Affinage

SSRP1

FACT complex subunit SSRP1 · UniProt Q08945

Length
709 aa
Mass
81.1 kDa
Annotated
2026-04-28
53 papers in source corpus 25 papers cited in narrative 25 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SSRP1 is a multifunctional chromatin-associated protein that serves as a subunit of the FACT histone chaperone complex (with SPT16) to facilitate RNA polymerase II elongation through nucleosomes by promoting histone H2A/H2B displacement, while also performing SPT16-independent functions in DNA repair, replication licensing, and transcriptional regulation. As part of FACT, SSRP1 binds nucleosomes and H2A/H2B dimers to enable chromatin-templated transcription, and its middle domain contains tandem pleckstrin homology folds that mediate DNA binding; SSRP1 also forms elongated homodimers via the same PH2 interface used for SPT16 heterodimerization, and these homodimers bind both H2A/H2B and H3/H4 histones (PMID:10421373, PMID:26687053, PMID:29764934). Beyond transcription elongation, SSRP1 scaffolds a CK2/FACT complex that phosphorylates p53-Ser392 after UV irradiation, is recruited to single-strand breaks in a PARP-dependent manner to promote XRCC1-mediated chromatin decondensation, suppresses homologous recombination by inhibiting Rad54-driven branch migration, and stimulates replication origin licensing by evicting linker histone H1 through its N-terminal domain (PMID:11239457, PMID:28416484, PMID:19639603, PMID:32165637). Ssrp1 is essential for early embryonic viability in mouse, with homozygous null embryos dying shortly after implantation in a p53-independent manner (PMID:12861016).

Mechanistic history

Synthesis pass · year-by-year structured walk · 17 steps
  1. 1995 Low

    Initial identification of SSRP1 as a protein interacting with the bHLH/LZ domain of c-Myc raised the question of whether SSRP1 plays a role in transcriptional regulation.

    Evidence Bacterial expression library screen for c-Myc-interacting proteins

    PMID:7862532

    Open questions at the time
    • Single screening assay without reciprocal validation or functional follow-up
    • No evidence SSRP1 affects Myc-dependent transcription
    • Interaction domain on SSRP1 unmapped
  2. 1998 High

    Demonstration that SSRP1 binds a specific promoter element (PRE II) of the embryonic epsilon-globin gene and is required for its activation established SSRP1 as a sequence-specific transcriptional regulator capable of DNA bending.

    Evidence Expression cloning, recombinant protein DNA binding and bending assays, stable reporter assays in erythroid cells

    PMID:9566881

    Open questions at the time
    • Whether SSRP1 functions at this promoter as part of FACT or independently was unknown
    • Genome-wide scope of SSRP1 sequence-specific binding not addressed
  3. 1999 High

    The discovery that SSRP1 and SPT16 form the FACT complex, which facilitates transcription elongation on chromatin by interacting with nucleosomes and H2A/H2B dimers, established the core molecular function of SSRP1 as a histone chaperone enabling transcription through chromatin.

    Evidence Biochemical purification of FACT, reconstituted in vitro chromatin transcription, nucleosome crosslinking experiments

    PMID:10421373

    Open questions at the time
    • Whether SSRP1 has functions independent of SPT16 was unresolved
    • In vivo relevance of FACT-mediated nucleosome disassembly during transcription not yet shown
    • Structural basis of SSRP1-nucleosome interaction unknown
  4. 1999 High

    Identification of SSRP1 interactions with SRF and CHD1 at transcriptionally active loci suggested SSRP1 functions as a co-activator for specific transcription factors beyond its general chromatin remodeling role.

    Evidence Yeast one-hybrid screen, co-IP, domain mapping, reporter assays for SRF; co-localization and interaction assays for CHD1

    PMID:10199952 PMID:10336466

    Open questions at the time
    • Whether SRF co-activation requires FACT or is an SSRP1-autonomous function was unclear
    • CHD1 interaction lacked functional consequence data
  5. 2001 High

    Discovery that FACT assembles with CK2 into a UV-activated kinase complex that selectively phosphorylates p53-Ser392 revealed a scaffolding role for SSRP1/SPT16 in modulating kinase substrate specificity during the DNA damage response.

