Q9H5Q4 (TFB2M_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dimethyladenosine transferase 2, mitochondrial
EC=2.1.1.-

Alternative name(s):
Hepatitis C virus NS5A-transactivated protein 5
Short name=HCV NS5A-transactivated protein 5
Mitochondrial 12S rRNA dimethylase 2
Mitochondrial transcription factor B2
Short name=h-mtTFB
Short name=h-mtTFB2
Short name=hTFB2M
Short name=mtTFB2
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2

Gene names

Name:	TFB2M
Synonyms:	NS5ATP5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Compared to TFB1M, it activates transcription of mitochondrial DNA more efficiently, while it has less methyltransferase activity. Ref.5 Ref.6 Ref.7 Ref.10
Subunit structure	Interacts with mitochondrial RNA polymerase POLRMT. Interacts with TFAM. Ref.5 Ref.6
Subcellular location	Mitochondrion.
Tissue specificity	Ubiquitously expressed. Ref.5
Induction	By the nuclear respiratory factors NRF1 and NRF2/GABPB2 and PGC-1 coactivators. Ref.8
Sequence similarities	Belongs to the methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. KsgA subfamily.
Sequence caution	The sequence BAB15441.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation rRNA processing
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.10. Source: UniProtKB transcription initiation from mitochondrial promoter Inferred from direct assay Ref.10. Source: UniProtKB
Cellular_component	mitochondrial nucleoid Inferred from direct assay PubMed 18063578. Source: BHF-UCL
Molecular_function	rRNA (adenine-N6,N6-)-dimethyltransferase activity Inferred from electronic annotation. Source: InterPro transcription cofactor activity Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 19	19	Mitochondrion Potential
	Chain	20 – 396	377	Dimethyladenosine transferase 2, mitochondrial		PRO_0000273179
Natural variations
	Natural variant	156	1	P → L. Corresponds to variant rs11585481 [ dbSNP | Ensembl ].		VAR_030097
	Natural variant	264	1	H → Y. Corresponds to variant rs12037377 [ dbSNP | Ensembl ].		VAR_030098
Experimental info
	Mutagenesis	105	1	G → A: Abolishes methyltransferase activity. Ref.9
	Sequence conflict	200 – 201	2	EK → GR in BAB15441. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9H5Q4 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: C13DC398974BB88F	FASTA	396	45,349
	10 20 30 40 50 60 MWIPVVGLPR RLRLSALAGA GRFCILGSEA ATRKHLPARN HCGLSDSSPQ LWPEPDFRNP 70 80 90 100 110 120 PRKASKASLD FKRYVTDRRL AETLAQIYLG KPSRPPHLLL ECNPGPGILT QALLEAGAKV 130 140 150 160 170 180 VALESDKTFI PHLESLGKNL DGKLRVIHCD FFKLDPRSGG VIKPPAMSSR GLFKNLGIEA 190 200 210 220 230 240 VPWTADIPLK VVGMFPSRGE KRALWKLAYD LYSCTSIYKF GRIEVNMFIG EKEFQKLMAD 250 260 270 280 290 300 PGNPDLYHVL SVIWQLACEI KVLHMEPWSS FDIYTRKGPL ENPKRRELLD QLQQKLYLIQ 310 320 330 340 350 360 MIPRQNLFTK NLTPMNYNIF FHLLKHCFGR RSATVIDHLR SLTPLDARDI LMQIGKQEDE 370 380 390 KVVNMHPQDF KTLFETIERS KDCAYKWLYD ETLEDR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and identification of human gene 5 transactivated by hepatitis C virus NS5A protein." Liu Y., Cheng J., Wang G., Wang J., Zhang L., Chen J., Li L. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung and Small intestine.
[3]	"The DNA sequence and biological annotation of human chromosome 1." 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. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: Placenta.
[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.
[7]	"The mitochondrial RNA polymerase contributes critically to promoter specificity in mammalian cells." Gaspari M., Falkenberg M., Larsson N.-G., Gustafsson C.M. EMBO J. 23:4606-4614(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"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.
[9]	"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." Cotney J., Shadel G.S. J. Mol. Evol. 63:707-717(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME ACTIVITY, MUTAGENESIS OF GLY-105.
[10]	"Human mitochondrial transcription revisited: only TFAM and TFB2M are required for transcription of the mitochondrial genes in vitro." Litonin D., Sologub M., Shi Y., Savkina M., Anikin M., Falkenberg M., Gustafsson C.M., Temiakov D. J. Biol. Chem. 285:18129-18133(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF529366 mRNA. Translation: AAQ09600.1. AK026314 mRNA. Translation: BAB15441.1. Different initiation. AK026835 mRNA. Translation: BAB15566.1. AL356583 Genomic DNA. Translation: CAI16399.1. BC003383 mRNA. Translation: AAH03383.1.
IPI	IPI00034069.
RefSeq	NP_071761.1. NM_022366.2.
UniGene	Hs.732088.
3D structure databases
ProteinModelPortal	Q9H5Q4.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-50540N.
IntAct	Q9H5Q4. 2 interactions.
STRING	9606.ENSP00000355471.
PTM databases
PhosphoSite	Q9H5Q4.
Polymorphism databases
DMDM	74752681.
Proteomic databases
PaxDb	Q9H5Q4.
PeptideAtlas	Q9H5Q4.
PRIDE	Q9H5Q4.
Protocols and materials databases
DNASU	64216.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000366514; ENSP00000355471; ENSG00000162851.
GeneID	64216.
KEGG	hsa:64216.
UCSC	uc001ibn.3. human.
Organism-specific databases
CTD	64216.
GeneCards	GC01M246703.
HGNC	HGNC:18559. TFB2M.
HPA	HPA030265.
MIM	607055. gene.
neXtProt	NX_Q9H5Q4.
PharmGKB	PA38348.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0030.
HOGENOM	HOG000060174.
HOVERGEN	HBG094037.
InParanoid	Q9H5Q4.
OMA	VIHCDFF.
OrthoDB	EOG43N7CQ.
Enzyme and pathway databases
Reactome	REACT_1788. Transcription. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q9H5Q4.
Bgee	Q9H5Q4.
CleanEx	HS_TFB2M.
Genevestigator	Q9H5Q4.
Family and domain databases
InterPro	IPR016861. Mt_di-Me-Ado_Trfase_2_prcur. IPR001737. rRNA_Ade_methylase_transferase. [Graphical view]
PANTHER	PTHR11727. PTHR11727. 1 hit.
Pfam	PF00398. RrnaAD. 1 hit. [Graphical view]
PIRSF	PIRSF027833. MtTFB2. 1 hit.
PROSITE	PS01131. RRNA_A_DIMETH. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	64216.
NextBio	66127.
SOURCE	Search...

Entry information

Entry name

TFB2M_HUMAN

Accession

Primary (citable) accession number: Q9H5Q4
Secondary accession number(s): Q9H626

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.