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P40630 (TFAM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor A, mitochondrial

Short name=mtTFA
Alternative name(s):
Testis-specific high mobility group protein
Short name=TS-HMG
Gene names
Name:Tfam
Synonyms:Hmgts
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length243 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform Mitochondrial binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation. Required for accurate and efficient promoter recognition by the mitochondrial RNA polymerase. Promotes transcription initiation from the HSP1 and the light strand promoter by binding immediately upstream of transcriptional start sites. Is able to unwind DNA. Bends the mitochondrial light strand promoter DNA into a U-turn shape via its HMG boxes. Required for maintenance of normal levels of mitochondrial DNA. May play a role in organizing and compacting mitochondrial DNA. Isoform Nuclear may also function as a transcriptional activator or may have a structural role in the compaction of nuclear DNA during spermatogenesis. Ref.1 Ref.6 Ref.7

Subunit structure

Monomer; binds DNA as a monomer. Interacts with TFB1M and TFB2M. Interacts with CLPX; this enhances DNA-binding By similarity. Ref.7

Subcellular location

Isoform Mitochondrial: Mitochondrion. Mitochondrion matrixmitochondrion nucleoid By similarity.

Isoform Nuclear: Nucleus.

Tissue specificity

The mitochondrial isoform iswidely expressed while the nuclear isoform istestis-specific.

Domain

Binds DNA via its HMG boxes. When bound to the mitochondrial light strand promoter, bends DNA into a U-turn shape, each HMG box bending the DNA by 90 degrees By similarity.

Post-translational modification

Phosphorylation by PKA within the HMG box 1 impairs DNA binding and promotes degradation by the AAA+ Lon protease By similarity.

Disruption phenotype

Embryonic lethal, due to absence of mitochondrial DNA. Mutant embryos die before 10.5 dpc. Ref.6

Sequence similarities

Contains 2 HMG box DNA-binding domains.

Sequence caution

The sequence AAA02579.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AK004857 differs from that shown. Reason: Frameshift at position 195.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentMitochondrion
Mitochondrion nucleoid
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Transit peptide
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmitochondrial respiratory chain complex assembly

Inferred from mutant phenotype PubMed 11259653. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

transcription from mitochondrial promoter

Inferred from sequence or structural similarity. Source: UniProtKB

transcription initiation from mitochondrial promoter

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentmitochondrial nucleoid

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015Ref.1. Source: MGI

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

transcription factor complex

Traceable author statement Ref.1. Source: MGI

   Molecular_functionDNA binding, bending

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial light strand promoter sense binding

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Mitochondrial (identifier: P40630-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Nuclear (identifier: P40630-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.
     29-34: IPSSIS → MAGAWG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4242Mitochondrion Potential
Chain43 – 243201Transcription factor A, mitochondrial
PRO_0000013471

Regions

DNA binding49 – 11769HMG box 1
DNA binding154 – 21865HMG box 2

Sites

Site571Intercalates between bases and promotes DNA bending By similarity
Site1811Intercalates between bases and promotes DNA bending By similarity

Amino acid modifications

Modified residue541Phosphoserine; by PKA By similarity
Modified residue551Phosphoserine; by PKA By similarity
Modified residue601Phosphoserine; by PKA By similarity
Modified residue661N6-succinyllysine Ref.8
Modified residue1591Phosphoserine; by PKA By similarity
Modified residue1921Phosphoserine By similarity

Natural variations

Alternative sequence1 – 2828Missing in isoform Nuclear.
VSP_002185
Alternative sequence29 – 346IPSSIS → MAGAWG in isoform Nuclear.
VSP_002186

Experimental info

Sequence conflict341S → R in AAA02579. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform Mitochondrial [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: 3477F6EEAD9A3EBF

FASTA24327,988
        10         20         30         40         50         60 
MALFRGMWSV LKALGRTGVE MCAGCGGRIP SSISLVCIPK CFSSMGSYPK KPMSSYLRFS 

        70         80         90        100        110        120 
TEQLPKFKAK HPDAKLSELV RKIAALWREL PEAEKKVYEA DFKAEWKAYK EAVSKYKEQL 

       130        140        150        160        170        180 
TPSQLMGMEK EARQRRLKKK ALVKRRELIL LGKPKRPRSA YNIYVSESFQ EAKDDSAQGK 

       190        200        210        220        230        240 
LKLVNEAWKN LSPEEKQAYI QLAKDDRIRY DNEMKSWEEQ MAEVGRSDLI RRSVKRSGDI 


SEH 

« Hide

Isoform Nuclear [UniParc].

Checksum: B728ED1DF9053452
Show »

FASTA21525,036

References

« Hide 'large scale' references
[1]"A single mouse gene encodes the mitochondrial transcription factor A and a testis-specific nuclear HMG-box protein."
Larsson N.G., Garman J.D., Oldfors A., Barsh G.S., Clayton D.A.
Nat. Genet. 13:296-302(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MITOCHONDRIAL AND NUCLEAR), FUNCTION, ALTERNATIVE SPLICING.
Tissue: Lymphocyte and Testis.
[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] (ISOFORM MITOCHONDRIAL).
[3]"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] (ISOFORM MITOCHONDRIAL).
Strain: C57BL/6J, DBA/2 and NOD.
Tissue: Liver and Thymus.
[4]Cermakian N., Cedergren R.
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-48 (ISOFORM MITOCHONDRIAL).
Strain: CD-1.
Tissue: Testis.
[5]"A testis-specific gene encoding a nuclear high-mobility-group box protein located in elongating spermatids."
Boissonneault G., Lau Y.-F.C.
Mol. Cell. Biol. 13:4323-4330(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 34-243 (ISOFORM MITOCHONDRIAL).
Strain: BALB/c.
Tissue: Testis.
[6]"Mitochondrial transcription factor A is necessary for mtDNA maintenance and embryogenesis in mice."
Larsson N.G., Wang J., Wilhelmsson H., Oldfors A., Rustin P., Lewandoski M., Barsh G.S., Clayton D.A.
Nat. Genet. 18:231-236(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]"The mitochondrial transcription factor TFAM coordinates the assembly of multiple DNA molecules into nucleoid-like structures."
Kaufman B.A., Durisic N., Mativetsky J.M., Costantino S., Hancock M.A., Grutter P., Shoubridge E.A.
Mol. Biol. Cell 18:3225-3236(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[8]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U57939 mRNA. Translation: AAC52815.1.
U63858 mRNA. Translation: AAC52816.1.
BC001987 mRNA. Translation: AAH01987.1.
BC083084 mRNA. Translation: AAH83084.1.
AK004857 mRNA. No translation available.
AK050446 mRNA. Translation: BAC34258.1.
AK167348 mRNA. Translation: BAE39447.1.
AK167777 mRNA. Translation: BAE39809.1.
AK169808 mRNA. Translation: BAE41382.1.
U63712 mRNA. Translation: AAB06395.1.
L07107 mRNA. Translation: AAA02579.1. Different initiation.
CCDSCCDS23916.1. [P40630-1]
PIRI49745.
RefSeqNP_033386.1. NM_009360.4. [P40630-1]
UniGeneMm.229292.

3D structure databases

ProteinModelPortalP40630.
SMRP40630. Positions 43-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204137. 2 interactions.
IntActP40630. 4 interactions.
MINTMINT-1861500.

PTM databases

PhosphoSiteP40630.

Proteomic databases

MaxQBP40630.
PaxDbP40630.
PRIDEP40630.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000092430; ENSMUSP00000090086; ENSMUSG00000003923. [P40630-1]
ENSMUST00000105432; ENSMUSP00000101072; ENSMUSG00000003923. [P40630-2]
ENSMUST00000121685; ENSMUSP00000113581; ENSMUSG00000003923.
GeneID21780.
KEGGmmu:21780.
UCSCuc007fol.1. mouse. [P40630-2]
uc007fom.1. mouse. [P40630-1]

Organism-specific databases

CTD7019.
MGIMGI:107810. Tfam.

Phylogenomic databases

eggNOGNOG297801.
GeneTreeENSGT00440000039001.
HOGENOMHOG000139423.
HOVERGENHBG106674.
InParanoidP40630.
KOK11830.
OMADDKIRYE.
OrthoDBEOG7CG724.
PhylomeDBP40630.
TreeFamTF318343.

Gene expression databases

ArrayExpressP40630.
BgeeP40630.
CleanExMM_TFAM.
GenevestigatorP40630.

Family and domain databases

Gene3D1.10.30.10. 2 hits.
InterProIPR009071. HMG_box_dom.
[Graphical view]
PfamPF00505. HMG_box. 1 hit.
PF09011. HMG_box_2. 1 hit.
[Graphical view]
SMARTSM00398. HMG. 2 hits.
[Graphical view]
SUPFAMSSF47095. SSF47095. 2 hits.
PROSITEPS50118. HMG_BOX_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTFAM. mouse.
NextBio301118.
PROP40630.
SOURCESearch...

Entry information

Entry nameTFAM_MOUSE
AccessionPrimary (citable) accession number: P40630
Secondary accession number(s): P97894 expand/collapse secondary AC list , P97906, Q543I8, Q9DBM9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: August 30, 2002
Last modified: July 9, 2014
This is version 125 of the entry and version 2 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