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Reviewed, UniProtKB/Swiss-Prot O43148 (MCES_HUMAN)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    mRNA cap guanine-N7 methyltransferase
    EC=2.1.1.56
Alternative name(s):
    mRNA (guanine-N(7)-)-methyltransferase
    RG7MT1
    mRNA cap methyltransferase
      Short name=hcm1p
      Short name=hCMT1
      Short name=hMet
Gene names
Name: RNMT
Synonyms: KIAA0398
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (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. Ref.1 Ref.2 Ref.6

Catalytic activity

S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.

Subunit structure

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. Ref.2 Ref.7

Subcellular location

Nucleus. Ref.7 Ref.8

Tissue specificity

Widely expressed. Ref.1 Ref.2

Sequence similarities

Belongs to the mRNA cap methyltransferase family.

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Ontologies

Keywords
   Biological processmRNA capping
mRNA processing
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
S-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processmRNA capping Ref.1 Ref.2

Inferred from mutant phenotype. Source: UniProtKB

   Cellular componentnucleoplasm Ref.1

Inferred from Experiment. Source: Reactome

   Molecular functionRNA binding Ref.1 Ref.2

Inferred from mutant phenotype. Source: UniProtKB

mRNA (guanine-N7-)-methyltransferase activity Ref.1 Ref.2

Inferred from mutant phenotype. Source: UniProtKB

Complete GO annotation...

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43148-1)

Also known as: hCMT1a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O43148-2)

Also known as: hCMT1b;

The sequence of this isoform differs from the canonical sequence as follows:
     465-476: SIYLVFAFEKQQ → RLTVTIMREAWLSTVGPGRAPVAASSVKWGTPRPAMQFIL

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 476476mRNA cap guanine-N7 methyltransferase
PRO_0000248321

Regions

Region176 – 1772mRNA cap binding By similarity
Motif126 – 1283Nuclear localization signal

Sites

Binding site1801S-adenosyl-L-methionine By similarity
Binding site2051S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site2081mRNA cap By similarity
Binding site2141mRNA cap By similarity
Binding site2271S-adenosyl-L-methionine By similarity
Binding site2391mRNA cap Probable
Binding site2611S-adenosyl-L-methionine By similarity
Binding site2841S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site2881mRNA cap By similarity
Binding site3701mRNA cap By similarity
Binding site4671mRNA cap By similarity

Amino acid modifications

Modified residue241Phosphoserine By similarity
Modified residue281Phosphoserine By similarity

Natural variations

Alternative sequence465 – 47612SIYLV…FEKQQ → RLTVTIMREAWLSTVGPGRA PVAASSVKWGTPRPAMQFIL in isoform 2.
VSP_020241

Experimental info

Mutagenesis80 – 834KKRK → AAAA: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 103-AAAAA-107 and I-127.
Mutagenesis103 – 1075KKRKR → AAAAA: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and I-127.
Mutagenesis1271R → I: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and 103-AAAAA-107. Ref.8
Mutagenesis2031D → A: Loss of activity. Ref.6
Mutagenesis2391R → A: Loss of activity. Ref.6
Mutagenesis2891Y → A: Loss of activity. Ref.6
Mutagenesis2911F → A: Strongly impairs enzyme activity. Ref.6
Mutagenesis3541F → A: Loss of activity. Ref.6
Sequence conflict1791M → I in BAA82447. Ref.3

Secondary structure

1 ................................................... 476
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (hCMT1a) [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: EC919BC41BD5E2B3

FASTA47654,844
        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

« Hide

Isoform 2 (hCMT1b).

Checksum: 00F822E6867D6D6A
Show »

FASTA50457,725

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References

« Hide 'large scale' references
[1]"Cloning and characterization of three human cDNAs encoding mRNA (guanine-7-)methyltransferase, an mRNA cap methylase."
Tsukamoto T., Shibagaki Y., Niikura Y., Kiyohisa M.
Biochem. Biophys. Res. Commun. 251:27-34(1998) [PubMed: 9790902] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY.
[2]"Recombinant human mRNA cap methyltransferase binds capping enzyme/RNA polymerase IIo complexes."
Pillutla R.C., Yue Z., Maldonado E., Shatkin A.J.
J. Biol. Chem. 273:21443-21446(1998) [PubMed: 9705270] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH POLYMERASE II AND RNGTT.
[3]"The Candida albicans gene for mRNA 5'-cap methyltransferase: identification of the additional residues essential for catalysis."
Yamada-Okabe T., Mio T., Kashima Y., Matsui M., Arisawa M., Yamada-Okabe H.
Microbiology 145:3023-3033(1999) [PubMed: 10589710] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:307-313(1997) [PubMed: 9455477] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Ovary.
[6]"Characterization of human, Schizosaccharomyces pombe, and Candida albicans mRNA cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes."
Saha N., Schwer B., Shuman S.
J. Biol. Chem. 274:16553-16562(1999) [PubMed: 10347220] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-203; ARG-239; TYR-289; PHE-291 AND PHE-354.
[7]"Cap methyltransferase selective binding and methylation of GpppG-RNA are stimulated by importin-alpha."
Wen Y., Shatkin A.J.
Genes Dev. 14:2944-2949(2000) [PubMed: 11114884] [Abstract]
Cited for: SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH IMPORTIN ALPHA.
[8]"Human mRNA cap methyltransferase: alternative nuclear localization signal motifs ensure nuclear localization required for viability."
Shafer B., Chu C., Shatkin A.J.
Mol. Cell. Biol. 25:2644-2649(2005) [PubMed: 15767670] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 80-LYS--LYS-83; 103-LYS--ARG-107 AND ARG-127.
[9]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

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Cross-references

Sequence databases

AB022604 mRNA. Translation: BAA74464.1.
AB022605 mRNA. Translation: BAA74463.1.
AF067791 mRNA. Translation: AAC63269.1.
AB020966 mRNA. Translation: BAA82447.1.
AB007858 mRNA. Translation: BAA23694.1.
BC036798 mRNA. Translation: AAH36798.1.
IPIIPI00410657.
IPI00747403.
RefSeqNP_003790.1.
UniGeneHs.592347

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3BGVX-ray2.30A/B/C/D165-476[»]
3EPPX-ray2.41A/B165-476[»]
ModBaseSearch...

PTM databases

PhosphoSiteO43148.

Proteomic databases

PRIDEO43148.

Genome annotation databases

EnsemblENSG00000101654. Homo sapiens. [Contig view]
GeneID8731.
KEGGhsa:8731.

Organism-specific databases

GeneCardsGC18P013716.
HGNCHGNC:10075. RNMT.
MIM603514. gene.
PharmGKBPA34448.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOVERGENO43148.
OMAO43148. KYMKNSQ.

Enzyme and pathway databases

BRENDA2.1.1.56. 247.
ReactomeREACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_6185. HIV Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressO43148.
BgeeO43148.
CleanExHS_RNMT.
GermOnlineENSG00000101654. Homo sapiens.

Family and domain databases

InterProIPR016899. mRNA_G-N7_MeTrfase.
IPR004971. Pox_MCEL.
[Graphical view]
PfamPF03291. Pox_MCEL. 1 hit.
[Graphical view]
PIRSFPIRSF028762. ABD1. 1 hit.
ProtoNetSearch...

Other Resources

NextBio32753.
SOURCESearch...

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Entry information

Entry nameMCES_HUMAN
AccessionPrimary (citable) accession number: O43148
Secondary accession number(s): O94996, Q9UIJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 1998
Last modified: June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents