| Tag | Content |
|---|
| CPLM ID | CPLM-000878 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | mRNA-capping enzyme |
Protein Synonyms/Alias | HCE; MCE1; Polynucleotide 5'-triphosphatase; TPase; mRNA 5'-triphosphatase; mRNA guanylyltransferase; GTP--RNA guanylyltransferase; GTase |
Gene Name | Rngtt |
Gene Synonyms/Alias | Cap1a |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 28 | AGRFLPLKTMLGPRY | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | 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. |
Sequence Annotation | REGION 1 212 TPase.
REGION 229 597 GTase.
ACT_SITE 126 126 For RNA 5'-triphosphatase activity (By
ACT_SITE 294 294 N6-GMP-lysine intermediate. |
Keyword | 3D-structure; Complete proteome; GTP-binding; Hydrolase; mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; Nucleus; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 597 AA |
Protein Sequence | MAYNKIPPRW LNCPRRGQPV AGRFLPLKTM LGPRYDSQVA EENRFHPSML SNYLKSLKVK 60
MSLLVDLTNT SRFYDRNDIE KEGIKYIKLQ CKGHGECPTT ENTETFIRLC ERFNERSPPE 120
LIGVHCTHGF NRTGFLICAF LVEKMDWSIE AAVATFAQAR PPGIYKGDYL KELFRRYGDI 180
EEAPPPPVLP DWCFEDEDEE DEDEDGKKDS EPGSSASFSK RRKERLKLGA IFLEGITVKG 240
VTQVTTQPKL GEVQQKCHQF CGWEGSGFPG AQPVSMDKQN IRLLEQKPYK VSWKADGTRY 300
MMLIDGTNEV FMIDRDNSVF HVSNLEFPFR KDLRMHLSNT LLDGEMIIDK VNGQAVPRYL 360
IYDIIKFNAQ PVGDCDFNIR LQCIEREIIS PRHEKMKTGL IDKTQEPFSV RPKQFFDINI 420
SRKLLEGNFA KEVSHEMDGL IFQPIGKYKP GRCDDILKWK PPSLNSVDFR LKITRMGGEG 480
LLPQNVGLLY VGGYERPFAQ IKVTKELKQY DNKIIECKFE NNSWVFMRQR IDKSFPNAYN 540
TAMAVCNSIS NPVTKEMLFE FIDRCAAAAQ GQKRKYPLDP DTELMPPPPP KRLHRPT 597 |
Gene Ontology | GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0005525; F:GTP binding; IEA:UniProtKB-KW. GO:0004484; F:mRNA guanylyltransferase activity; IEA:EC. GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:EC. GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro. GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro. GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW. GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |