TRDMT1: Difference between revisions

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'''tRNA (cytosine-5-)-methyltransferase''' is an [[enzyme]] that in humans is encoded by the ''TRDMT1'' [[gene]].<ref name="pmid9425235">{{cite journal | vauthors = Yoder JA, Bestor TH | title = A candidate mammalian DNA methyltransferase related to pmt1p of fission yeast | journal = Hum Mol Genet | volume = 7 | issue = 2 | pages = 279–84 |date=Mar 1998 | pmid = 9425235 | pmc =  | doi =10.1093/hmg/7.2.279 }}</ref><ref name="pmid9763678">{{cite journal | vauthors = Vilain A, Apiou F, Dutrillaux B, Malfoy B | title = Assignment of candidate DNA methyltransferase gene (DNMT2) to human chromosome band 10p15.1 by in situ hybridization | journal = Cytogenet Cell Genet | volume = 82 | issue = 1–2 | pages = 120 |date=Nov 1998 | pmid = 9763678 | pmc = | doi =10.1159/000015083  }}</ref><ref name="pmid16424344">{{cite journal | vauthors = Goll MG, Kirpekar F, Maggert KA, Yoder JA, Hsieh CL, Zhang X, Golic KG, Jacobsen SE, Bestor TH | title = Methylation of tRNAAsp by the DNA methyltransferase homolog Dnmt2 | journal = Science | volume = 311 | issue = 5759 | pages = 395–8 |date=Jan 2006 | pmid = 16424344 | pmc =  | doi = 10.1126/science.1120976 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TRDMT1 tRNA aspartic acid methyltransferase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1787| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = TRNA aspartic acid methyltransferase 1
| HGNCid = 2977
| Symbol = TRDMT1
| AltSymbols =; DNMT2; M.HsaIIP; PuMet; RNMT1
| OMIM = 602478
| ECnumber =
| Homologene = 3249
| MGIid = 1274787
  | GeneAtlas_image1 = PBB_GE_TRDMT1_206308_at_tn.png
  | Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0003886 |text = DNA (cytosine-5-)-methyltransferase activity}} {{GNF_GO|id=GO:0008168 |text = methyltransferase activity}} {{GNF_GO|id=GO:0016428 |text = tRNA (cytosine-5-)-methyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}  
| Process = {{GNF_GO|id=GO:0006306 |text = DNA methylation}} {{GNF_GO|id=GO:0008033 |text = tRNA processing}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1787
    | Hs_Ensembl = ENSG00000107614
    | Hs_RefseqProtein = NP_004403
    | Hs_RefseqmRNA = NM_004412
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 17224851
    | Hs_GenLoc_end = 17283665
    | Hs_Uniprot = O14717
    | Mm_EntrezGene = 13434
    | Mm_Ensembl = ENSMUSG00000026723
    | Mm_RefseqmRNA = NM_010067
    | Mm_RefseqProtein = NP_034197
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 13428017
    | Mm_GenLoc_end = 13462517
    | Mm_Uniprot = Q5I0V6
  }}
}}
'''TRNA aspartic acid methyltransferase 1''', also known as '''TRDMT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TRDMT1 tRNA aspartic acid methyltransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1787| accessdate = }}</ref>


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| section_title =  
| section_title =  
| summary_text = CpG methylation is an epigenetic modification that is important for embryonic development, imprinting, and X-chromosome inactivation. Studies in mice have demonstrated that DNA methylation is required for mammalian development. This gene encodes a protein with similarity to DNA methyltransferases, but this protein does not display methyltransferase activity. The protein strongly binds DNA, suggesting that it may mark specific sequences in the genome. Alternative splicing results in multiple transcript variants encoding different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: TRDMT1 tRNA aspartic acid methyltransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1787| accessdate = }}</ref>
| summary_text = CpG methylation is an epigenetic modification that is important for embryonic development, imprinting, and X-chromosome inactivation. Studies in mice have demonstrated that DNA methylation is required for mammalian development. This gene encodes a protein with similarity to DNA methyltransferases, but this protein does not display methyltransferase activity. The protein strongly binds DNA, suggesting that it may mark specific sequences in the genome. Alternative splicing results in multiple transcript variants encoding different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: TRDMT1 tRNA aspartic acid methyltransferase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1787| accessdate = }}</ref>
}}
}}
It has been shown that human DNMT2 does not methylate DNA but instead methylates cytosine 38 in the anticodon loop of aspartic acid transfer RNA ([[tRNA|tRNA(Asp)]]).<ref>{{cite journal  |vauthors=Goll MG, Kirpekar F, Maggert KA, etal |title=Methylation of tRNAAsp by the DNA methyltransferase homolog Dnmt2 |journal=Science |volume=311 |issue= 5759 |pages= 395–8 |year= 2006 |pmid= 16424344 |doi= 10.1126/science.1120976 }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Yoder JA, Bestor TH |title=A candidate mammalian DNA methyltransferase related to pmt1p of fission yeast. |journal=Hum. Mol. Genet. |volume=7 |issue= 2 |pages= 279-84 |year= 1998 |pmid= 9425235 |doi=  }}
*{{cite journal  | vauthors=Okano M, Xie S, Li E |title=Dnmt2 is not required for de novo and maintenance methylation of viral DNA in embryonic stem cells |journal=Nucleic Acids Res. |volume=26 |issue= 11 |pages= 2536–40 |year= 1998 |pmid= 9592134 |doi=10.1093/nar/26.11.2536  | pmc=147598 }}
*{{cite journal  | author=Okano M, Xie S, Li E |title=Dnmt2 is not required for de novo and maintenance methylation of viral DNA in embryonic stem cells. |journal=Nucleic Acids Res. |volume=26 |issue= 11 |pages= 2536-40 |year= 1998 |pmid= 9592134 |doi=  }}
*{{cite journal  | vauthors=Van den Wyngaert I, Sprengel J, Kass SU, Luyten WH |title=Cloning and analysis of a novel human putative DNA methyltransferase |journal=FEBS Lett. |volume=426 |issue= 2 |pages= 283–9 |year= 1998 |pmid= 9599025 |doi=10.1016/S0014-5793(98)00362-7 }}
*{{cite journal  | author=Van den Wyngaert I, Sprengel J, Kass SU, Luyten WH |title=Cloning and analysis of a novel human putative DNA methyltransferase. |journal=FEBS Lett. |volume=426 |issue= 2 |pages= 283-9 |year= 1998 |pmid= 9599025 |doi= }}
*{{cite journal   |vauthors=Dong A, Yoder JA, Zhang X, etal |title=Structure of human DNMT2, an enigmatic DNA methyltransferase homolog that displays denaturant-resistant binding to DNA |journal=Nucleic Acids Res. |volume=29 |issue= 2 |pages= 439–48 |year= 2001 |pmid= 11139614 |doi=10.1093/nar/29.2.439  | pmc=29660 }}
*{{cite journal  | author=Vilain A, Apiou F, Dutrillaux B, Malfoy B |title=Assignment of candidate DNA methyltransferase gene (DNMT2) to human chromosome band 10p15.1 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=82 |issue= 1-2 |pages= 120 |year= 1998 |pmid= 9763678 |doi= }}
*{{cite journal  | vauthors=Franchina M, Hooper J, Kay PH |title=Five novel alternatively spliced transcripts of DNA (cytosine-5) methyltransferase 2 in human peripheral blood leukocytes |journal=Int. J. Biochem. Cell Biol. |volume=33 |issue= 11 |pages= 1104–15 |year= 2001 |pmid= 11551826 |doi=10.1016/S1357-2725(01)00074-7 }}
*{{cite journal | author=Dong A, Yoder JA, Zhang X, ''et al.'' |title=Structure of human DNMT2, an enigmatic DNA methyltransferase homolog that displays denaturant-resistant binding to DNA. |journal=Nucleic Acids Res. |volume=29 |issue= 2 |pages= 439-48 |year= 2001 |pmid= 11139614 |doi=  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal  | author=Franchina M, Hooper J, Kay PH |title=Five novel alternatively spliced transcripts of DNA (cytosine-5) methyltransferase 2 in human peripheral blood leukocytes. |journal=Int. J. Biochem. Cell Biol. |volume=33 |issue= 11 |pages= 1104-15 |year= 2001 |pmid= 11551826 |doi=  }}
*{{cite journal  | vauthors=Hermann A, Schmitt S, Jeltsch A |title=The human Dnmt2 has residual DNA-(cytosine-C5) methyltransferase activity |journal=J. Biol. Chem. |volume=278 |issue= 34 |pages= 31717–21 |year= 2003 |pmid= 12794065 |doi= 10.1074/jbc.M305448200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Deloukas P, Earthrowl ME, Grafham DV, etal |title=The DNA sequence and comparative analysis of human chromosome 10 |journal=Nature |volume=429 |issue= 6990 |pages= 375–81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462 }}
*{{cite journal  | author=Hermann A, Schmitt S, Jeltsch A |title=The human Dnmt2 has residual DNA-(cytosine-C5) methyltransferase activity. |journal=J. Biol. Chem. |volume=278 |issue= 34 |pages= 31717-21 |year= 2003 |pmid= 12794065 |doi= 10.1074/jbc.M305448200 }}
*{{cite journal   |vauthors=Xiong Y, Dowdy SC, Xue A, etal |title=Opposite alterations of DNA methyltransferase gene expression in endometrioid and serous endometrial cancers |journal=Gynecol. Oncol. |volume=96 |issue= 3 |pages= 601–9 |year= 2005 |pmid= 15721400 |doi= 10.1016/j.ygyno.2004.11.047 }}
*{{cite journal | author=Deloukas P, Earthrowl ME, Grafham DV, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 10. |journal=Nature |volume=429 |issue= 6990 |pages= 375-81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462 }}
*{{cite journal   |vauthors=Stelzl U, Worm U, Lalowski M, etal |title=A human protein-protein interaction network: a resource for annotating the proteome |journal=Cell |volume=122 |issue= 6 |pages= 957–68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 }}
*{{cite journal | author=Xiong Y, Dowdy SC, Xue A, ''et al.'' |title=Opposite alterations of DNA methyltransferase gene expression in endometrioid and serous endometrial cancers. |journal=Gynecol. Oncol. |volume=96 |issue= 3 |pages= 601-9 |year= 2005 |pmid= 15721400 |doi= 10.1016/j.ygyno.2004.11.047 }}
*{{cite journal   |vauthors=Pang ST, Weng WH, Flores-Morales A, etal |title=Cytogenetic and expression profiles associated with transformation to androgen-resistant prostate cancer |journal=Prostate |volume=66 |issue= 2 |pages= 157–72 |year= 2006 |pmid= 16173030 |doi= 10.1002/pros.20328 }}
*{{cite journal | author=Stelzl U, Worm U, Lalowski M, ''et al.'' |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957-68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 }}
*{{cite journal | author=Pang ST, Weng WH, Flores-Morales A, ''et al.'' |title=Cytogenetic and expression profiles associated with transformation to androgen-resistant prostate cancer. |journal=Prostate |volume=66 |issue= 2 |pages= 157-72 |year= 2006 |pmid= 16173030 |doi= 10.1002/pros.20328 }}
*{{cite journal  | author=Goll MG, Kirpekar F, Maggert KA, ''et al.'' |title=Methylation of tRNAAsp by the DNA methyltransferase homolog Dnmt2. |journal=Science |volume=311 |issue= 5759 |pages= 395-8 |year= 2006 |pmid= 16424344 |doi= 10.1126/science.1120976 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 12:15, 15 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

tRNA (cytosine-5-)-methyltransferase is an enzyme that in humans is encoded by the TRDMT1 gene.[1][2][3][4]

CpG methylation is an epigenetic modification that is important for embryonic development, imprinting, and X-chromosome inactivation. Studies in mice have demonstrated that DNA methylation is required for mammalian development. This gene encodes a protein with similarity to DNA methyltransferases, but this protein does not display methyltransferase activity. The protein strongly binds DNA, suggesting that it may mark specific sequences in the genome. Alternative splicing results in multiple transcript variants encoding different isoforms.[4]

It has been shown that human DNMT2 does not methylate DNA but instead methylates cytosine 38 in the anticodon loop of aspartic acid transfer RNA (tRNA(Asp)).[5]

References

  1. Yoder JA, Bestor TH (Mar 1998). "A candidate mammalian DNA methyltransferase related to pmt1p of fission yeast". Hum Mol Genet. 7 (2): 279–84. doi:10.1093/hmg/7.2.279. PMID 9425235.
  2. Vilain A, Apiou F, Dutrillaux B, Malfoy B (Nov 1998). "Assignment of candidate DNA methyltransferase gene (DNMT2) to human chromosome band 10p15.1 by in situ hybridization". Cytogenet Cell Genet. 82 (1–2): 120. doi:10.1159/000015083. PMID 9763678.
  3. Goll MG, Kirpekar F, Maggert KA, Yoder JA, Hsieh CL, Zhang X, Golic KG, Jacobsen SE, Bestor TH (Jan 2006). "Methylation of tRNAAsp by the DNA methyltransferase homolog Dnmt2". Science. 311 (5759): 395–8. doi:10.1126/science.1120976. PMID 16424344.
  4. 4.0 4.1 "Entrez Gene: TRDMT1 tRNA aspartic acid methyltransferase 1".
  5. Goll MG, Kirpekar F, Maggert KA, et al. (2006). "Methylation of tRNAAsp by the DNA methyltransferase homolog Dnmt2". Science. 311 (5759): 395–8. doi:10.1126/science.1120976. PMID 16424344.

Further reading