Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8IYT2

- CMTR2_HUMAN

UniProt

Q8IYT2 - CMTR2_HUMAN

Protein

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

Gene

CMTR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 2 (24 Nov 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.1 Publication

    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).1 Publication

    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 acceptor1 Publication

    GO - Molecular functioni

    1. mRNA (nucleoside-2'-O-)-methyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. 7-methylguanosine mRNA capping Source: UniProtKB
    2. cap2 mRNA methylation Source: UniProtKB

    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:
    HMTr2
    Short name:
    MTr2
    FtsJ methyltransferase domain-containing protein 1
    Protein adrift homolog
    Gene namesi
    Name:CMTR2
    Synonyms:AFT, FTSJD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:25635. CMTR2.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication. Membrane Curated; Single-pass membrane protein Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. integral component of membrane Source: UniProtKB-KW
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi117 – 1171K → A: Abolishes catalytic activity. 1 Publication
    Mutagenesisi235 – 2351D → A: Abolishes catalytic activity. 1 Publication
    Mutagenesisi275 – 2751K → A: Abolishes catalytic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA162389041.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 770770Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2PRO_0000326180Add
    BLAST

    Proteomic databases

    MaxQBiQ8IYT2.
    PaxDbiQ8IYT2.
    PRIDEiQ8IYT2.

    PTM databases

    PhosphoSiteiQ8IYT2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8IYT2.
    BgeeiQ8IYT2.
    CleanExiHS_FTSJD1.
    GenevestigatoriQ8IYT2.

    Organism-specific databases

    HPAiHPA041700.
    HPA048265.

    Interactioni

    Protein-protein interaction databases

    BioGridi120897. 2 interactions.
    STRINGi9606.ENSP00000337512.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IYT2.
    SMRiQ8IYT2. Positions 208-317, 623-730.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei642 – 66221HelicalSequence AnalysisAdd
    BLAST

    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

    eggNOGiNOG311388.
    HOVERGENiHBG098139.
    InParanoidiQ8IYT2.
    KOiK14590.
    OMAiLQFVPME.
    OrthoDBiEOG7H1JJX.
    PhylomeDBiQ8IYT2.
    TreeFamiTF314897.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q8IYT2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKCRKTPVQ QLASPASFSP DILADIFELF AKNFSYGKPL NNEWQLPDPS    50
    EIFTCDHTEL NAFLDLKNSL NEVKNLLSDK KLDEWHEHTA FTNKAGKIIS 100
    HVRKSVNAEL CTQAWCKFHE ILCSFPLIPQ EAFQNGKLNS LHLCEAPGAF 150
    IASLNHYLKS HRFPCHWSWV ANTLNPYHEA NDDLMMIMDD RLIANTLHWW 200
    YFGPDNTGDI MTLKFLTGLQ NFISSMATVH LVTADGSFDC QGNPGEQEAL 250
    VSSLHYCEVV TALTTLGNGG SFVLKMFTMF EHCSINLMYL LNCCFDQVHV 300
    FKPATSKAGN SEVYVVCLHY KGREAIHPLL SKMTLNFGTE MKRKALFPHH 350
    VIPDSFLKRH EECCVFFHKY QLETISENIR LFECMGKAEQ EKLNNLRDCA 400
    IQYFMQKFQL KHLSRNNWLV KKSSIGCSTN TKWFGQRNKY FKTYNERKML 450
    EALSWKDKVA KGYFNSWAEE HGVYHPGQSS ILEGTASNLE CHLWHILEGK 500
    KLPKVKCSPF CNGEILKTLN EAIEKSLGGA FNLDSKFRPK QQYSCSCHVF 550
    SEELIFSELC SLTECLQDEQ VVVPSNQIKC LLVGFSTLRN IKMHIPLEVR 600
    LLESAELTTF SCSLLHDGDP TYQRLFLDCL LHSLRELHTG DVMILPVLSC 650
    FTRFMAGLIF VLHSCFRFIT FVCPTSSDPL RTCAVLLCVG YQDLPNPVFR 700
    YLQSVNELLS TLLNSDSPQQ VLQFVPMEVL LKGALLDFLW DLNAAIAKRH 750
    LHFIIQRERE EIINSLQLQN 770
    Length:770
    Mass (Da):88,120
    Last modified:November 24, 2009 - v2
    Checksum:iE5BE4A2B31AE3580
    GO

    Sequence cautioni

    The sequence AAM49718.1 differs from that shown. Reason: Frameshift at position 337.
    The sequence BAA91058.1 differs from that shown. Reason: Frameshift at position 739.
    The sequence BAB14452.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271F → L in AAM49718. 1 PublicationCurated
    Sequence conflicti53 – 531F → Y in AAM49718. 1 PublicationCurated
    Sequence conflicti56 – 561D → E in AAM49718. 1 PublicationCurated
    Sequence conflicti75 – 751N → K in AAM49718. 1 PublicationCurated
    Sequence conflicti85 – 862WH → LD in AAM49718. 1 PublicationCurated
    Sequence conflicti201 – 2022YF → HL in AAM49718. 1 PublicationCurated
    Sequence conflicti222 – 2221F → I in AAM49718. 1 PublicationCurated
    Sequence conflicti317 – 3171C → S in AAM49718. 1 PublicationCurated
    Sequence conflicti683 – 6831C → S in BAA92047. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti60 – 601L → F.2 Publications
    Corresponds to variant rs3096380 [ dbSNP | Ensembl ].
    VAR_039998
    Natural varianti163 – 1631F → Y.1 Publication
    Corresponds to variant rs17853360 [ dbSNP | Ensembl ].
    VAR_039999
    Natural varianti416 – 4161N → S.1 Publication
    Corresponds to variant rs3803704 [ dbSNP | Ensembl ].
    VAR_040000
    Natural varianti608 – 6081T → K.
    Corresponds to variant rs3096381 [ dbSNP | Ensembl ].
    VAR_040001
    Natural varianti753 – 7531F → L.
    Corresponds to variant rs16970857 [ dbSNP | Ensembl ].
    VAR_040002

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK000289 mRNA. Translation: BAA91058.1. Frameshift.
    AK002033 mRNA. Translation: BAA92047.1.
    AK023183 mRNA. Translation: BAB14452.1. Different initiation.
    AK315056 mRNA. Translation: BAG37532.1.
    AC106736 Genomic DNA. No translation available.
    CH471166 Genomic DNA. Translation: EAW59246.1.
    CH471166 Genomic DNA. Translation: EAW59247.1.
    BC034468 mRNA. Translation: AAH34468.1.
    BC035005 mRNA. Translation: AAH35005.1.
    AF458590 mRNA. Translation: AAM49718.1. Frameshift.
    CCDSiCCDS10898.1.
    RefSeqiNP_001093112.1. NM_001099642.1.
    NP_060818.4. NM_018348.5.
    XP_005256103.1. XM_005256046.1.
    XP_005256104.1. XM_005256047.1.
    UniGeneiHs.72782.

    Genome annotation databases

    EnsembliENST00000338099; ENSP00000337512; ENSG00000180917.
    ENST00000434935; ENSP00000411148; ENSG00000180917.
    GeneIDi55783.
    KEGGihsa:55783.
    UCSCiuc002ezy.4. human.

    Polymorphism databases

    DMDMi269849596.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK000289 mRNA. Translation: BAA91058.1 . Frameshift.
    AK002033 mRNA. Translation: BAA92047.1 .
    AK023183 mRNA. Translation: BAB14452.1 . Different initiation.
    AK315056 mRNA. Translation: BAG37532.1 .
    AC106736 Genomic DNA. No translation available.
    CH471166 Genomic DNA. Translation: EAW59246.1 .
    CH471166 Genomic DNA. Translation: EAW59247.1 .
    BC034468 mRNA. Translation: AAH34468.1 .
    BC035005 mRNA. Translation: AAH35005.1 .
    AF458590 mRNA. Translation: AAM49718.1 . Frameshift.
    CCDSi CCDS10898.1.
    RefSeqi NP_001093112.1. NM_001099642.1.
    NP_060818.4. NM_018348.5.
    XP_005256103.1. XM_005256046.1.
    XP_005256104.1. XM_005256047.1.
    UniGenei Hs.72782.

    3D structure databases

    ProteinModelPortali Q8IYT2.
    SMRi Q8IYT2. Positions 208-317, 623-730.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120897. 2 interactions.
    STRINGi 9606.ENSP00000337512.

    PTM databases

    PhosphoSitei Q8IYT2.

    Polymorphism databases

    DMDMi 269849596.

    Proteomic databases

    MaxQBi Q8IYT2.
    PaxDbi Q8IYT2.
    PRIDEi Q8IYT2.

    Protocols and materials databases

    DNASUi 55783.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338099 ; ENSP00000337512 ; ENSG00000180917 .
    ENST00000434935 ; ENSP00000411148 ; ENSG00000180917 .
    GeneIDi 55783.
    KEGGi hsa:55783.
    UCSCi uc002ezy.4. human.

    Organism-specific databases

    CTDi 55783.
    GeneCardsi GC16M071315.
    HGNCi HGNC:25635. CMTR2.
    HPAi HPA041700.
    HPA048265.
    neXtProti NX_Q8IYT2.
    PharmGKBi PA162389041.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG311388.
    HOVERGENi HBG098139.
    InParanoidi Q8IYT2.
    KOi K14590.
    OMAi LQFVPME.
    OrthoDBi EOG7H1JJX.
    PhylomeDBi Q8IYT2.
    TreeFami TF314897.

    Miscellaneous databases

    ChiTaRSi FTSJD1. human.
    GenomeRNAii 55783.
    NextBioi 60871.
    PROi Q8IYT2.

    Gene expression databases

    ArrayExpressi Q8IYT2.
    Bgeei Q8IYT2.
    CleanExi HS_FTSJD1.
    Genevestigatori Q8IYT2.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR025807. Adrift_MeTrfase.
    IPR002877. rRNA_MeTrfase_FtsJ_dom.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF01728. FtsJ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51614. SAM_MT_ADRIFT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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], VARIANTS PHE-60 AND SER-416.
      Tissue: Placenta and Trachea.
    2. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PHE-60.
    4. "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], VARIANT TYR-163.
      Tissue: Testis.
    5. Zan Q., Guo J.H., Yu L.
      Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-343.
      Tissue: Testis.
    6. "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-117; ASP-235 AND LYS-275.

    Entry informationi

    Entry nameiCMTR2_HUMAN
    AccessioniPrimary (citable) accession number: Q8IYT2
    Secondary accession number(s): B2RCD5
    , D3DWS1, Q8NE77, Q8NFR5, Q9H8Z4, Q9NUS3, Q9NXF5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 81 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3