CMTR2
entrez
55783
canonical
uniprot
Q8IYT2
canonical
ensembl
ENSG00000180917
resolver
ensembl
ENSG00000292378
resolver
ensp
ENSP00000337512
resolver
ensp
ENSP00000411148
resolver
ensp
ENSP00000518716
resolver
ensp
ENSP00000518717
resolver
ensp
ENSP00000518718
resolver
ensp
ENSP00000518719
resolver
ensp
ENSP00000564182
resolver
ensp
ENSP00000564183
resolver
ensp
ENSP00000564184
resolver
ensp
ENSP00000599185
resolver
ensp
ENSP00000599186
resolver
ensp
ENSP00000635646
resolver
ensp
ENSP00000635647
resolver
ensp
ENSP00000635648
resolver
enst
ENST00000338099
resolver
enst
ENST00000434935
resolver
enst
ENST00000711371
resolver
enst
ENST00000711372
resolver
enst
ENST00000711373
resolver
enst
ENST00000711374
resolver
enst
ENST00000894123
resolver
enst
ENST00000894124
resolver
enst
ENST00000894125
resolver
enst
ENST00000929126
resolver
enst
ENST00000929127
resolver
enst
ENST00000965587
resolver
enst
ENST00000965588
resolver
enst
ENST00000965589
resolver
genesymbol
CMTR2
resolver
genesymbol_syn
AFT
resolver
genesymbol_syn
FTSJD1
resolver
hgnc
HGNC:25635
resolver
uniprot
A0AAG2UX58
resolver
uniprot
B2RCD5
resolver
uniprot
D3DWS1
resolver
uniprot
Q8NE77
resolver
uniprot
Q8NFR5
resolver
uniprot
Q9H8Z4
resolver
uniprot
Q9NUS3
resolver
uniprot
Q9NXF5
resolver
uniprot_entry
A0AAG2UX58_HUMAN
resolver
uniprot_entry
CMTR2_HUMAN
resolver
uniprot_sec
B2RCD5
resolver
uniprot_sec
D3DWS1
resolver
uniprot_sec
Q8NE77
resolver
uniprot_sec
Q8NFR5
resolver
uniprot_sec
Q9H8Z4
resolver
uniprot_sec
Q9NUS3
resolver
uniprot_sec
Q9NXF5
resolver
amino_acid_sequence
MSKCRKTPVQQLASPASFSPDILADIFELFAKNFSYGKPLNNEWQLPDPSEIFTCDHTELNAFLDLKNSLNEVKNLLSDKKLDEWHEHTAFTNKAGKIISHVRKSVNAELCTQAWCKFHEILCSFPLIPQEAFQNGKLNSLHLCEAPGAFIASLNHYLKSHRFPCHWSWVANTLNPYHEANDDLMMIMDDRLIANTLHWWYFGPDNTGDIMTLKFLTGLQNFISSMATVHLVTADGSFDCQGNPGEQEALVSSLHYCEVVTALTTLGNGGSFVLKMFTMFEHCSINLMYLLNCCFDQVHVFKPATSKAGNSEVYVVCLHYKGREAIHPLLSKMTLNFGTEMKRKALFPHHVIPDSFLKRHEECCVFFHKYQLETISENIRLFECMGKAEQEKLNNLRDCAIQYFMQKFQLKHLSRNNWLVKKSSIGCSTNTKWFGQRNKYFKTYNERKMLEALSWKDKVAKGYFNSWAEEHGVYHPGQSSILEGTASNLECHLWHILEGKKLPKVKCSPFCNGEILKTLNEAIEKSLGGAFNLDSKFRPKQQYSCSCHVFSEELIFSELCSLTECLQDEQVVVPSNQIKCLLVGFSTLRNIKMHIPLEVRLLESAELTTFSCSLLHDGDPTYQRLFLDCLLHSLRELHTGDVMILPVLSCFTRFMAGLIFVLHSCFRFITFVCPTSSDPLRTCAVLLCVGYQDLPNPVFRYLQSVNELLSTLLNSDSPQQVLQFVPMEVLLKGALLDFLWDLNAAIAKRHLHFIIQREREEIINSLQLQN
uniprot
proteins
ec_number
2.1.1.296
uniprot
proteins
function
FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the second nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) (cap0) to produce m(7)GpppRmpNm (cap2). Recognizes a guanosine cap on RNA independently of its N(7) methylation status. Display cap2 methylation on both cap0 and cap1. Displays a preference for cap1 RNAs. {ECO:0000269|PubMed:21310715}.
uniprot
proteins
mass_dalton
88120
uniprot
proteins
mutagenesis
MUTAGEN 74; /note="K->A: Strongly reduces mRNA cap binding and catalytic activity of the enzyme."; /evidence="ECO:0000269|PubMed:24402442"; MUTAGEN 77; /note="L->A: Strongly reduces mRNA cap binding and catalytic activity of the enzyme."; /evidence="ECO:0000269|PubMed:24402442"; MUTAGEN 78; /note="S->A: Only mildly affects mRNA cap binding and catalytic activity of the enzyme."; /evidence="ECO:0000269|PubMed:24402442"; MUTAGEN 85; /note="W->A: Strongly reduces mRNA cap binding and catalytic activity of the enzyme."; /evidence="ECO:0000269|PubMed:24402442"; MUTAGEN 86; /note="H->A: Only mildly affects mRNA cap binding and catalytic activity of the enzyme."; /evidence="ECO:0000269|PubMed:24402442"; MUTAGEN 89; /note="T->A: Strongly reduces mRNA cap binding and catalytic activity of the enzyme."; /evidence="ECO:0000269|PubMed:24402442"; MUTAGEN 113; /note="Q->A: Only mildly affects mRNA cap binding and catalytic activity of the enzyme."; /evidence="ECO:0000269|PubMed:24402442"; MUTAGEN 117; /note="K->A: Abolishes catalytic activity."; /evidence="ECO:0000269|PubMed:21310715"; MUTAGEN 142; /note="H->A: Strongly reduces mRNA cap binding and catalytic activity of the enzyme."; /evidence="ECO:0000269|PubMed:24402442"; MUTAGEN 145; /note="E->A: Strongly reduces mRNA cap binding and catalytic activity of the enzyme."; /evidence="ECO:0000269|PubMed:24402442"; MUTAGEN 235; /note="D->A: Abolishes catalytic activity."; /evidence="ECO:0000269|PubMed:21310715"; MUTAGEN 275; /note="K->A: Abolishes catalytic activity."; /evidence="ECO:0000269|PubMed:21310715"; MUTAGEN 307; /note="K->A: Strongly reduces mRNA cap binding and catalytic activity of the enzyme."; /evidence="ECO:0000269|PubMed:24402442
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
21310715
uniprot
proteins
pubmed
24402442
uniprot
proteins
sequence_length
770
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21310715}. Cytoplasm {ECO:0000269|PubMed:21310715}.
uniprot
proteins