Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8WVM0 (TFB1M_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TFB1M
ORF Names:CGI-75
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5 Ref.6

Subunit structure

Interacts with mitochondrial RNA polymerase POLRMT. Interacts with TFAM. Ref.5 Ref.6

Subcellular location

Mitochondrion Ref.4.

Tissue specificity

Ubiquitously expressed. Ref.5

Induction

By the nuclear respiratory factors NRF1 and NRF2/GABPB2 and PGC-1 coactivators. Ref.9

Involvement in disease

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

Sequence similarities

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

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TFAMQ000592EBI-2615570,EBI-1049924

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion Potential
Chain28 – 346319Dimethyladenosine transferase 1, mitochondrial HAMAP-Rule MF_00607
PRO_0000273171

Regions

Region35 – 384S-adenosyl-L-methionine binding By similarity

Sites

Binding site361S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site381S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site631S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site851S-adenosyl-L-methionine By similarity
Binding site1111S-adenosyl-L-methionine By similarity
Binding site1411S-adenosyl-L-methionine By similarity

Experimental info

Mutagenesis651G → A: Abolishes methyltransferase activity, DNA-binding and SAM-binding. Does not abolish transcription activator function. Ref.6 Ref.7
Mutagenesis1411N → A: Does not affect SAM-binding, DNA-binding nor transcription activator function. Ref.6
Mutagenesis2201K → A: Abolishes methyltransferase activity. Does not affect SAM-binding, DNA-binding nor transcription activator function. Ref.6 Ref.7
Sequence conflict31 – 322KQ → NE in AAD34070. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8WVM0 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 4C34F4FD72B01286

FASTA34639,543
        10         20         30         40         50         60 
MAASGKLSTC RLPPLPTIRE IIKLLRLQAA KQLSQNFLLD LRLTDKIVRK AGNLTNAYVY 

        70         80         90        100        110        120 
EVGPGPGGIT RSILNADVAE LLVVEKDTRF IPGLQMLSDA APGKLRIVHG DVLTFKVEKA 

       130        140        150        160        170        180 
FSESLKRPWE DDPPNVHIIG NLPFSVSTPL IIKWLENISC RDGPFVYGRT QMTLTFQKEV 

       190        200        210        220        230        240 
AERLAANTGS KQRSRLSVMA QYLCNVRHIF TIPGQAFVPK PEVDVGVVHF TPLIQPKIEQ 

       250        260        270        280        290        300 
PFKLVEKVVQ NVFQFRRKYC HRGLRMLFPE AQRLESTGRL LELADIDPTL RPRQLSISHF 

       310        320        330        340 
KSLCDVYRKM CDEDPQLFAY NFREELKRRK SKNEEKEEDD AENYRL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF151833 mRNA. Translation: AAD34070.1.
AL139101 Genomic DNA. Translation: CAI20506.1.
BC005183 mRNA. Translation: AAH05183.1. Sequence problems.
BC017788 mRNA. Translation: AAH17788.1.
CCDSCCDS5248.1.
RefSeqNP_057104.2. NM_016020.3.
XP_005267062.1. XM_005267005.1.
UniGeneHs.279908.
Hs.655297.

3D structure databases

ProteinModelPortalQ8WVM0.
SMRQ8WVM0. Positions 36-306.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119295. 4 interactions.
IntActQ8WVM0. 3 interactions.
MINTMINT-8052614.
STRING9606.ENSP00000356134.

PTM databases

PhosphoSiteQ8WVM0.

Polymorphism databases

DMDM74751555.

Proteomic databases

MaxQBQ8WVM0.
PaxDbQ8WVM0.
PRIDEQ8WVM0.

Protocols and materials databases

DNASU51106.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367166; ENSP00000356134; ENSG00000029639.
GeneID51106.
KEGGhsa:51106.
UCSCuc003qqj.4. human.

Organism-specific databases

CTD51106.
GeneCardsGC06M155578.
HGNCHGNC:17037. TFB1M.
HPAHPA029428.
MIM607033. gene.
neXtProtNX_Q8WVM0.
Orphanet90641. Mitochondrial nonsyndromic sensorineural deafness.
PharmGKBPA38198.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0030.
HOGENOMHOG000227961.
HOVERGENHBG082484.
InParanoidQ8WVM0.
KOK15266.
OMAQKYCRRG.
OrthoDBEOG7DJSMJ.
PhylomeDBQ8WVM0.
TreeFamTF300798.

Enzyme and pathway databases

ReactomeREACT_200751. Organelle biogenesis and maintenance.

Gene expression databases

ArrayExpressQ8WVM0.
BgeeQ8WVM0.
CleanExHS_TFB1M.
GenevestigatorQ8WVM0.

Family and domain databases

Gene3D1.10.8.100. 1 hit.
3.40.50.150. 1 hit.
HAMAPMF_00607. 16SrRNA_methyltr_A.
InterProIPR023165. 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]
PANTHERPTHR11727. PTHR11727. 1 hit.
PfamPF00398. RrnaAD. 1 hit.
[Graphical view]
SMARTSM00650. rADc. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS01131. RRNA_A_DIMETH. 1 hit.
PS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTFB1M. human.
GeneWikiTFB1M.
GenomeRNAi51106.
NextBio53841.
PROQ8WVM0.
SOURCESearch...

Entry information

Entry nameTFB1M_HUMAN
AccessionPrimary (citable) accession number: Q8WVM0
Secondary accession number(s): Q05DR0, Q9Y384
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM