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Protein

mRNA cap guanine-N7 methyltransferase

Gene

RNMT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit of the mRNA-capping methyltransferase RNMT:RAM/FAM103A1 complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs (PubMed:9790902, PubMed:9705270, PubMed:10347220, PubMed:11114884, PubMed:22099306, PubMed:27422871). Binds RNA containing 5'-terminal GpppC (PubMed:11114884).6 Publications

Catalytic activityi

S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.PROSITE-ProRule annotation4 Publications

Enzyme regulationi

Methyltransferase activity is activated by RAM/FAM103A1 (PubMed:27422871).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei180S-adenosyl-L-methioninePROSITE-ProRule annotationCombined sources1 Publication1
Binding sitei205S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotationCombined sources1 Publication1
Sitei208mRNA cap bindingPROSITE-ProRule annotation1
Sitei214mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei227S-adenosyl-L-methioninePROSITE-ProRule annotationCombined sources1 Publication1
Sitei239mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei261S-adenosyl-L-methionine; via amide nitrogenCombined sources1 Publication1
Binding sitei284S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication1
Binding sitei288mRNA capPROSITE-ProRule annotation1
Binding sitei289S-adenosyl-L-methionineCombined sources1 Publication1
Binding sitei370mRNA capPROSITE-ProRule annotation1
Binding sitei467mRNA capPROSITE-ProRule annotation1

GO - Molecular functioni

  • mRNA (guanine-N7-)-methyltransferase activity Source: UniProtKB
  • RNA binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionMethyltransferase, RNA-binding, Transferase
Biological processmRNA capping, mRNA processing
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:HS02296-MONOMER.
ReactomeiR-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
R-HSA-72086. mRNA Capping.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA cap guanine-N7 methyltransferase (EC:2.1.1.564 Publications)
Alternative name(s):
RG7MT1
mRNA (guanine-N(7)-)-methyltransferase
mRNA cap methyltransferase
Short name:
hCMT1
Short name:
hMet
Short name:
hcm1p
Gene namesi
Name:RNMT
Synonyms:KIAA0398
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

EuPathDBiHostDB:ENSG00000101654.17.
HGNCiHGNC:10075. RNMT.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi80 – 83KKRK → AAAA: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 103-AAAAA-107 and I-127. 1 Publication4
Mutagenesisi103 – 107KKRKR → AAAAA: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and I-127. 1 Publication5
Mutagenesisi127R → I: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and 103-AAAAA-107. 1 Publication1
Mutagenesisi178W → C: Loss of methyltransferase activity in presence or absence of RAM/FAM103A1; when associated with C-417. Complete restored RAM/FAM103A1-mediated methyltransferase activity under reducing conditions; when associated with C-417. Loss of methyltransferase activity in presence or absence of RAM/FAM103A1; when associated with C-417; C-393 and C-398. Partially restored RAM/FAM103A1-mediated methyltransferase activity under reducing conditions; when associated with C-417; C-393 and C-398. 1 Publication1
Mutagenesisi203D → A: Loss of activity. 1 Publication1
Mutagenesisi239R → A: Loss of activity. 1 Publication1
Mutagenesisi289Y → A: Loss of activity. 1 Publication1
Mutagenesisi291F → A: Strongly impairs enzyme activity. 1 Publication1
Mutagenesisi354F → A: Loss of activity. 1 Publication1
Mutagenesisi393K → C: Loss of methyltransferase activity in presence or absence of RAM/FAM103A1; when associated with C-178; C-398 and C-417. Partially restored RAM/FAM103A1-mediated methyltransferase activity under reducing conditions; when associated with C-178; C-398 and C-417. 1 Publication1
Mutagenesisi398F → C: Loss of methyltransferase activity in presence or absence of RAM/FAM103A1; when associated with C-178; C-393 and C-417. Partially restored RAM/FAM103A1-mediated methyltransferase activity under reducing conditions; when associated with C-178; C-393 and C-417. 1 Publication1
Mutagenesisi409K → E: Decreased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAM/FAM103A1; when associated with E-413. Decreased interaction with RAM/FAM103A1; when associated with E-413. 1 Publication1
Mutagenesisi413K → E: Decreased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAM/FAM103A1; when associated with E-409. Decreased interaction with RAM/FAM103A1; when associated with E-409. 1 Publication1
Mutagenesisi417A → C: Loss of methyltransferase activity in presence or absence of RAM/FAM103A1; when associated with C-178. Complete restored RAM/FAM103A1-mediated methyltransferase activity under reducing conditions; when associated with C-178. Loss of methyltransferase activity in presence or absence of RAM/FAM103A1; when associated with C-178. Loss of methyltransferase activity in presence or absence of RAM/FAM103A1; when associated with C-178; C-393 and C-398. Partially restored RAM/FAM103A1-mediated methyltransferase activity under reducing conditions; when associated with C-178; C-393 and C-398. 1 Publication1
Mutagenesisi450R → E: Increased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAM/FAM103A1; when associated with E-452. No change in interaction with RAM/FAM103A1; when associated with E-452. 1 Publication1
Mutagenesisi452P → E: Increased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAM/FAM103A1; when associated with E-450. No change in interaction with RAM/FAM103A1; when associated with E-450. 1 Publication1

Organism-specific databases

DisGeNETi8731.
OpenTargetsiENSG00000101654.
PharmGKBiPA34448.

Polymorphism and mutation databases

BioMutaiRNMT.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002483211 – 476mRNA cap guanine-N7 methyltransferaseAdd BLAST476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei24PhosphoserineBy similarity1
Modified residuei28PhosphoserineBy similarity1
Modified residuei29PhosphoserineBy similarity1
Modified residuei118PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO43148.
MaxQBiO43148.
PaxDbiO43148.
PeptideAtlasiO43148.
PRIDEiO43148.

PTM databases

iPTMnetiO43148.
PhosphoSitePlusiO43148.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

BgeeiENSG00000101654.
CleanExiHS_RNMT.
ExpressionAtlasiO43148. baseline and differential.
GenevisibleiO43148. HS.

Organism-specific databases

HPAiHPA039409.

Interactioni

Subunit structurei

Interacts with importin alpha, leading to stimulate both RNA-binding and methyltransferase activity (PubMed:11114884). 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 (PubMed:11114884). Interacts with elongating form of polymerase II and RNGTT (PubMed:9705270). Interacts with RAM/FAM103A1, this interaction significantly enhances RNA-binding and cap methyltransferase activity (PubMed:22099306, Ref. 14).4 Publications

Protein-protein interaction databases

BioGridi114269. 19 interactors.
IntActiO43148. 8 interactors.
STRINGi9606.ENSP00000262173.

Structurei

Secondary structure

1476
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi170 – 193Combined sources24
Beta strandi200 – 204Combined sources5
Turni207 – 211Combined sources5
Helixi212 – 217Combined sources6
Beta strandi221 – 228Combined sources8
Helixi230 – 244Combined sources15
Beta strandi245 – 248Combined sources4
Beta strandi254 – 259Combined sources6
Turni262 – 264Combined sources3
Helixi267 – 269Combined sources3
Beta strandi271 – 273Combined sources3
Beta strandi278 – 285Combined sources8
Helixi287 – 292Combined sources6
Helixi294 – 305Combined sources12
Beta strandi308 – 319Combined sources12
Helixi321 – 330Combined sources10
Beta strandi331 – 337Combined sources7
Beta strandi339 – 346Combined sources8
Beta strandi357 – 362Combined sources6
Turni363 – 365Combined sources3
Beta strandi368 – 371Combined sources4
Helixi375 – 382Combined sources8
Helixi383 – 385Combined sources3
Beta strandi387 – 394Combined sources8
Helixi395 – 402Combined sources8
Helixi406 – 414Combined sources9
Beta strandi418 – 422Combined sources5
Turni434 – 437Combined sources4
Helixi438 – 443Combined sources6
Beta strandi453 – 456Combined sources4
Helixi458 – 464Combined sources7
Beta strandi467 – 474Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BGVX-ray2.30A/B/C/D165-476[»]
3EPPX-ray2.41A/B165-476[»]
5E8JX-ray2.35A/B167-476[»]
5E9JX-ray3.47A/B167-416[»]
A/B457-476[»]
5E9WX-ray2.28A/B/C/D167-476[»]
ProteinModelPortaliO43148.
SMRiO43148.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43148.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini128 – 476mRNA cap 0 methyltransferasePROSITE-ProRule annotationAdd BLAST349

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni176 – 177mRNA cap bindingPROSITE-ProRule annotation2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi126 – 128Nuclear localization signal3

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1975. Eukaryota.
ENOG410Y7HG. LUCA.
GeneTreeiENSGT00390000002368.
HOVERGENiHBG081963.
InParanoidiO43148.
KOiK00565.
OMAiLNLVSCQ.
OrthoDBiEOG091G0C9Y.
PhylomeDBiO43148.
TreeFamiTF314347.

Family and domain databases

InterProiView protein in InterPro
IPR016899. mRNA_G-N7_MeTrfase.
IPR004971. mRNA_G-N7_MeTrfase_dom.
IPR029063. SAM-dependent_MTases.
PfamiView protein in Pfam
PF03291. Pox_MCEL. 1 hit.
PIRSFiPIRSF028762. ABD1. 1 hit.
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiView protein in PROSITE
PS51562. RNA_CAP0_MT. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43148-1) [UniParc]FASTAAdd to basket
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.

« Hide

        10         20         30         40         50
MANSAKAEEY EKMSLEQAKA SVNSETESSF NINENTTASG TGLSEKTSVC
60 70 80 90 100
RQVDIARKRK EFEDDLVKES SSCGKDTPSK KRKLDPEIVP EEKDCGDAEG
110 120 130 140 150
NSKKRKRETE DVPKDKSSTG DGTQNKRKIA LEDVPEKQKN LEEGHSSTVA
160 170 180 190 200
AHYNELQEVG LEKRSQSRIF YLRNFNNWMK SVLIGEFLEK VRQKKKRDIT
210 220 230 240 250
VLDLGCGKGG DLLKWKKGRI NKLVCTDIAD VSVKQCQQRY EDMKNRRDSE
260 270 280 290 300
YIFSAEFITA DSSKELLIDK FRDPQMCFDI CSCQFVCHYS FESYEQADMM
310 320 330 340 350
LRNACERLSP GGYFIGTTPN SFELIRRLEA SETESFGNEI YTVKFQKKGD
360 370 380 390 400
YPLFGCKYDF NLEGVVDVPE FLVYFPLLNE MAKKYNMKLV YKKTFLEFYE
410 420 430 440 450
EKIKNNENKM LLKRMQALEP YPANESSKLV SEKVDDYEHA AKYMKNSQVR
460 470
LPLGTLSKSE WEATSIYLVF AFEKQQ
Length:476
Mass (Da):54,844
Last modified:June 1, 1998 - v1
Checksum:iEC919BC41BD5E2B3
GO
Isoform 2 (identifier: O43148-2) [UniParc]FASTAAdd to basket
Also known as: hCMT1b

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

Show »
Length:504
Mass (Da):57,725
Checksum:i00F822E6867D6D6A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti179M → I in BAA82447 (PubMed:10589710).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_020241465 – 476SIYLV…FEKQQ → RLTVTIMREAWLSTVGPGRA PVAASSVKWGTPRPAMQFIL in isoform 2. 1 PublicationAdd BLAST12

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
EF445026 Genomic DNA. Translation: ACA06068.1.
CH471113 Genomic DNA. Translation: EAX01505.1.
CH471113 Genomic DNA. Translation: EAX01506.1.
BC036798 mRNA. Translation: AAH36798.1.
CCDSiCCDS11867.1. [O43148-1]
CCDS77156.1. [O43148-2]
RefSeqiNP_001295192.1. NM_001308263.1. [O43148-2]
NP_003790.1. NM_003799.2. [O43148-1]
XP_005258219.1. XM_005258162.1. [O43148-1]
XP_016881550.1. XM_017026061.1. [O43148-2]
UniGeneiHs.592347.

Genome annotation databases

EnsembliENST00000262173; ENSP00000262173; ENSG00000101654. [O43148-1]
ENST00000383314; ENSP00000372804; ENSG00000101654. [O43148-1]
ENST00000543302; ENSP00000446426; ENSG00000101654. [O43148-1]
ENST00000589866; ENSP00000466252; ENSG00000101654. [O43148-1]
ENST00000592764; ENSP00000466111; ENSG00000101654. [O43148-2]
GeneIDi8731.
KEGGihsa:8731.
UCSCiuc002ksk.2. human. [O43148-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiMCES_HUMAN
AccessioniPrimary (citable) accession number: O43148
Secondary accession number(s): B0YJ90
, D3DUJ5, O94996, Q9UIJ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 1998
Last modified: October 25, 2017
This is version 137 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families