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Gene Review

Ssrp1  -  structure specific recognition protein 1

Mus musculus

Synonyms: C81323, FACT complex subunit SSRP1, Facilitates chromatin transcription complex subunit SSRP1, Hmg1-rs1, Hmgi-rs3, ...
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High impact information on Ssrp1


Biological context of Ssrp1


Anatomical context of Ssrp1


Associations of Ssrp1 with chemical compounds

  • In this study, the T160 protein or truncated forms made soluble through denaturing and renaturing cycles in urea were successfully used in gel-shift experiments showing that T160 binds to cruci-form or linear duplex DNA with no apparent sequence specificity [5].
  • Bacterially expressed p40MO15 was phosphorylated mainly on serine 170 (a p34cdc2 phosphorylation site) by mitotic cell extracts, but mutation of S170 to alanine did not affect the activation of p40MO15, whereas mutation of T176 (the equivalent site to T161/T160 in p34cdc2/p33cdk2) abolished the activation of P40MO15 [6].

Other interactions of Ssrp1

  • The RAG locus-associated gene T160 is located 1.8 kb upstream of the transcription start site of mouse P2X3 gene [7].
  • Both Daxx and SSRP1 were released from heterochromatin early in G(2) phase and Daxx was recruited back to ND10, indicating that both proteins localize to heterochromatin during a very short temporal window of the cell cycle [8].
  • Identification of a cDNA for SSRP1, an HMG-box protein, by interaction with the c-Myc oncoprotein in a novel bacterial expression screen [9].

Analytical, diagnostic and therapeutic context of Ssrp1


  1. SSRP1 functions as a co-activator of the transcriptional activator p63. Zeng, S.X., Dai, M.S., Keller, D.M., Lu, H. EMBO J. (2002) [Pubmed]
  2. The high-mobility-group box protein SSRP1/T160 is essential for cell viability in day 3.5 mouse embryos. Cao, S., Bendall, H., Hicks, G.G., Nashabi, A., Sakano, H., Shinkai, Y., Gariglio, M., Oltz, E.M., Ruley, H.E. Mol. Cell. Biol. (2003) [Pubmed]
  3. HMG1-related DNA-binding protein isolated with V-(D)-J recombination signal probes. Shirakata, M., Hüppi, K., Usuda, S., Okazaki, K., Yoshida, K., Sakano, H. Mol. Cell. Biol. (1991) [Pubmed]
  4. The HMG protein T160 colocalizes with DNA replication foci and is down-regulated during cell differentiation. Hertel, L., De Andrea, M., Bellomo, G., Santoro, P., Landolfo, S., Gariglio, M. Exp. Cell Res. (1999) [Pubmed]
  5. The high-mobility group protein T160 binds to both linear and cruciform DNA and mediates DNA bending as determined by ring closure. Gariglio, M., Ying, G.G., Hertel, L., Gaboli, M., Clerc, R.G., Landolfo, S. Exp. Cell Res. (1997) [Pubmed]
  6. Cell cycle regulation of the p34cdc2/p33cdk2-activating kinase p40MO15. Poon, R.Y., Yamashita, K., Howell, M., Ershler, M.A., Belyavsky, A., Hunt, T. J. Cell. Sci. (1994) [Pubmed]
  7. Structure and chromosomal mapping of the mouse P2X3 gene. Souslova, V., Ravenall, S., Fox, M., Wells, D., Wood, J.N., Akopian, A.N. Gene (1997) [Pubmed]
  8. Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX. Ishov, A.M., Vladimirova, O.V., Maul, G.G. J. Cell. Sci. (2004) [Pubmed]
  9. Identification of a cDNA for SSRP1, an HMG-box protein, by interaction with the c-Myc oncoprotein in a novel bacterial expression screen. Bunker, C.A., Kingston, R.E. Nucleic Acids Res. (1995) [Pubmed]
  10. Decreased expression of the high-mobility group protein T160 by antisense RNA impairs the growth of mouse fibroblasts. Hertel, L., Foresta, P., Barbiero, G., Ying, G.G., Bonelli, G., Baccino, F.M., Landolfo, S., Gariglio, M. Biochimie (1997) [Pubmed]
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