TGS1
Apariencia
Trimetilguanosina sintasa | ||||
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Estructuras disponibles | ||||
PDB | Buscar ortólogos: PDBe, RCSB | |||
Identificadores | ||||
Símbolos | TGS1 (HGNC: 17843) DKFZp762A163; FLJ22995; NCOA6IP; PIMT; PIPMT | |||
Identificadores externos | ||||
Locus | Cr. 8 q12.1 | |||
Ortólogos | ||||
Especies |
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Entrez |
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UniProt |
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RefSeq (ARNm) |
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La trimetilguanosina sintasa (TGS1) es una enzima codificada en humanos por el gen TGS1.[1][2][3]
Interacciones
[editar]La proteína TGS1 ha demostrado ser capaz de interaccionar con:
Referencias
[editar]- ↑ a b 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)».
- ↑ a b c d 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.