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Q9H5Q4

- TFB2M_HUMAN

UniProt

Q9H5Q4 - TFB2M_HUMAN

Protein

Dimethyladenosine transferase 2, mitochondrial

Gene

TFB2M

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    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. Compared to TFB1M, it activates transcription of mitochondrial DNA more efficiently, while it has less methyltransferase activity.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei75 – 751S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei124 – 1241S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei150 – 1501S-adenosyl-L-methioninePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. gene expression Source: Reactome
    2. positive regulation of transcription, DNA-templated Source: UniProtKB
    3. transcription from mitochondrial promoter Source: UniProtKB
    4. 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_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_367. Mitochondrial transcription initiation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dimethyladenosine transferase 2, mitochondrial (EC:2.1.1.-)
    Alternative name(s):
    Hepatitis C virus NS5A-transactivated protein 5
    Short name:
    HCV NS5A-transactivated protein 5
    Mitochondrial 12S rRNA dimethylase 2
    Mitochondrial transcription factor B2
    Short name:
    h-mtTFB
    Short name:
    h-mtTFB2
    Short name:
    hTFB2M
    Short name:
    mtTFB2
    S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2
    Gene namesi
    Name:TFB2M
    Synonyms:NS5ATP5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:18559. TFB2M.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB
    2. mitochondrial nucleoid Source: BHF-UCL

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi105 – 1051G → A: Abolishes methyltransferase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA38348.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1919MitochondrionSequence AnalysisAdd
    BLAST
    Chaini20 – 396377Dimethyladenosine transferase 2, mitochondrialPRO_0000273179Add
    BLAST

    Proteomic databases

    MaxQBiQ9H5Q4.
    PaxDbiQ9H5Q4.
    PeptideAtlasiQ9H5Q4.
    PRIDEiQ9H5Q4.

    PTM databases

    PhosphoSiteiQ9H5Q4.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Inductioni

    By the nuclear respiratory factors NRF1 and NRF2/GABPB2 and PGC-1 coactivators.1 Publication

    Gene expression databases

    ArrayExpressiQ9H5Q4.
    BgeeiQ9H5Q4.
    CleanExiHS_TFB2M.
    GenevestigatoriQ9H5Q4.

    Organism-specific databases

    HPAiHPA030265.

    Interactioni

    Subunit structurei

    Interacts with mitochondrial RNA polymerase POLRMT. Interacts with TFAM.2 Publications

    Protein-protein interaction databases

    BioGridi122106. 7 interactions.
    DIPiDIP-50540N.
    IntActiQ9H5Q4. 2 interactions.
    STRINGi9606.ENSP00000355471.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H5Q4.
    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.
    HOGENOMiHOG000060174.
    HOVERGENiHBG094037.
    InParanoidiQ9H5Q4.
    KOiK17653.
    OMAiVIHCDFF.
    OrthoDBiEOG7RNK0M.
    PhylomeDBiQ9H5Q4.
    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.

    Q9H5Q4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWIPVVGLPR RLRLSALAGA GRFCILGSEA ATRKHLPARN HCGLSDSSPQ    50
    LWPEPDFRNP PRKASKASLD FKRYVTDRRL AETLAQIYLG KPSRPPHLLL 100
    ECNPGPGILT QALLEAGAKV VALESDKTFI PHLESLGKNL DGKLRVIHCD 150
    FFKLDPRSGG VIKPPAMSSR GLFKNLGIEA VPWTADIPLK VVGMFPSRGE 200
    KRALWKLAYD LYSCTSIYKF GRIEVNMFIG EKEFQKLMAD PGNPDLYHVL 250
    SVIWQLACEI KVLHMEPWSS FDIYTRKGPL ENPKRRELLD QLQQKLYLIQ 300
    MIPRQNLFTK NLTPMNYNIF FHLLKHCFGR RSATVIDHLR SLTPLDARDI 350
    LMQIGKQEDE KVVNMHPQDF KTLFETIERS KDCAYKWLYD ETLEDR 396
    Length:396
    Mass (Da):45,349
    Last modified:March 1, 2001 - v1
    Checksum:iC13DC398974BB88F
    GO

    Sequence cautioni

    The sequence BAB15441.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti200 – 2012EK → GR in BAB15441. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti156 – 1561P → L.
    Corresponds to variant rs11585481 [ dbSNP | Ensembl ].
    VAR_030097
    Natural varianti264 – 2641H → Y.
    Corresponds to variant rs12037377 [ dbSNP | Ensembl ].
    VAR_030098

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF529366 mRNA. Translation: AAQ09600.1.
    AK026314 mRNA. Translation: BAB15441.1. Different initiation.
    AK026835 mRNA. Translation: BAB15566.1.
    AL356583 Genomic DNA. Translation: CAI16399.1.
    BC003383 mRNA. Translation: AAH03383.1.
    CCDSiCCDS1627.1.
    RefSeqiNP_071761.1. NM_022366.2.
    UniGeneiHs.7395.

    Genome annotation databases

    EnsembliENST00000366514; ENSP00000355471; ENSG00000162851.
    GeneIDi64216.
    KEGGihsa:64216.
    UCSCiuc001ibn.3. human.

    Polymorphism databases

    DMDMi74752681.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF529366 mRNA. Translation: AAQ09600.1 .
    AK026314 mRNA. Translation: BAB15441.1 . Different initiation.
    AK026835 mRNA. Translation: BAB15566.1 .
    AL356583 Genomic DNA. Translation: CAI16399.1 .
    BC003383 mRNA. Translation: AAH03383.1 .
    CCDSi CCDS1627.1.
    RefSeqi NP_071761.1. NM_022366.2.
    UniGenei Hs.7395.

    3D structure databases

    ProteinModelPortali Q9H5Q4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122106. 7 interactions.
    DIPi DIP-50540N.
    IntActi Q9H5Q4. 2 interactions.
    STRINGi 9606.ENSP00000355471.

    PTM databases

    PhosphoSitei Q9H5Q4.

    Polymorphism databases

    DMDMi 74752681.

    Proteomic databases

    MaxQBi Q9H5Q4.
    PaxDbi Q9H5Q4.
    PeptideAtlasi Q9H5Q4.
    PRIDEi Q9H5Q4.

    Protocols and materials databases

    DNASUi 64216.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366514 ; ENSP00000355471 ; ENSG00000162851 .
    GeneIDi 64216.
    KEGGi hsa:64216.
    UCSCi uc001ibn.3. human.

    Organism-specific databases

    CTDi 64216.
    GeneCardsi GC01M246703.
    HGNCi HGNC:18559. TFB2M.
    HPAi HPA030265.
    MIMi 607055. gene.
    neXtProti NX_Q9H5Q4.
    PharmGKBi PA38348.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0030.
    HOGENOMi HOG000060174.
    HOVERGENi HBG094037.
    InParanoidi Q9H5Q4.
    KOi K17653.
    OMAi VIHCDFF.
    OrthoDBi EOG7RNK0M.
    PhylomeDBi Q9H5Q4.
    TreeFami TF325100.

    Enzyme and pathway databases

    Reactomei REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_367. Mitochondrial transcription initiation.

    Miscellaneous databases

    GeneWikii TFB2M.
    GenomeRNAii 64216.
    NextBioi 66127.
    PROi Q9H5Q4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H5Q4.
    Bgeei Q9H5Q4.
    CleanExi HS_TFB2M.
    Genevestigatori Q9H5Q4.

    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. "Cloning and identification of human gene 5 transactivated by hepatitis C virus NS5A protein."
      Liu Y., Cheng J., Wang G., Wang J., Zhang L., Chen J., Li L.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: Lung and Small intestine.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Placenta.
    5. "Mitochondrial transcription factors B1 and B2 activate transcription of human mtDNA."
      Falkenberg M., Gaspari M., Rantanen A., Trifunovic A., Larsson N.-G., Gustafsson C.M.
      Nat. Genet. 31:289-294(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH POLRMT.
    6. "Human mitochondrial transcription factor B1 interacts with the C-terminal activation region of h-mtTFA and stimulates transcription independently of its RNA methyltransferase activity."
      McCulloch V., Shadel G.S.
      Mol. Cell. Biol. 23:5816-5824(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TFAM.
    7. "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.
    8. "Control of mitochondrial transcription specificity factors (TFB1M and TFB2M) by nuclear respiratory factors (NRF-1 and NRF-2) and PGC-1 family coactivators."
      Gleyzer N., Vercauteren K., Scarpulla R.C.
      Mol. Cell. Biol. 25:1354-1366(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    9. "Evidence for an early gene duplication event in the evolution of the mitochondrial transcription factor B family and maintenance of rRNA methyltransferase activity in human mtTFB1 and mtTFB2."
      Cotney J., Shadel G.S.
      J. Mol. Evol. 63:707-717(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, MUTAGENESIS OF GLY-105.
    10. "Human mitochondrial transcription revisited: only TFAM and TFB2M are required for transcription of the mitochondrial genes in vitro."
      Litonin D., Sologub M., Shi Y., Savkina M., Anikin M., Falkenberg M., Gustafsson C.M., Temiakov D.
      J. Biol. Chem. 285:18129-18133(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTFB2M_HUMAN
    AccessioniPrimary (citable) accession number: Q9H5Q4
    Secondary accession number(s): Q9H626
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 118 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3