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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC00307
HMG14 and HMG17 signature


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PURL: https://purl.expasy.org/prosite/documentation/PDOC00307

Description

High mobility group (HMG) proteins are a family of relatively low molecular weight non-histone components in chromatin. HMG14 and HMG17 [1], two related proteins of about 100 amino acid residues, bind to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. These two proteins may be involved in the process which maintains transcribable genes in a unique chromatin conformation.

The trout nonhistone chromosomal protein H6 (histone T) also belongs to this family.

As a signature pattern we selected a conserved stretch of 10 residues located in the N-terminal section of HMG14 and HMG17.

Expert(s) to contact by email:

Landsman D.

Last update:

December 2004 / Pattern and text revised.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

HMG14_17, PS00355; HMG14 and HMG17 signature  (PATTERN)


Reference

1AuthorsBustin M. Reeves R.
TitleHigh-mobility-group chromosomal proteins: architectural components that facilitate chromatin function.
SourceProg. Nucleic Acid Res. Mol. Biol. 54:35-100(1996).
PubMed ID8768072



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