    Evidence Biochemical purification of the kinase complex, in vitro kinase assays comparing CK2 alone vs. CK2/FACT, co-IP, domain mapping

    PMID:11239457 PMID:12393879

    Open questions at the time
    • In vivo contribution of FACT-directed p53 phosphorylation to UV survival not tested genetically
    • Whether FACT alters CK2 specificity for substrates beyond p53 was unknown
  6. 2001 High

    Showing that FACT specifically recognizes cisplatin-damaged DNA via the HMG domain of SSRP1 — whose accessibility requires SPT16 — linked SSRP1 to DNA damage recognition and suggested a conformational gating mechanism within the heterodimer.

    Evidence Gel mobility shift assays with purified FACT, free SSRP1, and isolated HMG domain on cisplatin-modified DNA

    PMID:11344167

    Open questions at the time
    • Functional consequence of FACT binding to cisplatin adducts for repair or cytotoxicity was not established
    • Structural basis for SPT16-mediated unmasking of the HMG domain unknown
  7. 2002 High

    Identification of SSRP1 as a p63 co-activator that co-occupies p53-responsive promoters extended SSRP1's transcriptional co-activation role to the p53 family.

    Evidence Co-IP, GST pulldown, ChIP at MDM2 and p21 promoters, luciferase reporter assays

    PMID:12374749

    Open questions at the time
    • Whether SSRP1 co-activation of p63 requires FACT or is SPT16-independent was not tested
    • In vivo developmental significance of SSRP1-p63 interaction unresolved
  8. 2003 High

    Mapping CK2 phosphorylation sites on SSRP1 and showing that phosphorylation induces a conformational change in the HMG domain that enables UV-damaged DNA recognition provided a post-translational mechanism regulating SSRP1 DNA binding specificity.

    Evidence Mass spectrometry phosphosite mapping, circular dichroism spectroscopy, DNA binding assays with UV-damaged DNA, mutagenesis

    PMID:12571244 PMID:15659405

    Open questions at the time
    • Whether CK2-phosphorylated SSRP1 functions during nucleotide excision repair in cells was not tested
    • Structural details of the conformational switch at atomic resolution were lacking
  9. 2003 High

    Ssrp1 knockout in mice causing peri-implantation lethality — not rescued by p53 loss — established SSRP1 as an essential gene whose critical function is p53-independent, consistent with a fundamental role in chromatin dynamics rather than solely in p53 regulation.

    Evidence Gene targeting in ES cells, blastocyst outgrowth assays, genetic cross with p53-null mice

    PMID:12861016

    Open questions at the time
    • Which specific SSRP1 function (transcription elongation, replication, or other) accounts for embryonic lethality was undetermined
    • Cell-type-specific requirements not addressed
  10. 2006 High

    Demonstrating that SSRP1 is cleaved by caspase-3/7 during apoptosis followed by ubiquitin-proteasome degradation of the N-terminal fragment revealed a regulated two-step destruction mechanism that inactivates FACT during programmed cell death.

    Evidence In vitro caspase cleavage, cleavage-site mutagenesis, proteasome inhibitor treatment, ubiquitylation detection

    PMID:16498457

    Open questions at the time
    • Functional consequence of SSRP1 destruction for chromatin state during apoptosis not defined
    • E3 ligase responsible for N-terminal fragment ubiquitylation not identified
  11. 2007 High

    Genome-wide expression profiling after selective knockdown of SSRP1 or SPT16 revealed that SSRP1 regulates a subset of genes independently of SPT16, establishing that SSRP1 has functions beyond the FACT heterodimer.

    Evidence siRNA knockdown, microarray profiling of 8308 genes, ChIP for RNA Pol II occupancy

    PMID:17209051

    Open questions at the time
    • Nature of the SPT16-independent SSRP1 complex or mechanism at those genes was unknown
    • Whether SSRP1 homodimer mediates the independent functions was not tested
  12. 2009 High

    Discovery that SSRP1 directly binds Rad54 and inhibits its branch migration activity established a role for SSRP1 in suppressing homologous recombination, expanding its function beyond transcription to recombination control.

    Evidence Co-IP, GST pulldown, in vitro branch migration assays with purified proteins, cellular HR frequency assays

    PMID:19639603

    Open questions at the time
    • Whether HR suppression operates through the FACT complex or SSRP1 alone was not resolved
    • Physiological context (e.g., replication-associated HR) not clarified
  13. 2015 High

    Crystal structure of the SSRP1 middle domain revealed tandem PH domains mediating DNA binding but not histone binding, providing the first high-resolution structural insight into SSRP1's domain architecture.

    Evidence X-ray crystallography, pull-down assays, DNA binding assays

    PMID:26687053

    Open questions at the time
    • Structure of SSRP1 in complex with nucleosome or with SPT16 not determined
    • How the PH domains cooperate with the HMG domain for DNA recognition was unknown
  14. 2017 High

    Showing that SSRP1 is recruited to single-strand breaks via PARP and retained by XRCC1 to promote chromatin decondensation and histone H2B exchange established SSRP1 as a histone chaperone directly functioning in single-strand break repair independently of SPT16.

    Evidence Live-cell imaging of laser-induced SSBs, FRAP for H2B exchange, co-IP with XRCC1, domain deletions, clonogenic survival assays

    PMID:28416484

    Open questions at the time
    • Whether SSRP1 homodimer or monomer is the active species at SSBs was untested
    • Contribution to base excision repair vs. other SSB repair sub-pathways not delineated
  15. 2018 High

    Biophysical demonstration that SSRP1 forms an elongated homodimer through the PH2 interface — the same surface used for SPT16 heterodimerization — and that homodimerization enhances histone binding provided a structural explanation for SPT16-independent SSRP1 functions.

    Evidence Analytical ultracentrifugation, SAXS, ITC, PH2 surface mutagenesis

    PMID:29764934

    Open questions at the time
    • Cellular prevalence of homodimer vs. FACT heterodimer not quantified
    • Whether homodimer has distinct genomic occupancy or function from FACT in cells was unknown
  16. 2020 High

    Demonstration that SSRP1 promotes replication origin licensing by evicting linker histone H1 via its N-terminal domain in Xenopus egg extracts linked SSRP1 to replication initiation and revealed how maternally loaded SSRP1 controls the timing of the midblastula transition.

    Evidence Xenopus cell-free replication assays, chromatin binding of ORC/MCM, domain deletions, developmental timing experiments

    PMID:32165637

    Open questions at the time
    • Whether mammalian SSRP1 similarly regulates replication licensing was not tested
    • Mechanism by which SSRP1 N-terminal domain evicts H1 at molecular level was undefined
  17. 2024 Medium

    Identification of a TRIB3/USP10/SSRP1 ternary complex in which USP10-mediated deubiquitination stabilizes SSRP1 protein revealed a post-translational mechanism controlling SSRP1 abundance with implications for cancer cell proliferation.

    Evidence Co-IP, ubiquitination assays, stapled peptide disruption, in vitro and in vivo proliferation assays

    PMID:39653795

    Open questions at the time
    • E3 ubiquitin ligase targeting SSRP1 for degradation not identified
    • Whether USP10-mediated stabilization affects FACT vs. SSRP1 homodimer differentially is unknown
    • Single study awaiting independent replication

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include the structural basis of full-length SSRP1 within FACT bound to a nucleosome, the cellular determinants governing partitioning between SSRP1 homodimer and FACT heterodimer pools, and the in vivo mechanisms by which SSRP1 coordinates its transcription elongation, replication licensing, and DNA repair functions.
  • No high-resolution structure of human FACT-nucleosome complex
  • Relative cellular abundance and genomic occupancy of SSRP1 homodimer vs. FACT undetermined
  • How SSRP1 is differentially recruited to transcription, replication, and repair sites remains unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003677 DNA binding 4 GO:0044183 protein folding chaperone 4 GO:0042393 histone binding 3 GO:0140110 transcription regulator activity 3 GO:0098772 molecular function regulator activity 2
Localization
GO:0005654 nucleoplasm 4 GO:0005694 chromosome 3
Pathway
R-HSA-4839726 Chromatin organization 4 R-HSA-73894 DNA Repair 4 R-HSA-74160 Gene expression (Transcription) 4 R-HSA-5357801 Programmed Cell Death 1 R-HSA-69306 DNA Replication 1
Complex memberships
CK2/FACT kinase complexFACT (SPT16/SSRP1)SSRP1 homodimer

Evidence

Reading pass · 25 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 FACT complex comprises human SPT16 and SSRP1 proteins, functions as a chromatin-specific transcription elongation factor that interacts with nucleosomes and histone H2A/H2B dimers, and facilitates transcription of chromatin templates in vitro; FACT activity is abrogated by covalent crosslinking of nucleosomal histones, indicating it works by promoting nucleosome disassembly during transcription. Biochemical purification, reconstituted in vitro transcription on chromatin templates, nucleosome binding assays, crosslinking experiments Nature High 10421373
2001 SSRP1 (as part of FACT) forms a UV-activated kinase complex with CK2 and hSPT16 that phosphorylates p53 at Ser-392; within this complex, FACT alters CK2 specificity such that it selectively phosphorylates p53 over other substrates including casein, and phosphorylation by the complex enhances p53 transcriptional activity. Biochemical purification of kinase complex, in vitro kinase assays, co-immunoprecipitation Molecular cell High 11239457
2002 SSRP1 and hSPT16 interact with CK2 via non-overlapping domains in vitro and in cells; UV irradiation induces assembly of the CK2/hSPT16/SSRP1 complex, increasing CK2 specificity for p53 Ser-392 phosphorylation over other cellular CK2 substrates. In vitro interaction assays, domain mapping, co-immunoprecipitation, in-cell complex assembly after UV irradiation The Journal of biological chemistry High 12393879
2001 FACT (SPT16/SSRP1 heterodimer) exhibits affinity and specificity for cisplatin-damaged DNA, recognizing the major 1,2-d(GpG) intrastrand cisplatin adduct; the isolated HMG domain of SSRP1 is sufficient for specific binding to cisplatin-damaged DNA, while SSRP1 alone (without SPT16) fails to form discrete high-affinity complexes, suggesting SPT16 primes SSRP1 for cisplatin-damaged DNA recognition by unveiling its HMG domain. Gel mobility shift assays with purified FACT, SSRP1, and isolated HMG domain; comparison of cisplatin-modified vs. unmodified and trans-DDP-modified DNA The Journal of biological chemistry High 11344167
2002 SSRP1 functions as a co-activator of the transcriptional activator p63; SSRP1 physically interacts with p63γ in vitro and in cells via SSRP1's central domain and p63's N-terminus, and co-occupies p53-responsive elements at MDM2 and p21 promoters; overexpression of SSRP1 enhances p63γ-dependent transcription, G1 arrest, and apoptosis. Co-immunoprecipitation, GST pulldown, luciferase reporter assays, chromatin immunoprecipitation, dominant-negative overexpression The EMBO journal High 12374749
1999 CHD1 interacts with SSRP1 in vivo via an amino-terminal segment of CHD1 that does not include the chromodomain; CHD1 and SSRP1 co-localize in mammalian nuclei and at transcriptionally active regions in Drosophila polytene chromosomes. Transient transfection with wild-type and mutant CHD1 constructs, immunocytochemical co-localization, in vivo interaction assays Chromosoma Medium 10199952
1999 SSRP1 interacts with serum response factor (SRF) through the MADS box of SRF and a basic region of SSRP1 (amino acids 489-542) adjacent to the HMG domain; SSRP1 dramatically increases SRF DNA-binding activity and synergistically activates SRF-dependent promoters without itself binding the CArG box. Yeast one-hybrid screen, co-immunoprecipitation in yeast and mammalian cells, domain mapping, DNA binding assays, luciferase reporter assays The Journal of biological chemistry High 10336466
1998 SSRP1 (identified as PREIIBF) binds with sequence specificity to the PRE II element of the human embryonic epsilon-globin gene, bends target DNA, and is required for promoter activation in stable erythroid cell lines; recombinant SSRP1 is biochemically identical to the endogenous erythroid PREIIBF. cDNA expression cloning, recombinant protein characterization, DNA binding assays, DNA bending assays, stable transfection reporter assays Molecular and cellular biology High 9566881
1995 SSRP1 was identified as a protein that interacts specifically with the basic helix-loop-helix/leucine zipper domains of c-Myc. Bacterial cDNA expression library screen based on protein-protein interaction with lambda cl repressor fusion proteins Nucleic acids research Low 7862532
2003 CK2 phosphorylates SSRP1 at multiple sites in the C-terminal region and within the acidic domain; CK2-mediated phosphorylation of two C-terminal sites causes a conformational change in the HMG box domain region and induces recognition of UV-damaged DNA by SSRP1, whereas non-phosphorylated SSRP1 does not discriminate between UV-damaged and control DNA. Acetic acid-urea PAGE, mass spectrometry phosphosite mapping, circular dichroism, DNA binding assays with UV-damaged DNA, yeast complementation assay The Journal of biological chemistry High 12571244
2005 CK2 phosphorylates SSRP1 at Ser-510, Ser-657, and Ser-688 in vitro; phosphorylation inhibits the nonspecific DNA-binding activity of both SSRP1 and the FACT complex in vitro; Ser-510 is the most important site for regulation of SSRP1 DNA-binding activity; SSRP1 is phosphorylated in cells specifically in response to UV but not gamma irradiation. Serine/threonine-scanning Auto-spot peptide array kinase assay, site-directed mutagenesis, in vitro DNA binding assays, in-cell phosphorylation detection after UV/gamma irradiation The Journal of biological chemistry High 15659405
2003 Ssrp1 homozygous null embryos die soon after implantation (day 3.5); preimplantation blastocysts are defective for cell outgrowth and/or survival in vitro; the essential function of Ssrp1 is p53-independent, as crossing into a p53-null background does not rescue the growth/survival defects. Gene targeting in mouse embryonic stem cells, germline transmission, blastocyst outgrowth assays, genetic epistasis with p53-null background Molecular and cellular biology High 12861016
2007 SSRP1 has both SPT16-dependent and SPT16-independent roles in regulating gene transcription in human cells; SSRP1 and SPT16 are required for progression of elongating RNA pol II on the egr1 gene; a subset of genes regulated by SSRP1 is not affected by Spt16 knockdown. siRNA knockdown of SSRP1 or SPT16, spotted microarray analysis of 8308 genes, ChIP for RNA pol II occupancy on specific genes The Journal of biological chemistry High 17209051
2009 SSRP1 physically interacts with the HR repair protein Rad54 in vitro and in vivo; SSRP1 inhibits Rad54-promoted branch migration of Holliday junctions in vitro; overexpression of SSRP1 reduces HR frequency while knockdown increases HR events, suggesting SSRP1 suppresses homologous recombination. Co-immunoprecipitation, GST pulldown, branch migration assays with purified proteins, hprt recombination assay, Rad51 and H2AX foci quantification Journal of cellular biochemistry High 19639603
2009 SSRP1 (as a subunit of FACT) forms complexes with LANA at the minimal replicon (MR) region of KSHV latent origin; siRNA knockdown of SSRP1 significantly decreases LANA-dependent latent DNA replication efficiency, establishing SSRP1 as a cellular factor required for KSHV latent replication. Biotinylated DNA pulldown/mass spectrometry to identify origin-binding proteins, co-immunoprecipitation with LANA, siRNA knockdown with replication assay Journal of virology Medium 19710137
2015 SSRP1 (as part of FACT) suppresses HIV-1 and HTLV-1 transcription and promotes viral latency; SSRP1 is recruited to the HIV-1 LTR promoter; depletion of SSRP1 de-represses Tat-mediated HIV-1 LTR activity and spontaneously reverses HIV-1 latency in multiple cell models; SSRP1 affects both HIV-1 transcriptional initiation and elongation. Functional genomic RNAi screen, luciferase reporter assays, ChIP, siRNA knockdown with HIV-1 replication assays, primary CD4+ T cell latency model The Journal of biological chemistry High 26378236
2015 Crystal structure of the SSRP1 middle domain reveals tandem pleckstrin homology (PH) domains (PH1 with an extra conserved βαβ topology); the middle domain participates in DNA binding via a positively charged surface patch; the middle domain does not bind histones. X-ray crystallography, pull-down assays for histone binding, DNA binding assays Scientific reports High 26687053
2017 SSRP1 is recruited to single-strand DNA breaks (SSBs) in a PARP-dependent manner and is retained at damage sites via N-terminal interactions with XRCC1; SSRP1 (but not SPT16) is critical for cell survival after SSB-inducing damage; SSRP1 is required for chromatin decondensation and histone H2B exchange at SSB sites to prime chromatin for efficient repair. Live-cell imaging of SSRP1 recruitment to laser-induced SSBs, co-immunoprecipitation with XRCC1, mutational analysis of N-terminal domain, histone H2B exchange assays (FRAP), clonogenic survival after IR/MMS Cancer research High 28416484
2018 Human SSRP1 forms an elongated homodimer in solution; SSRP1 homodimerization and heterodimerization with SPT16 both involve the same PH2 surface region and are mutually exclusive; FACT contains only one molecule of SSRP1; SSRP1 binds both histones H2A-H2B and H3-H4, and disruption of homodimerization decreases histone-binding affinity. Analytical ultracentrifugation (AUC), small-angle X-ray scattering (SAXS), isothermal titration calorimetry (ITC), site-directed mutagenesis of PH2 domain The Journal of biological chemistry High 29764934
2006 SSRP1 is cleaved during apoptosis by caspase-3 and/or caspase-7 at the DQHD450 site; cleavage generates a truncated chromatin-associated form of FACT; the N-terminal cleavage product is ubiquitylated and degraded through the ubiquitin-proteasome pathway, making SSRP1 degradation during apoptosis a two-step process coupling caspase cleavage and ubiquitin-dependent proteolysis. In vitro caspase cleavage assays, site-directed mutagenesis, proteasome inhibitor treatment, ubiquitylation detection, subcellular fractionation Cell death and differentiation High 16498457
2020 SSRP1 stimulates replication origin assembly on somatic chromatin in Xenopus laevis by promoting eviction of histone H1 through its N-terminal domain; H1 removal derepresses ORC and MCM chromatin binding; SSRP1 protein decays at mid-blastula transition (MBT), and increasing SSRP1 levels delays MBT while accelerating post-MBT cell cycle speed and embryo development. Xenopus laevis cell-free replication system, chromatin assembly/disassembly assays, ORC/MCM chromatin binding assays, domain deletion analysis, developmental timing assays Nature communications High 32165637
2024 TRIB3 directly interacts with SSRP1 and USP10, forming a TRIB3/USP10/SSRP1 ternary complex; USP10-mediated deubiquitination stabilizes SSRP1 protein, and TRIB3 enhances this deubiquitinating activity; disruption of this complex with a stapled peptide (SP-A) leads to SSRP1 protein degradation. Co-immunoprecipitation, ubiquitination assays, stapled peptide disruption experiments, in vitro and in vivo proliferation assays Oncogene Medium 39653795
2016 SSRP1 facilitates the translocation of phospho-Ets-1 from cytoplasm to cell nucleus in nasopharyngeal carcinoma cells, thereby positively regulating Pim-3 expression (which is downstream of Ets-1); SSRP1 knockdown diminishes phospho-Ets-1 nuclear localization without affecting Ets-1 expression or phosphorylation levels. siRNA knockdown, western blot, immunocytochemistry for subcellular localization of phospho-Ets-1 Biomedicine & pharmacotherapy Low 27525970
2016 SSRP1 is essential for Wnt signaling pathway activity during osteoblast differentiation; SSRP1 depletion in human mesenchymal stem cells decreases Wnt target gene expression and reduces nuclear localization of active β-catenin during osteoblast differentiation. siRNA knockdown in human mesenchymal stem cells, RNA-seq transcriptome analysis, immunofluorescence for β-catenin nuclear localization Stem cells Medium 27146025
2024 The FACT complex (hSpt16/SSRP1) mediates an interferon-independent antiviral innate immune response (FEAR pathway) by remodeling chromatin to activate expression of the antiviral transcription factor ETS-1; poxvirus A51R proteins antagonize this by tethering SUMOylated hSpt16 to microtubules; VSV M protein promotes proteasome-dependent degradation of SUMOylated hSpt16 to block ETS-1 nuclear import and counter FEAR pathway restriction. RNAi depletion, viral replication assays, overexpression of viral antagonists, genetic rescue experiments, FACT inhibitor treatment bioRxivpreprint Medium bio_10.1101_2024.08.22.609092

Source papers

Stage 0 corpus · 53 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1999 The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins. Nature 459 10421373
2001 A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1. Molecular cell 253 11239457
2001 A bipartite yeast SSRP1 analog comprised of Pob3 and Nhp6 proteins modulates transcription. Molecular and cellular biology 108 11313475
2002 p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex. The Journal of biological chemistry 104 12393879
1999 CHD1 interacts with SSRP1 and depends on both its chromodomain and its ATPase/helicase-like domain for proper association with chromatin. Chromosoma 97 10199952
2001 Interaction of FACT, SSRP1, and the high mobility group (HMG) domain of SSRP1 with DNA damaged by the anticancer drug cisplatin. The Journal of biological chemistry 79 11344167
2002 SSRP1 functions as a co-activator of the transcriptional activator p63. The EMBO journal 78 12374749
2011 HMG domain containing SSRP1 is required for DNA demethylation and genomic imprinting in Arabidopsis. Developmental cell 73 21920319
2016 SSRP1 Contributes to the Malignancy of Hepatocellular Carcinoma and Is Negatively Regulated by miR-497. Molecular therapy : the journal of the American Society of Gene Therapy 57 26755331
2007 Human SSRP1 has Spt16-dependent and -independent roles in gene transcription. The Journal of biological chemistry 57 17209051
2003 Protein kinase CK2 phosphorylates the high mobility group domain protein SSRP1, inducing the recognition of UV-damaged DNA. The Journal of biological chemistry 57 12571244
2003 The high-mobility-group box protein SSRP1/T160 is essential for cell viability in day 3.5 mouse embryos. Molecular and cellular biology 57 12861016
2001 Differential chromatin association and nucleosome binding of the maize HMGA, HMGB, and SSRP1 proteins. Biochemistry 51 11425313
2005 CK2 phosphorylates SSRP1 and inhibits its DNA-binding activity. The Journal of biological chemistry 49 15659405
2015 FACT Proteins, SUPT16H and SSRP1, Are Transcriptional Suppressors of HIV-1 and HTLV-1 That Facilitate Viral Latency. The Journal of biological chemistry 44 26378236
1999 Cooperative transcriptional activation by serum response factor and the high mobility group protein SSRP1. The Journal of biological chemistry 44 10336466
2019 SSRP1 promotes colorectal cancer progression and is negatively regulated by miR-28-5p. Journal of cellular and molecular medicine 43 30762286
2017 SSRP1 Cooperates with PARP and XRCC1 to Facilitate Single-Strand DNA Break Repair by Chromatin Priming. Cancer research 40 28416484
2009 A role for SSRP1 in recombination-mediated DNA damage response. Journal of cellular biochemistry 34 19639603
2015 Crystal Structure of Human SSRP1 Middle Domain Reveals a Role in DNA Binding. Scientific reports 33 26687053
2000 DNA-interactions and nuclear localisation of the chromosomal HMG domain protein SSRP1 from maize. The Plant journal : for cell and molecular biology 33 10929132
1995 Identification of a cDNA for SSRP1, an HMG-box protein, by interaction with the c-Myc oncoprotein in a novel bacterial expression screen. Nucleic acids research 32 7862532
2016 Histone Chaperone SSRP1 is Essential for Wnt Signaling Pathway Activity During Osteoblast Differentiation. Stem cells (Dayton, Ohio) 31 27146025
1998 The HMG domain protein SSRP1/PREIIBF is involved in activation of the human embryonic beta-like globin gene. Molecular and cellular biology 30 9566881
2025 Therapeutic potential of miR-204-5p in intervertebral disc degeneration: targeting the SSRP1/NF-κB pathway to inhibit apoptosis. Journal of orthopaedic surgery and research 29 40514727
2009 Involvement of SSRP1 in latent replication of Kaposi's sarcoma-associated herpesvirus. Journal of virology 24 19710137
2017 SSRP1 silencing inhibits the proliferation and malignancy of human glioma cells via the MAPK signaling pathway. Oncology reports 23 29048646
2018 Uncovering the fine print of the CreERT2-LoxP system while generating a conditional knockout mouse model of Ssrp1 gene. PloS one 20 29953487
