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)

Q3TL26

- TFB2M_MOUSE

UniProt

Q3TL26 - TFB2M_MOUSE

Protein

Dimethyladenosine transferase 2, mitochondrial

Gene

Tfb2m

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (11 Oct 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei74 – 741S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei123 – 1231S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei149 – 1491S-adenosyl-L-methioninePROSITE-ProRule annotation

    GO - Molecular functioni

    1. RNA binding Source: UniProtKB-KW
    2. rRNA (adenine-N6,N6-)-dimethyltransferase activity Source: InterPro
    3. transcription cofactor activity Source: InterPro

    GO - Biological processi

    1. positive regulation of transcription, DNA-templated Source: UniProtKB
    2. transcription initiation from mitochondrial promoter Source: UniProtKB

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    rRNA processing, Transcription, Transcription regulation

    Keywords - Ligandi

    RNA-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    ReactomeiREACT_205251. Transcriptional activation of mitochondrial biogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dimethyladenosine transferase 2, mitochondrial (EC:2.1.1.-)
    Alternative name(s):
    Mitochondrial 12S rRNA dimethylase 2
    Mitochondrial transcription factor B2
    Short name:
    mTFB2M
    Short name:
    mtTFB2
    S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2
    Gene namesi
    Name:Tfb2m
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:107937. Tfb2m.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4343MitochondrionSequence AnalysisAdd
    BLAST
    Chaini44 – 396353Dimethyladenosine transferase 2, mitochondrialPRO_0000273180Add
    BLAST

    Proteomic databases

    PaxDbiQ3TL26.
    PRIDEiQ3TL26.

    PTM databases

    PhosphoSiteiQ3TL26.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    BgeeiQ3TL26.
    CleanExiMM_TFB2M.
    GenevestigatoriQ3TL26.

    Interactioni

    Subunit structurei

    Interacts with mitochondrial RNA polymerase POLRMT. Interacts with TFAM By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ3TL26.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. KsgA subfamily.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0030.
    GeneTreeiENSGT00510000048533.
    HOGENOMiHOG000060174.
    HOVERGENiHBG094037.
    InParanoidiQ3TL26.
    KOiK17653.
    OMAiLLMMIKQ.
    OrthoDBiEOG7RNK0M.
    PhylomeDBiQ3TL26.
    TreeFamiTF325100.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR016861. Mt_di-Me-Ado_Trfase_2_prcur.
    IPR001737. rRNA_Ade_methylase_transferase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PANTHERiPTHR11727. PTHR11727. 1 hit.
    PfamiPF00398. RrnaAD. 1 hit.
    [Graphical view]
    PIRSFiPIRSF027833. MtTFB2. 1 hit.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51689. SAM_RNA_A_N6_MT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q3TL26-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRGPAMRLPP RIALSALARG PSCILGSGAA TRKDWQTRNR RGFSDFNIEP    50
    LPDSDLEESS PWTSRNRSEP TRHIACKKAA RNLVRDLLEH QNPSRQIILE 100
    CNPGPGILTG ALLKAGARVV AFESEKTFIP HLEPLQRNMD GELQVVHCDF 150
    FKMDPRYQEV VRPDVSSQAI FQNLGIKAVP WSAGVPIKVF GILPYKHERR 200
    ILWKILFDLY SCESIYRYGR VELNMFVSEK EFRKLIATPK RPDLYQVMAV 250
    LWQVACDVKF LHMEPWSSFS VHTENGHLEK SKHGESVNLL KQNLYLVRMT 300
    PRRTLFTENL SPLNYDIFFH LVKHCFGKRN APIIRHLRSL STVDPINILR 350
    QIRKNPGDTA ARMYPHDFKK LFETIEQSED SVFKWIYDYC PEDMEF 396
    Length:396
    Mass (Da):45,864
    Last modified:October 11, 2005 - v1
    Checksum:iD276BD58D595F111
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121I → L in AAA37817. 1 PublicationCurated
    Sequence conflicti40 – 401R → G in AAA37817. 1 PublicationCurated
    Sequence conflicti273 – 2731T → M in AAA37817. 1 PublicationCurated
    Sequence conflicti292 – 2921Q → P in BAC41095. (PubMed:16141072)Curated
    Sequence conflicti308 – 3081E → G in BAC41095. (PubMed:16141072)Curated
    Sequence conflicti324 – 3241H → P in BAC41095. (PubMed:16141072)Curated
    Sequence conflicti330 – 3301N → H in BAC41095. (PubMed:16141072)Curated
    Sequence conflicti338 – 3381R → P in BAC41095. (PubMed:16141072)Curated
    Sequence conflicti377 – 3771Q → P in BAC41095. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74555 mRNA. Translation: AAA37817.1.
    AK090106 mRNA. Translation: BAC41095.1.
    AK146563 mRNA. Translation: BAE27262.1.
    AK166717 mRNA. Translation: BAE38967.1.
    AK167930 mRNA. Translation: BAE39934.1.
    AK168970 mRNA. Translation: BAE40774.1.
    AK169138 mRNA. Translation: BAE40917.1.
    CCDSiCCDS15561.1.
    PIRiS27870.
    RefSeqiNP_032275.2. NM_008249.4.
    UniGeneiMm.293529.

    Genome annotation databases

    EnsembliENSMUST00000027769; ENSMUSP00000027769; ENSMUSG00000026492.
    GeneIDi15278.
    KEGGimmu:15278.
    UCSCiuc007dvl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74555 mRNA. Translation: AAA37817.1 .
    AK090106 mRNA. Translation: BAC41095.1 .
    AK146563 mRNA. Translation: BAE27262.1 .
    AK166717 mRNA. Translation: BAE38967.1 .
    AK167930 mRNA. Translation: BAE39934.1 .
    AK168970 mRNA. Translation: BAE40774.1 .
    AK169138 mRNA. Translation: BAE40917.1 .
    CCDSi CCDS15561.1.
    PIRi S27870.
    RefSeqi NP_032275.2. NM_008249.4.
    UniGenei Mm.293529.

    3D structure databases

    ProteinModelPortali Q3TL26.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q3TL26.

    Proteomic databases

    PaxDbi Q3TL26.
    PRIDEi Q3TL26.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027769 ; ENSMUSP00000027769 ; ENSMUSG00000026492 .
    GeneIDi 15278.
    KEGGi mmu:15278.
    UCSCi uc007dvl.1. mouse.

    Organism-specific databases

    CTDi 64216.
    MGIi MGI:107937. Tfb2m.

    Phylogenomic databases

    eggNOGi COG0030.
    GeneTreei ENSGT00510000048533.
    HOGENOMi HOG000060174.
    HOVERGENi HBG094037.
    InParanoidi Q3TL26.
    KOi K17653.
    OMAi LLMMIKQ.
    OrthoDBi EOG7RNK0M.
    PhylomeDBi Q3TL26.
    TreeFami TF325100.

    Enzyme and pathway databases

    Reactomei REACT_205251. Transcriptional activation of mitochondrial biogenesis.

    Miscellaneous databases

    NextBioi 287913.
    PROi Q3TL26.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3TL26.
    CleanExi MM_TFB2M.
    Genevestigatori Q3TL26.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR016861. Mt_di-Me-Ado_Trfase_2_prcur.
    IPR001737. rRNA_Ade_methylase_transferase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR11727. PTHR11727. 1 hit.
    Pfami PF00398. RrnaAD. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF027833. MtTFB2. 1 hit.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51689. SAM_RNA_A_N6_MT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Wang B., Hunsperger J.P., Laib J., Fan D.
      Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Lymphoma.
    2. "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].
      Strain: BALB/c and C57BL/6J.
      Tissue: Heart.
    3. "Characterization of the mouse genes for mitochondrial transcription factors B1 and B2."
      Rantanen A., Gaspari M., Falkenberg M., Gustafsson C.M., Larsson N.-G.
      Mamm. Genome 14:1-6(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    4. "The mitochondrial RNA polymerase contributes critically to promoter specificity in mammalian cells."
      Gaspari M., Falkenberg M., Larsson N.-G., Gustafsson C.M.
      EMBO J. 23:4606-4614(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiTFB2M_MOUSE
    AccessioniPrimary (citable) accession number: Q3TL26
    Secondary accession number(s): Q61669, Q8BTJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 81 of the entry and version 1 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