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Protein

Dimethyladenosine transferase 1, mitochondrial

Gene

Tfb1m

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei38 – 381S-adenosyl-L-methionine; via amide nitrogenBy similarity
Binding sitei63 – 631S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei85 – 851S-adenosyl-L-methionine1 Publication
Binding sitei111 – 1111S-adenosyl-L-methionine1 Publication
Binding sitei141 – 1411S-adenosyl-L-methionineBy similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: MGI
  3. rRNA (adenine-N6,N6-)-dimethyltransferase activity Source: InterPro

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

rRNA processing, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_328033. Transcriptional activation of mitochondrial biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Dimethyladenosine transferase 1, mitochondrial (EC:2.1.1.-)
Alternative name(s):
Mitochondrial 12S rRNA dimethylase 1
Mitochondrial transcription factor B1
Short name:
mtTFB1
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 1
Gene namesi
Name:Tfb1m
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:2146851. Tfb1m.

Subcellular locationi

  1. Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrial nucleoid Source: MGI
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionSequence AnalysisAdd
BLAST
Chaini28 – 345318Dimethyladenosine transferase 1, mitochondrialPRO_0000273173Add
BLAST

Proteomic databases

MaxQBiQ8JZM0.
PaxDbiQ8JZM0.
PRIDEiQ8JZM0.

PTM databases

PhosphoSiteiQ8JZM0.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ8JZM0.
CleanExiMM_TFB1M.
GenevestigatoriQ8JZM0.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000035291.

Structurei

Secondary structure

1
345
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 3013Combined sources
Beta strandi31 – 333Combined sources
Helixi41 – 5111Combined sources
Beta strandi58 – 625Combined sources
Turni65 – 673Combined sources
Helixi68 – 747Combined sources
Turni75 – 773Combined sources
Beta strandi79 – 846Combined sources
Helixi88 – 903Combined sources
Helixi91 – 10010Combined sources
Turni102 – 1043Combined sources
Beta strandi105 – 1084Combined sources
Turni112 – 1143Combined sources
Turni118 – 1203Combined sources
Helixi123 – 1253Combined sources
Beta strandi135 – 1406Combined sources
Helixi144 – 16017Combined sources
Helixi163 – 1675Combined sources
Beta strandi171 – 1777Combined sources
Helixi178 – 1858Combined sources
Helixi195 – 2017Combined sources
Beta strandi204 – 2129Combined sources
Helixi214 – 2163Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi225 – 2328Combined sources
Helixi242 – 25312Combined sources
Helixi260 – 2645Combined sources
Helixi265 – 2673Combined sources
Helixi270 – 2723Combined sources
Helixi273 – 28412Combined sources
Helixi292 – 2943Combined sources
Helixi297 – 31317Combined sources
Helixi317 – 3193Combined sources
Helixi322 – 3265Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GC5X-ray1.80A1-345[»]
4GC9X-ray2.10A1-345[»]
ProteinModelPortaliQ8JZM0.
SMRiQ8JZM0. Positions 10-328.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 384S-adenosyl-L-methionine binding

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0030.
GeneTreeiENSGT00530000063389.
HOGENOMiHOG000227961.
HOVERGENiHBG082484.
InParanoidiQ8JZM0.
KOiK15266.
OMAiFRLQAVK.
OrthoDBiEOG7DJSMJ.
PhylomeDBiQ8JZM0.
TreeFamiTF300798.

Family and domain databases

Gene3Di1.10.8.100. 1 hit.
3.40.50.150. 1 hit.
HAMAPiMF_00607. 16SrRNA_methyltr_A.
InterProiIPR001737. KsgA/Erm.
IPR023165. rRNA_Ade_diMease-like.
IPR020596. rRNA_Ade_Mease_Trfase_CS.
IPR020598. rRNA_Ade_methylase_Trfase_N.
IPR011530. rRNA_adenine_dimethylase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11727. PTHR11727. 1 hit.
PfamiPF00398. RrnaAD. 1 hit.
[Graphical view]
SMARTiSM00650. rADc. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00755. ksgA. 1 hit.
PROSITEiPS01131. RRNA_A_DIMETH. 1 hit.
PS51689. 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.

