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Q9H5Q4 (TFB2M_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length396 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. 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 class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. KsgA subfamily.

Sequence caution

The sequence BAB15441.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1919Mitochondrion Potential
Chain20 – 396377Dimethyladenosine transferase 2, mitochondrial
PRO_0000273179

Sites

Binding site751S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site1241S-adenosyl-L-methionine By similarity
Binding site1501S-adenosyl-L-methionine By similarity

Natural variations

Natural variant1561P → L.
Corresponds to variant rs11585481 [ dbSNP | Ensembl ].
VAR_030097
Natural variant2641H → Y.
Corresponds to variant rs12037377 [ dbSNP | Ensembl ].
VAR_030098

Experimental info

Mutagenesis1051G → A: Abolishes methyltransferase activity. Ref.9
Sequence conflict200 – 2012EK → GR in BAB15441. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9H5Q4 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: C13DC398974BB88F

FASTA39645,349
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_071761.1. NM_022366.2.
UniGeneHs.7395.

3D structure databases

ProteinModelPortalQ9H5Q4.
SMRQ9H5Q4. Positions 78-154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122106. 7 interactions.
DIPDIP-50540N.
IntActQ9H5Q4. 2 interactions.
STRING9606.ENSP00000355471.

PTM databases

PhosphoSiteQ9H5Q4.

Polymorphism databases

DMDM74752681.

Proteomic databases

PaxDbQ9H5Q4.
PeptideAtlasQ9H5Q4.
PRIDEQ9H5Q4.

Protocols and materials databases

DNASU64216.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366514; ENSP00000355471; ENSG00000162851.
GeneID64216.
KEGGhsa:64216.
UCSCuc001ibn.3. human.

Organism-specific databases

CTD64216.
GeneCardsGC01M246703.
HGNCHGNC:18559. TFB2M.
HPAHPA030265.
MIM607055. gene.
neXtProtNX_Q9H5Q4.
PharmGKBPA38348.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0030.
HOGENOMHOG000060174.
HOVERGENHBG094037.
InParanoidQ9H5Q4.
KOK17653.
OMAVIHCDFF.
OrthoDBEOG7RNK0M.
PhylomeDBQ9H5Q4.
TreeFamTF325100.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9H5Q4.
BgeeQ9H5Q4.
CleanExHS_TFB2M.
GenevestigatorQ9H5Q4.

Family and domain databases

InterProIPR016861. Mt_di-Me-Ado_Trfase_2_prcur.
IPR001737. rRNA_Ade_methylase_transferase.
[Graphical view]
PANTHERPTHR11727. PTHR11727. 1 hit.
PfamPF00398. RrnaAD. 1 hit.
[Graphical view]
PIRSFPIRSF027833. MtTFB2. 1 hit.
PROSITEPS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTFB2M.
GenomeRNAi64216.
NextBio66127.
PROQ9H5Q4.
SOURCESearch...

Entry information

Entry nameTFB2M_HUMAN
AccessionPrimary (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: April 16, 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM