Affinage

SSRP1

FACT complex subunit SSRP1 · UniProt Q08945

Length
709 aa
Mass
81.1 kDa
Annotated
2026-06-10
50 papers in source corpus 25 papers cited in narrative 25 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SSRP1 is an essential histone chaperone that, as one subunit of the heterodimeric FACT complex with SPT16, binds nucleosomes and histone H2A/H2B dimers to drive nucleosome disassembly and facilitate RNA polymerase II elongation through chromatin (PMID:10421373, PMID:17209051). Its essentiality is intrinsic and p53-independent: homozygous loss is lethal at the mouse blastocyst stage (PMID:12861016). The protein is built from defined modules — a middle region of tandem pleckstrin-homology domains that contributes DNA binding but not histone binding (PMID:26687053), and a PH2 surface that mediates either heterodimerization with SPT16 or, mutually exclusively, formation of an elongated SSRP1 homodimer that binds both H2A-H2B and H3-H4 independently of SPT16 (PMID:29764934). Beyond transcription elongation, SSRP1 carries out SPT16-independent chromatin functions: it is recruited to DNA single-strand breaks in a PARP-dependent manner, retained through N-terminal XRCC1 interactions, and required for chromatin decondensation and H2B exchange that prime single-strand break repair (PMID:28416484); it suppresses inappropriate homologous recombination by binding Rad54 and inhibiting Holliday-junction branch migration (PMID:19639603); and it promotes replication origin assembly by evicting histone H1 via its N-terminal domain to derepress ORC/MCM loading (PMID:32165637). SSRP1 also acts in transcription factor–directed gene control, serving as a co-activator of p63 (PMID:12374749) and SRF (PMID:10336466) and as a sequence-specific activator of the embryonic ε-globin promoter (PMID:9566881), and it modulates p53 by reprogramming CK2 substrate specificity toward p53 Ser-392, while reciprocal CK2 phosphorylation of SSRP1 at Ser-510/657/688 inhibits its DNA binding (PMID:11239457, PMID:15659405). The protein is regulated by competing post-translational programs: caspase-3/7 cleavage at Asp-450 followed by ubiquitin-proteasome degradation during apoptosis (PMID:16498457), and USP10-mediated deubiquitination within a TRIB3/USP10/SSRP1 complex that stabilizes it (PMID:39653795). Through its FACT-resident chromatin-remodeling activity, SSRP1 additionally participates in antiviral and viral-replication control, restricting HIV-1 transcription and supporting KSHV latent replication (PMID:26378236, PMID:19710137).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 1998 Medium

    Established that SSRP1 can act directly in transcription through sequence-specific DNA binding, before its chromatin chaperone role was defined.

    Evidence cDNA cloning, EMSA, DNA bending, and erythroid reporter assays at the ε-globin PRE II element

    PMID:9566881

    Open questions at the time
    • Does not connect sequence-specific binding to the later-defined FACT nucleosome activity
    • No structural basis for PRE II recognition
  2. 1999 High

    Defined SSRP1 as half of the FACT heterodimer that disassembles nucleosomes to enable transcription elongation, the core function of the protein.

    Evidence Biochemical purification and in vitro transcription reconstitution on chromatin with nucleosome binding and crosslinking assays

    PMID:10421373

    Open questions at the time
    • Did not resolve which subunit contacts which histone surface
    • In vitro chromatin templates only
  3. 1999 Medium

    Identified SSRP1 partnerships beyond SPT16, linking it to SRF-dependent transcription and to the remodeler CHD1.

    Evidence Yeast one-hybrid, Co-IP, EMSA, reporter assays (SRF) and in vivo Co-IP with co-localization (CHD1)

    PMID:10199952 PMID:10336466

    Open questions at the time
    • Whether these interactions occur within FACT or via free SSRP1 unresolved
    • No structural model of the SRF or CHD1 contact
  4. 2001 High

    Revealed that SSRP1/FACT reprograms CK2 substrate specificity toward p53 Ser-392 and recognizes damaged DNA, expanding its role into the DNA-damage/p53 axis.

    Evidence UV-activated kinase complex purification with in vitro kinase assays; EMSA with cisplatin-damaged DNA using FACT, isolated SSRP1, and the HMG domain

    PMID:11239457 PMID:11344167

    Open questions at the time
    • In vitro kinase context only
    • Functional consequence of damaged-DNA binding for repair not directly tested
  5. 2002 Medium

    Mapped the molecular logic of FACT subunit interaction and CK2 conformational steering, and established SSRP1 as a p63 transcriptional co-activator.

