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Collapse Statistics
226 human active and 11 inactive phosphatases in total;
194 phosphatases have substrate data;
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305 protein substrates;
89 non-protein substrates;
1114 dephosphorylation interactions;
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213 KEGG pathways;
206 NCI Nature PID pathways
560 Reactome pathways;
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last update: 18 Feb, 2016

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RNGTT

Gene Name RNGTT (QuickGO)
Structure of phosphatase catalytic domain

PDB ID: 2C46
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SynonymsRNGTT CAP1A
Protein NamemRNA-capping enzyme
Alternative Name(s)
mRNA-capping enzyme (HCAP1) (HCE) [Includes: Polynucleotide 5'-triphosphatase (EC 3.1.3.33) (mRNA 5'-triphosphatase) (TPase); mRNA guanylyltransferase (EC 2.7.7.50) (GTP--RNA guanylyltransferase) (GTase)]
Ensembl Gene IDENSG00000111880
EntrezGene ID8732
UniProt AC (Human)O60942 (protein sequence)
Enzyme ClassEC 3.1.3.33, 2.7.7.50 (BRENDA )
Molecular Weight68557
Protein Length597
Phosphatase activityactive
Protein DomainInterPro | Pfam3D Structure * PDB | PDBe | DrugPort
* ModBase | SwissModel
Structure-based FamilyFamily 1 (CATH: 3.90.190.10)Historical ClassPTPs >> Class I Cys-based PTPs >> VH1-like or dual-specificity phosphatases (DSPs) >> Atypical DSPs
Localization nucleus (PubMed: 9512541, 9790902 | Europe PMC)
Catalytic SiteCatalytic Site Atlas Target by Small MoleculesN/A
Gene ExpressionGene Expression Atlas

The Human Protein Atlas

Function and DiseaseOMIM
Protein-protein Interaction Database STRING | IntAct | MINT
Kinase Database Phospho.ELM | PhosphoSite | NetworKIN
Function (UniProt annotation)
FUNCTION: Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the gmp moiety of GTP to the 5'-diphosphate terminus.
Catalytic Activity (UniProt annotation)
CATALYTIC ACTIVITY: A 5'-phosphopolynucleotide + H(2)O = a polynucleotide + phosphate.; CATALYTIC ACTIVITY: GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.
Protein Sequence
MAHNKIPPRW LNCPRRGQPV AGRFLPLKTM LGPRYDSQVA EENRFHPSML SNYLKSLKVK MGLLVDLTNT SRFYDRNDIE KEGIKYIKLQ CKGHGECPTT ENTETFIRLC ERFNERNPPE LIGVHCTHGF NRTGFLICAF LVEKMDWSIE AAVATFAQAR PPGIYKGDYL KELFRRYGDI EEAPPPPLLP DWCFEDDEDE DEDEDGKKES EPGSSASFGK RRKERLKLGA IFLEGVTVKG VTQVTTQPKL GEVQQKCHQF CGWEGSGFPG AQPVSMDKQN IKLLDLKPYK VSWKADGTRY MMLIDGTNEV FMIDRDNSVF HVSNLEFPFR KDLRMHLSNT LLDGEMIIDR VNGQAVPRYL IYDIIKFNSQ PVGDCDFNVR LQCIEREIIS PRHEKMKTGL IDKTQEPFSV RNKPFFDICT SRKLLEGNFA KEVSHEMDGL IFQPTGKYKP GRCDDILKWK PPSLNSVDFR LKITRMGGEG LLPQNVGLLY VGGYERPFAQ IKVTKELKQY DNKIIECKFE NNSWVFMRQR TDKSFPNAYN TAMAVCNSIS NPVTKEMLFE FIDRCTAASQ GQKRKHHLDP DTELMPPPPP KRPRPLT
ELM motif
N/A
Gene Ontology
GO:0005525GTP binding
GO:0044419interspecies interaction between organisms
GO:0006370mRNA capping
GO:0004484mRNA guanylyltransferase activity
GO:0005654nucleoplasm
GO:0004651polynucleotide 5'-phosphatase activity
GO:0004725protein tyrosine phosphatase activity
GO:0008138protein tyrosine/serine/threonine phosphatase activity
GO:0006366transcription from RNA polymerase II promoter
GO:0016032viral reproduction

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