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InterPro: IPR000910 High mobility group, HMG1/HMG2

Protein matchesHelp
UniProtKB
Matches:
4239 proteins
AccessionHelp IPR000910 HMG_HMG1/HMG2
SecondaryHelp IPR009071
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR009071 High mobility group, superfamily
Children IPR000135 High mobility group, HMG1/HMG2, subgroup
Found in IPR017253 Sex-determining region Y protein
IPR017386 SOX-12/11/4a
Contains IPR017967 HMG box A DNA-binding domain, conserved site
GO Term annotationHelp
Function GO:0003677 DNA binding
Component GO:0005634 nucleus
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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.

Structural linksHelp
Database linksHelp
PROSITE doc: PDOC00305
PANDIT: PF00505
Pfam Clan: CL0114.8

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000910 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. Thomas JO.
HMG1 and 2: architectural DNA-binding proteins.
Biochem. Soc. Trans. 29 395-401 2001 [PubMed: 11497996]
http://www.biochemsoctrans.org/bst/029/0395/0290395.pdf
2. 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
3. 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
4. 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

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
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
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
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
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
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
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
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
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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