2022 Exosomes loaded with circPARD3 promotes EBV-miR-BART4-induced stemness and cisplatin resistance in nasopharyngeal carcinoma side population cells through the miR-579-3p/SIRT1/SSRP1 axis. Cell biology and toxicology 19 35844005
2019 A novel lncRNA LOC101927746 accelerates progression of colorectal cancer via inhibiting miR-584-3p and activating SSRP1. Biochemical and biophysical research communications 17 30616889
2018 The Arabidopsis Histone Chaperone FACT: Role of the HMG-Box Domain of SSRP1. Journal of molecular biology 17 29966609
2020 SSRP1-mediated histone H1 eviction promotes replication origin assembly and accelerated development. Nature communications 16 32165637
2019 SSRP1 influences colorectal cancer cell growth and apoptosis via the AKT pathway. International journal of medical sciences 16 31839745
2016 Blockage of SSRP1/Ets-1/Pim-3 signalling enhances chemosensitivity of nasopharyngeal carcinoma to docetaxel in vitro. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 16 27525970
2022 Mir204 and Mir211 suppress synovial inflammation and proliferation in rheumatoid arthritis by targeting Ssrp1. eLife 14 36511897
2019 The SSRP1 subunit of the histone chaperone FACT is required for seed dormancy in Arabidopsis. Journal of plant physiology 14 30947026
2018 Structure-specific recognition protein-1 (SSRP1) is an elongated homodimer that binds histones. The Journal of biological chemistry 13 29764934
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. The Journal of rheumatology 13 11824977
2006 Coupling caspase cleavage and ubiquitin-proteasome-dependent degradation of SSRP1 during apoptosis. Cell death and differentiation 12 16498457
2018 MiR-223 inhibits the proliferation, invasion and EMT of nasopharyngeal carcinoma cells by targeting SSRP1. International journal of clinical and experimental pathology 9 31949834
2014 Protein Phosphatase 2C of Toxoplasma Gondii Interacts with Human SSRP1 and Negatively Regulates Cell Apoptosis. Biomedical and environmental sciences : BES 9 25374021
2025 SSRP1/SLC3A2 Axis in Arginine Transport: A New Target for Overcoming Immune Evasion and Tumor Progression in Peripheral T-Cell Lymphoma. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 7 40344476
2021 DLG1-AS1 is activated by MYC and drives the proliferation and migration of hepatocellular carcinoma cells through miR-497-5p/SSRP1 axis. Cancer cell international 7 33407499
2022 The Current Status of SSRP1 in Cancer: Tribulation and Road Ahead. Journal of healthcare engineering 5 35463672
2024 Pseudokinase TRIB3 stabilizes SSRP1 via USP10-mediated deubiquitination to promote multiple myeloma progression. Oncogene 3 39653795
2022 SSRP1 affects the growth and apoptosis of gastric cancer cells through AKT pathway. Journal of medical biochemistry 3 35291495
2021 SSRP1 Worsens Malignant Melanoma Progression by Activating MAPKs Pathway. Annals of clinical and laboratory science 3 34921031
2025 A Novel ceRNA Axis LOC121818100/Novel-miR-400/SSRP1 Regulated Muscle Growth and Injury Repair in Sheep. Journal of cachexia, sarcopenia and muscle 2 40468947
1997 Characterisation of bovine structure-specific recognition protein 1 (SSRP1) cDNA. Biochemistry and molecular biology international 1 9385438
2026 Arachidonic acid analog AACOCF3 suppresses cPLA2-negative NSCLC cell proliferation by targeting SSRP1 to activate the IFNα/β pathway. Biochemical pharmacology 0 41544858
2024 Retraction: SSRP1 Promotes Colorectal Cancer Progression and is Negatively Regulated by miR-28-5p. Journal of cellular and molecular medicine 0 39267240
2024 Evolution of the chromatin remodeling complex FACT: Functional analysis of SSRP1 and SPT16 in early anther development. International journal of biological macromolecules 0 39615716
2023 Histone chaperone SSRP1 is required for apoptosis inhibition and mitochondrial function in HCC via transcriptional promotion of TRAP1. Biochemistry and cell biology = Biochimie et biologie cellulaire 0 37084412