TGS1

TGS1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3EGI, 3GDH
Identifiers
Aliases	TGS1, NCOA6IP, PIMT, PIPMT, trimethylguanosine synthase 1
External IDs	MGI: 2151797 HomoloGene: 32608 GeneCards: TGS1
Gene location (Human)
Chr.	Chromosome 8 (human)[1]
End	55,825,448 bp[1]
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)[2]
End	3,616,619 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• methyltransferase activity; • transferase activity; • RNA trimethylguanosine synthase activity; • protein binding; • RNA methyltransferase activity;
Cellular component	• cytoplasm; • Cajal body; • nucleoplasm; • nucleolus; • small nuclear ribonucleoprotein complex; • cell nucleus; • extracellular space; • cytosol;
Biological process	• regulation of transcription, DNA-templated; • ribonucleoprotein complex import into nucleus; • transcription, DNA-templated; • spliceosomal snRNP assembly; • methylation; • 7-methylguanosine RNA capping; • 7-methylguanosine cap hypermethylation; • ribonucleoprotein complex biogenesis; • RNA methylation; • regulation of lipid metabolic process;
	Sources:Amigo / QuickGO
Orthologs
	96764
	116940
	ENSG00000137574
	ENSMUSG00000028233
	Q96RS0
	Q923W1
	NM_024831; NM_001317902; NM_001363184
	NM_054089
	NP_001304831; NP_079107; NP_001350113
	NP_473430
	Wikidata
View/Edit Human	View/Edit Mouse

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

Interactions

TGS1 has been shown to interact with:

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000137574 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028233 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 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. doi:10.1073/pnas.181347498. PMC 56969. PMID 11517327.
↑ 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.
↑ "Entrez Gene: TGS1 trimethylguanosine synthase homolog (S. cerevisiae)".
1 2 3 4 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.
↑ 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.

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. 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. 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000137574 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028233 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid11517327-5] 1 2 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. doi:10.1073/pnas.181347498. PMC 56969. PMID 11517327.

[pmid11983179-6] 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.

[entrez-7] "Entrez Gene: TGS1 trimethylguanosine synthase homolog (S. cerevisiae)".

[pmid11912212-8] 1 2 3 4 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.

[pmid12943661-9] 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.

TGS1

Interactions

References

Further reading