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Wikipedia

TGS1

December 15, 2023

Trimethylguanosine synthase is an enzyme that in humans is encoded by the TGS1 gene.[5][6][7]

TGS1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesTGS1, NCOA6IP, PIMT, PIPMT, trimethylguanosine synthase 1
External IDsOMIM: 606461 MGI: 2151797 HomoloGene: 32608 GeneCards: TGS1
Orthologs
SpeciesHumanMouse
Entrez

96764

116940

Ensembl

ENSG00000137574

ENSMUSG00000028233

UniProt

Q96RS0

Q923W1

RefSeq (mRNA)

NM_024831
NM_001317902
NM_001363184

NM_054089

RefSeq (protein)

NP_001304831
NP_079107
NP_001350113

NP_473430

Location (UCSC)Chr 8: 55.77 – 55.83 MbChr 4: 3.57 – 3.62 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Interactions edit

TGS1 has been shown to interact with:

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000137574 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028233 - 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. ^ a b Zhu Y, Qi C, Cao WQ, Yeldandi AV, Rao MS, Reddy JK (Aug 2001). "Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function". Proc Natl Acad Sci U S A. 98 (18): 10380–5. Bibcode:2001PNAS...9810380Z. doi:10.1073/pnas.181347498. PMC 56969. PMID 11517327.
  6. ^ Mouaikel J, Verheggen C, Bertrand E, Tazi J, Bordonné R (May 2002). "Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus". Mol Cell. 9 (4): 891–901. doi:10.1016/S1097-2765(02)00484-7. PMID 11983179.
  7. ^ "Entrez Gene: TGS1 trimethylguanosine synthase homolog (S. cerevisiae)".
  8. ^ a b c d Misra P, Qi C, Yu S, Shah SH, Cao WQ, Rao MS, Thimmapaya B, Zhu Y, Reddy JK (May 2002). "Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation". J. Biol. Chem. 277 (22): 20011–9. doi:10.1074/jbc.M201739200. PMID 11912212.
  9. ^ Enünlü I, Pápai G, Cserpán I, Udvardy A, Jeang KT, Boros I (Sep 2003). "Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localizes to the cytoplasm and nucleus". Biochem. Biophys. Res. Commun. 309 (1): 44–51. doi:10.1016/s0006-291x(03)01514-6. PMID 12943661.

Further reading edit

  • Misra P, Qi C, Yu S, Shah SH, Cao WQ, Rao MS, Thimmapaya B, Zhu Y, Reddy JK (2002). "Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation". J. Biol. Chem. 277 (22): 20011–9. doi:10.1074/jbc.M201739200. PMID 11912212.
  • Verheggen C, Lafontaine DL, Samarsky D, Mouaikel J, Blanchard JM, Bordonné R, Bertrand E (2002). "Mammalian and yeast U3 snoRNPs are matured in specific and related nuclear compartments". EMBO J. 21 (11): 2736–45. doi:10.1093/emboj/21.11.2736. PMC 126019. PMID 12032086.
  • Wang Y, Han KJ, Pang XW, Vaughan HA, Qu W, Dong XY, Peng JR, Zhao HT, Rui JA, Leng XS, Cebon J, Burgess AW, Chen WF (2002). "Large scale identification of human hepatocellular carcinoma-associated antigens by autoantibodies". J. Immunol. 169 (2): 1102–9. doi:10.4049/jimmunol.169.2.1102. PMID 12097419.
  • Surapureddi S, Yu S, Bu H, Hashimoto T, Yeldandi AV, Kashireddy P, Cherkaoui-Malki M, Qi C, Zhu YJ, Rao MS, Reddy JK (2002). "Identification of a transcriptionally active peroxisome proliferator-activated receptor α-interacting cofactor complex in rat liver and characterization of PRIC285 as a coactivator". Proc. Natl. Acad. Sci. U.S.A. 99 (18): 11836–41. Bibcode:2002PNAS...9911836S. doi:10.1073/pnas.182426699. PMC 129355. PMID 12189208.
  • Krackhardt AM, Witzens M, Harig S, Hodi FS, Zauls AJ, Chessia M, Barrett P, Gribben JG (2002). "Identification of tumor-associated antigens in chronic lymphocytic leukemia by SEREX". Blood. 100 (6): 2123–31. doi:10.1182/blood-2002-02-0513. PMID 12200376.
  • Mouaikel J, Narayanan U, Verheggen C, Matera AG, Bertrand E, Tazi J, Bordonné R (2004). "Interaction between the small-nuclear-RNA cap hypermethylase and the spinal muscular atrophy protein, survival of motor neuron". EMBO Rep. 4 (6): 616–22. doi:10.1038/sj.embor.embor863. PMC 1319203. PMID 12776181.
  • Enünlü I, Pápai G, Cserpán I, Udvardy A, Jeang KT, Boros I (2003). "Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localizes to the cytoplasm and nucleus". Biochem. Biophys. Res. Commun. 309 (1): 44–51. doi:10.1016/S0006-291X(03)01514-6. PMID 12943661.
  • Watkins NJ, Lemm I, Ingelfinger D, Schneider C, Hossbach M, Urlaub H, Lührmann R (2005). "Assembly and maturation of the U3 snoRNP in the nucleoplasm in a large dynamic multiprotein complex". Mol. Cell. 16 (5): 789–98. doi:10.1016/j.molcel.2004.11.012. hdl:11858/00-001M-0000-0012-EB89-8. PMID 15574333.
  • Oh JH, Yang JO, Hahn Y, Kim MR, Byun SS, Jeon YJ, Kim JM, Song KS, Noh SM, Kim S, Yoo HS, Kim YS, Kim NS (2006). "Transcriptome analysis of human gastric cancer". Mamm. Genome. 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID 16341674. S2CID 69278.


