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Q8N1G2 (CMTR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Short name=hMTr1
FtsJ methyltransferase domain-containing protein 2
Interferon-stimulated gene 95 kDa protein
Short name=ISG95
Gene names
Name:CMTR1
Synonyms:FTSJD2, KIAA0082, MTR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length835 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.13 Ref.16

Catalytic activity

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). Ref.16

Subunit structure

Interacts with POLR2A (via C-terminus). Ref.9

Subcellular location

Nucleus Ref.9 Ref.16.

Induction

By interferons alpha and beta, and by Vaccinia virus infection. Ref.6 Ref.7 Ref.9

Sequence similarities

Contains 1 G-patch domain.

Contains 1 RrmJ-type SAM-dependent 2'-O-MTase domain.

Contains 1 WW domain.

Sequence caution

The sequence BAA07893.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 835835Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1
PRO_0000251239

Regions

Domain87 – 13347G-patch
Domain231 – 450220RrmJ-type SAM-dependent 2'-O-MTase
Domain752 – 78635WW
Region727 – 835109Interaction with POLR2A

Sites

Active site4041Proton acceptor Probable
Binding site2811S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site3111S-adenosyl-L-methionine By similarity
Binding site3641S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue281Phosphoserine By similarity
Modified residue311Phosphoserine By similarity
Modified residue1081N6-acetyllysine Ref.12

Experimental info

Mutagenesis2391K → A: Abolishes catalytic activity. Ref.16
Mutagenesis3641D → A: Abolishes catalytic activity. Ref.16
Mutagenesis4041K → A: Abolishes catalytic activity. Ref.16
Sequence conflict7951Y → H in BAF85253. Ref.3

Secondary structure

.................................................................. 835
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8N1G2 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 03919512A73C30FB

FASTA83595,321
        10         20         30         40         50         60 
MKRRTDPECT APIKKQKKRV AELALSLSST SDDEPPSSVS HGAKASTTSL SGSDSETEGK 

        70         80         90        100        110        120 
QHSSDSFDDA FKADSLVEGT SSRYSMYNSV SQKLMAKMGF REGEGLGKYS QGRKDIVEAS 

       130        140        150        160        170        180 
SQKGRRGLGL TLRGFDQELN VDWRDEPEPS ACEQVSWFPE CTTEIPDTQE MSDWMVVGKR 

       190        200        210        220        230        240 
KMIIEDETEF CGEELLHSVL QCKSVFDVLD GEEMRRARTR ANPYEMIRGV FFLNRAAMKM 

       250        260        270        280        290        300 
ANMDFVFDRM FTNPRDSYGK PLVKDREAEL LYFADVCAGP GGFSEYVLWR KKWHAKGFGM 

       310        320        330        340        350        360 
TLKGPNDFKL EDFYSASSEL FEPYYGEGGI DGDGDITRPE NISAFRNFVL DNTDRKGVHF 

       370        380        390        400        410        420 
LMADGGFSVE GQENLQEILS KQLLLCQFLM ALSIVRTGGH FICKTFDLFT PFSVGLVYLL 

       430        440        450        460        470        480 
YCCFERVCLF KPITSRPANS ERYVVCKGLK VGIDDVRDYL FAVNIKLNQL RNTDSDVNLV 

       490        500        510        520        530        540 
VPLEVIKGDH EFTDYMIRSN ESHCSLQIKA LAKIHAFVQD TTLSEPRQAE IRKECLRLWG 

       550        560        570        580        590        600 
IPDQARVAPS SSDPKSKFFE LIQGTEIDIF SYKPTLLTSK TLEKIRPVFD YRCMVSGSEQ 

       610        620        630        640        650        660 
KFLIGLGKSQ IYTWDGRQSD RWIKLDLKTE LPRDTLLSVE IVHELKGEGK AQRKISAIHI 

       670        680        690        700        710        720 
LDVLVLNGTD VREQHFNQRI QLAEKFVKAV SKPSRPDMNP IRVKEVYRLE EMEKIFVRLE 

       730        740        750        760        770        780 
MKIIKGSSGT PKLSYTGRDD RHFVPMGLYI VRTVNEPWTM GFSKSFKKKF FYNKKTKDST 

