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Protein

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1

Gene

Cmtr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m7GpppG-capped mRNA and small nuclear RNA (snRNA) to produce m7GpppRm (cap1). Displays a preference for cap0 transcripts. Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei280 – 2801S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Binding sitei310 – 3101S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei363 – 3631S-adenosyl-L-methioninePROSITE-ProRule annotation
Active sitei403 – 4031Proton 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 1 (EC:2.1.1.57)
Alternative name(s):
Cap methyltransferase 1
Cap1 2'O-ribose methyltransferase 1
Short name:
MTr1
FtsJ methyltransferase domain-containing protein 2
Gene namesi
Name:Cmtr1
Synonyms:Ftsjd2, Kiaa0082
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1921407. Cmtr1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 837837Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1PRO_0000251240Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271PhosphoserineCombined sources
Modified residuei30 – 301PhosphoserineCombined sources
Modified residuei52 – 521PhosphoserineBy similarity
Modified residuei90 – 901PhosphoserineBy similarity
Modified residuei107 – 1071N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9DBC3.
MaxQBiQ9DBC3.
PaxDbiQ9DBC3.
PeptideAtlasiQ9DBC3.
PRIDEiQ9DBC3.

PTM databases

iPTMnetiQ9DBC3.
PhosphoSiteiQ9DBC3.

Expressioni

Gene expression databases

BgeeiQ9DBC3.
CleanExiMM_1300018I05RIK.
ExpressionAtlasiQ9DBC3. baseline.
GenevisibleiQ9DBC3. MM.

Interactioni

Subunit structurei

Interacts with POLR2A (via C-terminus).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024816.

Structurei

3D structure databases

ProteinModelPortaliQ9DBC3.
SMRiQ9DBC3. Positions 140-546.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini86 – 13247G-patchPROSITE-ProRule annotationAdd
BLAST
Domaini230 – 449220RrmJ-type SAM-dependent 2'-O-MTasePROSITE-ProRule annotationAdd
BLAST
Domaini751 – 78535WWPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni726 – 834109Interaction with POLR2ABy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 G-patch domain.PROSITE-ProRule annotation
Contains 1 RrmJ-type SAM-dependent 2'-O-MTase domain.PROSITE-ProRule annotation
Contains 1 WW domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3673. Eukaryota.
ENOG410XP08. LUCA.
GeneTreeiENSGT00530000063742.
HOVERGENiHBG057271.
InParanoidiQ9DBC3.
KOiK14589.
OMAiSRLFWEW.
OrthoDBiEOG78D7JK.
PhylomeDBiQ9DBC3.
TreeFamiTF314897.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR030376. Cap_mRNA_MeTrfase_1.
IPR000467. G_patch_dom.
IPR025816. RrmJ-type_MeTrfase.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
IPR001202. WW_dom.
[Graphical view]
PANTHERiPTHR16121:SF0. PTHR16121:SF0. 1 hit.
PfamiPF01728. FtsJ. 1 hit.
PF01585. G-patch. 1 hit.
[Graphical view]
SMARTiSM00443. G_patch. 1 hit.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS50174. G_PATCH. 1 hit.
PS51613. SAM_MT_RRMJ. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DBC3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRRTDPECT APLKKQKRIG ELARHLSSTS DDEPLSSVNH AAKASATSLS
60 70 80 90 100
GSDSETEGKQ PCSDDFKDAF KADSLVEGTS SRYSMYNSVS QRLMAKMGFR
110 120 130 140 150
EGEGLGKYSQ GRKDIVETSN QKGRRGLGLT LQGFDQELNV DWRDEPEPNA
160 170 180 190 200
CEQVSWFPEC TTEIPDSREM SDWMVVGKRK MVIEDETEFC GEELLHSMLK
210 220 230 240 250
CKSVFDILDG EEMRRARTRA NPYEMIRGVF FLNRAAMKMA NMDFVFDRMF
260 270 280 290 300
TNPLDSSGKP LLKESDIDLL YFADVCAGPG GFSEYVLWRK KWHAKGFGMT
310 320 330 340 350
LKGPNDFKLE DFYSASSELF EPYYGEGGVD GDGDITRPEN INAFRNFVLD
360 370 380 390 400
NTDRKGVHFV MADGGFSVEG QENLQEILSK QLLLCQFLMA LSVVRTGGHF
410 420 430 440 450
VCKTFDLFTP FSVGLIYLLY CCFERVCLFK PITSRPANSE RYVVCKGLKV
460 470 480 490 500
GIDDVREYLF SVNIKLNQLR NTESDVNLVV PLMVIKGDHE FNDYMIRSNE
510 520 530 540 550
SYCSLQIKAL AKIHAFVQDT TLSEPRQAEI RKECLQLWKI PDQARVAPSS
560 570 580 590 600
SDPKFKFFEL IKDTDINIFS YKPTLLTAKT LEKIRPVLEY RCMVSGSEQK
610 620 630 640 650
FLLGLGKSQI YTWDGRQSDR WVKLDLKTEL PRDTLLCVEI VHELKGEGKA
660 670 680 690 700
QRKISAIHIL DVLVLNGSDV REQHFNQRIQ LAEKFVKAVS KPSRPDMNPI
710 720 730 740 750
RVKEVYRLEE MEKIFVRLEM KLIKGSGGTP KLSYTGRDDR HFVPTGVYIV
760 770 780 790 800
RTVNEPWTMG FSKSNNRKFF YNKKTQKSVY ALPTESIAPF HTCYYSRLFW
810 820 830
EWGDGFHMRD SQKPQDPDKL SKEDVLSFIQ SHNPLGP
Length:837
Mass (Da):95,676
Last modified:June 1, 2001 - v1
Checksum:i8DB980D2FFA4F9C7
GO

