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InterPro: IPR009071 High mobility group, superfamily
Protein matches
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UniProtKB Matches: 4391 proteins |
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Accession
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IPR009071 HMG_superfamily |
Type
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Domain |
Signatures
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InterPro Relationships
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Children
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IPR000910 High mobility group, HMG1/HMG2
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Found in
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IPR006780 YABBY protein
IPR010477 Protein of unknown function DUF1074
IPR015101 Domain of unknown function DUF1898
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Contains
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IPR017967 HMG box A DNA-binding domain, conserved site
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InterPro annotation
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Entry Details in BioMart
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Abstract
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High mobility group (HMG) box domains are involved in binding DNA, and may be involved in protein-protein interactions as well. The structure of the HMG-box domain consists of three helices in an irregular array. HMG-box domains are found in one or more copies in HMG-box proteins, which form a large, diverse family involved in the regulation of DNA-dependent processes such as transcription, replication, and strand repair, all of which require the bending and unwinding of chromatin. Many of these proteins are regulators of gene expression. HMG-box proteins are found in a variety of eukaryotic organisms, and can be broadly divided into two groups, based on sequence-dependent and sequence-independent DNA recognition; the former usually contain one HMG-box motif, while the latter can contain multiple HMG-box motifs.
HMG-box domains can be found in single or multiple copies in the following protein classes: HMG1 and HMG2 non-histone components of chromatin; SRY (sex determining region Y protein) involved in differential gonadogenesis; the SOX family of transcription factors [1]; sequence-specific LEF1 (lymphoid enhancer binding factor 1) and TCF-1 (T-cell factor 1) involved in regulation of organogenesis and thymocyte differentiation [2]; structure-specific recognition protein SSRP involved in transcription and replication; MTF1 mitochondrial transcription factor; nucleolar transcription factors UBF 1/2 (upstream binding factor) involved in transcription by RNA polymerase I; Abf2 yeast ARS-binding factor [3]; yeast transcription factors lxr1, Rox1, Nhp6b and Spp41; mating type proteins (MAT) involved in the sexual reproduction of fungi [4]; and the YABBY plant-specific transcription factors.
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Structural links
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Interactions
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This domain has been experimentally proven to be involved in Protein:Protein interactions. Representative
data is shown with the following
example proteins:
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Publications
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1.
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Harley VR, Clarkson MJ, Argentaro A.
The molecular action and regulation of the testis-determining factors, SRY (sex-determining region on the Y chromosome) and SOX9 [SRY-related high-mobility group (HMG) box 9].
Endocr. Rev. 24 466-87 2003
[PubMed: 12920151]
http://dx.doi.org/10.1210/er.2002-0025
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2.
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Labbe E, Letamendia A, Attisano L.
Association of Smads with lymphoid enhancer binding factor 1/T cell-specific factor mediates cooperative signaling by the transforming growth factor-beta and wnt pathways.
Proc. Natl. Acad. Sci. U.S.A. 97 8358-63 2000
[PubMed: 10890911]
http://dx.doi.org/10.1073/pnas.150152697
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3.
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Cho JH, Lee YK, Chae CB.
The modulation of the biological activities of mitochondrial histone Abf2p by yeast PKA and its possible role in the regulation of mitochondrial DNA content during glucose repression.
Biochim. Biophys. Acta 1522 175-86 2001
[PubMed: 11779632]
http://dx.doi.org/10.1016/S0167-4781(01)00333-5
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4.
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Barve MP, Arie T, Salimath SS, Muehlbauer FJ, Peever TL.
Cloning and characterization of the mating type (MAT) locus from Ascochyta rabiei (teleomorph: Didymella rabiei) and a MAT phylogeny of legume-associated Ascochyta spp.
Fungal Genet. Biol. 39 151-67 2003
[PubMed: 12781674]
http://dx.doi.org/10.1016/S1087-1845(03)00015-X
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Additional Reading
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Williams DC Jr, Cai M, Clore GM.
Molecular basis for synergistic transcriptional activation by Oct1 and Sox2 revealed from the solution structure of the 42-kDa Oct1.Sox2.Hoxb1-DNA ternary transcription factor complex.
J. Biol. Chem. 279 2004 1449-57
[PubMed: 14559893]
http://dx.doi.org/10.1074/jbc.M309790200
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Remenyi A, Lins K, Nissen LJ, Reinbold R, Scholer HR, Wilmanns M.
Crystal structure of a POU/HMG/DNA ternary complex suggests differential assembly of Oct4 and Sox2 on two enhancers.
Genes Dev. 17 2003 2048-59
[PubMed: 12923055]
http://dx.doi.org/10.1101/gad.269303
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Idogawa M, Masutani M, Shitashige M, Honda K, Tokino T, Shinomura Y, Imai K, Hirohashi S, Yamada T.
Ku70 and poly(ADP-ribose) polymerase-1 competitively regulate beta-catenin and T-cell factor-4-mediated gene transactivation: possible linkage of DNA damage recognition and Wnt signaling.
Cancer Res. 67 2007 911-8
[PubMed: 17283121]
http://dx.doi.org/10.1158/0008-5472.CAN-06-2360
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Schlierf B, Lang S, Kosian T, Werner T, Wegner M.
The high-mobility group transcription factor Sox10 interacts with the N-myc-interacting protein Nmi.
J. Mol. Biol. 353 2005 1033-42
[PubMed: 16214168]
http://dx.doi.org/10.1016/j.jmb.2005.09.013
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Stott K, Tang GS, Lee KB, Thomas JO.
Structure of a complex of tandem HMG boxes and DNA.
J. Mol. Biol. 360 2006 90-104
[PubMed: 16813837]
http://dx.doi.org/10.1016/j.jmb.2006.04.059
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Lim J, Hao T, Shaw C, Patel AJ, Szabo G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabasi AL, Vidal M, Zoghbi HY.
A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration.
Cell 125 2006 801-14
[PubMed: 16713569]
http://dx.doi.org/10.1016/j.cell.2006.03.032
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Yang W, Xu Y, Wu J, Zeng W, Shi Y.
Solution structure and DNA binding property of the fifth HMG box domain in comparison with the first HMG box domain in human upstream binding factor.
Biochemistry 42 2003 1930-8
[PubMed: 12590579]
http://dx.doi.org/10.1021/bi026372x
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Kasai N, Tsunaka Y, Ohki I, Hirose S, Morikawa K, Tate S.
Solution structure of the HMG-box domain in the SSRP1 subunit of FACT.
J. Biomol. NMR 32 2005 83-8
[PubMed: 16041486]
http://dx.doi.org/10.1007/s10858-005-3662-3
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InterPro 24.0
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