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Q8C3P7

- MTA70_MOUSE

UniProt

Q8C3P7 - MTA70_MOUSE

Protein

N6-adenosine-methyltransferase subunit METTL3

Gene

Mettl3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (25 Jul 2003)
      Previous versions | rss
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    Functioni

    N6-methyltransferase that methylates adenosine residues of some mRNAs and acts as a regulator of the circadian clock and self-renewal of embryonic stem cells. N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in the efficiency of mRNA splicing and processing and mRNA stability. M6A regulates the length of the circadian clock: acts as a early pace-setter in the circadian loop by putting mRNA production on a fast-track for facilitating nuclear processing, thereby providing an early point of control in setting the dynamics of the feedback loop. M6A also acts as a regulator of mRNA stability: in embryonic stem cells (ESCs), m6A methylation of mRNAs encoding developmental regulators, results in transcript destabilization, maintaining the groung state of ESCs, thereby promoting self-renewal of ESCs.2 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + m7G(5')pppAm = S-adenosyl-L-homocysteine + m7G(5')pppm6Am.1 Publication

    GO - Molecular functioni

    1. mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity Source: UniProtKB
    2. mRNA (N6-adenosine)-methyltransferase activity Source: MGI
    3. protein binding Source: UniProtKB
    4. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. circadian rhythm Source: UniProtKB
    2. mRNA destabilization Source: UniProtKB
    3. mRNA methylation Source: UniProtKB
    4. mRNA modification Source: MGI
    5. mRNA processing Source: UniProtKB
    6. RNA methylation Source: UniProtKB
    7. stem cell maintenance Source: UniProtKB

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Biological rhythms

    Keywords - Ligandi

    RNA-binding, S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N6-adenosine-methyltransferase subunit METTL3 (EC:2.1.1.62)
    Alternative name(s):
    Methyltransferase-like protein 3
    N6-adenosine-methyltransferase 70 kDa subunit
    Short name:
    MT-A70
    Gene namesi
    Name:Mettl3
    Synonyms:Mta70
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1927165. Mettl3.

    Subcellular locationi

    Nucleus speckle By similarity
    Note: Colocalizes with speckles in interphase nuclei. Suggesting that it may be associated with nuclear pre-mRNA splicing components By similarity.By similarity

    GO - Cellular componenti

    1. MIS complex Source: UniProtKB
    2. nuclear speck Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi395 – 3984DPPW → APPA: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 580579N6-adenosine-methyltransferase subunit METTL3PRO_0000207631Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei43 – 431PhosphoserineBy similarity
    Modified residuei219 – 2191PhosphoserineBy similarity
    Modified residuei243 – 2431PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ8C3P7.
    PRIDEiQ8C3P7.

    PTM databases

    PhosphoSiteiQ8C3P7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8C3P7.
    BgeeiQ8C3P7.
    CleanExiMM_METTL3.
    GenevestigatoriQ8C3P7.

    Interactioni

    Subunit structurei

    Component of the WMM complex, a N6-methyltransferase complex composed of WTAP, METTL3 and METTL14.

    Protein-protein interaction databases

    BioGridi207910. 1 interaction.
    DIPiDIP-60724N.
    IntActiQ8C3P7. 1 interaction.
    MINTiMINT-4102524.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C3P7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the MT-A70-like family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG4725.
    GeneTreeiENSGT00550000075058.
    HOGENOMiHOG000012669.
    HOVERGENiHBG052521.
    InParanoidiQ8C3P7.
    KOiK05925.
    OrthoDBiEOG7PZRWV.
    PhylomeDBiQ8C3P7.
    TreeFamiTF323854.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025848. MT-A70.
    IPR007757. MT-A70-like.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF05063. MT-A70. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51143. MT_A70. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8C3P7-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSDTWSSIQA HKKQLDSLRE RLQRRRKQDS GHLDLRNPEA ALSPTFRSDS    50
    PVPTAPTSSG PKPSTTSVAP ELATDPELEK KLLHHLSDLA LTLPTDAVSI 100
    RLAISTPDAP ATQDGVESLL QKFAAQELIE VKRGLLQDDA HPTLVTYADH 150
    SKLSAMMGAV ADKKGLGEVA GTIAGQKRRA EQDLTTVTTF ASSLASGLAS 200
    SASEPAKEPA KKSRKHAASD VDLEIESLLN QQSTKEQQSK KVSQEILELL 250
    NTTTAKEQSI VEKFRSRGRA QVQEFCDYGT KEECMKASDA DRPCRKLHFR 300
    RIINKHTDES LGDCSFLNTC FHMDTCKYVH YEIDACVDSE SPGSKEHMPS 350
    QELALTQSVG GDSSADRLFP PQWICCDIRY LDVSILGKFA VVMADPPWDI 400
    HMELPYGTLT DDEMRRLNIP VLQDDGFLFL WVTGRAMELG RECLNLWGYE 450
    RVDEIIWVKT NQLQRIIRTG RTGHWLNHGK EHCLVGVKGN PQGFNQGLDC 500
    DVIVAEVRST SHKPDEIYGM IERLSPGTRK IELFGRPHNV QPNWITLGNQ 550
    LDGIHLLDPD VVARFKQRYP DGIISKPKNL 580
    Length:580
    Mass (Da):64,616
    Last modified:July 25, 2003 - v2
    Checksum:i0DBDA2392A37A018
    GO
    Isoform 2 (identifier: Q8C3P7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         34-106: Missing.
         241-299: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:448
    Mass (Da):50,157
    Checksum:i95539DAD61854334
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1621D → E in AAD33673. (PubMed:11389549)Curated
    Sequence conflicti162 – 1621D → E in BAC39385. (PubMed:16141072)Curated
    Sequence conflicti471 – 4711R → P in BAB26322. (PubMed:16141072)Curated
    Sequence conflicti475 – 4751W → L in BAB26322. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei34 – 10673Missing in isoform 2. 1 PublicationVSP_007867Add
    BLAST
    Alternative sequencei241 – 29959Missing in isoform 2. 1 PublicationVSP_007868Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF283992 Genomic DNA. Translation: AAG13957.1.
    AF135789 mRNA. Translation: AAD33673.1.
    AK009492 mRNA. Translation: BAB26322.1.
    AK085189 mRNA. Translation: BAC39385.1.
    BC012526 mRNA. Translation: AAH12526.1.
    CCDSiCCDS27053.1. [Q8C3P7-1]
    RefSeqiNP_062695.2. NM_019721.2.
    UniGeneiMm.271759.

    Genome annotation databases

    EnsembliENSMUST00000022767; ENSMUSP00000022767; ENSMUSG00000022160.
    GeneIDi56335.
    KEGGimmu:56335.
    UCSCiuc007tpc.1. mouse. [Q8C3P7-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF283992 Genomic DNA. Translation: AAG13957.1 .
    AF135789 mRNA. Translation: AAD33673.1 .
    AK009492 mRNA. Translation: BAB26322.1 .
    AK085189 mRNA. Translation: BAC39385.1 .
    BC012526 mRNA. Translation: AAH12526.1 .
    CCDSi CCDS27053.1. [Q8C3P7-1 ]
    RefSeqi NP_062695.2. NM_019721.2.
    UniGenei Mm.271759.

    3D structure databases

    ProteinModelPortali Q8C3P7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207910. 1 interaction.
    DIPi DIP-60724N.
    IntActi Q8C3P7. 1 interaction.
    MINTi MINT-4102524.

    PTM databases

    PhosphoSitei Q8C3P7.

    Proteomic databases

    PaxDbi Q8C3P7.
    PRIDEi Q8C3P7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022767 ; ENSMUSP00000022767 ; ENSMUSG00000022160 .
    GeneIDi 56335.
    KEGGi mmu:56335.
    UCSCi uc007tpc.1. mouse. [Q8C3P7-1 ]

    Organism-specific databases

    CTDi 56339.
    MGIi MGI:1927165. Mettl3.

    Phylogenomic databases

    eggNOGi COG4725.
    GeneTreei ENSGT00550000075058.
    HOGENOMi HOG000012669.
    HOVERGENi HBG052521.
    InParanoidi Q8C3P7.
    KOi K05925.
    OrthoDBi EOG7PZRWV.
    PhylomeDBi Q8C3P7.
    TreeFami TF323854.

    Miscellaneous databases

    ChiTaRSi METTL3. mouse.
    NextBioi 312322.
    PROi Q8C3P7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8C3P7.
    Bgeei Q8C3P7.
    CleanExi MM_METTL3.
    Genevestigatori Q8C3P7.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR025848. MT-A70.
    IPR007757. MT-A70-like.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF05063. MT-A70. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51143. MT_A70. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification and cDNA cloning of the AdoMet-binding subunit of the human mRNA (N6-adenosine)-methyltransferase."
      Bokar J.A., Shambaugh M.E., Polayes D., Matera A.G., Rottman F.M.
      RNA 3:1233-1247(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
      Strain: 129/Sv.
    2. "Expression of genes involved in mammalian meiosis during the transition from egg to embryo."
      Hwang S.-Y., Oh B., Knowles B.B., Solter D., Lee J.-S.
      Mol. Reprod. Dev. 59:144-158(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: C57BL/6 X DBA/2.
    3. "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] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Stomach and Tongue.
    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] (ISOFORM 1).
      Tissue: Mammary tumor.
    5. "RNA-methylation-dependent RNA processing controls the speed of the circadian clock."
      Fustin J.M., Doi M., Yamaguchi Y., Hida H., Nishimura S., Yoshida M., Isagawa T., Morioka M.S., Kakeya H., Manabe I., Okamura H.
      Cell 155:793-806(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 395-ASP--TRP-398.
    6. "N-methyladenosine modification destabilizes developmental regulators in embryonic stem cells."
      Wang Y., Li Y., Toth J.I., Petroski M.D., Zhang Z., Zhao J.C.
      Nat. Cell Biol. 16:191-198(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH METTL14.

    Entry informationi

    Entry nameiMTA70_MOUSE
    AccessioniPrimary (citable) accession number: Q8C3P7
    Secondary accession number(s): Q9CV54, Q9ERS9, Q9WUI4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2003
    Last sequence update: July 25, 2003
    Last modified: October 1, 2014
    This is version 92 of the entry and version 2 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

    External Data

    Dasty 3