Sequence cautioni

The sequence BAD32161.1 differs from that shown. Reason: Frameshift at position 532. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti151 – 1511C → W in BAE32821 (PubMed:16141072).Curated
Sequence conflicti378 – 3781L → F in BAE31091 (PubMed:16141072).Curated
Sequence conflicti378 – 3781L → F in BAE31230 (PubMed:16141072).Curated
Sequence conflicti459 – 4591L → I in BAE31091 (PubMed:16141072).Curated
Sequence conflicti459 – 4591L → I in BAE31230 (PubMed:16141072).Curated
Sequence conflicti500 – 5001E → V in BAE31091 (PubMed:16141072).Curated
Sequence conflicti500 – 5001E → V in BAE31230 (PubMed:16141072).Curated
Sequence conflicti689 – 6891V → I in BAC33600 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005044 mRNA. Translation: BAB23771.1.
AK042060 mRNA. Translation: BAC31146.1.
AK043733 mRNA. Translation: BAC31634.1.
AK049190 mRNA. Translation: BAC33600.1.
AK080379 mRNA. Translation: BAC37899.1.
AK150392 mRNA. Translation: BAE29520.1.
AK151194 mRNA. Translation: BAE30191.1.
AK152276 mRNA. Translation: BAE31091.1.
AK152452 mRNA. Translation: BAE31230.1.
AK152799 mRNA. Translation: BAE31504.1.
AK153021 mRNA. Translation: BAE31655.1.
AK153066 mRNA. Translation: BAE31692.1.
AK154773 mRNA. Translation: BAE32821.1.
BC024691 mRNA. Translation: AAH24691.1.
AK172883 Transcribed RNA. Translation: BAD32161.1. Frameshift.
CCDSiCCDS37539.1.
RefSeqiNP_083067.1. NM_028791.6.
UniGeneiMm.390979.
Mm.397786.
Mm.475060.

Genome annotation databases

EnsembliENSMUST00000024816; ENSMUSP00000024816; ENSMUSG00000024019.
GeneIDi74157.
KEGGimmu:74157.
UCSCiuc008bth.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005044 mRNA. Translation: BAB23771.1.
AK042060 mRNA. Translation: BAC31146.1.
AK043733 mRNA. Translation: BAC31634.1.
AK049190 mRNA. Translation: BAC33600.1.
AK080379 mRNA. Translation: BAC37899.1.
AK150392 mRNA. Translation: BAE29520.1.
AK151194 mRNA. Translation: BAE30191.1.
AK152276 mRNA. Translation: BAE31091.1.
AK152452 mRNA. Translation: BAE31230.1.
AK152799 mRNA. Translation: BAE31504.1.
AK153021 mRNA. Translation: BAE31655.1.
AK153066 mRNA. Translation: BAE31692.1.
AK154773 mRNA. Translation: BAE32821.1.
BC024691 mRNA. Translation: AAH24691.1.
AK172883 Transcribed RNA. Translation: BAD32161.1. Frameshift.
CCDSiCCDS37539.1.
RefSeqiNP_083067.1. NM_028791.6.
UniGeneiMm.390979.
Mm.397786.
Mm.475060.

3D structure databases

ProteinModelPortaliQ9DBC3.
SMRiQ9DBC3. Positions 140-546.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024816.

PTM databases

iPTMnetiQ9DBC3.
PhosphoSiteiQ9DBC3.

Proteomic databases

EPDiQ9DBC3.
MaxQBiQ9DBC3.
PaxDbiQ9DBC3.
PeptideAtlasiQ9DBC3.
PRIDEiQ9DBC3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024816; ENSMUSP00000024816; ENSMUSG00000024019.
GeneIDi74157.
KEGGimmu:74157.
UCSCiuc008bth.1. mouse.

Organism-specific databases

CTDi23070.
MGIiMGI:1921407. Cmtr1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG3673. Eukaryota.
ENOG410XP08. LUCA.
GeneTreeiENSGT00530000063742.
HOVERGENiHBG057271.
InParanoidiQ9DBC3.
KOiK14589.
OMAiSRLFWEW.
OrthoDBiEOG78D7JK.
PhylomeDBiQ9DBC3.
TreeFamiTF314897.

Miscellaneous databases

PROiQ9DBC3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBC3.
CleanExiMM_1300018I05RIK.
ExpressionAtlasiQ9DBC3. baseline.
GenevisibleiQ9DBC3. MM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR030376. Cap_mRNA_MeTrfase_1.
IPR000467. G_patch_dom.
IPR025816. RrmJ-type_MeTrfase.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
IPR001202. WW_dom.
[Graphical view]
PANTHERiPTHR16121:SF0. PTHR16121:SF0. 1 hit.
PfamiPF01728. FtsJ. 1 hit.
PF01585. G-patch. 1 hit.
[Graphical view]
SMARTiSM00443. G_patch. 1 hit.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS50174. G_PATCH. 1 hit.
PS51613. SAM_MT_RRMJ. 1 hit.
PS50020. WW_DOMAIN_2. 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 and NOD.
    Tissue: Brain cortex, Dendritic cell, Embryonic stem cell, Liver, Macrophage and Thymus.
  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].
    Tissue: Mammary tumor.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. 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."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-837.
    Tissue: Embryonic tail.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiCMTR1_MOUSE
AccessioniPrimary (citable) accession number: Q9DBC3
Secondary accession number(s): Q3U3G5
, Q3U7Y9, Q6A0D5, Q8C7V0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 114 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.