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Q8N1G2

- CMTR1_HUMAN

UniProt

Q8N1G2 - CMTR1_HUMAN

Protein

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

Gene

CMTR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    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.3 Publications

    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).1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei281 – 2811S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei311 – 3111S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei364 – 3641S-adenosyl-L-methioninePROSITE-ProRule annotation
    Active sitei404 – 4041Proton acceptor1 Publication

    GO - Molecular functioni

    1. mRNA (nucleoside-2'-O-)-methyltransferase activity Source: UniProtKB
    2. nucleic acid binding Source: InterPro

    GO - Biological processi

    1. 7-methylguanosine mRNA capping Source: UniProtKB
    2. cap1 mRNA methylation Source: UniProtKB
    3. mRNA methylation Source: UniProtKB

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    mRNA capping, mRNA processing

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000137200-MONOMER.

    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
    Short name:
    hMTr1
    FtsJ methyltransferase domain-containing protein 2
    Interferon-stimulated gene 95 kDa protein
    Short name:
    ISG95
    Gene namesi
    Name:CMTR1
    Synonyms:FTSJD2, KIAA0082, MTR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21077. CMTR1.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi239 – 2391K → A: Abolishes catalytic activity. 1 Publication
    Mutagenesisi364 – 3641D → A: Abolishes catalytic activity. 1 Publication
    Mutagenesisi404 – 4041K → A: Abolishes catalytic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA162389052.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 835835Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1PRO_0000251239Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei28 – 281PhosphoserineBy similarity
    Modified residuei31 – 311PhosphoserineBy similarity
    Modified residuei108 – 1081N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8N1G2.
    PaxDbiQ8N1G2.
    PeptideAtlasiQ8N1G2.
    PRIDEiQ8N1G2.

    PTM databases

    PhosphoSiteiQ8N1G2.

    Expressioni

    Inductioni

    By interferons alpha and beta, and by Vaccinia virus infection.3 Publications

    Gene expression databases

    ArrayExpressiQ8N1G2.
    BgeeiQ8N1G2.
    CleanExiHS_FTSJD2.
    GenevestigatoriQ8N1G2.

    Organism-specific databases

    HPAiHPA029954.
    HPA029979.
    HPA029980.

    Interactioni

    Subunit structurei

    Interacts with POLR2A (via C-terminus).1 Publication

    Protein-protein interaction databases

    BioGridi116703. 2 interactions.
    IntActiQ8N1G2. 2 interactions.
    STRINGi9606.ENSP00000362550.

    Structurei

    Secondary structure

    1
    835
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi143 – 1464
    Turni168 – 1747
    Beta strandi176 – 1794
    Helixi184 – 1863
    Beta strandi189 – 1913
    Helixi193 – 20412
    Helixi205 – 2084
    Helixi211 – 22111
    Helixi225 – 2273
    Turni228 – 2314
    Beta strandi232 – 2343
    Helixi235 – 24612
    Turni247 – 2526
    Helixi265 – 2673
    Beta strandi271 – 2777
    Helixi282 – 29110
    Beta strandi293 – 3008
    Helixi310 – 3123
    Turni313 – 3164
    Turni318 – 3203
    Beta strandi321 – 3233
    Beta strandi326 – 3283
    Helixi329 – 3313
    Helixi339 – 35113
    Turni352 – 3554
    Beta strandi358 – 3636
    Turni370 – 3723
    Helixi373 – 3753
    Helixi376 – 3794
    Helixi381 – 39414
    Beta strandi395 – 40511
    Helixi411 – 42313
    Beta strandi424 – 4307
    Beta strandi442 – 4498
    Helixi454 – 47017
    Beta strandi473 – 4819
    Helixi483 – 4875
    Helixi490 – 51930
    Helixi528 – 53912

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4N48X-ray2.70A/B126-550[»]
    4N49X-ray1.90A126-550[»]
    4N4AX-ray2.35A126-550[»]
    ProteinModelPortaliQ8N1G2.
    SMRiQ8N1G2. Positions 141-547.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini87 – 13347G-patchPROSITE-ProRule annotationAdd
    BLAST
    Domaini231 – 450220RrmJ-type SAM-dependent 2'-O-MTasePROSITE-ProRule annotationAdd
    BLAST
    Domaini752 – 78635WWAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni727 – 835109Interaction with POLR2AAdd
    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.Curated

    Phylogenomic databases

    eggNOGiNOG319576.
    HOGENOMiHOG000021970.
    HOVERGENiHBG057271.
    InParanoidiQ8N1G2.
    KOiK14589.
    OMAiSRLFWEW.
    OrthoDBiEOG78D7JK.
    PhylomeDBiQ8N1G2.
    TreeFamiTF314897.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025816. Cap_mRNA_MeTrfase_1.
    IPR000467. G_patch_dom.
    IPR002877. rRNA_MeTrfase_FtsJ_dom.
    IPR029063. SAM-dependent_MTases-like.
    IPR001202. WW_dom.
    [Graphical view]
    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.
    PS01159. WW_DOMAIN_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8N1G2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRRTDPECT APIKKQKKRV AELALSLSST SDDEPPSSVS HGAKASTTSL    50
    SGSDSETEGK QHSSDSFDDA FKADSLVEGT SSRYSMYNSV SQKLMAKMGF 100
    REGEGLGKYS QGRKDIVEAS SQKGRRGLGL TLRGFDQELN VDWRDEPEPS 150
    ACEQVSWFPE CTTEIPDTQE MSDWMVVGKR KMIIEDETEF CGEELLHSVL 200
    QCKSVFDVLD GEEMRRARTR ANPYEMIRGV FFLNRAAMKM ANMDFVFDRM 250
    FTNPRDSYGK PLVKDREAEL LYFADVCAGP GGFSEYVLWR KKWHAKGFGM 300
    TLKGPNDFKL EDFYSASSEL FEPYYGEGGI DGDGDITRPE NISAFRNFVL 350
    DNTDRKGVHF LMADGGFSVE GQENLQEILS KQLLLCQFLM ALSIVRTGGH 400
    FICKTFDLFT PFSVGLVYLL YCCFERVCLF KPITSRPANS ERYVVCKGLK 450
    VGIDDVRDYL FAVNIKLNQL RNTDSDVNLV VPLEVIKGDH EFTDYMIRSN 500
    ESHCSLQIKA LAKIHAFVQD TTLSEPRQAE IRKECLRLWG IPDQARVAPS 550
    SSDPKSKFFE LIQGTEIDIF SYKPTLLTSK TLEKIRPVFD YRCMVSGSEQ 600
    KFLIGLGKSQ IYTWDGRQSD RWIKLDLKTE LPRDTLLSVE IVHELKGEGK 650
    AQRKISAIHI LDVLVLNGTD VREQHFNQRI QLAEKFVKAV SKPSRPDMNP 700
    IRVKEVYRLE EMEKIFVRLE MKIIKGSSGT PKLSYTGRDD RHFVPMGLYI 750
    VRTVNEPWTM GFSKSFKKKF FYNKKTKDST FDLPADSIAP FHICYYGRLF 800
    WEWGDGIRVH DSQKPQDQDK LSKEDVLSFI QMHRA 835
    Length:835
    Mass (Da):95,321
    Last modified:October 1, 2002 - v1
    Checksum:i03919512A73C30FB
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti795 – 7951Y → H in BAF85253. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS4835.1.
    RefSeqiNP_055865.1. NM_015050.2.
    UniGeneiHs.520102.

    Genome annotation databases

    EnsembliENST00000373451; ENSP00000362550; ENSG00000137200.
    GeneIDi23070.
    KEGGihsa:23070.
    UCSCiuc003ons.3. human.

    Polymorphism databases

    DMDMi74750894.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS4835.1.
    RefSeqi NP_055865.1. NM_015050.2.
    UniGenei Hs.520102.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4N48 X-ray 2.70 A/B 126-550 [» ]
    4N49 X-ray 1.90 A 126-550 [» ]
    4N4A X-ray 2.35 A 126-550 [» ]
    ProteinModelPortali Q8N1G2.
    SMRi Q8N1G2. Positions 141-547.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116703. 2 interactions.
    IntActi Q8N1G2. 2 interactions.
    STRINGi 9606.ENSP00000362550.

    PTM databases

    PhosphoSitei Q8N1G2.

    Polymorphism databases

    DMDMi 74750894.

    Proteomic databases

    MaxQBi Q8N1G2.
    PaxDbi Q8N1G2.
    PeptideAtlasi Q8N1G2.
    PRIDEi Q8N1G2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373451 ; ENSP00000362550 ; ENSG00000137200 .
    GeneIDi 23070.
    KEGGi hsa:23070.
    UCSCi uc003ons.3. human.

    Organism-specific databases

    CTDi 23070.
    GeneCardsi GC06P037401.
    HGNCi HGNC:21077. CMTR1.
    HPAi HPA029954.
    HPA029979.
    HPA029980.
    neXtProti NX_Q8N1G2.
    PharmGKBi PA162389052.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG319576.
    HOGENOMi HOG000021970.
    HOVERGENi HBG057271.
    InParanoidi Q8N1G2.
    KOi K14589.
    OMAi SRLFWEW.
    OrthoDBi EOG78D7JK.
    PhylomeDBi Q8N1G2.
    TreeFami TF314897.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000137200-MONOMER.

    Miscellaneous databases

    ChiTaRSi FTSJD2. human.
    GenomeRNAii 23070.
    NextBioi 44167.
    PROi Q8N1G2.

    Gene expression databases

    ArrayExpressi Q8N1G2.
    Bgeei Q8N1G2.
    CleanExi HS_FTSJD2.
    Genevestigatori Q8N1G2.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR025816. Cap_mRNA_MeTrfase_1.
    IPR000467. G_patch_dom.
    IPR002877. rRNA_MeTrfase_FtsJ_dom.
    IPR029063. SAM-dependent_MTases-like.
    IPR001202. WW_dom.
    [Graphical view ]
    Pfami PF01728. FtsJ. 1 hit.
    PF01585. G-patch. 1 hit.
    [Graphical view ]
    SMARTi SM00443. G_patch. 1 hit.
    SM00456. WW. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS50174. G_PATCH. 1 hit.
    PS51613. SAM_MT_RRMJ. 1 hit.
    PS01159. WW_DOMAIN_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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.

    Entry informationi

    Entry nameiCMTR1_HUMAN
    AccessioniPrimary (citable) accession number: Q8N1G2
    Secondary accession number(s): A8K949, Q14670, Q96FJ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3