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Dimethyladenosine transferase 1, mitochondrial (EC 2.1.1.-) (Mitochondrial 12S rRNA dimethylase 1) (Mitochondrial transcription factor B1) (h-mtTFB) (h-mtTFB1) (hTFB1M) (mtTFB1) (S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 1)

 TFB1M_HUMAN             Reviewed;         346 AA.
Q8WVM0; Q05DR0; Q9Y384;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
12-SEP-2018, entry version 145.
RecName: Full=Dimethyladenosine transferase 1, mitochondrial;
EC=2.1.1.-;
AltName: Full=Mitochondrial 12S rRNA dimethylase 1;
AltName: Full=Mitochondrial transcription factor B1;
Short=h-mtTFB;
Short=h-mtTFB1;
Short=hTFB1M;
Short=mtTFB1;
AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 1;
Flags: Precursor;
Name=TFB1M; ORFNames=CGI-75;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, AND SAM-BINDING.
PubMed=11809803; DOI=10.1128/MCB.22.4.1116-1125.2002;
McCulloch V., Seidel-Rogol B.L., Shadel G.S.;
"A human mitochondrial transcription factor is related to RNA adenine
methyltransferases and binds S-adenosylmethionine.";
Mol. Cell. Biol. 22:1116-1125(2002).
[5]
FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH POLRMT.
PubMed=12068295; DOI=10.1038/ng909;
Falkenberg M., Gaspari M., Rantanen A., Trifunovic A., Larsson N.-G.,
Gustafsson C.M.;
"Mitochondrial transcription factors B1 and B2 activate transcription
of human mtDNA.";
Nat. Genet. 31:289-294(2002).
[6]
FUNCTION, INTERACTION WITH TFAM, AND MUTAGENESIS OF GLY-65; ASN-141
AND LYS-220.
PubMed=12897151; DOI=10.1128/MCB.23.16.5816-5824.2003;
McCulloch V., Shadel G.S.;
"Human mitochondrial transcription factor B1 interacts with the C-
terminal activation region of h-mtTFA and stimulates transcription
independently of its RNA methyltransferase activity.";
Mol. Cell. Biol. 23:5816-5824(2003).
[7]
ENZYME ACTIVITY, AND MUTAGENESIS OF GLY-65 AND LYS-220.
PubMed=12496758; DOI=10.1038/ng1064;
Seidel-Rogol B.L., McCulloch V., Shadel G.S.;
"Human mitochondrial transcription factor B1 methylates ribosomal RNA
at a conserved stem-loop.";
Nat. Genet. 33:23-24(2003).
[8]
POSSIBLE INVOLVEMENT IN AMINOGLYCOSIDE-INDUCED DEAFNESS.
PubMed=15110318; DOI=10.1016/j.ymgme.2004.01.020;
Bykhovskaya Y., Mengesha E., Wang D., Yang H., Estivill X., Shohat M.,
Fischel-Ghodsian N.;
"Human mitochondrial transcription factor B1 as a modifier gene for
hearing loss associated with the mitochondrial A1555G mutation.";
Mol. Genet. Metab. 82:27-32(2004).
[9]
INDUCTION.
PubMed=15684387; DOI=10.1128/MCB.25.4.1354-1366.2005;
Gleyzer N., Vercauteren K., Scarpulla R.C.;
"Control of mitochondrial transcription specificity factors (TFB1M and
TFB2M) by nuclear respiratory factors (NRF-1 and NRF-2) and PGC-1
family coactivators.";
Mol. Cell. Biol. 25:1354-1366(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
VARIANTS PRO-120; ALA-211 AND GLN-256.
PubMed=19096125; DOI=10.1155/2008/575323;
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.;
"Mitochondrial transcription factors TFA, TFB1 and TFB2: a search for
DNA variants/haplotypes and the risk of cardiac hypertrophy.";
Dis. Markers 25:131-139(2008).
-!- 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. {ECO:0000269|PubMed:11809803,
ECO:0000269|PubMed:12068295, ECO:0000269|PubMed:12897151}.
-!- SUBUNIT: Interacts with mitochondrial RNA polymerase POLRMT.
Interacts with TFAM. {ECO:0000269|PubMed:12068295,
ECO:0000269|PubMed:12897151}.
-!- INTERACTION:
Q00059:TFAM; NbExp=2; IntAct=EBI-2615570, EBI-1049924;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11809803}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:12068295}.
-!- INDUCTION: By the nuclear respiratory factors NRF1 and NRF2/GABPB2
and PGC-1 coactivators. {ECO:0000269|PubMed:15684387}.
-!- DISEASE: Note=Variations in TFB1M may influence the clinical
expression of aminoglycoside-induced deafness caused by the A1555G
mutation in the mitochondrial 12S rRNA.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. rRNA adenine N(6)-methyltransferase
family. KsgA subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH05183.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF151833; AAD34070.1; -; mRNA.
EMBL; AL139101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC005183; AAH05183.1; ALT_SEQ; mRNA.
EMBL; BC017788; AAH17788.1; -; mRNA.
CCDS; CCDS5248.1; -.
RefSeq; NP_057104.2; NM_016020.3.
UniGene; Hs.279908; -.
UniGene; Hs.655297; -.
ProteinModelPortal; Q8WVM0; -.
SMR; Q8WVM0; -.
BioGrid; 119295; 20.
IntAct; Q8WVM0; 11.
MINT; Q8WVM0; -.
STRING; 9606.ENSP00000356134; -.
iPTMnet; Q8WVM0; -.
PhosphoSitePlus; Q8WVM0; -.
BioMuta; TFB1M; -.
DMDM; 74751555; -.
EPD; Q8WVM0; -.
MaxQB; Q8WVM0; -.
PaxDb; Q8WVM0; -.
PeptideAtlas; Q8WVM0; -.
PRIDE; Q8WVM0; -.
ProteomicsDB; 74803; -.
DNASU; 51106; -.
Ensembl; ENST00000367166; ENSP00000356134; ENSG00000029639.
GeneID; 51106; -.
KEGG; hsa:51106; -.
UCSC; uc003qqj.5; human.
CTD; 51106; -.
DisGeNET; 51106; -.
EuPathDB; HostDB:ENSG00000029639.10; -.
GeneCards; TFB1M; -.
HGNC; HGNC:17037; TFB1M.
HPA; HPA029428; -.
MalaCards; TFB1M; -.
MIM; 607033; gene.
neXtProt; NX_Q8WVM0; -.
OpenTargets; ENSG00000029639; -.
Orphanet; 90641; Mitochondrial non-syndromic sensorineural deafness.
PharmGKB; PA38198; -.
eggNOG; KOG0821; Eukaryota.
eggNOG; COG0030; LUCA.
GeneTree; ENSGT00530000063389; -.
HOGENOM; HOG000227961; -.
HOVERGEN; HBG082484; -.
InParanoid; Q8WVM0; -.
KO; K15266; -.
OMA; SVMSQIW; -.
OrthoDB; EOG091G0ALA; -.
PhylomeDB; Q8WVM0; -.
TreeFam; TF300798; -.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-6793080; rRNA modification in the mitochondrion.
ChiTaRS; TFB1M; human.
GeneWiki; TFB1M; -.
GenomeRNAi; 51106; -.
PRO; PR:Q8WVM0; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000029639; Expressed in 205 organ(s), highest expression level in right adrenal gland cortex.
CleanEx; HS_TFB1M; -.
ExpressionAtlas; Q8WVM0; baseline and differential.
Genevisible; Q8WVM0; HS.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; EXP:Reactome.
GO; GO:0007005; P:mitochondrion organization; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0000154; P:rRNA modification; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.8.100; -; 1.
HAMAP; MF_00607; 16SrRNA_methyltr_A; 1.
InterPro; IPR001737; KsgA/Erm.
InterPro; IPR023165; rRNA_Ade_diMease-like.
InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
InterPro; IPR011530; rRNA_adenine_dimethylase.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR11727; PTHR11727; 1.
Pfam; PF00398; RrnaAD; 1.
SMART; SM00650; rADc; 1.
SUPFAM; SSF53335; SSF53335; 1.
TIGRFAMs; TIGR00755; ksgA; 1.
PROSITE; PS01131; RRNA_A_DIMETH; 1.
PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
1: Evidence at protein level;
Complete proteome; DNA-binding; Methyltransferase; Mitochondrion;
Polymorphism; Reference proteome; RNA-binding; rRNA processing;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase; Transit peptide.
TRANSIT 1 27 Mitochondrion. {ECO:0000255}.
CHAIN 28 346 Dimethyladenosine transferase 1,
mitochondrial.
/FTId=PRO_0000273171.
REGION 35 38 S-adenosyl-L-methionine binding.
{ECO:0000250}.
BINDING 36 36 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250}.
BINDING 38 38 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000250}.
BINDING 63 63 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250}.
BINDING 85 85 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 111 111 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 141 141 S-adenosyl-L-methionine. {ECO:0000250}.
VARIANT 120 120 A -> P (in dbSNP:rs144355958).
{ECO:0000269|PubMed:19096125}.
/FTId=VAR_071246.
VARIANT 211 211 T -> A (in dbSNP:rs769497533).
{ECO:0000269|PubMed:19096125}.
/FTId=VAR_071247.
VARIANT 256 256 R -> Q (in dbSNP:rs73579353).
{ECO:0000269|PubMed:19096125}.
/FTId=VAR_071248.
MUTAGEN 65 65 G->A: Abolishes methyltransferase
activity, DNA-binding and SAM-binding.
Does not abolish transcription activator
function. {ECO:0000269|PubMed:12496758,
ECO:0000269|PubMed:12897151}.
MUTAGEN 141 141 N->A: Does not affect SAM-binding, DNA-
binding nor transcription activator
function. {ECO:0000269|PubMed:12897151}.
MUTAGEN 220 220 K->A: Abolishes methyltransferase
activity. Does not affect SAM-binding,
DNA-binding nor transcription activator
function. {ECO:0000269|PubMed:12496758,
ECO:0000269|PubMed:12897151}.
CONFLICT 31 32 KQ -> NE (in Ref. 1; AAD34070).
{ECO:0000305}.
SEQUENCE 346 AA; 39543 MW; 4C34F4FD72B01286 CRC64;
MAASGKLSTC RLPPLPTIRE IIKLLRLQAA KQLSQNFLLD LRLTDKIVRK AGNLTNAYVY
EVGPGPGGIT RSILNADVAE LLVVEKDTRF IPGLQMLSDA APGKLRIVHG DVLTFKVEKA
FSESLKRPWE DDPPNVHIIG NLPFSVSTPL IIKWLENISC RDGPFVYGRT QMTLTFQKEV
AERLAANTGS KQRSRLSVMA QYLCNVRHIF TIPGQAFVPK PEVDVGVVHF TPLIQPKIEQ
PFKLVEKVVQ NVFQFRRKYC HRGLRMLFPE AQRLESTGRL LELADIDPTL RPRQLSISHF
KSLCDVYRKM CDEDPQLFAY NFREELKRRK SKNEEKEEDD AENYRL


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