Open Access Articles- Top Results for Structure specific recognition protein 1

Structure specific recognition protein 1

SymbolsSSRP1 ; FACT; FACT80; T160
External IDsOMIM604328 MGI107912 HomoloGene110735 GeneCards: SSRP1 Gene
RNA expression pattern
File:PBB GE SSRP1 200957 s at tn.png
File:PBB GE SSRP1 200956 s at tn.png
More reference expression data
RefSeq (mRNA)NM_003146NM_001136081
RefSeq (protein)NP_003137NP_001129553
Location (UCSC)Chr 11:
57.09 – 57.1 Mb
Chr 2:
85.04 – 85.05 Mb
PubMed search[1][2]

FACT complex subunit SSRP1 also known as structure specific recognition protein 1 is a protein that in humans is encoded by the SSRP1 gene.[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] SSRP1 further interacts with transcriptional activator p63.[3] SSRP1 enhances the activity of full-length p63, but it has no effect on the N-terminus-deleted p63 (DeltaN-p63) variant.


  1. ^ a b "Entrez Gene: SSRP1 structure specific recognition protein 1". 
  2. ^ Tan BC, Lee SC (Mar 2004). "Nek9, a novel FACT-associated protein, modulates interphase progression". J. Biol. Chem. 279 (10): 9321–30. PMID 14660563. doi:10.1074/jbc.M311477200. 
  3. ^ Zeng SX, Dai MS, Keller DM, Lu H (15 Oct 2002). "SSRP1 functions as a co-activator of the transcriptional activator p63". EMBO J. 21 (20): 5487–97. PMC 129072. PMID 12374749. doi:10.1093/emboj/cdf540. 

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External links

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

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