[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND TISSUE SPECIFICITY. DOI=10.1006/bbrc.1998.9402; PubMed=9790902 [NCBI, ExPASy, EBI, Israel, Japan] Tsukamoto T., Shibagaki Y., Niikura Y., Kiyohisa M.; "Cloning and characterization of three human cDNAs encoding mRNA (guanine-7-)methyltransferase, an mRNA cap methylase."; Biochem. Biophys. Res. Commun. 251:27-34(1998).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH POLYMERASE II AND RNGTT. DOI=10.1074/jbc.273.34.21443; PubMed=9705270 [NCBI, ExPASy, EBI, Israel, Japan] Pillutla R.C., Yue Z., Maldonado E., Shatkin A.J.; "Recombinant human mRNA cap methyltransferase binds capping enzyme/RNA polymerase IIo complexes."; J. Biol. Chem. 273:21443-21446(1998).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). PubMed=10589710 [NCBI, ExPASy, EBI, Israel, Japan] Yamada-Okabe T., Mio T., Kashima Y., Matsui M., Arisawa M., Yamada-Okabe H.; "The Candida albicans gene for mRNA 5'-cap methyltransferase: identification of the additional residues essential for catalysis."; Microbiology 145:3023-3033(1999).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Brain; DOI=10.1093/dnares/4.5.307; PubMed=9455477 [NCBI, ExPASy, EBI, Israel, Japan] Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.; "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."; DNA Res. 4:307-313(1997).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Ovary; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	FUNCTION, AND MUTAGENESIS OF ASP-203; ARG-239; TYR-289; PHE-291 AND PHE-354. DOI=10.1074/jbc.274.23.16553; PubMed=10347220 [NCBI, ExPASy, EBI, Israel, Japan] Saha N., Schwer B., Shuman S.; "Characterization of human, Schizosaccharomyces pombe, and Candida albicans mRNA cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes."; J. Biol. Chem. 274:16553-16562(1999).
[7]	SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION WITH IMPORTIN ALPHA. DOI=10.1101/gad.848200; PubMed=11114884 [NCBI, ExPASy, EBI, Israel, Japan] Wen Y., Shatkin A.J.; "Cap methyltransferase selective binding and methylation of GpppG-RNA are stimulated by importin-alpha."; Genes Dev. 14:2944-2949(2000).
[8]	SUBCELLULAR LOCATION, AND MUTAGENESIS OF 80-LYS--LYS-83; 103-LYS--ARG-107 AND ARG-127. DOI=10.1128/MCB.25.7.2644-2649.2005; PubMed=15767670 [NCBI, ExPASy, EBI, Israel, Japan] Shafer B., Chu C., Shatkin A.J.; "Human mRNA cap methyltransferase: alternative nuclear localization signal motifs ensure nuclear localization required for viability."; Mol. Cell. Biol. 25:2644-2649(2005).

Comments

FUNCTION: mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m₇G(5')pppR-RNA.
SUBUNIT: Interacts with importin alpha, leading to stimulate both RNA-binding and methyltransferase activity. Interaction with importin alpha and beta is required for its nuclear localization, importin beta dissociating in response to RanGTP, allowing RNMT-importin alpha to bind RNA substrates. Interacts with elongating form of polymerase II and RNGTT.
SUBCELLULAR LOCATION: Nucleus.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	hCMT1a
Isoform ID	O43148-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	hCMT1b
Isoform ID	O43148-2
Features which should be applied to build the isoform sequence: VSP_020241.

TISSUE SPECIFICITY: Widely expressed.
SIMILARITY: Belongs to the mRNA cap methyltransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB022604; BAA74464.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB022605; BAA74463.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF067791; AAC63269.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB020966; BAA82447.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB007858; BAA23694.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC036798; AAH36798.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_003790.1; -.

UniGene

Hs.592347

3D structure databases

PDB

3BGV; X-ray; 2.30 A; A/B/C/D=165-476.

[ExPASy / RCSB / EBI]

3BGV; -.

PTM databases

O43148; -.

Enzyme and pathway databases

Reactome

REACT_1675; mRNA Processing.
REACT_1788; Transcription.
REACT_6185; HIV Infection.
REACT_71; Gene Expression.

Organism-specific databases

HGNC:10075; RNMT.

603514; gene. [NCBI / EBI]

PA34448; -.

Gene expression databases

ArrayExpress

O43148; -.

CleanEx

HS_RNMT; -.

GermOnline

ENSG00000101654; Homo sapiens.

Ontologies

GO:0005654;	Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0004482;	Molecular function: mRNA (guanine-N7-)-methyltransferase activity (inferred from mutant phenotype from UniProtKB).
GO:0003723;	Molecular function: RNA binding (inferred from mutant phenotype from UniProtKB).
GO:0006370;	Biological process: mRNA capping (inferred from mutant phenotype from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR016899; mRNA_G-N7_MeTrfase.
IPR004971; Pox_MCEL.
Graphical view of domain structure.

