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Dimethyladenosine transferase 2, mitochondrial (EC 2.1.1.-) (Hepatitis C virus NS5A-transactivated protein 5) (HCV NS5A-transactivated protein 5) (Mitochondrial 12S rRNA dimethylase 2) (Mitochondrial transcription factor B2) (h-mtTFB) (h-mtTFB2) (hTFB2M) (mtTFB2) (S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2)

 TFB2M_HUMAN             Reviewed;         396 AA.
Q9H5Q4; Q9H626;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
05-DEC-2018, entry version 158.
RecName: Full=Dimethyladenosine transferase 2, mitochondrial;
EC=2.1.1.-;
AltName: Full=Hepatitis C virus NS5A-transactivated protein 5;
Short=HCV NS5A-transactivated protein 5;
AltName: Full=Mitochondrial 12S rRNA dimethylase 2;
AltName: Full=Mitochondrial transcription factor B2;
Short=h-mtTFB;
Short=h-mtTFB2;
Short=hTFB2M;
Short=mtTFB2;
AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2;
Flags: Precursor;
Name=TFB2M; Synonyms=NS5ATP5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Liu Y., Cheng J., Wang G., Wang J., Zhang L., Chen J., Li L.;
"Cloning and identification of human gene 5 transactivated by
hepatitis C virus NS5A protein.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Small intestine;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
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).
[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, AND INTERACTION WITH TFAM.
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]
FUNCTION.
PubMed=15526033; DOI=10.1038/sj.emboj.7600465;
Gaspari M., Falkenberg M., Larsson N.-G., Gustafsson C.M.;
"The mitochondrial RNA polymerase contributes critically to promoter
specificity in mammalian cells.";
EMBO J. 23:4606-4614(2004).
[8]
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).
[9]
ENZYME ACTIVITY, AND MUTAGENESIS OF GLY-105.
PubMed=17031457; DOI=10.1007/s00239-006-0075-1;
Cotney J., Shadel G.S.;
"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.";
J. Mol. Evol. 63:707-717(2006).
[10]
FUNCTION.
PubMed=20410300; DOI=10.1074/jbc.C110.128918;
Litonin D., Sologub M., Shi Y., Savkina M., Anikin M., Falkenberg M.,
Gustafsson C.M., Temiakov D.;
"Human mitochondrial transcription revisited: only TFAM and TFB2M are
required for transcription of the mitochondrial genes in vitro.";
J. Biol. Chem. 285:18129-18133(2010).
[11]
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).
[12]
VARIANTS THR-64 AND TYR-264.
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).
[13]
VARIANTS PHE-48 AND THR-64.
PubMed=18980857; DOI=10.1016/j.parkreldis.2008.09.004;
Sanchez-Ferrero E., Coto E., Blazquez M., Ribacoba R., Guisasola L.M.,
Salvador C., Alvarez V.;
"Mutational screening of the mitochondrial transcription factors B1
and B2 (TFB1M and TFB2M) in Parkinson's disease.";
Parkinsonism Relat. Disord. 15:468-470(2009).
-!- 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. Compared to TFB1M, it activates
transcription of mitochondrial DNA more efficiently, while it has
less methyltransferase activity. {ECO:0000269|PubMed:12068295,
ECO:0000269|PubMed:12897151, ECO:0000269|PubMed:15526033,
ECO:0000269|PubMed:20410300}.
-!- SUBUNIT: Interacts with mitochondrial RNA polymerase POLRMT.
Interacts with TFAM. {ECO:0000269|PubMed:12068295,
ECO:0000269|PubMed:12897151}.
-!- SUBCELLULAR LOCATION: Mitochondrion.
-!- 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}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. rRNA adenine N(6)-methyltransferase
family. KsgA subfamily. {ECO:0000255|PROSITE-ProRule:PRU01026}.
-!- SEQUENCE CAUTION:
Sequence=BAB15441.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF529366; AAQ09600.1; -; mRNA.
EMBL; AK026314; BAB15441.1; ALT_INIT; mRNA.
EMBL; AK026835; BAB15566.1; -; mRNA.
EMBL; AL356583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003383; AAH03383.1; -; mRNA.
CCDS; CCDS1627.1; -.
RefSeq; NP_071761.1; NM_022366.2.
