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InterPro: IPR009071 High mobility group, superfamily

Protein matchesHelp
UniProtKB
Matches:
4391 proteins
AccessionHelp IPR009071 HMG_superfamily
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR000910 High mobility group, HMG1/HMG2
Found in IPR006780 YABBY protein
IPR010477 Protein of unknown function DUF1074
IPR015101 Domain of unknown function DUF1898
Contains IPR017967 HMG box A DNA-binding domain, conserved site
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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.

Structural linksHelp
InteractionsHelp
This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR009071 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O01683 FACT complex subunit ssrp1-B

O15347 High mobility group protein B3

P11632 Non-histone chromosomal protein 6A

P25976 Nucleolar transcription factor 1

Q05344 FACT complex subunit Ssrp1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000969 Structure-specific recognition protein
IPR000135 High mobility group, HMG1/HMG2, subgroup
IPR009071 High mobility group, superfamily
IPR000910 High mobility group, HMG1/HMG2
IPR017967 HMG box A DNA-binding domain, conserved site
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. 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
2. 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
3. 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
4. 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

Additional ReadingHelp
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
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
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
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
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
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
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
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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