       790        800        810        820        830 
FDLPADSIAP FHICYYGRLF WEWGDGIRVH DSQKPQDQDK LSKEDVLSFI QMHRA 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow.
[2]Ohara O., Nagase T., Kikuno R., Nomura N.
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Lung.
[6]"Gene expression profiling of the cellular transcriptional network regulated by alpha/beta interferon and its partial attenuation by the hepatitis C virus nonstructural 5A protein."
Geiss G.K., Carter V.S., He Y., Kwieciszewski B.K., Holzman T., Korth M.J., Lazaro C.A., Fausto N., Bumgarner R.E., Katze M.G.
J. Virol. 77:6367-6375(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY INTERFERONS ALPHA AND BETA.
[7]"Cellular gene expression survey of vaccinia virus infection of human HeLa cells."
Guerra S., Lopez-Fernandez L.A., Pascual-Montano A., Munoz M., Harshman K., Esteban M.
J. Virol. 77:6493-6506(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY VIRAL INFECTION.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"The human interferon-regulated ISG95 protein interacts with RNA polymerase II and shows methyltransferase activity."
Haline-Vaz T., Silva T.C.L., Zanchin N.I.T.
Biochem. Biophys. Res. Commun. 372:719-724(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH POLR2A, SUBCELLULAR LOCATION, INDUCTION.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Characterization of hMTr1, a human Cap1 2'-O-Ribose methyltransferase."
Belanger F., Stepinski J., Darzynkiewicz E., Pelletier J.
J. Biol. Chem. 285:33037-33044(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"2'-O-ribose methylation of cap2 in human: function and evolution in a horizontally mobile family."
Werner M., Purta E., Kaminska K.H., Cymerman I.A., Campbell D.A., Mittra B., Zamudio J.R., Sturm N.R., Jaworski J., Bujnicki J.M.
Nucleic Acids Res. 39:4756-4768(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-239; ASP-364 AND LYS-404.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D43949 mRNA. Translation: BAA07893.2. Different initiation.
AK292564 mRNA. Translation: BAF85253.1.
AL353597 Genomic DNA. Translation: CAI19603.1.
BC010731 mRNA. Translation: AAH10731.2.
BC031890 mRNA. Translation: AAH31890.1.
CCDSCCDS4835.1.
RefSeqNP_055865.1. NM_015050.2.
UniGeneHs.520102.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4N48X-ray2.70A/B126-550[»]
4N49X-ray1.90A126-550[»]
4N4AX-ray2.35A126-550[»]
ProteinModelPortalQ8N1G2.
SMRQ8N1G2. Positions 141-547.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116703. 2 interactions.
IntActQ8N1G2. 2 interactions.
STRING9606.ENSP00000362550.

PTM databases

PhosphoSiteQ8N1G2.

Polymorphism databases

DMDM74750894.

Proteomic databases

MaxQBQ8N1G2.
PaxDbQ8N1G2.
PeptideAtlasQ8N1G2.
PRIDEQ8N1G2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373451; ENSP00000362550; ENSG00000137200.
GeneID23070.
KEGGhsa:23070.
UCSCuc003ons.3. human.

Organism-specific databases

CTD23070.
GeneCardsGC06P037401.
HGNCHGNC:21077. CMTR1.
HPAHPA029954.
HPA029979.
HPA029980.
neXtProtNX_Q8N1G2.
PharmGKBPA162389052.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG319576.
HOGENOMHOG000021970.
HOVERGENHBG057271.
InParanoidQ8N1G2.
KOK14589.
OMASRLFWEW.
OrthoDBEOG78D7JK.
PhylomeDBQ8N1G2.
TreeFamTF314897.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000137200-MONOMER.

Gene expression databases

ArrayExpressQ8N1G2.
BgeeQ8N1G2.
CleanExHS_FTSJD2.
GenevestigatorQ8N1G2.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR025816. Cap_mRNA_MeTrfase_1.
IPR000467. G_patch_dom.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases-like.
IPR001202. WW_dom.
[Graphical view]
PfamPF01728. FtsJ. 1 hit.
PF01585. G-patch. 1 hit.
[Graphical view]
SMARTSM00443. G_patch. 1 hit.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS50174. G_PATCH. 1 hit.
PS51613. SAM_MT_RRMJ. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFTSJD2. human.
GenomeRNAi23070.
NextBio44167.
PROQ8N1G2.

Entry information

Entry nameCMTR1_HUMAN
AccessionPrimary (citable) accession number: Q8N1G2
Secondary accession number(s): A8K949, Q14670, Q96FJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM