RNGTT

From Wikipedia, the free encyclopedia

RNA guanylyltransferase and 5'-phosphatase

PDB rendering based on 1i9s.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2C46, 3S24

Identifiers

Symbols

RNGTT; CAP1A; HCE; HCE1; hCAP

External IDs

OMIM: 603512 MGI: 1329041 HomoloGene: 37851 GeneCards: RNGTT Gene

EC number

2.7.7.50, 3.1.3.33

Gene Ontology
Molecular function	• mRNA guanylyltransferase activity • polynucleotide 5'-phosphatase activity • protein tyrosine phosphatase activity • GTP binding • protein tyrosine/serine/threonine phosphatase activity
Cellular component	• nucleus • nucleoplasm
Biological process	• transcription from RNA polymerase II promoter • 7-methylguanosine mRNA capping • RNA processing • gene expression • viral reproduction • virus-host interaction • viral reproductive process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 6:
89.32 – 89.67 Mb

Chr 4:
33.31 – 33.5 Mb

PubMed search

mRNA-capping enzyme is a protein that in humans is encoded by the RNGTT gene.^[1]^[2]^[3]

References

↑ Pillutla RC, Shimamoto A, Furuichi Y, Shatkin AJ (Jan 1999). "Human mRNA capping enzyme (RNGTT) and cap methyltransferase (RNMT) map to 6q16 and 18p11.22-p11.23, respectively". Genomics 54 (2): 351–3. doi:10.1006/geno.1998.5604. PMID 9828141.
↑ Yamada-Okabe T, Doi R, Shimmi O, Arisawa M, Yamada-Okabe H (May 1998). "Isolation and characterization of a human cDNA for mRNA 5'-capping enzyme". Nucleic Acids Res 26 (7): 1700–6. doi:10.1093/nar/26.7.1700. PMC 147440. PMID 9512541.
↑ "Entrez Gene: RNGTT RNA guanylyltransferase and 5'-phosphatase".

Yue Z, Maldonado E, Pillutla R et al. (1998). "Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II". Proc. Natl. Acad. Sci. U.S.A. 94 (24): 12898–903. doi:10.1073/pnas.94.24.12898. PMC 24235. PMID 9371772.
Tsukamoto T, Shibagaki Y, Murakoshi T et al. (1998). "Cloning and characterization of two human cDNAs encoding the mRNA capping enzyme". Biochem. Biophys. Res. Commun. 243 (1): 101–8. doi:10.1006/bbrc.1997.8038. PMID 9473487.
Pillutla RC, Yue Z, Maldonado E, Shatkin AJ (1998). "Recombinant human mRNA cap methyltransferase binds capping enzyme/RNA polymerase IIo complexes". J. Biol. Chem. 273 (34): 21443–6. doi:10.1074/jbc.273.34.21443. PMID 9705270.
Wen Y, Shatkin AJ (1999). "Transcription elongation factor hSPT5 stimulates mRNA capping". Genes Dev. 13 (14): 1774–9. doi:10.1101/gad.13.14.1774. PMC 316881. PMID 10421630.
Chiu YL, Coronel E, Ho CK et al. (2001). "HIV-1 Tat protein interacts with mammalian capping enzyme and stimulates capping of TAR RNA". J. Biol. Chem. 276 (16): 12959–66. doi:10.1074/jbc.M007901200. PMID 11278368.
Chiu YL, Ho CK, Saha N et al. (2002). "Tat stimulates cotranscriptional capping of HIV mRNA". Mol. Cell 10 (3): 585–97. doi:10.1016/S1097-2765(02)00630-5. PMID 12408826.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Zhou M, Deng L, Kashanchi F et al. (2004). "The Tat/TAR-dependent phosphorylation of RNA polymerase II C-terminal domain stimulates cotranscriptional capping of HIV-1 mRNA". Proc. Natl. Acad. Sci. U.S.A. 100 (22): 12666–71. doi:10.1073/pnas.1835726100. PMC 240675. PMID 14569024.
Suzuki Y, Yamashita R, Shirota M et al. (2004). "Sequence Comparison of Human and Mouse Genes Reveals a Homologous Block Structure in the Promoter Regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
Olsen JV, Blagoev B, Gnad F et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.

PDB gallery

1i9s: CRYSTAL STRUCTURE OF THE RNA TRIPHOSPHATASE DOMAIN OF MOUSE MRNA CAPPING ENZYME

1i9t: CRYSTAL STRUCTURE OF THE OXIDIZED RNA TRIPHOSPHATASE DOMAIN OF MOUSE MRNA CAPPING ENZYME

2c46: CRYSTAL STRUCTURE OF THE HUMAN RNA GUANYLYLTRANSFERASE AND 5'-PHOSPHATASE

Esterase: protein tyrosine phosphatases (EC 3.1.3.48)

Class I

Classical PTPs	Receptor type PTPs PTPRA PTPRB PTPRC PTPRD PTPRE PTPRF PTPRG PTPRH PTPRJ PTPRK PTPRM PTPRN PTPRN2 PTPRO PTPRQ PTPRR PTPRS PTPRT PTPRU PTPRZ1 PTPRZ2 Non receptor type PTPs PTPN1 PTPN2 PTPN3 PTPN4 PTPN5 PTPN6 PTPN7 PTPN9 PTPN11 PTPN12 PTPN13 PTPN14 PTPN18 PTPN20 PTPN21 PTPN22 PTPN23

VH1-like or dual specific phosphatases (DSPs)	MAPK phosphatases (MKPs) DUSP1 DUSP2 DUSP4 DUSP5 DUSP6 DUSP7 DUSP8 DUSP9 DUSP10 DUSP16 MK-STYX Slingshots SSH1 SSH2 SSH3 PRLs PTP4A1 PTP4A2 PTP4A3 CDC14s CDC14A CDC14B CDKN3 PTP9Q22 Atypical DSPs DUSP3 DUSP11 DUSP12 DUSP13A DUSP13B DUSP14 DUSP15 DUSP18 DUSP19 DUSP21 DUSP22 DUSP23 DUSP24 DUSP25 DUSP26 DUSP27 EMP2A RNGTT STYX Phosphatase and tensin homologs (PTENs) PTEN TPIP TPTE TNS TENC1 Myotubularins MTM1 MTMR2 MTMR3 MTMR4 MTMR5 MTMR6 MTMR7 MTMR8 MTMR9 MTMR10 MTMR11 MTMR12 MTMR13 MTMR14 MTMR15

Class II

ACP1

Class III

Cdc25
- CDC25A
- CDC25B
- CDC25C

Class IV

Eyes absent homolog
- EYA1
- EYA2
- EYA3
- EYA4

B
enzm
1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
2.1
- 2
- 3
- 4
- 5
- 6
- 7
  - 2.7.10
  - 11-12
- 8
3.1
- - 3.1.3.48
- 2
- 3
- 4
  - 3.4.21
  - 22
  - 23
  - 24
- 5
- 6
- 7
4.1
- 2
- 3
- 4
- 5
- 6
5.1
- 2
- 3
- 4
- 99
6.1-3
- 4
- 5-6

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RNGTT

References

Further reading