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Protein

Dimethyladenosine transferase 1, mitochondrial

Gene

TFB1M

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

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_264212. 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 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:17037. TFB1M.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: Reactome
  • mitochondrial nucleoid Source: BHF-UCL
Complete GO annotation...

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 non-syndromic sensorineural deafness.
PharmGKBiPA38198.

Polymorphism and mutation databases

BioMutaiTFB1M.
DMDMi74751555.

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

BgeeiQ8WVM0.
CleanExiHS_TFB1M.
ExpressionAtlasiQ8WVM0. baseline and differential.
GenevisibleiQ8WVM0. HS.

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. 8 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.
GeneTreeiENSGT00530000063389.
HOGENOMiHOG000227961.
HOVERGENiHBG082484.
InParanoidiQ8WVM0.
KOiK15266.
OMAiFRLQAVK.
OrthoDBiEOG7DJSMJ.
PhylomeDBiQ8WVM0.
TreeFamiTF300798.

Family and domain databases

Gene3Di1.10.8.100. 1 hit.
3.40.50.150. 1 hit.
HAMAPiMF_00607. 16SrRNA_methyltr_A.
InterProiIPR001737. KsgA/Erm.
IPR023165. rRNA_Ade_diMease-like.
IPR020596. rRNA_Ade_Mease_Trfase_CS.
IPR020598. rRNA_Ade_methylase_Trfase_N.
IPR011530. rRNA_adenine_dimethylase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11727. PTHR11727. 1 hit.
PfamiPF00398. RrnaAD. 1 hit.
[Graphical view]
SMARTiSM00650. rADc. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00755. ksgA. 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

        10         20         30         40         50
MAASGKLSTC RLPPLPTIRE IIKLLRLQAA KQLSQNFLLD LRLTDKIVRK
60 70 80 90 100
AGNLTNAYVY EVGPGPGGIT RSILNADVAE LLVVEKDTRF IPGLQMLSDA
110 120 130 140 150
APGKLRIVHG DVLTFKVEKA FSESLKRPWE DDPPNVHIIG NLPFSVSTPL
160 170 180 190 200
IIKWLENISC RDGPFVYGRT QMTLTFQKEV AERLAANTGS KQRSRLSVMA
210 220 230 240 250
QYLCNVRHIF TIPGQAFVPK PEVDVGVVHF TPLIQPKIEQ PFKLVEKVVQ
260 270 280 290 300
NVFQFRRKYC HRGLRMLFPE AQRLESTGRL LELADIDPTL RPRQLSISHF
310 320 330 340
KSLCDVYRKM CDEDPQLFAY NFREELKRRK SKNEEKEEDD AENYRL
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.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti120 – 1201A → P.1 Publication
VAR_071246
Natural varianti211 – 2111T → A.1 Publication
VAR_071247
Natural varianti256 – 2561R → Q.1 Publication
Corresponds to variant rs73579353 [ dbSNP | Ensembl ].
VAR_071248

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
UniGeneiHs.279908.
Hs.655297.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
UniGeneiHs.279908.
Hs.655297.

3D structure databases

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

Protein-protein interaction databases

BioGridi119295. 8 interactions.
IntActiQ8WVM0. 3 interactions.
MINTiMINT-8052614.
STRINGi9606.ENSP00000356134.

PTM databases

PhosphoSiteiQ8WVM0.

Polymorphism and mutation databases

BioMutaiTFB1M.
DMDMi74751555.

Proteomic databases

MaxQBiQ8WVM0.
PaxDbiQ8WVM0.
PRIDEiQ8WVM0.

Protocols and materials databases

DNASUi51106.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51106.
GeneCardsiGC06M155578.
HGNCiHGNC:17037. TFB1M.
HPAiHPA029428.
MIMi607033. gene.
neXtProtiNX_Q8WVM0.
Orphaneti90641. Mitochondrial non-syndromic sensorineural deafness.
PharmGKBiPA38198.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0030.
GeneTreeiENSGT00530000063389.
HOGENOMiHOG000227961.
HOVERGENiHBG082484.
InParanoidiQ8WVM0.
KOiK15266.
OMAiFRLQAVK.
OrthoDBiEOG7DJSMJ.
PhylomeDBiQ8WVM0.
TreeFamiTF300798.

Enzyme and pathway databases

ReactomeiREACT_264212. Transcriptional activation of mitochondrial biogenesis.

Miscellaneous databases

ChiTaRSiTFB1M. human.
GeneWikiiTFB1M.
GenomeRNAii51106.
NextBioi53841.
PROiQ8WVM0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WVM0.
CleanExiHS_TFB1M.
ExpressionAtlasiQ8WVM0. baseline and differential.
GenevisibleiQ8WVM0. HS.

Family and domain databases

Gene3Di1.10.8.100. 1 hit.
3.40.50.150. 1 hit.
HAMAPiMF_00607. 16SrRNA_methyltr_A.
InterProiIPR001737. KsgA/Erm.
IPR023165. rRNA_Ade_diMease-like.
IPR020596. rRNA_Ade_Mease_Trfase_CS.
IPR020598. rRNA_Ade_methylase_Trfase_N.
IPR011530. rRNA_adenine_dimethylase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11727. PTHR11727. 1 hit.
PfamiPF00398. RrnaAD. 1 hit.
[Graphical view]
SMARTiSM00650. rADc. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00755. ksgA. 1 hit.
PROSITEiPS01131. RRNA_A_DIMETH. 1 hit.
PS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
  12. "Mitochondrial transcription factors TFA, TFB1 and TFB2: a search for DNA variants/haplotypes and the risk of cardiac hypertrophy."
    Alonso-Montes C., Castro M.G., Reguero J.R., Perrot A., Ozcelik C., Geier C., Posch M.G., Moris C., Alvarez V., Ruiz-Ortega M., Coto E.
    Dis. Markers 25:131-139(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PRO-120; ALA-211 AND GLN-256.

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: June 24, 2015
This is version 121 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. 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.