Pfam

PF03291; Pox_MCEL; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF028762; ABD1; 1.

BLOCKS

O43148.

Genome annotation databases

Ensembl

ENSG00000101654; Homo sapiens. [Contig view]

GeneID

8731; -.

KEGG

hsa:8731; -.

Phylogenomic databases

HOVERGEN

O43148; -.

Other

RNMT; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Methyltransferase; mRNA capping; mRNA processing; Nucleus; Phosphoprotein; RNA-binding; S-adenosyl-L-methionine; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 476`	`476`	`mRNA cap guanine-N7 methyltransferase.`	`PRO_0000248321`
`REGION`	`176 177`	`2`	`mRNA cap binding (By similarity).`
`MOTIF`	`126 128`	`3`	`Nuclear localization signal.`
`BINDING`	`180 180`		`S-adenosyl-L-methionine (By similarity).`
`BINDING`	`205 205`		`S-adenosyl-L-methionine; via carbonyl oxygen (By similarity).`
`BINDING`	`208 208`		`mRNA cap (By similarity).`
`BINDING`	`214 214`		`mRNA cap (By similarity).`
`BINDING`	`227 227`		`S-adenosyl-L-methionine (By similarity).`
`BINDING`	`239 239`		`mRNA cap (Probable).`
`BINDING`	`261 261`		`S-adenosyl-L-methionine (By similarity).`
`BINDING`	`284 284`		`S-adenosyl-L-methionine; via carbonyl oxygen (By similarity).`
`BINDING`	`288 288`		`mRNA cap (By similarity).`
`BINDING`	`370 370`		`mRNA cap (By similarity).`
`BINDING`	`467 467`		`mRNA cap (By similarity).`
`MOD_RES`	`24 24`		`Phosphoserine (By similarity).`
`MOD_RES`	`28 28`		`Phosphoserine (By similarity).`
`VAR_SEQ`	`465 476`		`SIYLVFAFEKQQ -> RLTVTIMREAWLSTVGPGRAPVAASSVKWGTPRPAMQFIL (in isoform 2).`	`VSP_020241`
`MUTAGEN`	`80 83`		`KKRK->AAAA: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 103-AAAAA-107 and I-127.`
`MUTAGEN`	`103 107`		`KKRKR->AAAAA: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and I-127.`
`MUTAGEN`	`127 127`		`R->I: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and 103-AAAAA-107.`
`MUTAGEN`	`203 203`		`D->A: Loss of activity.`
`MUTAGEN`	`239 239`		`R->A: Loss of activity.`
`MUTAGEN`	`289 289`		`Y->A: Loss of activity.`
`MUTAGEN`	`291 291`		`F->A: Strongly impairs enzyme activity.`
`MUTAGEN`	`354 354`		`F->A: Loss of activity.`
`CONFLICT`	`179 179`		`M -> I (in Ref. 3; BAA82447).`

Sequence information

Length: 476 AA [This is the length of the unprocessed precursor]

Molecular weight: 54844 Da [This is the MW of the unprocessed precursor]

CRC64: EC919BC41BD5E2B3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MANSAKAEEY EKMSLEQAKA SVNSETESSF NINENTTASG TGLSEKTSVC RQVDIARKRK 

        70         80         90        100        110        120 
EFEDDLVKES SSCGKDTPSK KRKLDPEIVP EEKDCGDAEG NSKKRKRETE DVPKDKSSTG 

       130        140        150        160        170        180 
DGTQNKRKIA LEDVPEKQKN LEEGHSSTVA AHYNELQEVG LEKRSQSRIF YLRNFNNWMK 

       190        200        210        220        230        240 
SVLIGEFLEK VRQKKKRDIT VLDLGCGKGG DLLKWKKGRI NKLVCTDIAD VSVKQCQQRY 

       250        260        270        280        290        300 
EDMKNRRDSE YIFSAEFITA DSSKELLIDK FRDPQMCFDI CSCQFVCHYS FESYEQADMM 

       310        320        330        340        350        360 
LRNACERLSP GGYFIGTTPN SFELIRRLEA SETESFGNEI YTVKFQKKGD YPLFGCKYDF 

       370        380        390        400        410        420 
NLEGVVDVPE FLVYFPLLNE MAKKYNMKLV YKKTFLEFYE EKIKNNENKM LLKRMQALEP 

       430        440        450        460        470 
YPANESSKLV SEKVDDYEHA AKYMKNSQVR LPLGTLSKSE WEATSIYLVF AFEKQQ

O43148 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools