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Q3TL26 (TFB2M_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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):
Mitochondrial 12S rRNA dimethylase 2
Mitochondrial transcription factor B2
Short name=mTFB2M
Short name=mtTFB2
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2
Gene names
Name:Tfb2m
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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

Subunit structure

Interacts with mitochondrial RNA polymerase POLRMT. Interacts with TFAM By similarity.

Subcellular location

Mitochondrion By similarity.

Tissue specificity

Ubiquitously expressed. Ref.3

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Mitochondrion Potential
Chain44 – 396353Dimethyladenosine transferase 2, mitochondrial
PRO_0000273180

Sites

Binding site741S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site1231S-adenosyl-L-methionine By similarity
Binding site1491S-adenosyl-L-methionine By similarity

Experimental info

Sequence conflict121I → L in AAA37817. Ref.1
Sequence conflict401R → G in AAA37817. Ref.1
Sequence conflict2731T → M in AAA37817. Ref.1
Sequence conflict2921Q → P in BAC41095. Ref.2
Sequence conflict3081E → G in BAC41095. Ref.2
Sequence conflict3241H → P in BAC41095. Ref.2
Sequence conflict3301N → H in BAC41095. Ref.2
Sequence conflict3381R → P in BAC41095. Ref.2
Sequence conflict3771Q → P in BAC41095. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q3TL26 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: D276BD58D595F111

FASTA39645,864
        10         20         30         40         50         60 
MRGPAMRLPP RIALSALARG PSCILGSGAA TRKDWQTRNR RGFSDFNIEP LPDSDLEESS 

        70         80         90        100        110        120 
PWTSRNRSEP TRHIACKKAA RNLVRDLLEH QNPSRQIILE CNPGPGILTG ALLKAGARVV 

       130        140        150        160        170        180 
AFESEKTFIP HLEPLQRNMD GELQVVHCDF FKMDPRYQEV VRPDVSSQAI FQNLGIKAVP 

       190        200        210        220        230        240 
WSAGVPIKVF GILPYKHERR ILWKILFDLY SCESIYRYGR VELNMFVSEK EFRKLIATPK 

       250        260        270        280        290        300 
RPDLYQVMAV LWQVACDVKF LHMEPWSSFS VHTENGHLEK SKHGESVNLL KQNLYLVRMT 

       310        320        330        340        350        360 
PRRTLFTENL SPLNYDIFFH LVKHCFGKRN APIIRHLRSL STVDPINILR QIRKNPGDTA 

       370        380        390 
ARMYPHDFKK LFETIEQSED SVFKWIYDYC PEDMEF 

« Hide

References

« Hide 'large scale' references
[1]Wang B., Hunsperger J.P., Laib J., Fan D.
Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Lymphoma.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: BALB/c and C57BL/6J.
Tissue: Heart.
[3]"Characterization of the mouse genes for mitochondrial transcription factors B1 and B2."
Rantanen A., Gaspari M., Falkenberg M., Gustafsson C.M., Larsson N.-G.
Mamm. Genome 14:1-6(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[4]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74555 mRNA. Translation: AAA37817.1.
AK090106 mRNA. Translation: BAC41095.1.
AK146563 mRNA. Translation: BAE27262.1.
AK166717 mRNA. Translation: BAE38967.1.
AK167930 mRNA. Translation: BAE39934.1.
AK168970 mRNA. Translation: BAE40774.1.
AK169138 mRNA. Translation: BAE40917.1.
PIRS27870.
RefSeqNP_032275.2. NM_008249.4.
UniGeneMm.293529.

3D structure databases

ProteinModelPortalQ3TL26.
SMRQ3TL26. Positions 90-155.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ3TL26.

Proteomic databases

PaxDbQ3TL26.
PRIDEQ3TL26.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027769; ENSMUSP00000027769; ENSMUSG00000026492.
GeneID15278.
KEGGmmu:15278.
UCSCuc007dvl.1. mouse.

Organism-specific databases

CTD64216.
MGIMGI:107937. Tfb2m.

Phylogenomic databases

eggNOGCOG0030.
GeneTreeENSGT00510000048533.
HOGENOMHOG000060174.
HOVERGENHBG094037.
InParanoidQ3TL26.
KOK17653.
OMALLMMIKQ.
OrthoDBEOG7RNK0M.
PhylomeDBQ3TL26.
TreeFamTF325100.

Gene expression databases

BgeeQ3TL26.
CleanExMM_TFB2M.
GenevestigatorQ3TL26.

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

NextBio287913.
PROQ3TL26.
SOURCESearch...

Entry information

Entry nameTFB2M_MOUSE
AccessionPrimary (citable) accession number: Q3TL26
Secondary accession number(s): Q61669, Q8BTJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: October 11, 2005
Last modified: April 16, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot