| Tag | Content |
|---|
| CPLM ID | CPLM-014061 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 |
Protein Synonyms/Alias | Cap1 2'O-ribose methyltransferase 1; MTr1; FtsJ methyltransferase domain-containing protein 2 |
Gene Name | Ftsjd2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 107 | REGEGLGKYSQGRKD | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1). Cap1 modification is linked to higher levels of translation (By similarity). |
Sequence Annotation | DOMAIN 86 132 G-patch.
DOMAIN 751 785 WW.
REGION 726 834 Interaction with POLR2A (By similarity).
ACT_SITE 403 403 Proton acceptor (By similarity).
BINDING 280 280 S-adenosyl-L-methionine; via amide
BINDING 310 310 S-adenosyl-L-methionine (By similarity).
BINDING 363 363 S-adenosyl-L-methionine (By similarity).
MOD_RES 27 27 Phosphoserine (By similarity).
MOD_RES 30 30 Phosphoserine (By similarity).
MOD_RES 107 107 N6-acetyllysine (By similarity). |
Keyword | Acetylation; Complete proteome; Methyltransferase; mRNA capping; mRNA processing; Nucleus; Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 837 AA |
Protein Sequence | MKRRTDPECT APLKKQKRIG ELARHLSSTS DDEPLSSVSH AAKASTTSLS GSDSETEGKQ 60
PCSDGFKDAF KADSLVEGTS SRYSMYNSVS QKLMAKMGFR EGEGLGKYSQ GRKDIVETSN 120
QKGRRGLGLT LQGFDQELNV DWRDEPEPNA CEQVSWFPEC TTEIPDSREM SDWMVVGKRK 180
MVIEDETEFC GEELLHSMLK CKSVFDILDG EEMRRARTRA NPYEMIRGVF FLNRAAMKMA 240
NMDFVFDRMF TNPLDSSGKP LLKESDIDLL YFADVCAGPG GFSEYVLWRR KWHAKGFGMT 300
LKGPNDFKLE DFYSASSELF EPYYGEGGVD GDGDITRPEN INAFRNFVLD NTDRKGVHFV 360
MADGGFSVEG QENLQEILSK QLLLCQFLMA LSVVRTGGHF VCKTFDLFTP FSVGLIYLLY 420
CCFERVCLFK PVTSRPANSE RYVVCKGLKV GIDDVREYLF SVNIQLNQLR NTDSDVNLVV 480
PLSVIKGDHE FNDYMIRSNE SYCSLQIKAL AKIHAFVQDT TLSEPRQAEI RKECLQLWEI 540
PDRARVAPSP SDPKFKFFEL IKDTDINIFS YKPTLLTAKT LEKIRPVLEY RCMVSGSEQK 600
FLLGLGKSQI YTWDGRQSDR WVKLDLKTEL PRDTLLCVEI VHELKGEGKA QRKISAIHIL 660
DVLVLNGSDV REQHFNQRIQ LAEKFVKAVS KPSRPDMNPI RVKEVYRLEE MEKIFVRLEM 720
KLIKGSGGTP KLSYTGRDDR HFVPTGVYIV RTVTEPWTMA FSKGWKKKFF YNKKTGESFF 780
TLPPESIAPF HTCYYTRLFW EWGDGFHMRD SQKPQDPDKL SKEDVLSFIQ SHNPLGP 837 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:Compara. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; ISS:UniProtKB. GO:0003676; F:nucleic acid binding; IEA:InterPro. GO:0006370; P:7-methylguanosine mRNA capping; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |