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)

Q8WVM0

- TFB1M_HUMAN

UniProt

Q8WVM0 - TFB1M_HUMAN

Protein

Dimethyladenosine transferase 1, mitochondrial

Gene

TFB1M

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 115 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      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.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
    Binding sitei38 – 381S-adenosyl-L-methionine; via amide nitrogenBy similarity
    Binding sitei63 – 631S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
    Binding sitei85 – 851S-adenosyl-L-methionineBy similarity
    Binding sitei111 – 1111S-adenosyl-L-methionineBy similarity
    Binding sitei141 – 1411S-adenosyl-L-methionineBy similarity

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. rRNA (adenine-N6,N6-)-dimethyltransferase activity Source: InterPro

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    rRNA processing, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, RNA-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    ReactomeiREACT_200608. Transcriptional activation of mitochondrial biogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dimethyladenosine transferase 1, mitochondrial (EC:2.1.1.-)
    Alternative name(s):
    Mitochondrial 12S rRNA dimethylase 1
    Mitochondrial transcription factor B1
    Short name:
    h-mtTFB
    Short name:
    h-mtTFB1
    Short name:
    hTFB1M
    Short name:
    mtTFB1
    S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 1
    Gene namesi
    Name:TFB1M
    ORF Names:CGI-75
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:17037. TFB1M.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrial nucleoid Source: BHF-UCL

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Variations in TFB1M may influence the clinical expression of aminoglycoside-induced deafness caused by the A1555G mutation in the mitochondrial 12S rRNA.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi65 – 651G → A: Abolishes methyltransferase activity, DNA-binding and SAM-binding. Does not abolish transcription activator function. 2 Publications
    Mutagenesisi141 – 1411N → A: Does not affect SAM-binding, DNA-binding nor transcription activator function. 1 Publication
    Mutagenesisi220 – 2201K → A: Abolishes methyltransferase activity. Does not affect SAM-binding, DNA-binding nor transcription activator function. 2 Publications

    Organism-specific databases

    Orphaneti90641. Mitochondrial nonsyndromic sensorineural deafness.
    PharmGKBiPA38198.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2727MitochondrionSequence AnalysisAdd
    BLAST
    Chaini28 – 346319Dimethyladenosine transferase 1, mitochondrialPRO_0000273171Add
    BLAST

    Proteomic databases

    MaxQBiQ8WVM0.
    PaxDbiQ8WVM0.
    PRIDEiQ8WVM0.

    PTM databases

    PhosphoSiteiQ8WVM0.

    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

    ArrayExpressiQ8WVM0.
    BgeeiQ8WVM0.
    CleanExiHS_TFB1M.
    GenevestigatoriQ8WVM0.

    Organism-specific databases

    HPAiHPA029428.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TFAMQ000592EBI-2615570,EBI-1049924

    Protein-protein interaction databases

    BioGridi119295. 4 interactions.
    IntActiQ8WVM0. 3 interactions.
    MINTiMINT-8052614.
    STRINGi9606.ENSP00000356134.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8WVM0.
    SMRiQ8WVM0. Positions 36-306.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 384S-adenosyl-L-methionine bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0030.
    HOGENOMiHOG000227961.
    HOVERGENiHBG082484.
    InParanoidiQ8WVM0.
    KOiK15266.
    OMAiQKYCRRG.
    OrthoDBiEOG7DJSMJ.
    PhylomeDBiQ8WVM0.
    TreeFamiTF300798.

    Family and domain databases

    Gene3Di1.10.8.100. 1 hit.
    3.40.50.150. 1 hit.
    HAMAPiMF_00607. 16SrRNA_methyltr_A.
    InterProiIPR023165. rRNA_Ade_diMease-like.
    IPR020596. rRNA_Ade_Mease_Trfase_CS.
    IPR001737. rRNA_Ade_methylase_transferase.
    IPR020598. rRNA_Ade_methylase_Trfase_N.
    IPR011530. rRNA_adenine_dimethylase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PANTHERiPTHR11727. PTHR11727. 1 hit.
    PfamiPF00398. RrnaAD. 1 hit.
    [Graphical view]
    SMARTiSM00650. rADc. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS01131. RRNA_A_DIMETH. 1 hit.
    PS51689. 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.

    Q8WVM0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASGKLSTC RLPPLPTIRE IIKLLRLQAA KQLSQNFLLD LRLTDKIVRK    50
    AGNLTNAYVY EVGPGPGGIT RSILNADVAE LLVVEKDTRF IPGLQMLSDA 100
    APGKLRIVHG DVLTFKVEKA FSESLKRPWE DDPPNVHIIG NLPFSVSTPL 150
    IIKWLENISC RDGPFVYGRT QMTLTFQKEV AERLAANTGS KQRSRLSVMA 200
    QYLCNVRHIF TIPGQAFVPK PEVDVGVVHF TPLIQPKIEQ PFKLVEKVVQ 250
    NVFQFRRKYC HRGLRMLFPE AQRLESTGRL LELADIDPTL RPRQLSISHF 300
    KSLCDVYRKM CDEDPQLFAY NFREELKRRK SKNEEKEEDD AENYRL 346
    Length:346
    Mass (Da):39,543
    Last modified:March 1, 2002 - v1
    Checksum:i4C34F4FD72B01286
    GO

    Sequence cautioni

    The sequence AAH05183.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 322KQ → NE in AAD34070. (PubMed:10810093)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF151833 mRNA. Translation: AAD34070.1.
    AL139101 Genomic DNA. Translation: CAI20506.1.
    BC005183 mRNA. Translation: AAH05183.1. Sequence problems.
    BC017788 mRNA. Translation: AAH17788.1.
    CCDSiCCDS5248.1.
    RefSeqiNP_057104.2. NM_016020.3.
    XP_005267062.1. XM_005267005.1.
    UniGeneiHs.279908.
    Hs.655297.

    Genome annotation databases

    EnsembliENST00000367166; ENSP00000356134; ENSG00000029639.
    GeneIDi51106.
    KEGGihsa:51106.
    UCSCiuc003qqj.4. human.

    Polymorphism databases

    DMDMi74751555.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF151833 mRNA. Translation: AAD34070.1 .
    AL139101 Genomic DNA. Translation: CAI20506.1 .
    BC005183 mRNA. Translation: AAH05183.1 . Sequence problems.
    BC017788 mRNA. Translation: AAH17788.1 .
    CCDSi CCDS5248.1.
    RefSeqi NP_057104.2. NM_016020.3.
    XP_005267062.1. XM_005267005.1.
    UniGenei Hs.279908.
    Hs.655297.

    3D structure databases

    ProteinModelPortali Q8WVM0.
    SMRi Q8WVM0. Positions 36-306.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119295. 4 interactions.
    IntActi Q8WVM0. 3 interactions.
    MINTi MINT-8052614.
    STRINGi 9606.ENSP00000356134.

    PTM databases

    PhosphoSitei Q8WVM0.

    Polymorphism databases

    DMDMi 74751555.

    Proteomic databases

    MaxQBi Q8WVM0.
    PaxDbi Q8WVM0.
    PRIDEi Q8WVM0.

    Protocols and materials databases

    DNASUi 51106.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367166 ; ENSP00000356134 ; ENSG00000029639 .
    GeneIDi 51106.
    KEGGi hsa:51106.
    UCSCi uc003qqj.4. human.

    Organism-specific databases

    CTDi 51106.
    GeneCardsi GC06M155578.
    HGNCi HGNC:17037. TFB1M.
    HPAi HPA029428.
    MIMi 607033. gene.
    neXtProti NX_Q8WVM0.
    Orphaneti 90641. Mitochondrial nonsyndromic sensorineural deafness.
    PharmGKBi PA38198.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0030.
    HOGENOMi HOG000227961.
    HOVERGENi HBG082484.
    InParanoidi Q8WVM0.
    KOi K15266.
    OMAi QKYCRRG.
    OrthoDBi EOG7DJSMJ.
    PhylomeDBi Q8WVM0.
    TreeFami TF300798.

    Enzyme and pathway databases

    Reactomei REACT_200608. Transcriptional activation of mitochondrial biogenesis.

    Miscellaneous databases

    ChiTaRSi TFB1M. human.
    GeneWikii TFB1M.
    GenomeRNAii 51106.
    NextBioi 53841.
    PROi Q8WVM0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WVM0.
    Bgeei Q8WVM0.
    CleanExi HS_TFB1M.
    Genevestigatori Q8WVM0.

    Family and domain databases

    Gene3Di 1.10.8.100. 1 hit.
    3.40.50.150. 1 hit.
    HAMAPi MF_00607. 16SrRNA_methyltr_A.
    InterProi IPR023165. rRNA_Ade_diMease-like.
    IPR020596. rRNA_Ade_Mease_Trfase_CS.
    IPR001737. rRNA_Ade_methylase_transferase.
    IPR020598. rRNA_Ade_methylase_Trfase_N.
    IPR011530. rRNA_adenine_dimethylase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR11727. PTHR11727. 1 hit.
    Pfami PF00398. RrnaAD. 1 hit.
    [Graphical view ]
    SMARTi SM00650. rADc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS01131. RRNA_A_DIMETH. 1 hit.
    PS51689. SAM_RNA_A_N6_MT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. "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].
    3. "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: Kidney and Lung.
    4. "A human mitochondrial transcription factor is related to RNA adenine methyltransferases and binds S-adenosylmethionine."
      McCulloch V., Seidel-Rogol B.L., Shadel G.S.
      Mol. Cell. Biol. 22:1116-1125(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, SAM-BINDING.
    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, MUTAGENESIS OF GLY-65; ASN-141 AND LYS-220.
    7. "Human mitochondrial transcription factor B1 methylates ribosomal RNA at a conserved stem-loop."
      Seidel-Rogol B.L., McCulloch V., Shadel G.S.
      Nat. Genet. 33:23-24(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, MUTAGENESIS OF GLY-65 AND LYS-220.
    8. "Human mitochondrial transcription factor B1 as a modifier gene for hearing loss associated with the mitochondrial A1555G mutation."
      Bykhovskaya Y., Mengesha E., Wang D., Yang H., Estivill X., Shohat M., Fischel-Ghodsian N.
      Mol. Genet. Metab. 82:27-32(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE INVOLVEMENT IN AMINOGLYCOSIDE-INDUCED DEAFNESS.
    9. "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.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTFB1M_HUMAN
    AccessioniPrimary (citable) accession number: Q8WVM0
    Secondary accession number(s): Q05DR0, Q9Y384
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 115 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 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3