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Q00059

- TFAM_HUMAN

UniProt

Q00059 - TFAM_HUMAN

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Protein
Transcription factor A, mitochondrial
Gene
TFAM, TCF6, TCF6L2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei58 – 581Intercalates between bases and promotes DNA bending
Sitei182 – 1821Intercalates between bases and promotes DNA bending

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi50 – 11869HMG box 12 Publications
Add
BLAST
DNA bindingi155 – 21965HMG box 22 Publications
Add
BLAST

GO - Molecular functioni

  1. DNA binding, bending Source: UniProtKB
  2. chromatin binding Source: UniProtKB
  3. mitochondrial light strand promoter sense binding Source: UniProtKB
  4. poly(A) RNA binding Source: UniProtKB
  5. protein binding Source: IntAct
  6. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. DNA-dependent DNA replication Source: ProtInc
  2. gene expression Source: Reactome
  3. mitochondrial respiratory chain complex assembly Source: Ensembl
  4. positive regulation of transcription, DNA-templated Source: UniProtKB
  5. regulation of transcription from RNA polymerase I promoter Source: ProtInc
  6. transcription from mitochondrial promoter Source: UniProtKB
  7. transcription initiation from mitochondrial promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_367. Mitochondrial transcription initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor A, mitochondrial
Short name:
mtTFA
Alternative name(s):
Mitochondrial transcription factor 1
Short name:
MtTF1
Transcription factor 6
Short name:
TCF-6
Transcription factor 6-like 2
Gene namesi
Name:TFAM
Synonyms:TCF6, TCF6L2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:11741. TFAM.

Subcellular locationi

Mitochondrion. Mitochondrion matrixmitochondrion nucleoid 3 Publications

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrial nucleoid Source: BHF-UCL
  3. mitochondrion Source: HPA
  4. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Mitochondrion nucleoid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi77 – 771T → A: Moderate reduction in DNA bending. 1 Publication
Mutagenesisi162 – 1621Y → A: Moderate reduction in DNA bending. 1 Publication

Organism-specific databases

PharmGKBiPA36458.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4242Mitochondrion Reviewed prediction
Add
BLAST
Chaini43 – 246204Transcription factor A, mitochondrial
PRO_0000013470Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551Phosphoserine; by PKA1 Publication
Modified residuei56 – 561Phosphoserine; by PKA1 Publication
Modified residuei61 – 611Phosphoserine; by PKA1 Publication
Modified residuei160 – 1601Phosphoserine; by PKA1 Publication
Modified residuei193 – 1931Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ00059.
PaxDbiQ00059.
PRIDEiQ00059.

PTM databases

PhosphoSiteiQ00059.

Expressioni

Gene expression databases

ArrayExpressiQ00059.
BgeeiQ00059.
CleanExiHS_TFAM.
GenevestigatoriQ00059.

Organism-specific databases

HPAiHPA040648.

Interactioni

Subunit structurei

Monomer; binds DNA as a monomer. Interacts with TFB1M and TFB2M. Interacts with CLPX; this enhances DNA-binding.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TFB1MQ8WVM02EBI-1049924,EBI-2615570

Protein-protein interaction databases

BioGridi112877. 15 interactions.
IntActiQ00059. 7 interactions.
STRINGi9606.ENSP00000420588.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi45 – 484
Helixi56 – 7116
Beta strandi73 – 753
Helixi77 – 9014
Helixi93 – 12028
Helixi123 – 15129
Helixi161 – 17313
Beta strandi175 – 1773
Helixi178 – 19013
Helixi194 – 21724
Helixi228 – 2303

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FGHX-ray1.35A153-218[»]
3TMMX-ray2.50A43-246[»]
3TQ6X-ray2.45A/B43-246[»]
4NNUX-ray2.81A/B43-237[»]
4NODX-ray2.90A/B/G/H43-237[»]
ProteinModelPortaliQ00059.
SMRiQ00059. Positions 44-237.

Miscellaneous databases

EvolutionaryTraceiQ00059.

Family & Domainsi

Domaini

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.2 Publications

Sequence similaritiesi

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiNOG297801.
HOGENOMiHOG000139423.
HOVERGENiHBG106674.
InParanoidiQ00059.
KOiK11830.
OMAiDDKIRYE.
OrthoDBiEOG7CG724.
PhylomeDBiQ00059.
TreeFamiTF318343.

Family and domain databases

Gene3Di1.10.30.10. 2 hits.
InterProiIPR009071. HMG_box_dom.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
PF09011. HMG_box_2. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 2 hits.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 2 hits.
PROSITEiPS50118. HMG_BOX_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q00059-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAFLRSMWGV LSALGRSGAE LCTGCGSRLR SPFSFVYLPR WFSSVLASCP    50
KKPVSSYLRF SKEQLPIFKA QNPDAKTTEL IRRIAQRWRE LPDSKKKIYQ 100
DAYRAEWQVY KEEISRFKEQ LTPSQIMSLE KEIMDKHLKR KAMTKKKELT 150
LLGKPKRPRS AYNVYVAERF QEAKGDSPQE KLKTVKENWK NLSDSEKELY 200
IQHAKEDETR YHNEMKSWEE QMIEVGRKDL LRRTIKKQRK YGAEEC 246
Length:246
Mass (Da):29,097
Last modified:October 1, 1993 - v1
Checksum:i81F00CFA12DA4924
GO
Isoform 2 (identifier: Q00059-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     148-179: Missing.

Note: Gene prediction based on EST data.

Show »
Length:214
Mass (Da):25,466
Checksum:iC3802AD446D4764D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121S → T.2 Publications
Corresponds to variant rs1937 [ dbSNP | Ensembl ].
VAR_016124

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei148 – 17932Missing in isoform 2.
VSP_047019Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341S → R in CAA45562. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M62810 mRNA. Translation: AAA59849.1.
EU279428 mRNA. Translation: ABX72056.1.
BT019658 mRNA. Translation: AAV38464.1.
BT019659 mRNA. Translation: AAV38465.1.
AK312558 mRNA. Translation: BAG35455.1.
AB451241 mRNA. Translation: BAG70055.1.
AB451366 mRNA. Translation: BAG70180.1.
AC023170 Genomic DNA. No translation available.
BC126366 mRNA. Translation: AAI26367.1.
X64269 Genomic DNA. Translation: CAA45562.1.
CCDSiCCDS59217.1. [Q00059-2]
CCDS7253.1. [Q00059-1]
PIRiJC1496.
RefSeqiNP_001257711.1. NM_001270782.1. [Q00059-2]
NP_003192.1. NM_003201.2. [Q00059-1]
UniGeneiHs.594250.

Genome annotation databases

EnsembliENST00000373895; ENSP00000363002; ENSG00000108064. [Q00059-2]
ENST00000487519; ENSP00000420588; ENSG00000108064. [Q00059-1]
GeneIDi7019.
KEGGihsa:7019.
UCSCiuc001jkf.4. human. [Q00059-1]

Polymorphism databases

DMDMi417324.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M62810 mRNA. Translation: AAA59849.1 .
EU279428 mRNA. Translation: ABX72056.1 .
BT019658 mRNA. Translation: AAV38464.1 .
BT019659 mRNA. Translation: AAV38465.1 .
AK312558 mRNA. Translation: BAG35455.1 .
AB451241 mRNA. Translation: BAG70055.1 .
AB451366 mRNA. Translation: BAG70180.1 .
AC023170 Genomic DNA. No translation available.
BC126366 mRNA. Translation: AAI26367.1 .
X64269 Genomic DNA. Translation: CAA45562.1 .
CCDSi CCDS59217.1. [Q00059-2 ]
CCDS7253.1. [Q00059-1 ]
PIRi JC1496.
RefSeqi NP_001257711.1. NM_001270782.1. [Q00059-2 ]
NP_003192.1. NM_003201.2. [Q00059-1 ]
UniGenei Hs.594250.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3FGH X-ray 1.35 A 153-218 [» ]
3TMM X-ray 2.50 A 43-246 [» ]
3TQ6 X-ray 2.45 A/B 43-246 [» ]
4NNU X-ray 2.81 A/B 43-237 [» ]
4NOD X-ray 2.90 A/B/G/H 43-237 [» ]
ProteinModelPortali Q00059.
SMRi Q00059. Positions 44-237.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112877. 15 interactions.
IntActi Q00059. 7 interactions.
STRINGi 9606.ENSP00000420588.

PTM databases

PhosphoSitei Q00059.

Polymorphism databases

DMDMi 417324.

Proteomic databases

MaxQBi Q00059.
PaxDbi Q00059.
PRIDEi Q00059.

Protocols and materials databases

DNASUi 7019.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373895 ; ENSP00000363002 ; ENSG00000108064 . [Q00059-2 ]
ENST00000487519 ; ENSP00000420588 ; ENSG00000108064 . [Q00059-1 ]
GeneIDi 7019.
KEGGi hsa:7019.
UCSCi uc001jkf.4. human. [Q00059-1 ]

Organism-specific databases

CTDi 7019.
GeneCardsi GC10P060146.
HGNCi HGNC:11741. TFAM.
HPAi HPA040648.
MIMi 600438. gene.
neXtProti NX_Q00059.
PharmGKBi PA36458.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG297801.
HOGENOMi HOG000139423.
HOVERGENi HBG106674.
InParanoidi Q00059.
KOi K11830.
OMAi DDKIRYE.
OrthoDBi EOG7CG724.
PhylomeDBi Q00059.
TreeFami TF318343.

Enzyme and pathway databases

Reactomei REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_367. Mitochondrial transcription initiation.

Miscellaneous databases

ChiTaRSi TFAM. human.
EvolutionaryTracei Q00059.
GeneWikii TFAM.
GenomeRNAii 7019.
NextBioi 27419.
PROi Q00059.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q00059.
Bgeei Q00059.
CleanExi HS_TFAM.
Genevestigatori Q00059.

Family and domain databases

Gene3Di 1.10.30.10. 2 hits.
InterProi IPR009071. HMG_box_dom.
[Graphical view ]
Pfami PF00505. HMG_box. 1 hit.
PF09011. HMG_box_2. 1 hit.
[Graphical view ]
SMARTi SM00398. HMG. 2 hits.
[Graphical view ]
SUPFAMi SSF47095. SSF47095. 2 hits.
PROSITEi PS50118. HMG_BOX_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Similarity of human mitochondrial transcription factor 1 to high mobility group proteins."
    Parisi M.A., Clayton D.A.
    Science 252:965-969(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 1-21.
  2. Li K.N., Zhang Y.Q., Yang S.J.
    Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Hepatoma.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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.
    , 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] (ISOFORM 1).
    Tissue: Tongue.
  5. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-12.
  6. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 1).
  8. "Upstream region of a genomic gene for human mitochondrial transcription factor 1."
    Tominaga K., Akiyama S., Kagawa Y., Ohta S.
    Biochim. Biophys. Acta 1131:217-219(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34, VARIANT THR-12.
    Tissue: Lymphocyte.
  9. "DNA wrapping and bending by a mitochondrial high mobility group-like transcriptional activator protein."
    Fisher R.P., Lisowsky T., Parisi M.A., Clayton D.A.
    J. Biol. Chem. 267:3358-3367(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "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: INTERACTION WITH TFB1M AND TFB2M.
  11. "The layered structure of human mitochondrial DNA nucleoids."
    Bogenhagen D.F., Rousseau D., Burke S.
    J. Biol. Chem. 283:3665-3675(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH MITOCHONDRIAL DNA, IDENTIFICATION BY MASS SPECTROMETRY.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Maintenance of mitochondrial genome distribution by mitochondrial AAA+ protein ClpX."
    Kasashima K., Sumitani M., Endo H.
    Exp. Cell Res. 318:2335-2343(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CLPX.
  17. "Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease."
    Lu B., Lee J., Nie X., Li M., Morozov Y.I., Venkatesh S., Bogenhagen D.F., Temiakov D., Suzuki C.K.
    Mol. Cell 49:121-132(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-55; SER-56; SER-61 AND SER-160.
  18. "Structural analysis and DNA binding of the HMG domains of the human mitochondrial transcription factor A."
    Gangelhoff T.A., Mungalachetty P.S., Nix J.C., Churchill M.E.
    Nucleic Acids Res. 37:3153-3164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 153-218, FUNCTION, SUBUNIT.
  19. "Human mitochondrial transcription factor A induces a U-turn structure in the light strand promoter."
    Rubio-Cosials A., Sidow J.F., Jimenez-Menendez N., Fernandez-Millan P., Montoya J., Jacobs H.T., Coll M., Bernado P., Sola M.
    Nat. Struct. Mol. Biol. 18:1281-1289(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 43-246 IN COMPLEX WITH DNA, DNA-BINDING, DOMAIN, SUBUNIT, SITE, FUNCTION.
  20. "The mitochondrial transcription and packaging factor Tfam imposes a U-turn on mitochondrial DNA."
    Ngo H.B., Kaiser J.T., Chan D.C.
    Nat. Struct. Mol. Biol. 18:1290-1296(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 43-246 IN COMPLEX WITH DNA, FUNCTION, DNA-BINDING, DOMAIN, SUBUNIT, MUTAGENESIS OF THR-77 AND TYR-162.

Entry informationi

Entry nameiTFAM_HUMAN
AccessioniPrimary (citable) accession number: Q00059
Secondary accession number(s): A8MRB2
, A9QXC6, B5BU05, Q5U0C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 3, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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