 

This article on a gene on human chromosome 8 is a stub. You can help Wikipedia by expanding it.

December 15, 2023
tgs1, trimethylguanosine, synthase, enzyme, that, humans, encoded, gene, available, structurespdbortholog, search, pdbe, rcsblist, codes3egi, 3gdhidentifiersaliases, ncoa6ip, pimt, pipmt, trimethylguanosine, synthase, 1external, idsomim, 606461, 2151797, homol. Trimethylguanosine synthase is an enzyme that in humans is encoded by the TGS1 gene 5 6 7 TGS1Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes3EGI 3GDHIdentifiersAliasesTGS1 NCOA6IP PIMT PIPMT trimethylguanosine synthase 1External IDsOMIM 606461 MGI 2151797 HomoloGene 32608 GeneCards TGS1Gene location Human Chr Chromosome 8 human 1 Band8q12 1Start55 773 446 bp 1 End55 826 445 bp 1 Gene location Mouse Chr Chromosome 4 mouse 2 Band4 A1 4 1 99 cMStart3 574 875 bp 2 End3 616 619 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inoocytesecondary oocyteAchilles tendonnipplepylorusinternal globus pallidusrenal medullacorpus epididymislactiferous ductcaput epididymisTop expressed incondylecumulus cellureterprimitive streakpineal glandrenal corpusclefossaabdominal wallconjunctival fornixPaneth cellMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionmethyltransferase activity transferase activity RNA trimethylguanosine synthase activity protein binding RNA methyltransferase activityCellular componentcytoplasm Cajal body nucleoplasm nucleolus small nuclear ribonucleoprotein complex nucleus extracellular space cytosolBiological processregulation of transcription DNA templated transcription DNA templated spliceosomal snRNP assembly methylation 7 methylguanosine RNA capping 7 methylguanosine cap hypermethylation ribonucleoprotein complex biogenesis RNA methylation regulation of lipid metabolic processSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez96764116940EnsemblENSG00000137574ENSMUSG00000028233UniProtQ96RS0Q923W1RefSeq mRNA NM 024831NM 001317902NM 001363184NM 054089RefSeq protein NP 001304831NP 079107NP 001350113NP 473430Location UCSC Chr 8 55 77 55 83 MbChr 4 3 57 3 62 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseInteractions editTGS1 has been shown to interact with CREB binding protein 8 and EED 9 EP300 8 MED1 8 and NCOA6 5 8 References edit a b c GRCh38 Ensembl release 89 ENSG00000137574 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000028233 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 a b Zhu Y Qi C Cao WQ Yeldandi AV Rao MS Reddy JK Aug 2001 Cloning and characterization of PIMT a protein with a methyltransferase domain which interacts with and enhances nuclear receptor coactivator PRIP function Proc Natl Acad Sci U S A 98 18 10380 5 Bibcode 2001PNAS 9810380Z doi 10 1073 pnas 181347498 PMC 56969 PMID 11517327 Mouaikel J Verheggen C Bertrand E Tazi J Bordonne R May 2002 Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus Mol Cell 9 4 891 901 doi 10 1016 S1097 2765 02 00484 7 PMID 11983179 Entrez Gene TGS1 trimethylguanosine synthase homolog S cerevisiae a b c d Misra P Qi C Yu S Shah SH Cao WQ Rao MS Thimmapaya B Zhu Y Reddy JK May 2002 Interaction of PIMT with transcriptional coactivators CBP p300 and PBP differential role in transcriptional regulation J Biol Chem 277 22 20011 9 doi 10 1074 jbc M201739200 PMID 11912212 Enunlu I Papai G Cserpan I Udvardy A Jeang KT Boros I Sep 2003 Different isoforms of PRIP interacting protein with methyltransferase domain trimethylguanosine synthase localizes to the cytoplasm and nucleus Biochem Biophys Res Commun 309 1 44 51 doi 10 1016 s0006 291x 03 01514 6 PMID 12943661 Further reading editMisra P Qi C Yu S Shah SH Cao WQ Rao MS Thimmapaya B Zhu Y Reddy JK 2002 Interaction of PIMT with transcriptional coactivators CBP p300 and PBP differential role in transcriptional regulation J Biol Chem 277 22 20011 9 doi 10 1074 jbc M201739200 PMID 11912212 Verheggen C Lafontaine DL Samarsky D Mouaikel J Blanchard JM Bordonne R Bertrand E 2002 Mammalian and yeast U3 snoRNPs are matured in specific and related nuclear compartments EMBO J 21 11 2736 45 doi 10 1093 emboj 21 11 2736 PMC 126019 PMID 12032086 Wang Y Han KJ Pang XW Vaughan HA Qu W Dong XY Peng JR Zhao HT Rui JA Leng XS Cebon J Burgess AW Chen WF 2002 Large scale identification of human hepatocellular carcinoma associated antigens by autoantibodies J Immunol 169 2 1102 9 doi 10 4049 jimmunol 169 2 1102 PMID 12097419 Surapureddi S Yu S Bu H Hashimoto T Yeldandi AV Kashireddy P Cherkaoui Malki M Qi C Zhu YJ Rao MS Reddy JK 2002 Identification of a transcriptionally active peroxisome proliferator activated receptor a interacting cofactor complex in rat liver and characterization of PRIC285 as a coactivator Proc Natl Acad Sci U S A 99 18 11836 41 Bibcode 2002PNAS 9911836S doi 10 1073 pnas 182426699 PMC 129355 PMID 12189208 Krackhardt AM Witzens M Harig S Hodi FS Zauls AJ Chessia M Barrett P Gribben JG 2002 Identification of tumor associated antigens in chronic lymphocytic leukemia by SEREX Blood 100 6 2123 31 doi 10 1182 blood 2002 02 0513 PMID 12200376 Mouaikel J Narayanan U Verheggen C Matera AG Bertrand E Tazi J Bordonne R 2004 Interaction between the small nuclear RNA cap hypermethylase and the spinal muscular atrophy protein survival of motor neuron EMBO Rep 4 6 616 22 doi 10 1038 sj embor embor863 PMC 1319203 PMID 12776181 Enunlu I Papai G Cserpan I Udvardy A Jeang KT Boros I 2003 Different isoforms of PRIP interacting protein with methyltransferase domain trimethylguanosine synthase localizes to the cytoplasm and nucleus Biochem Biophys Res Commun 309 1 44 51 doi 10 1016 S0006 291X 03 01514 6 PMID 12943661 Watkins NJ Lemm I Ingelfinger D Schneider C Hossbach M Urlaub H Luhrmann R 2005 Assembly and maturation of the U3 snoRNP in the nucleoplasm in a large dynamic multiprotein complex Mol Cell 16 5 789 98 doi 10 1016 j molcel 2004 11 012 hdl 11858 00 001M 0000 0012 EB89 8 PMID 15574333 Oh JH Yang JO Hahn Y Kim MR Byun SS Jeon YJ Kim JM Song KS Noh SM Kim S Yoo HS Kim YS Kim NS 2006 Transcriptome analysis of human gastric cancer Mamm Genome 16 12 942 54 doi 10 1007 s00335 005 0075 2 PMID 16341674 S2CID 69278 nbsp This article on a gene on human chromosome 8 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title TGS1 amp oldid 1171080560, wikipedia, wiki, book, books, library,

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