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Q3TL26

- TFB2M_MOUSE

UniProt

Q3TL26 - TFB2M_MOUSE

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Protein
Dimethyladenosine transferase 2, mitochondrial
Gene
Tfb2m
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei74 – 741S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding sitei123 – 1231S-adenosyl-L-methionine By similarity
Binding sitei149 – 1491S-adenosyl-L-methionine By similarity

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW
  2. rRNA (adenine-N6,N6-)-dimethyltransferase activity Source: InterPro
  3. transcription cofactor activity Source: InterPro

GO - Biological processi

  1. positive regulation of transcription, DNA-templated Source: UniProtKB
  2. transcription initiation from mitochondrial promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

rRNA processing, Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_205251. Transcriptional activation of mitochondrial biogenesis.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Tfb2m
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:107937. Tfb2m.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343Mitochondrion Reviewed prediction
Add
BLAST
Chaini44 – 396353Dimethyladenosine transferase 2, mitochondrial
PRO_0000273180Add
BLAST

Proteomic databases

PaxDbiQ3TL26.
PRIDEiQ3TL26.

PTM databases

PhosphoSiteiQ3TL26.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ3TL26.
CleanExiMM_TFB2M.
GenevestigatoriQ3TL26.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ3TL26.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0030.
GeneTreeiENSGT00510000048533.
HOGENOMiHOG000060174.
HOVERGENiHBG094037.
InParanoidiQ3TL26.
KOiK17653.
OMAiLLMMIKQ.
OrthoDBiEOG7RNK0M.
PhylomeDBiQ3TL26.
TreeFamiTF325100.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR016861. Mt_di-Me-Ado_Trfase_2_prcur.
IPR001737. rRNA_Ade_methylase_transferase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERiPTHR11727. PTHR11727. 1 hit.
PfamiPF00398. RrnaAD. 1 hit.
[Graphical view]
PIRSFiPIRSF027833. MtTFB2. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3TL26-1 [UniParc]FASTAAdd to Basket

« Hide

MRGPAMRLPP RIALSALARG PSCILGSGAA TRKDWQTRNR RGFSDFNIEP    50
LPDSDLEESS PWTSRNRSEP TRHIACKKAA RNLVRDLLEH QNPSRQIILE 100
CNPGPGILTG ALLKAGARVV AFESEKTFIP HLEPLQRNMD GELQVVHCDF 150
FKMDPRYQEV VRPDVSSQAI FQNLGIKAVP WSAGVPIKVF GILPYKHERR 200
ILWKILFDLY SCESIYRYGR VELNMFVSEK EFRKLIATPK RPDLYQVMAV 250
LWQVACDVKF LHMEPWSSFS VHTENGHLEK SKHGESVNLL KQNLYLVRMT 300
PRRTLFTENL SPLNYDIFFH LVKHCFGKRN APIIRHLRSL STVDPINILR 350
QIRKNPGDTA ARMYPHDFKK LFETIEQSED SVFKWIYDYC PEDMEF 396
Length:396
Mass (Da):45,864
Last modified:October 11, 2005 - v1
Checksum:iD276BD58D595F111
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121I → L in AAA37817. 1 Publication
Sequence conflicti40 – 401R → G in AAA37817. 1 Publication
Sequence conflicti273 – 2731T → M in AAA37817. 1 Publication
Sequence conflicti292 – 2921Q → P in BAC41095. 1 Publication
Sequence conflicti308 – 3081E → G in BAC41095. 1 Publication
Sequence conflicti324 – 3241H → P in BAC41095. 1 Publication
Sequence conflicti330 – 3301N → H in BAC41095. 1 Publication
Sequence conflicti338 – 3381R → P in BAC41095. 1 Publication
Sequence conflicti377 – 3771Q → P in BAC41095. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS15561.1.
PIRiS27870.
RefSeqiNP_032275.2. NM_008249.4.
UniGeneiMm.293529.

Genome annotation databases

EnsembliENSMUST00000027769; ENSMUSP00000027769; ENSMUSG00000026492.
GeneIDi15278.
KEGGimmu:15278.
UCSCiuc007dvl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS15561.1.
PIRi S27870.
RefSeqi NP_032275.2. NM_008249.4.
UniGenei Mm.293529.

3D structure databases

ProteinModelPortali Q3TL26.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q3TL26.

Proteomic databases

PaxDbi Q3TL26.
PRIDEi Q3TL26.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027769 ; ENSMUSP00000027769 ; ENSMUSG00000026492 .
GeneIDi 15278.
KEGGi mmu:15278.
UCSCi uc007dvl.1. mouse.

Organism-specific databases

CTDi 64216.
MGIi MGI:107937. Tfb2m.

Phylogenomic databases

eggNOGi COG0030.
GeneTreei ENSGT00510000048533.
HOGENOMi HOG000060174.
HOVERGENi HBG094037.
InParanoidi Q3TL26.
KOi K17653.
OMAi LLMMIKQ.
OrthoDBi EOG7RNK0M.
PhylomeDBi Q3TL26.
TreeFami TF325100.

Enzyme and pathway databases

Reactomei REACT_205251. Transcriptional activation of mitochondrial biogenesis.

Miscellaneous databases

NextBioi 287913.
PROi Q3TL26.
SOURCEi Search...

Gene expression databases

Bgeei Q3TL26.
CleanExi MM_TFB2M.
Genevestigatori Q3TL26.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR016861. Mt_di-Me-Ado_Trfase_2_prcur.
IPR001737. rRNA_Ade_methylase_transferase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
PANTHERi PTHR11727. PTHR11727. 1 hit.
Pfami PF00398. RrnaAD. 1 hit.
[Graphical view ]
PIRSFi PIRSF027833. MtTFB2. 1 hit.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiTFB2M_MOUSE
AccessioniPrimary (citable) accession number: Q3TL26
Secondary accession number(s): Q61669, Q8BTJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: October 11, 2005
Last modified: September 3, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi