Q8N1G2 (MTR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1
EC=2.1.1.57

Alternative name(s):
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:	FTSJD2
Synonyms:	KIAA0082, MTR1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	835 AA.
Sequence status	Complete.
Protein existence	Evidence 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 to produce m7GpppNmp (cap1). Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway. Ref.9 Ref.12
Catalytic activity	S-adenosyl-L-methionine + m7G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA.
Subunit structure	Interacts with POLR2A (via C-terminus). Ref.9
Subcellular location	Nucleus Ref.9.
Induction	By interferons alpha and beta, and by Vaccinia virus infection. Ref.6 Ref.7 Ref.9
Sequence similarities	Belongs to the methyltransferase superfamily. RrmJ family. Contains 1 G-patch domain. Contains 1 WW domain.
Sequence caution	The sequence BAA07893.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	mRNA capping mRNA processing
Cellular component	Nucleus
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	7-methylguanosine mRNA capping Inferred from mutant phenotype Ref.12. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular_function	mRNA (nucleoside-2'-O-)-methyltransferase activity Inferred from direct assay Ref.12. Source: UniProtKB nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 835	835	Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1		PRO_0000251239
Regions
	Domain	87 – 133	47	G-patch
	Domain	752 – 786	35	WW
	Region	727 – 835	109	Interaction with POLR2A
Sites
	Active site	404	1	Proton acceptor By similarity
	Binding site	281	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	311	1	S-adenosyl-L-methionine By similarity
	Binding site	364	1	S-adenosyl-L-methionine By similarity
Amino acid modifications
	Modified residue	28	1	Phosphoserine By similarity
	Modified residue	31	1	Phosphoserine By similarity
	Modified residue	108	1	N6-acetyllysine Ref.11
Experimental info
	Sequence conflict	795	1	Y → H in BAF85253. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8N1G2 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 03919512A73C30FB	FASTA	835	95,321
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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, MASS SPECTROMETRY.
[12]	"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.
[13]	"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.
[14]	"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].

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.
IPI	IPI00166153.
RefSeq	NP_055865.1. NM_015050.2.
UniGene	Hs.520102.
3D structure databases
ProteinModelPortal	Q8N1G2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8N1G2. 1 interaction.
STRING	9606.ENSP00000362550.
PTM databases
PhosphoSite	Q8N1G2.
Polymorphism databases
DMDM	74750894.
Proteomic databases
PaxDb	Q8N1G2.
PeptideAtlas	Q8N1G2.
PRIDE	Q8N1G2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000373451; ENSP00000362550; ENSG00000137200.
GeneID	23070.
KEGG	hsa:23070.
UCSC	uc003ons.3. human.
Organism-specific databases
CTD	23070.
GeneCards	GC06P037400.
HGNC	HGNC:21077. FTSJD2.
HPA	HPA029954. HPA029979. HPA029980.
neXtProt	NX_Q8N1G2.
PharmGKB	PA162389052.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG319576.
HOGENOM	HOG000021970.
HOVERGEN	HBG057271.
InParanoid	Q8N1G2.
KO	K14589.
OMA	SRLFWEW.
OrthoDB	EOG45X7VF.
PhylomeDB	Q8N1G2.
Gene expression databases
ArrayExpress	Q8N1G2.
Bgee	Q8N1G2.
CleanEx	HS_FTSJD2.
Genevestigator	Q8N1G2.
GermOnline	ENSG00000137200. Homo sapiens.
Family and domain databases
InterPro	IPR025816. Cap_mRNA_MeTrfase_1. IPR000467. G_patch_dom. IPR002877. rRNA_MeTrfase_FtsJ_dom. IPR001202. WW_dom. [Graphical view]
Pfam	PF01728. FtsJ. 1 hit. PF01585. G-patch. 1 hit. [Graphical view]
SMART	SM00443. G_patch. 1 hit. SM00456. WW. 1 hit. [Graphical view]
PROSITE	PS50174. G_PATCH. 1 hit. PS01159. WW_DOMAIN_1. 1 hit. PS50020. WW_DOMAIN_2. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	FTSJD2. human.
GenomeRNAi	23070.
NextBio	44167.

Entry information

Entry name

MTR1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.