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Structure specific recognition protein 1
Symbols SSRP1; FACT; FACT80; T160
External IDs OMIM604328 MGI107912 HomoloGene2370 GeneCards: SSRP1 Gene
RNA expression pattern
PBB GE SSRP1 200957 s at tn.png
PBB GE SSRP1 200956 s at tn.png
More reference expression data
Species Human Mouse
Entrez 6749 20833
Ensembl ENSG00000149136 ENSMUSG00000027067
UniProt Q08945 Q05DR5
RefSeq (mRNA) NM_003146 NM_182990
RefSeq (protein) NP_003137 NP_892035
Location (UCSC) Chr 11:
56.85 - 56.86 Mb
Chr 2:
84.84 - 84.85 Mb
PubMed search [1] [2]

Structure specific recognition protein 1, also known as SSRP1, is a human protein.[1]

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.[1]



Structure specific recognition protein 1 has been shown to interact with NEK9.[2]


  1. ^ a b "Entrez Gene: SSRP1 structure specific recognition protein 1".  
  2. ^ Tan, Bertrand Chin-Ming; Lee Sheng-Chung (Mar. 2004). "Nek9, a novel FACT-associated protein, modulates interphase progression". J. Biol. Chem. (United States) 279 (10): 9321–30. doi:10.1074/jbc.M311477200. ISSN 0021-9258. PMID 14660563.  

Further reading

  • Bruhn SL, Pil PM, Essigmann JM, et al. (1992). "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. doi:10.1073/pnas.89.6.2307. PMID 1372440.  
  • Toney JH, Donahue BA, Kellett PJ, et al. (1989). "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. doi:10.1073/pnas.86.21.8328. PMID 2530581.  
  • Nagulapalli S, Pongubala JM, Atchison ML (1995). "Multiple proteins physically interact with PU.1. Transcriptional synergy with NF-IL6 beta (C/EBP delta, CRP3).". J. Immunol. 155 (9): 4330–8. PMID 7594592.  
  • Orphanides G, LeRoy G, Chang CH, et al. (1998). "FACT, a factor that facilitates transcript elongation through nucleosomes.". Cell 92 (1): 105–16. doi:10.1016/S0092-8674(00)80903-4. PMID 9489704.  
  • Dyer MA, Hayes PJ, Baron MH (1998). "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. PMID 9566881.  
  • LeRoy G, Orphanides G, Lane WS, Reinberg D (1998). "Requirement of RSF and FACT for transcription of chromatin templates in vitro.". Science 282 (5395): 1900–4. doi:10.1126/science.282.5395.1900. PMID 9836642.  
  • Kelley DE, Stokes DG, Perry RP (1999). "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. doi:10.1007/s004120050347. PMID 10199952.  
  • Spencer JA, Baron MH, Olson EN (1999). "Cooperative transcriptional activation by serum response factor and the high mobility group protein SSRP1.". J. Biol. Chem. 274 (22): 15686–93. doi:10.1074/jbc.274.22.15686. PMID 10336466.  
  • Orphanides G, Wu WH, Lane WS, et al. (1999). "The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins.". Nature 400 (6741): 284–8. doi:10.1038/22350. PMID 10421373.  
  • Wada T, Orphanides G, Hasegawa J, et al. (2000). "FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH.". Mol. Cell 5 (6): 1067–72. doi:10.1016/S1097-2765(00)80272-5. PMID 10912001.  
  • Keller DM, Zeng X, Wang Y, et al. (2001). "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1.". Mol. Cell 7 (2): 283–92. doi:10.1016/S1097-2765(01)00176-9. PMID 11239457.  
  • Yarnell AT, Oh S, Reinberg D, Lippard SJ (2001). "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. doi:10.1074/jbc.M101208200. PMID 11344167.  
  • Santoro P, De Andrea M, Migliaretti G, et al. (2002). "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. PMID 11824977.  
  • Roig J, Mikhailov A, Belham C, Avruch J (2002). "Nercc1, a mammalian NIMA-family kinase, binds the Ran GTPase and regulates mitotic progression.". Genes Dev. 16 (13): 1640–58. doi:10.1101/gad.972202. PMID 12101123.  
  • Zeng SX, Dai MS, Keller DM, Lu H (2002). "SSRP1 functions as a co-activator of the transcriptional activator p63.". Embo J. 21 (20): 5487–97. doi:10.1093/emboj/cdf540. PMID 12374749.  
  • Keller DM, Lu H (2003). "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. doi:10.1074/jbc.M209820200. PMID 12393879.  
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.  
  • Belotserkovskaya R, Oh S, Bondarenko VA, et al. (2003). "FACT facilitates transcription-dependent nucleosome alteration.". Science 301 (5636): 1090–3. doi:10.1126/science.1085703. PMID 12934006.  
  • Li J, Hawkins IC, Harvey CD, et al. (2003). "Regulation of alternative splicing by SRrp86 and its interacting proteins.". Mol. Cell. Biol. 23 (21): 7437–47. doi:10.1128/MCB.23.21.7437-7447.2003. PMID 14559993.  
  • Tan BC, Lee SC (2004). "Nek9, a novel FACT-associated protein, modulates interphase progression.". J. Biol. Chem. 279 (10): 9321–30. doi:10.1074/jbc.M311477200. PMID 14660563.  

External links

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



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