[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Brain; DOI=10.1093/dnares/10.4.167; PubMed=14621295 [NCBI, ExPASy, EBI, Israel, Japan] Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.; "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."; DNA Res. 10:167-180(2003).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Testis; DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan] Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; "The transcriptional landscape of the mammalian genome."; Science 309:1559-1563(2005).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). STRAIN=FVB/N; TISSUE=Colon; 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).
[4]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-15 AND SER-64, AND MASS SPECTROMETRY. TISSUE=Brain; DOI=10.1074/mcp.M400085-MCP200; PubMed=15345747 [NCBI, ExPASy, EBI, Israel, Japan] Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; "Phosphoproteomic analysis of the developing mouse brain."; Mol. Cell. Proteomics 3:1093-1101(2004).
[5]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan] Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; "Large-scale phosphorylation analysis of mouse liver."; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).

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 (By similarity).
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 (By similarity).
SUBCELLULAR LOCATION: Nucleus (By similarity).

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q9D0L8-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q9D0L8-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_020243.

Name	3
Isoform ID	Q9D0L8-3
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_020242.

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

AK129130; BAC97940.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011300; BAB27527.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK015403; BAB29834.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK031780; BAE43278.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021794; AAH21794.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK082331; BAC38469.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_080716.1; -.

UniGene

Mm.27544

3D structure databases

ModBase

Q9D0L8.

PTM databases

PhosphoSite

Q9D0L8; -.

Organism-specific databases

MGI

MGI:1915147; Rnmt.

Gene expression databases

ArrayExpress

Q9D0L8; -.

CleanEx

MM_RNMT; -.

GermOnline

ENSMUSG00000009535; Mus musculus.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from sequence or structural similarity from UniProtKB).
GO:0004482;	Molecular function: mRNA (guanine-N7-)-methyltransferase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0003723;	Molecular function: RNA binding (inferred from sequence or structural similarity from UniProtKB).
GO:0006370;	Biological process: mRNA capping (inferred from sequence or structural similarity 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

Q9D0L8.

Genome annotation databases

Ensembl

ENSMUSG00000009535; Mus musculus. [Contig view]

GeneID

67897; -.

KEGG

mmu:67897; -.

Phylogenomic databases

HOVERGEN

Q9D0L8; -.

Other

Rnmt; Mus musculus.

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

Keywords

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`	`1 465`	`465`	`mRNA cap guanine-N7 methyltransferase.`	`PRO_0000248323`
`REGION`	`165 166`	`2`	`mRNA cap binding (By similarity).`
`MOTIF`	`113 115`	`3`	`Nuclear localization signal (By similarity).`
`BINDING`	`169 169`		`S-adenosyl-L-methionine (By similarity).`
`BINDING`	`194 194`		`S-adenosyl-L-methionine; via carbonyl oxygen (By similarity).`
`BINDING`	`197 197`		`mRNA cap (By similarity).`
`BINDING`	`203 203`		`mRNA cap (By similarity).`
`BINDING`	`216 216`		`S-adenosyl-L-methionine (By similarity).`
`BINDING`	`228 228`		`mRNA cap (By similarity).`
`BINDING`	`250 250`		`S-adenosyl-L-methionine (By similarity).`
`BINDING`	`273 273`		`S-adenosyl-L-methionine; via carbonyl oxygen (By similarity).`
`BINDING`	`277 277`		`mRNA cap (By similarity).`
`BINDING`	`359 359`		`mRNA cap (By similarity).`
`BINDING`	`456 456`		`mRNA cap (By similarity).`
`MOD_RES`	`11 11`		`Phosphoserine.`
`MOD_RES`	`15 15`		`Phosphoserine.`
`MOD_RES`	`64 64`		`Phosphoserine.`
`VAR_SEQ`	`315 369`		`Missing (in isoform 3).`	`VSP_020242`
`VAR_SEQ`	`370 465`		`Missing (in isoform 2).`	`VSP_020243`
`CONFLICT`	`32 32`		`E -> K (in Ref. 2; BAB29834).`
`CONFLICT`	`53 53`		`L -> H (in Ref. 2; BAE43278).`

Sequence information

Length: 465 AA [This is the length of the unprocessed precursor]

Molecular weight: 53291 Da [This is the MW of the unprocessed precursor]

CRC64: D1422D9621EE2A1A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEGSAKASVA SDPESPPGGN EPAAASGQRL PENTPPCQQV DQPKMQKEFG EDLVEQNSSY 

        70         80         90        100        110        120 
VQDSPSKKRK LDVEIILEEK HSEDDGGSAK RSKLERGDVS EDEPSLGRLN QTKRKLQPQD 

       130        140        150        160        170        180 
DEVPQKLQKL EEGHSSAVAA HYNELQEVGL AKRSQSRIFY LRNFNNWIKS ILIGEILEKV 

       190        200        210        220        230        240 
RQRKTRDITV LDLGCGKGGD LLKWRKGRIS RLVCADIADI SMKQCQQRYE DMRCRRDNEH 

       250        260        270        280        290        300 
IFSAEFITAD CSKELLVEKF RDPEMYFDVC SCQFACHYSF ESQVQADTML RNACGRLNPG 

       310        320        330        340        350        360 
GYFIGTTPNS FELIRRLEAS ETESFGNEIY TVKFQKKGNY PLFGCKYDFN LEGVVDVPEF 

       370        380        390        400        410        420 
LVYFPLLTEM AKKYNMKLIY KKTFLEFYEE KIKNNENKML LKRMQALEQY PAHENSKLAS 

       430        440        450        460 
EKVGDYTHAA EYLKKSQVRL PLGTLSKSEW EATSIYLVFA FEKQQ

Q9D0L8 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