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InterPro: IPR000910 High mobility group, HMG1/HMG2
Protein matches
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UniProtKB Matches: 4239 proteins |
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Accession
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IPR000910 HMG_HMG1/HMG2 |
Secondary
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IPR009071
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Type
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Domain |
Signatures
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InterPro Relationships
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Parent
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IPR009071 High mobility group, superfamily
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Children
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IPR000135 High mobility group, HMG1/HMG2, subgroup
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Found in
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IPR017253 Sex-determining region Y protein
IPR017386 SOX-12/11/4a
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Contains
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IPR017967 HMG box A DNA-binding domain, conserved site
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GO Term annotation
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Function
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GO:0003677 DNA binding
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Component
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GO:0005634 nucleus
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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 or HMGB) proteins are a family of relatively low molecular weight non-histone components in chromatin. HMG1 (also called HMG-T in fish) and HMG2 are two highly related proteins that bind single-stranded DNA preferentially and unwind double-stranded DNA. Although they have no sequence specificity, they have a high affinity for bent or distorted DNA, and bend linear DNA. HMG1 and HMG2 contain two DNA-binding HMG-box domains (A and B) that show structural and functional differences, and have a long acidic C-terminal domain rich in aspartic and glutamic acid residues. The acidic tail modulates the affinity of the tandem HMG boxes in HMG1 and 2 for a variety of DNA targets. HMG1 and 2 appear to play important architectural roles in the assembly of nucleoprotein complexes in a variety of biological processes, for example V(D)J recombination, the initiation of transcription, and DNA repair [1].
The profile in this entry describing the HMG-domains is much more general than the signature. In addition to the HMG1 and HMG2 proteins, HMG-domains occur in single or multiple copies in the following protein classes; the SOX family of transcription factors; SRY sex determining region Y protein and related proteins [2]; LEF1 lymphoid enhancer binding factor 1 [3]; SSRP recombination signal recognition protein; MTF1 mitochondrial transcription factor 1; UBF1/2 nucleolar transcription factors; Abf2 yeast ARS-binding factor [4]; and Saccharomyces cerevisiae transcription factors Ixr1, Rox1, Nhp6a, Nhp6b and Spp41.
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Structural links
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Database links
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Pfam Clan: CL0114.8
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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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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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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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Werner MH, Huth JR, Gronenborn AM, Clore GM.
Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex.
Cell 81 1995 705-14
[PubMed: 7774012]
http://dx.doi.org/10.1016/0092-8674(95)90532-4
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Hardman CH, Broadhurst RW, Raine AR, Grasser KD, Thomas JO, Laue ED.
Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy.
Biochemistry 34 1995 16596-607
[PubMed: 8527432]
http://dx.doi.org/10.1021/bi00051a007
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Love JJ, Li X, Case DA, Giese K, Grosschedl R, Wright PE.
Structural basis for DNA bending by the architectural transcription factor LEF-1.
Nature 376 1995 791-5
[PubMed: 7651541]
http://dx.doi.org/10.1038/376791a0
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Bustin M, Lehn DA, Landsman D.
Structural features of the HMG chromosomal proteins and their genes.
Biochim. Biophys. Acta 1049 1990 231-43
[PubMed: 2200521]
http://dx.doi.org/10.1016/0167-4781(90)90092-G
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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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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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InterPro 24.0
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