UniGene; Hs.7395; -.
PDB; 6ERO; X-ray; 1.75 A; A/B=63-267, A/B=295-396.
PDB; 6ERP; X-ray; 4.50 A; F/J=21-396.
PDB; 6ERQ; X-ray; 4.50 A; F/J=22-396.
PDBsum; 6ERO; -.
PDBsum; 6ERP; -.
PDBsum; 6ERQ; -.
ProteinModelPortal; Q9H5Q4; -.
SMR; Q9H5Q4; -.
BioGrid; 122106; 29.
DIP; DIP-50540N; -.
IntAct; Q9H5Q4; 15.
STRING; 9606.ENSP00000355471; -.
iPTMnet; Q9H5Q4; -.
PhosphoSitePlus; Q9H5Q4; -.
SwissPalm; Q9H5Q4; -.
BioMuta; TFB2M; -.
DMDM; 74752681; -.
EPD; Q9H5Q4; -.
MaxQB; Q9H5Q4; -.
PaxDb; Q9H5Q4; -.
PeptideAtlas; Q9H5Q4; -.
PRIDE; Q9H5Q4; -.
ProteomicsDB; 80926; -.
DNASU; 64216; -.
Ensembl; ENST00000366514; ENSP00000355471; ENSG00000162851.
GeneID; 64216; -.
KEGG; hsa:64216; -.
UCSC; uc001ibn.4; human.
CTD; 64216; -.
DisGeNET; 64216; -.
EuPathDB; HostDB:ENSG00000162851.7; -.
GeneCards; TFB2M; -.
HGNC; HGNC:18559; TFB2M.
HPA; HPA028482; -.
HPA; HPA028554; -.
HPA; HPA030265; -.
MIM; 607055; gene.
neXtProt; NX_Q9H5Q4; -.
OpenTargets; ENSG00000162851; -.
PharmGKB; PA38348; -.
eggNOG; KOG0820; Eukaryota.
eggNOG; COG0030; LUCA.
GeneTree; ENSGT00510000048533; -.
HOGENOM; HOG000060174; -.
HOVERGEN; HBG094037; -.
InParanoid; Q9H5Q4; -.
KO; K17653; -.
OMA; KWVPGCG; -.
OrthoDB; EOG091G0DOP; -.
PhylomeDB; Q9H5Q4; -.
TreeFam; TF325100; -.
Reactome; R-HSA-163282; Mitochondrial transcription initiation.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
GeneWiki; TFB2M; -.
GenomeRNAi; 64216; -.
PRO; PR:Q9H5Q4; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162851; Expressed in 220 organ(s), highest expression level in secondary oocyte.
CleanEx; HS_TFB2M; -.
Genevisible; Q9H5Q4; HS.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central.
GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
GO; GO:0006390; P:mitochondrial transcription; IDA:UniProtKB.
GO; GO:0007005; P:mitochondrion organization; TAS:Reactome.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
GO; GO:0006391; P:transcription initiation from mitochondrial promoter; IDA:UniProtKB.
InterPro; IPR001737; KsgA/Erm.
InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR016861; TFB2M.
PANTHER; PTHR11727; PTHR11727; 1.
PANTHER; PTHR11727:SF13; PTHR11727:SF13; 1.
Pfam; PF00398; RrnaAD; 1.
SMART; SM00650; rADc; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Methyltransferase; Mitochondrion;
Polymorphism; Reference proteome; RNA-binding; rRNA processing;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase; Transit peptide.
TRANSIT 1 19 Mitochondrion. {ECO:0000255}.
CHAIN 20 396 Dimethyladenosine transferase 2,
mitochondrial.
/FTId=PRO_0000273179.
BINDING 75 75 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000255|PROSITE-
ProRule:PRU01026}.
BINDING 124 124 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU01026}.
BINDING 150 150 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU01026}.
VARIANT 48 48 S -> F (in dbSNP:rs148620105).
{ECO:0000269|PubMed:18980857}.
/FTId=VAR_071249.
VARIANT 64 64 A -> T (in dbSNP:rs143880306).
{ECO:0000269|PubMed:18980857,
ECO:0000269|PubMed:19096125}.
/FTId=VAR_071250.
VARIANT 156 156 P -> L (in dbSNP:rs11585481).
/FTId=VAR_030097.
VARIANT 264 264 H -> Y (in dbSNP:rs12037377).
{ECO:0000269|PubMed:19096125}.
/FTId=VAR_030098.
MUTAGEN 105 105 G->A: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:17031457}.
CONFLICT 200 201 EK -> GR (in Ref. 2; BAB15441).
{ECO:0000305}.
HELIX 78 89 {ECO:0000244|PDB:6ERO}.
STRAND 99 102 {ECO:0000244|PDB:6ERO}.
HELIX 108 115 {ECO:0000244|PDB:6ERO}.
STRAND 120 125 {ECO:0000244|PDB:6ERO}.
HELIX 127 129 {ECO:0000244|PDB:6ERO}.
HELIX 130 139 {ECO:0000244|PDB:6ERO}.
STRAND 140 142 {ECO:0000244|PDB:6ERO}.
STRAND 144 148 {ECO:0000244|PDB:6ERO}.
HELIX 151 153 {ECO:0000244|PDB:6ERO}.
STRAND 157 159 {ECO:0000244|PDB:6ERO}.
STRAND 164 166 {ECO:0000244|PDB:6ERO}.
HELIX 169 176 {ECO:0000244|PDB:6ERO}.
STRAND 190 194 {ECO:0000244|PDB:6ERO}.
HELIX 200 213 {ECO:0000244|PDB:6ERO}.
HELIX 216 220 {ECO:0000244|PDB:6ERO}.
STRAND 299 304 {ECO:0000244|PDB:6ERO}.
HELIX 305 311 {ECO:0000244|PDB:6ERO}.
HELIX 317 319 {ECO:0000244|PDB:6ERO}.
HELIX 323 329 {ECO:0000244|PDB:6ERO}.
STRAND 333 335 {ECO:0000244|PDB:6ERO}.
TURN 340 342 {ECO:0000244|PDB:6ERO}.
STRAND 354 356 {ECO:0000244|PDB:6ERO}.
HELIX 362 364 {ECO:0000244|PDB:6ERO}.
HELIX 369 379 {ECO:0000244|PDB:6ERO}.
SEQUENCE 396 AA; 45349 MW; C13DC398974BB88F CRC64;
MWIPVVGLPR RLRLSALAGA GRFCILGSEA ATRKHLPARN HCGLSDSSPQ LWPEPDFRNP
PRKASKASLD FKRYVTDRRL AETLAQIYLG KPSRPPHLLL ECNPGPGILT QALLEAGAKV
VALESDKTFI PHLESLGKNL DGKLRVIHCD FFKLDPRSGG VIKPPAMSSR GLFKNLGIEA
VPWTADIPLK VVGMFPSRGE KRALWKLAYD LYSCTSIYKF GRIEVNMFIG EKEFQKLMAD
PGNPDLYHVL SVIWQLACEI KVLHMEPWSS FDIYTRKGPL ENPKRRELLD QLQQKLYLIQ
MIPRQNLFTK NLTPMNYNIF FHLLKHCFGR RSATVIDHLR SLTPLDARDI LMQIGKQEDE
KVVNMHPQDF KTLFETIERS KDCAYKWLYD ETLEDR


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EIAAB29713 HCV NS5A-transactivated protein 9 homolog,Mouse,Mus musculus,Ns5atp9,p15PAF,Paf,PCNA-associated factor
bs-8158R Rabbit Anti-HCV NS5A transactivated protein 8 Polyclonal Antibody 100ul
bs-8158R-Cy7 Rabbit Anti-HCV NS5A transactivated protein 8 Polyclonal Antibody, Cy7 Conjugated 100ul
bs-8158R-Cy3 Rabbit Anti-HCV NS5A transactivated protein 8 Polyclonal Antibody, Cy3 Conjugated 100ul
bs-8158R-Cy5.5 Rabbit Anti-HCV NS5A transactivated protein 8 Polyclonal Antibody, Cy5.5 Conjugated 100ul
bs-8158R Rabbit Anti-BTBD1_HCV NS5A transactivated protein 8 Polyclonal Antibody 100ug Lyophilized
bs-8158R-Cy5 Rabbit Anti-HCV NS5A transactivated protein 8 Polyclonal Antibody, Cy5 Conjugated 100ul


 

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