RNMT
entrez
8731
canonical
uniprot
O43148
canonical
ensembl
ENSG00000101654
resolver
ensp
ENSP00000372804
resolver
ensp
ENSP00000446426
resolver
ensp
ENSP00000466111
resolver
ensp
ENSP00000467171
resolver
ensp
ENSP00000577504
resolver
ensp
ENSP00000668181
resolver
ensp
ENSP00000793174
resolver
enst
ENST00000588457
resolver
genesymbol
RNMT
resolver
genesymbol_syn
KIAA0398
resolver
hgnc
HGNC:10075
resolver
uniprot
A8K946
resolver
uniprot
B0YJ90
resolver
uniprot
D3DUJ5
resolver
uniprot
K7EP06
resolver
uniprot
O94996
resolver
uniprot
Q9UIJ9
resolver
uniprot_entry
A8K946_HUMAN
resolver
uniprot_entry
K7EP06_HUMAN
resolver
uniprot_entry
MCES_HUMAN
resolver
uniprot_sec
B0YJ90
resolver
uniprot_sec
D3DUJ5
resolver
uniprot_sec
O94996
resolver
uniprot_sec
Q9UIJ9
resolver
activity_regulation
ACTIVITY REGULATION: Methyltransferase activity is activated by RAMAC (PubMed:27422871). {ECO:0000269|PubMed:27422871}.
uniprot
proteins
amino_acid_sequence
MANSAKAEEYEKMSLEQAKASVNSETESSFNINENTTASGTGLSEKTSVCRQVDIARKRKEFEDDLVKESSSCGKDTPSKKRKLDPEIVPEEKDCGDAEGNSKKRKRETEDVPKDKSSTGDGTQNKRKIALEDVPEKQKNLEEGHSSTVAAHYNELQEVGLEKRSQSRIFYLRNFNNWMKSVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYPLFGCKYDFNLEGVVDVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMQALEPYPANESSKLVSEKVDDYEHAAKYMKNSQVRLPLGTLSKSEWEATSIYLVFAFEKQQ
uniprot
proteins
ec_number
2.1.1.56
uniprot
proteins
function
FUNCTION: Catalytic subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs (PubMed:10347220, PubMed:11114884, PubMed:22099306, PubMed:27422871, PubMed:9705270, PubMed:9790902). Binds RNA containing 5'-terminal GpppC (PubMed:11114884). {ECO:0000269|PubMed:10347220, ECO:0000269|PubMed:11114884, ECO:0000269|PubMed:22099306, ECO:0000269|PubMed:27422871, ECO:0000269|PubMed:9705270, ECO:0000269|PubMed:9790902}.
uniprot
proteins
mass_dalton
54844
uniprot
proteins
mutagenesis
MUTAGEN 80..83; /note="KKRK->AAAA: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 103-AAAAA-107 and I-127."; /evidence="ECO:0000269|PubMed:15767670"; MUTAGEN 103..107; /note="KKRKR->AAAAA: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and I-127."; /evidence="ECO:0000269|PubMed:15767670"; MUTAGEN 127; /note="R->I: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and 103-AAAAA-107."; /evidence="ECO:0000269|PubMed:15767670"; MUTAGEN 178; /note="W->C: Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-417. Complete restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-417. Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-417; C-393 and C-398. Partially restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-417; C-393 and C-398."; /evidence="ECO:0000269|PubMed:27422871"; MUTAGEN 203; /note="D->A: Loss of activity."; /evidence="ECO:0000269|PubMed:10347220"; MUTAGEN 239; /note="R->A: Loss of activity."; /evidence="ECO:0000269|PubMed:10347220"; MUTAGEN 289; /note="Y->A: Loss of activity."; /evidence="ECO:0000269|PubMed:10347220"; MUTAGEN 291; /note="F->A: Strongly impairs enzyme activity."; /evidence="ECO:0000269|PubMed:10347220"; MUTAGEN 354; /note="F->A: Loss of activity."; /evidence="ECO:0000269|PubMed:10347220"; MUTAGEN 393; /note="K->C: Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-178; C-398 and C-417. Partially restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-178; C-398 and C-417."; /evidence="ECO:0000269|PubMed:27422871"; MUTAGEN 398; /note="F->C: Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-178; C-393 and C-417. Partially restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-178; C-393 and C-417."; /evidence="ECO:0000269|PubMed:27422871"; MUTAGEN 409; /note="K->E: Decreased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAMAC; when associated with E-413. Decreased interaction with RAMAC; when associated with E-413."; /evidence="ECO:0000269|PubMed:27422871"; MUTAGEN 413; /note="K->E: Decreased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAMAC; when associated with E-409. Decreased interaction with RAMAC; when associated with E-409."; /evidence="ECO:0000269|PubMed:27422871"; MUTAGEN 417; /note="A->C: Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-178. Complete restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-178. Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-178. Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-178; C-393 and C-398. Partially restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-178; C-393 and C-398."; /evidence="ECO:0000269|PubMed:27422871"; MUTAGEN 450; /note="R->E: Increased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAMAC; when associated with E-452. No change in interaction with RAMAC; when associated with E-452."; /evidence="ECO:0000269|PubMed:27422871"; MUTAGEN 452; /note="P->E: Increased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAMAC; when associated with E-450. No change in interaction with RAMAC; when associated with E-450."; /evidence="ECO:0000269|PubMed:27422871
uniprot
proteins
protein_family
Class I-like SAM-binding methyltransferase superfamily
uniprot
proteins
protein_family
mRNA cap 0 methyltransferase family
uniprot
proteins
pubmed
10347220
uniprot
proteins
pubmed
10589710
uniprot
proteins
pubmed
11114884
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15767670
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22099306
uniprot
proteins
pubmed
27422871
uniprot
proteins
pubmed
9455477
uniprot
proteins
pubmed
9705270
uniprot
proteins
pubmed
9790902
uniprot
proteins
sequence_length
476
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11114884, ECO:0000269|PubMed:15767670}.
uniprot
proteins