Biology:Structure specific recognition protein 1

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

FACT complex subunit SSRP1 also known as structure specific recognition protein 1 is a protein that in humans is encoded by the SSRP1 gene.

Function

The protein encoded by this gene is a subunit of a heterodimer that, along with SUPT16H, forms chromatin transcriptional elongation factor FACT. FACT interacts specifically with histones H2A/H2B to effect nucleosome disassembly and transcription elongation. FACT and cisplatin-damaged DNA may be crucial to the anticancer mechanism of cisplatin. This encoded protein contains a high mobility group box which most likely constitutes the structure recognition element for cisplatin-modified DNA. This protein also functions as a co-activator of the transcriptional activator p63.

Interactions

Structure specific recognition protein 1 has been shown to interact with NEK9. SSRP1 further interacts with transcriptional activator p63. SSRP1 enhances the activity of full-length p63, but it has no effect on the N-terminus-deleted p63 (DeltaN-p63) variant.

Further reading

• "Isolation and characterization of human cDNA clones encoding a high mobility group box protein that recognizes structural distortions to DNA caused by binding of the anticancer agent cisplatin.". Proc. Natl. Acad. Sci. U.S.A. 89 (6): 2307–11. 1992. doi:10.1073/pnas.89.6.2307. PMID 1372440. Bibcode: 1992PNAS...89.2307B. 
• "Isolation of cDNAs encoding a human protein that binds selectively to DNA modified by the anticancer drug cis-diamminedichloroplatinum(II)". Proc. Natl. Acad. Sci. U.S.A. 86 (21): 8328–32. 1989. doi:10.1073/pnas.86.21.8328. PMID 2530581. Bibcode: 1989PNAS...86.8328T. 
• "Multiple proteins physically interact with PU.1. Transcriptional synergy with NF-IL6 beta (C/EBP delta, CRP3).". J. Immunol. 155 (9): 4330–8. 1995. doi:10.4049/jimmunol.155.9.4330. PMID 7594592. 
• "FACT, a factor that facilitates transcript elongation through nucleosomes.". Cell 92 (1): 105–16. 1998. doi:10.1016/S0092-8674(00)80903-4. PMID 9489704. 
• "The HMG domain protein SSRP1/PREIIBF is involved in activation of the human embryonic beta-like globin gene.". Mol. Cell. Biol. 18 (5): 2617–28. 1998. doi:10.1128/MCB.18.5.2617. PMID 9566881. 
• "Requirement of RSF and FACT for transcription of chromatin templates in vitro.". Science 282 (5395): 1900–4. 1998. doi:10.1126/science.282.5395.1900. PMID 9836642. 
• "CHD1 interacts with SSRP1 and depends on both its chromodomain and its ATPase/helicase-like domain for proper association with chromatin.". Chromosoma 108 (1): 10–25. 1999. doi:10.1007/s004120050347. PMID 10199952. 
• "Cooperative transcriptional activation by serum response factor and the high mobility group protein SSRP1.". J. Biol. Chem. 274 (22): 15686–93. 1999. doi:10.1074/jbc.274.22.15686. PMID 10336466. 
• "The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins.". Nature 400 (6741): 284–8. 1999. doi:10.1038/22350. PMID 10421373. Bibcode: 1999Natur.400..284O. 
• "FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH.". Mol. Cell 5 (6): 1067–72. 2000. doi:10.1016/S1097-2765(00)80272-5. PMID 10912001. 
• "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1.". Mol. Cell 7 (2): 283–92. 2001. doi:10.1016/S1097-2765(01)00176-9. PMID 11239457. 
• "Interaction of FACT, SSRP1, and the high mobility group (HMG) domain of SSRP1 with DNA damaged by the anticancer drug cisplatin.". J. Biol. Chem. 276 (28): 25736–41. 2001. doi:10.1074/jbc.M101208200. PMID 11344167. 
• "High prevalence of autoantibodies against the nuclear high mobility group (HMG) protein SSRP1 in sera from patients with systemic lupus erythematosus, but not other rheumatic diseases.". J. Rheumatol. 29 (1): 90–3. 2002. PMID 11824977. 
• "Nercc1, a mammalian NIMA-family kinase, binds the Ran GTPase and regulates mitotic progression.". Genes Dev. 16 (13): 1640–58. 2002. doi:10.1101/gad.972202. PMID 12101123. 
• "SSRP1 functions as a co-activator of the transcriptional activator p63.". EMBO J. 21 (20): 5487–97. 2002. doi:10.1093/emboj/cdf540. PMID 12374749. 
• "p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex.". J. Biol. Chem. 277 (51): 50206–13. 2003. doi:10.1074/jbc.M209820200. PMID 12393879. 
• "FACT facilitates transcription-dependent nucleosome alteration.". Science 301 (5636): 1090–3. 2003. doi:10.1126/science.1085703. PMID 12934006. Bibcode: 2003Sci...301.1090B. 
• "Regulation of alternative splicing by SRrp86 and its interacting proteins.". Mol. Cell. Biol. 23 (21): 7437–47. 2003. doi:10.1128/MCB.23.21.7437-7447.2003. PMID 14559993. 
• "Nek9, a novel FACT-associated protein, modulates interphase progression.". J. Biol. Chem. 279 (10): 9321–30. 2004. doi:10.1074/jbc.M311477200. PMID 14660563. 

External links

• SSRP1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.