Q8JZM0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASGKLGTF RLPPLPTIRE IIKLFGLRAV KQLSQNFLLD LRLTDKIVRK
60 70 80 90 100
AGSLADVYVY EVGPGPGGIT RSILNANVAE LLVVEKDTRF IPGLQMLSDA
110 120 130 140 150
APGKLRIVHG DVLTYKIEKA FPGNIRRQWE DDPPNVHIIG NLPFSVSTPL
160 170 180 190 200
IIKWLENISL KDGPFVYGRT KMTLTFQKEV AERLVATTGS KQHSRLSIMA
210 220 230 240 250
QYLCNVEHLF TIPGKAFVPK PKVDVGVVHL TPLIEPKIKQ PFKLVEKVVQ
260 270 280 290 300
NAFQFRRKYC HRGLGMLFPE AQRLESTGRL LQLADIDPTL RPTHLSLMHF
310 320 330 340
KSLCDVYRKM CDEDPQLFTY NFREELKQKK SKGQEKDGDP ESCGF
Length:345
Mass (Da):38,962
Last modified:October 1, 2002 - v1
Checksum:i97BF51EC95328AD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF508971 mRNA. Translation: AAM33651.1.
BC032930 mRNA. Translation: AAH32930.1.
CCDSiCCDS28363.1.
RefSeqiNP_666186.1. NM_146074.1.
UniGeneiMm.226554.

Genome annotation databases

EnsembliENSMUST00000041003; ENSMUSP00000035291; ENSMUSG00000036983.
GeneIDi224481.
KEGGimmu:224481.
UCSCiuc008aes.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF508971 mRNA. Translation: AAM33651.1.
BC032930 mRNA. Translation: AAH32930.1.
CCDSiCCDS28363.1.
RefSeqiNP_666186.1. NM_146074.1.
UniGeneiMm.226554.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GC5X-ray1.80A1-345[»]
4GC9X-ray2.10A1-345[»]
ProteinModelPortaliQ8JZM0.
SMRiQ8JZM0. Positions 10-328.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000035291.

PTM databases

PhosphoSiteiQ8JZM0.

Proteomic databases

MaxQBiQ8JZM0.
PaxDbiQ8JZM0.
PRIDEiQ8JZM0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041003; ENSMUSP00000035291; ENSMUSG00000036983.
GeneIDi224481.
KEGGimmu:224481.
UCSCiuc008aes.1. mouse.

Organism-specific databases

CTDi51106.
MGIiMGI:2146851. Tfb1m.

Phylogenomic databases

eggNOGiCOG0030.
GeneTreeiENSGT00530000063389.
HOGENOMiHOG000227961.
HOVERGENiHBG082484.
InParanoidiQ8JZM0.
KOiK15266.
OMAiFRLQAVK.
OrthoDBiEOG7DJSMJ.
PhylomeDBiQ8JZM0.
TreeFamiTF300798.

Enzyme and pathway databases

ReactomeiREACT_328033. Transcriptional activation of mitochondrial biogenesis.

Miscellaneous databases

NextBioi377199.
PROiQ8JZM0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8JZM0.
CleanExiMM_TFB1M.
GenevestigatoriQ8JZM0.

Family and domain databases

Gene3Di1.10.8.100. 1 hit.
3.40.50.150. 1 hit.
HAMAPiMF_00607. 16SrRNA_methyltr_A.
InterProiIPR001737. KsgA/Erm.
IPR023165. rRNA_Ade_diMease-like.
IPR020596. rRNA_Ade_Mease_Trfase_CS.
IPR020598. rRNA_Ade_methylase_Trfase_N.
IPR011530. rRNA_adenine_dimethylase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11727. PTHR11727. 1 hit.
PfamiPF00398. RrnaAD. 1 hit.
[Graphical view]
SMARTiSM00650. rADc. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00755. ksgA. 1 hit.
PROSITEiPS01131. RRNA_A_DIMETH. 1 hit.
PS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129.
  2. "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: Mammary gland.
  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. "Structural basis for S-adenosylmethionine binding and methyltransferase activity by mitochondrial transcription factor B1."
    Guja K.E., Venkataraman K., Yakubovskaya E., Shi H., Mejia E., Hambardjieva E., Karzai A.W., Garcia-Diaz M.
    Nucleic Acids Res. 41:7947-7959(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.

Entry informationi

Entry nameiTFB1M_MOUSE
AccessioniPrimary (citable) accession number: Q8JZM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: October 1, 2002
Last modified: April 29, 2015
This is version 99 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

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.