TGS1

Trimetilguanosina sintasa
Estructuras disponibles
PDB	Buscar ortólogos: PDBe, RCSB
Identificadores
Símbolos	TGS1 (HGNC: 17843) DKFZp762A163; FLJ22995; NCOA6IP; PIMT; PIPMT
Identificadores; externos	OMIM: 606461 ; EBI: TGS1; GeneCards: Gen TGS1; UniProt: TGS1;
Locus	Cr. 8 q12.1
	Referencias: AmiGO / QuickGO
Ortólogos
Humano	Ratón
96764
Q96RS0	n/a
NP_079107	n/a
	[editar datos en Wikidata]

La trimetilguanosina sintasa (TGS1) es una enzima codificada en humanos por el gen TGS1.

Interacciones

La proteína TGS1 ha demostrado ser capaz de interaccionar con:

Significación clínica

Existen 49 enfermedades descritas que coinciden con TGS1

Referencias

1 2 Zhu, Y; Qi C, Cao W Q, Yeldandi A V, Rao M S, Reddy J K (Aug. de 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. (United States) 98 (18): 10380-5. ISSN 0027-8424. PMID 11517327. doi:10.1073/pnas.181347498.
↑ Mouaikel J, Verheggen C, Bertrand E, Tazi J, Bordonne R (mayo de 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. PMID 11983179.
↑ «Entrez Gene: TGS1 trimethylguanosine synthase homolog (S. cerevisiae)».
1 2 3 4 Misra, Parimal; Qi Chao, Yu Songtao, Shah Sejal H, Cao Wen-Qing, Rao M Sambasiva, Thimmapaya Bayar, Zhu Yijun, Reddy Janardan K (mayo. de 2002). «Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation». J. Biol. Chem. (United States) 277 (22): 20011-9. ISSN 0021-9258. PMID 11912212. doi:10.1074/jbc.M201739200.
↑ Enünlü, Izzet; Pápai Gábor, Cserpán Imre, Udvardy Andor, Jeang Kuan-Teh, Boros Imre (Sep. de 2003). «Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localizes to the cytoplasm and nucleus». Biochem. Biophys. Res. Commun. (United States) 309 (1): 44-51. ISSN 0006-291X. PMID 12943661.
↑ «MalaCards». Consultado el 7 de enero de 2026.

Enlaces externos

En HomoloGene: TGS1

En Genome:TGS1
En MalaCards.Enfermedades que coinciden con:TGS1
En Estudio de asociación del genoma completo (GWAS) TGS1

Datos: Q18048839

[pmid11517327-1] 1 2 Zhu, Y; Qi C, Cao W Q, Yeldandi A V, Rao M S, Reddy J K (Aug. de 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. (United States) 98 (18): 10380-5. ISSN 0027-8424. PMID 11517327. doi:10.1073/pnas.181347498.

[pmid11983179-2] Mouaikel J, Verheggen C, Bertrand E, Tazi J, Bordonne R (mayo de 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. PMID 11983179.

[entrez-3] «Entrez Gene: TGS1 trimethylguanosine synthase homolog (S. cerevisiae)».

[pmid11912212-4] 1 2 3 4 Misra, Parimal; Qi Chao, Yu Songtao, Shah Sejal H, Cao Wen-Qing, Rao M Sambasiva, Thimmapaya Bayar, Zhu Yijun, Reddy Janardan K (mayo. de 2002). «Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation». J. Biol. Chem. (United States) 277 (22): 20011-9. ISSN 0021-9258. PMID 11912212. doi:10.1074/jbc.M201739200.

[pmid12943661-5] Enünlü, Izzet; Pápai Gábor, Cserpán Imre, Udvardy Andor, Jeang Kuan-Teh, Boros Imre (Sep. de 2003). «Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localizes to the cytoplasm and nucleus». Biochem. Biophys. Res. Commun. (United States) 309 (1): 44-51. ISSN 0006-291X. PMID 12943661.

[6] «MalaCards». Consultado el 7 de enero de 2026.