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Q00059

- TFAM_HUMAN

UniProt

Q00059 - TFAM_HUMAN

Protein

Transcription factor A, mitochondrial

Gene

TFAM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    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 1PROSITE-ProRule annotationAdd
    BLAST
    DNA bindingi155 – 21965HMG box 2PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. DNA binding, bending 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

    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

    GO - Cellular componenti

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

    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 – 4242MitochondrionSequence AnalysisAdd
    BLAST
    Chaini43 – 246204Transcription factor A, mitochondrialPRO_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.2 Publications

    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

    1
    246
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Contains 2 HMG box DNA-binding domains.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341S → R in CAA45562. (PubMed:1610904)Curated

    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. CuratedVSP_047019Add
    BLAST

    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

    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: October 1, 2014
    This is version 136 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