47, SIFD, tRNA nucleotidyl transferase 1, RPEM

External IDs

OMIM: 612907; MGI: 1917297; HomoloGene: 9333; GeneCards: TRNT1; OMA:TRNT1 - orthologs

Gene location (Human)

Chr.	Chromosome 3 (human)^[1]

Band	3p26.2	Start	3,126,916 bp^[1]
Band	3p26.2	End	3,150,879 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 6 (mouse)^[2]

Band	6\|6 E1	Start	106,746,081 bp^[2]
Band	6\|6 E1	End	106,759,435 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

endothelial cell

secondary oocyte

Achilles tendon

parietal pleura

pancreatic epithelial cell

metanephros

tibia

appendix

sural nerve

bone marrow cells

Top expressed in

spermatocyte

spermatid

secondary oocyte

yolk sac

atrioventricular valve

morula

otic placode

somite

cerebellar cortex

superior frontal gyrus

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

Species

Human

Mouse

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 Mb

Chr 6: 106.75 – 106.76 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000072756 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000013736 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ "Entrez Gene: TRNT1 tRNA nucleotidyl transferase, CCA-adding, 1".
^ 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.

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 t e PDB gallery
1ou5: Crystal structure of human CCA-adding enzyme

Transferases: phosphorus-containing groups (EC 2.7)

2.7.1-2.7.4:
phosphotransferase/kinase
(PO₄)

2.7.1: OH acceptor	Hexo- Gluco- Fructo- Hepatic Galacto- Phosphofructo- 1 Liver Muscle Platelet 2 Riboflavin Shikimate Thymidine ADP-thymidine NAD⁺ Glycerol Pantothenate Mevalonate Pyruvate Deoxycytidine PFP Diacylglycerol Phosphoinositide 3 Class I PI 3 Class II PI 3 Sphingosine Glucose-1,6-bisphosphate synthase
2.7.2: COOH acceptor	Phosphoglycerate Aspartate kinase
2.7.3: N acceptor	Creatine
2.7.4: PO₄ acceptor	Phosphomevalonate Adenylate Nucleoside-diphosphate Uridylate Guanylate Thiamine-diphosphate

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	Template-directed RNA polymerase I II III IV V ssRNAP POLRMT Primase 1 2 PrimPol RNA-dependent RNA polymerase Polyadenylation PAP PNPase

Phosphorolytic
3' to 5' exoribonuclease

Nucleotidyltransferase

Guanylyltransferase

mRNA capping enzyme

Other

2.7.8: miscellaneous

Phosphatidyltransferases	CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase CDP-diacylglycerol—serine O-phosphatidyltransferase CDP-diacylglycerol—inositol 3-phosphatidyltransferase CDP-diacylglycerol—choline O-phosphatidyltransferase
Glycosyl-1-phosphotransferase	N-acetylglucosamine-1-phosphate transferase

2.7.10-2.7.13: protein kinase
(PO₄; protein acceptor)

2.7.10: protein-tyrosine	see tyrosine kinases
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	Protein-histidine pros-kinase Protein-histidine tele-kinase Histidine kinase

This article on a gene on human chromosome 3 is a stub. You can help Wikipedia by expanding it.

This page was last edited on 13 August 2023, at 05:06

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References

Further reading