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Q00059 (TFAM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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):
Mitochondrial transcription factor 1
Short name=MtTF1
Transcription factor 6
Short name=TCF-6
Transcription factor 6-like 2
Gene names
Name:TFAM
Synonyms:TCF6, TCF6L2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.13 Ref.16 Ref.18 Ref.19 Ref.20

Subunit structure

Monomer; binds DNA as a monomer. Interacts with TFB1M and TFB2M. Interacts with CLPX; this enhances DNA-binding. Ref.10 Ref.16 Ref.18 Ref.19 Ref.20

Subcellular location

Mitochondrion. Mitochondrion matrixmitochondrion nucleoid Ref.9 Ref.11 Ref.16.

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. Ref.19 Ref.20

Post-translational modification

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

Sequence similarities

Contains 2 HMG box DNA-binding domains.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentMitochondrion
Mitochondrion nucleoid
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Transit peptide
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA-dependent DNA replication

Traceable author statement PubMed 8333869. Source: ProtInc

gene expression

Traceable author statement. Source: Reactome

mitochondrial respiratory chain complex assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.13. Source: UniProtKB

regulation of transcription from RNA polymerase I promoter

Traceable author statement PubMed 8333869. Source: ProtInc

transcription from mitochondrial promoter

Inferred from mutant phenotype Ref.20. Source: UniProtKB

transcription initiation from mitochondrial promoter

Inferred from direct assay Ref.13. Source: UniProtKB

   Cellular_componentmitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrial nucleoid

Inferred from direct assay Ref.11. Source: BHF-UCL

mitochondrion

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

   Molecular_functionDNA binding, bending

Inferred from direct assay Ref.20. Source: UniProtKB

chromatin binding

Inferred from direct assay Ref.11. Source: UniProtKB

mitochondrial light strand promoter sense binding

Inferred from direct assay Ref.18. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10. Source: IntAct

sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype Ref.20. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TFB1MQ8WVM02EBI-1049924,EBI-2615570

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q00059-1)

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 2 (identifier: Q00059-2)

The sequence of this isoform differs from the canonical sequence as follows:
     148-179: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4242Mitochondrion Potential
Chain43 – 246204Transcription factor A, mitochondrial
PRO_0000013470

Regions

DNA binding50 – 11869HMG box 1 Ref.19 Ref.20
DNA binding155 – 21965HMG box 2 Ref.19 Ref.20

Sites

Site581Intercalates between bases and promotes DNA bending
Site1821Intercalates between bases and promotes DNA bending

Amino acid modifications

Modified residue551Phosphoserine; by PKA Ref.17
Modified residue561Phosphoserine; by PKA Ref.17
Modified residue611Phosphoserine; by PKA Ref.17
Modified residue1601Phosphoserine; by PKA Ref.17
Modified residue1931Phosphoserine Ref.12

Natural variations

Alternative sequence148 – 17932Missing in isoform 2.
VSP_047019
Natural variant121S → T. Ref.5 Ref.8
Corresponds to variant rs1937 [ dbSNP | Ensembl ].
VAR_016124

Experimental info

Mutagenesis771T → A: Moderate reduction in DNA bending. Ref.20
Mutagenesis1621Y → A: Moderate reduction in DNA bending. Ref.20
Sequence conflict341S → R in CAA45562. Ref.8

Secondary structure

...................... 246
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 81F00CFA12DA4924

FASTA24629,097
        10         20         30         40         50         60 
MAFLRSMWGV LSALGRSGAE LCTGCGSRLR SPFSFVYLPR WFSSVLASCP KKPVSSYLRF 

        70         80         90        100        110        120 
SKEQLPIFKA QNPDAKTTEL IRRIAQRWRE LPDSKKKIYQ DAYRAEWQVY KEEISRFKEQ 

       130        140        150        160        170        180 
LTPSQIMSLE KEIMDKHLKR KAMTKKKELT LLGKPKRPRS AYNVYVAERF QEAKGDSPQE 

       190        200        210        220        230        240 
KLKTVKENWK NLSDSEKELY IQHAKEDETR YHNEMKSWEE QMIEVGRKDL LRRTIKKQRK 


YGAEEC 

« Hide

Isoform 2 [UniParc].

Checksum: C3802AD446D4764D
Show »

FASTA21425,466

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS59217.1. [Q00059-2]
CCDS7253.1. [Q00059-1]
PIRJC1496.
RefSeqNP_001257711.1. NM_001270782.1. [Q00059-2]
NP_003192.1. NM_003201.2. [Q00059-1]
UniGeneHs.594250.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ00059.
SMRQ00059. Positions 44-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112877. 15 interactions.
IntActQ00059. 7 interactions.
STRING9606.ENSP00000420588.

PTM databases

PhosphoSiteQ00059.

Polymorphism databases

DMDM417324.

Proteomic databases

MaxQBQ00059.
PaxDbQ00059.
PRIDEQ00059.

Protocols and materials databases

DNASU7019.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373895; ENSP00000363002; ENSG00000108064. [Q00059-2]
ENST00000487519; ENSP00000420588; ENSG00000108064. [Q00059-1]
GeneID7019.
KEGGhsa:7019.
UCSCuc001jkf.4. human. [Q00059-1]

Organism-specific databases

CTD7019.
GeneCardsGC10P060146.
HGNCHGNC:11741. TFAM.
HPAHPA040648.
MIM600438. gene.
neXtProtNX_Q00059.
PharmGKBPA36458.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG297801.
HOGENOMHOG000139423.
HOVERGENHBG106674.
InParanoidQ00059.
KOK11830.
OMADDKIRYE.
OrthoDBEOG7CG724.
PhylomeDBQ00059.
TreeFamTF318343.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_200751. Organelle biogenesis and maintenance.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ00059.
BgeeQ00059.
CleanExHS_TFAM.
GenevestigatorQ00059.

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. human.
EvolutionaryTraceQ00059.
GeneWikiTFAM.
GenomeRNAi7019.
NextBio27419.
PROQ00059.
SOURCESearch...

Entry information

Entry nameTFAM_HUMAN
AccessionPrimary (citable) accession number: Q00059
Secondary accession number(s): A8MRB2 expand/collapse secondary AC list , A9QXC6, B5BU05, Q5U0C6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 9, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM