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Protein

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

Gene

Cmtr2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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.By similarity

Catalytic activityi

S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei148 – 1481S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Binding sitei167 – 1671S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Binding sitei235 – 2351S-adenosyl-L-methioninePROSITE-ProRule annotation
Active sitei275 – 2751Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

mRNA capping, mRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC:2.1.1.296)
Alternative name(s):
Cap methyltransferase 2
Cap2 2'O-ribose methyltransferase 2
Short name:
MTr2
FtsJ methyltransferase domain-containing protein 1
Gene namesi
Name:Cmtr2
Synonyms:Ftsjd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2384580. Cmtr2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei641 – 66121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 767767Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2PRO_0000326181Add
BLAST

Proteomic databases

EPDiQ8BWQ4.
MaxQBiQ8BWQ4.
PaxDbiQ8BWQ4.
PeptideAtlasiQ8BWQ4.
PRIDEiQ8BWQ4.

PTM databases

iPTMnetiQ8BWQ4.
PhosphoSiteiQ8BWQ4.

Expressioni

Gene expression databases

BgeeiQ8BWQ4.
ExpressionAtlasiQ8BWQ4. baseline and differential.
GenevisibleiQ8BWQ4. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000060558.

Structurei

3D structure databases

ProteinModelPortaliQ8BWQ4.
SMRiQ8BWQ4. Positions 229-317.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini109 – 322214Adrift-type SAM-dependent 2'-O-MTasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Adrift-type SAM-dependent 2'-O-MTase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3674. Eukaryota.
ENOG410XQ0Z. LUCA.
GeneTreeiENSGT00530000063742.
HOGENOMiHOG000112666.
HOVERGENiHBG098139.
InParanoidiQ8BWQ4.
KOiK14590.
OMAiLQFVPME.
OrthoDBiEOG7H1JJX.
PhylomeDBiQ8BWQ4.
TreeFamiTF314897.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025807. Adrift-typ_MeTrfase.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01728. FtsJ. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51614. SAM_MT_ADRIFT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BWQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKRRKLPAR QPACLETFSP DVLNDVSELF AKSFSYRKPL DNEWQLPAPT
60 70 80 90 100
ESFSCGHLEF RALLDLKNSL NEVKNLLSDK KLDEWHRHTA FTNKAGKIIS
110 120 130 140 150
HVKKAVNAEL CTQAWCKFQE ILCSFPLIPQ EAFQSGRLNS LHLCEAPGAF
160 170 180 190 200
IASLNHYLKS HRFPCEWSWV ANSLNPYHEA NDNLRMITDD RLMANTLHCW
210 220 230 240 250
YFGPDNTGDI MTLKYLTGLQ DFLSGMSPIH LVTADGSFDC QGNPGEQEAL
260 270 280 290 300
VSSLHYCEAV TALITLGDGG SFVLKMFTLF EHCSVNLMYL LNCSFDQVHV
310 320 330 340 350
FKPATSKAGN SEVYVVCLRY KGREAVQPLL SRMVLNFGTE MTRKALFPHH
360 370 380 390 400
VIPKSFLERH EECCTFFHRY QLETISENIR LFESMGTGEQ ERLNNLRDCA
410 420 430 440 450
VQYFMQKFQL KPLSRNHWLV KKSNIGCSMN TKWFGQRNKY FKTYNERKMM
460 470 480 490 500
ETLSWKDKVA KGYFNSWAEE HTVYHPGQNS LLEGTASSLE YQSWQVLEGK
510 520 530 540 550
KLPKVKCSPF CDGEILKTLN EAIEKSLGEA LSVDAKVSSK QQYRCCPVFS
560 570 580 590 600
EESVLSELLR LTKCLPDEQG AEPSGPVKCL LVGSPAVCDL QMPAPLEIQL
610 620 630 640 650
VESVELTAFS CSLLHDGDPA YQHLFLDCLL HSLRRLHRGD VMVLPILSCF
660 670 680 690 700
TRFMAGLTFV LHGCFRFITF SCPTSLEPLR TCAVLLCIGY QNLPDAVFQF
710 720 730 740 750
LQNVHDLLSK LLHPSAPRQI LQFLPMEALL QGTLLDFLWD LNAAIAKRHL
760
HLIIQGERDQ AIGSLEL
Length:767
Mass (Da):87,143
Last modified:March 1, 2003 - v1
Checksum:iDB08D0490B89F22B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081A → T in AAH25546 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050315 mRNA. Translation: BAC34184.1.
AK158368 mRNA. Translation: BAE34476.1.
BC025546 mRNA. Translation: AAH25546.1.
CCDSiCCDS22662.1.
RefSeqiNP_666327.2. NM_146215.4.
XP_006530979.1. XM_006530916.2.
XP_006530980.1. XM_006530917.2.
UniGeneiMm.275341.

Genome annotation databases

EnsembliENSMUST00000056972; ENSMUSP00000060558; ENSMUSG00000046441.
GeneIDi234728.
KEGGimmu:234728.
UCSCiuc009nkp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050315 mRNA. Translation: BAC34184.1.
AK158368 mRNA. Translation: BAE34476.1.
BC025546 mRNA. Translation: AAH25546.1.
CCDSiCCDS22662.1.
RefSeqiNP_666327.2. NM_146215.4.
XP_006530979.1. XM_006530916.2.
XP_006530980.1. XM_006530917.2.
UniGeneiMm.275341.

3D structure databases

ProteinModelPortaliQ8BWQ4.
SMRiQ8BWQ4. Positions 229-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000060558.

PTM databases

iPTMnetiQ8BWQ4.
PhosphoSiteiQ8BWQ4.

Proteomic databases

EPDiQ8BWQ4.
MaxQBiQ8BWQ4.
PaxDbiQ8BWQ4.
PeptideAtlasiQ8BWQ4.
PRIDEiQ8BWQ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056972; ENSMUSP00000060558; ENSMUSG00000046441.
GeneIDi234728.
KEGGimmu:234728.
UCSCiuc009nkp.2. mouse.

Organism-specific databases

CTDi55783.
MGIiMGI:2384580. Cmtr2.

Phylogenomic databases

eggNOGiKOG3674. Eukaryota.
ENOG410XQ0Z. LUCA.
GeneTreeiENSGT00530000063742.
HOGENOMiHOG000112666.
HOVERGENiHBG098139.
InParanoidiQ8BWQ4.
KOiK14590.
OMAiLQFVPME.
OrthoDBiEOG7H1JJX.
PhylomeDBiQ8BWQ4.
TreeFamiTF314897.

Miscellaneous databases

PROiQ8BWQ4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BWQ4.
ExpressionAtlasiQ8BWQ4. baseline and differential.
GenevisibleiQ8BWQ4. MM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025807. Adrift-typ_MeTrfase.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01728. FtsJ. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51614. SAM_MT_ADRIFT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Inner ear and Liver.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiCMTR2_MOUSE
AccessioniPrimary (citable) accession number: Q8BWQ4
Secondary accession number(s): Q3TYT6, Q8R3E7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.