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Protein

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2

Gene

CMTR2

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

Functioni

S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the second nucleotide of a m7GpppG-capped mRNA and small nuclear RNA (snRNA) (cap0) to produce m7GpppRmpNm (cap2). Recognizes a guanosine cap on RNA independently of its N7 methylation status. Display cap2 methylation on both cap0 and cap1. Displays a preference for cap1 RNAs.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA].1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1171 Publication1
Binding sitei148S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation1
Binding sitei167S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation1
Active sitei2351 Publication1
Binding sitei235S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei275Proton acceptorPROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

  • mRNA (nucleoside-2'-O-)-methyltransferase activity Source: UniProtKB

GO - Biological processi

  • 7-methylguanosine mRNA capping Source: UniProtKB
  • cap2 mRNA methylation Source: UniProtKB

Keywordsi

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

Enzyme and pathway databases

BRENDAi2.1.1.296 2681

Names & Taxonomyi

Protein namesi
Recommended name:
Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC:2.1.1.2961 Publication)
Alternative name(s):
Cap methyltransferase 2
Cap2 2'O-ribose methyltransferase 2
Short name:
HMTr2
Short name:
MTr2
FtsJ methyltransferase domain-containing protein 1
Protein adrift homolog
Gene namesi
Name:CMTR2
Synonyms:AFT, FTSJD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000180917.16
HGNCiHGNC:25635 CMTR2
MIMi616190 gene
neXtProtiNX_Q8IYT2

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

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi74K → A: Strongly reduces mRNA cap binding and catalytic activity of the enzyme. 1 Publication1
Mutagenesisi77L → A: Strongly reduces mRNA cap binding and catalytic activity of the enzyme. 1 Publication1
Mutagenesisi78S → A: Only mildly affects mRNA cap binding and catalytic activity of the enzyme. 1 Publication1
Mutagenesisi85W → A: Strongly reduces mRNA cap binding and catalytic activity of the enzyme. 1 Publication1
Mutagenesisi86H → A: Only mildly affects mRNA cap binding and catalytic activity of the enzyme. 1 Publication1
Mutagenesisi89T → A: Strongly reduces mRNA cap binding and catalytic activity of the enzyme. 1 Publication1
Mutagenesisi113Q → A: Only mildly affects mRNA cap binding and catalytic activity of the enzyme. 1 Publication1
Mutagenesisi117K → A: Abolishes catalytic activity. 1 Publication1
Mutagenesisi142H → A: Strongly reduces mRNA cap binding and catalytic activity of the enzyme. 1 Publication1
Mutagenesisi145E → A: Strongly reduces mRNA cap binding and catalytic activity of the enzyme. 1 Publication1
Mutagenesisi235D → A: Abolishes catalytic activity. 1 Publication1
Mutagenesisi275K → A: Abolishes catalytic activity. 1 Publication1
Mutagenesisi307K → A: Strongly reduces mRNA cap binding and catalytic activity of the enzyme. 1 Publication1

Organism-specific databases

DisGeNETi55783
OpenTargetsiENSG00000180917
PharmGKBiPA162389041

Polymorphism and mutation databases

BioMutaiFTSJD1
DMDMi269849596

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003261801 – 770Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2Add BLAST770

Proteomic databases

EPDiQ8IYT2
MaxQBiQ8IYT2
PaxDbiQ8IYT2
PeptideAtlasiQ8IYT2
PRIDEiQ8IYT2
ProteomicsDBi71233

PTM databases

iPTMnetiQ8IYT2
PhosphoSitePlusiQ8IYT2

Expressioni

Gene expression databases

BgeeiENSG00000180917
CleanExiHS_FTSJD1
ExpressionAtlasiQ8IYT2 baseline and differential
GenevisibleiQ8IYT2 HS

Organism-specific databases

HPAiHPA041700
HPA048265

Interactioni

Protein-protein interaction databases

BioGridi120897, 9 interactors
STRINGi9606.ENSP00000337512

Structurei

3D structure databases

ProteinModelPortaliQ8IYT2
SMRiQ8IYT2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini109 – 322Adrift-type SAM-dependent 2'-O-MTasePROSITE-ProRule annotationAdd BLAST214

Phylogenomic databases

eggNOGiKOG3674 Eukaryota
ENOG410XQ0Z LUCA
GeneTreeiENSGT00530000063742
HOVERGENiHBG098139
InParanoidiQ8IYT2
KOiK14590
OMAiQVLQFVP
OrthoDBiEOG091G0EIW
PhylomeDBiQ8IYT2
TreeFamiTF314897

Family and domain databases

InterProiView protein in InterPro
IPR025807 Adrift-typ_MeTrfase
IPR002877 rRNA_MeTrfase_FtsJ_dom
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
PF01728 FtsJ, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51614 SAM_MT_ADRIFT, 1 hit

Sequencei

Sequence statusi: Complete.

Q8IYT2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKCRKTPVQ QLASPASFSP DILADIFELF AKNFSYGKPL NNEWQLPDPS
60 70 80 90 100
EIFTCDHTEL NAFLDLKNSL NEVKNLLSDK KLDEWHEHTA FTNKAGKIIS
110 120 130 140 150
HVRKSVNAEL CTQAWCKFHE ILCSFPLIPQ EAFQNGKLNS LHLCEAPGAF
160 170 180 190 200
IASLNHYLKS HRFPCHWSWV ANTLNPYHEA NDDLMMIMDD RLIANTLHWW
210 220 230 240 250
YFGPDNTGDI MTLKFLTGLQ NFISSMATVH LVTADGSFDC QGNPGEQEAL
260 270 280 290 300
VSSLHYCEVV TALTTLGNGG SFVLKMFTMF EHCSINLMYL LNCCFDQVHV
310 320 330 340 350
FKPATSKAGN SEVYVVCLHY KGREAIHPLL SKMTLNFGTE MKRKALFPHH
360 370 380 390 400
VIPDSFLKRH EECCVFFHKY QLETISENIR LFECMGKAEQ EKLNNLRDCA
410 420 430 440 450
IQYFMQKFQL KHLSRNNWLV KKSSIGCSTN TKWFGQRNKY FKTYNERKML
460 470 480 490 500
EALSWKDKVA KGYFNSWAEE HGVYHPGQSS ILEGTASNLE CHLWHILEGK
510 520 530 540 550
KLPKVKCSPF CNGEILKTLN EAIEKSLGGA FNLDSKFRPK QQYSCSCHVF
560 570 580 590 600
SEELIFSELC SLTECLQDEQ VVVPSNQIKC LLVGFSTLRN IKMHIPLEVR
610 620 630 640 650
LLESAELTTF SCSLLHDGDP TYQRLFLDCL LHSLRELHTG DVMILPVLSC
660 670 680 690 700
FTRFMAGLIF VLHSCFRFIT FVCPTSSDPL RTCAVLLCVG YQDLPNPVFR
710 720 730 740 750
YLQSVNELLS TLLNSDSPQQ VLQFVPMEVL LKGALLDFLW DLNAAIAKRH
760 770
LHFIIQRERE EIINSLQLQN
Length:770
Mass (Da):88,120
Last modified:November 24, 2009 - v2
Checksum:iE5BE4A2B31AE3580
GO

Sequence cautioni

The sequence AAM49718 differs from that shown. Reason: Frameshift at position 337.Curated
The sequence BAA91058 differs from that shown. Reason: Frameshift at position 739.Curated
The sequence BAB14452 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti27F → L in AAM49718 (Ref. 5) Curated1
Sequence conflicti53F → Y in AAM49718 (Ref. 5) Curated1
Sequence conflicti56D → E in AAM49718 (Ref. 5) Curated1
Sequence conflicti75N → K in AAM49718 (Ref. 5) Curated1
Sequence conflicti85 – 86WH → LD in AAM49718 (Ref. 5) Curated2
Sequence conflicti201 – 202YF → HL in AAM49718 (Ref. 5) Curated2
Sequence conflicti222F → I in AAM49718 (Ref. 5) Curated1
Sequence conflicti317C → S in AAM49718 (Ref. 5) Curated1
Sequence conflicti683C → S in BAA92047 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03999860L → F2 PublicationsCorresponds to variant dbSNP:rs3096380Ensembl.1
Natural variantiVAR_039999163F → Y1 PublicationCorresponds to variant dbSNP:rs17853360Ensembl.1
Natural variantiVAR_040000416N → S1 PublicationCorresponds to variant dbSNP:rs3803704Ensembl.1
Natural variantiVAR_040001608T → K. Corresponds to variant dbSNP:rs3096381Ensembl.1
Natural variantiVAR_040002753F → L. Corresponds to variant dbSNP:rs16970857Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000289 mRNA Translation: BAA91058.1 Frameshift.
AK002033 mRNA Translation: BAA92047.1
AK023183 mRNA Translation: BAB14452.1 Different initiation.
AK315056 mRNA Translation: BAG37532.1
AC106736 Genomic DNA No translation available.
CH471166 Genomic DNA Translation: EAW59246.1
CH471166 Genomic DNA Translation: EAW59247.1
BC034468 mRNA Translation: AAH34468.1
BC035005 mRNA Translation: AAH35005.1
AF458590 mRNA Translation: AAM49718.1 Frameshift.
CCDSiCCDS10898.1
RefSeqiNP_001093112.1, NM_001099642.1
NP_001311303.1, NM_001324374.1
NP_001311306.1, NM_001324377.1
NP_001311307.1, NM_001324378.1
NP_001311308.1, NM_001324379.1
NP_060818.4, NM_018348.5
XP_011521530.1, XM_011523228.1
XP_011521531.1, XM_011523229.1
XP_016878933.1, XM_017023444.1
UniGeneiHs.72782

Genome annotation databases

EnsembliENST00000338099; ENSP00000337512; ENSG00000180917
ENST00000434935; ENSP00000411148; ENSG00000180917
GeneIDi55783
KEGGihsa:55783
UCSCiuc002ezy.5 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCMTR2_HUMAN
AccessioniPrimary (citable) accession number: Q8IYT2
Secondary accession number(s): B2RCD5
, D3DWS1, Q8NE77, Q8NFR5, Q9H8Z4, Q9NUS3, Q9NXF5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 24, 2009
Last modified: June 20, 2018
This is version 107 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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