    Evidence Domain-mapped Co-IP and in vitro kinase assays (CK2 complex); reciprocal Co-IP, GST pulldown, ChIP, and reporter/phenotype assays (p63γ)

    PMID:12374749 PMID:12393879

    Open questions at the time
    • Single-lab interaction mapping
    • Endogenous stoichiometry of the CK2·SPT16·SSRP1 complex unknown
  6. 2003 High

    Demonstrated SSRP1 is genetically essential for early embryonic viability independent of p53, separating its core function from its p53-modulating role.

    Evidence Mouse gene targeting, embryo outgrowth assays, and crosses to a p53-null background

    PMID:12861016

    Open questions at the time
    • Lethality precludes assignment to a single molecular process
    • Which essential activity (elongation vs replication) drives lethality not defined
  7. 2005 High

    Established reciprocal regulation: CK2 phosphorylation of SSRP1 at Ser-510/657/688 inhibits its DNA-binding activity, a UV-responsive control point.

    Evidence In vitro CK2 kinase assays, site-directed mutagenesis, EMSA, and in-cell 32P labeling (with supporting maize data on HMG-adjacent phosphosites)

    PMID:12571244 PMID:15659405

    Open questions at the time
    • Cellular consequences of phospho-inhibition for transcription/repair not directly tested
    • Cross-species site correspondence inferred
  8. 2006 Medium

    Showed SSRP1 is dismantled during apoptosis by ordered caspase cleavage and proteasomal degradation, linking FACT inactivation to cell death.

    Evidence In vitro caspase cleavage with site mutagenesis, proteasome inhibitor and ubiquitylation assays, and fractionation

    PMID:16498457

    Open questions at the time
    • Functional consequence of the truncated chromatin-bound form not defined
    • Which apoptotic signals trigger this in vivo unclear
  9. 2007 Medium

    Distinguished SPT16-dependent from SPT16-independent SSRP1 transcriptional functions genome-wide.

    Evidence Microarray after siRNA of SSRP1 or Spt16 plus ChIP for elongating Pol II on egr1

    PMID:17209051

    Open questions at the time
    • Mechanism of SSRP1-only gene regulation not resolved
    • Direct vs indirect targets not separated
  10. 2009 Medium

    Extended SSRP1 into genome maintenance and viral DNA replication: suppression of homologous recombination via Rad54 and support of KSHV latent origin replication.

    Evidence Co-IP and in vitro branch-migration assay with recombination/foci readouts (Rad54); DNA affinity pulldown, Co-IP, and replication assays (KSHV origin/LANA)

    PMID:19639603 PMID:19710137

    Open questions at the time
    • Whether HR suppression requires FACT or free SSRP1 unclear
    • Single-lab functional assays
  11. 2015 High

    Provided structural and biophysical definition of SSRP1 architecture: a DNA-binding tandem-PH middle domain and a PH2-mediated homodimer that binds histones independently of SPT16.

    Evidence X-ray crystallography with DNA/histone binding assays; AUC, SAXS, ITC, and mutagenesis

    PMID:26687053 PMID:29764934

    Open questions at the time
    • In vivo prevalence and function of the homodimer not established
    • How homo/heterodimer switching is controlled in cells unknown
  12. 2017 High

    Defined an SPT16-independent role for SSRP1 in single-strand break repair, recruited via PARP and retained by XRCC1 to remodel chromatin for repair.

    Evidence Laser microirradiation live imaging, Co-IP, domain mutants, FRAP histone exchange, and survival assays

    PMID:28416484

    Open questions at the time
    • Direct vs PARP-bridged SSRP1–XRCC1 contact not fully resolved
    • Relationship to FACT elongation activity unclear
  13. 2020 High

    Showed SSRP1 promotes replication origin assembly by N-terminal eviction of histone H1, derepressing ORC/MCM loading and timing developmental cell-cycle transitions.

    Evidence Xenopus egg-extract replication assays, chromatin fractionation, depletion, domain mutants, and embryo microinjection

    PMID:32165637

    Open questions at the time
    • Whether mammalian somatic origins use the same H1-eviction mechanism untested
    • Selectivity of H1 over other linker histones not defined
  14. 2024 Medium

    Identified post-translational stabilization of SSRP1 through a TRIB3/USP10 deubiquitination complex, and broadened its FACT-dependent antiviral role through the FEAR/ETS-1 pathway.

    Evidence Co-IP, ubiquitination and peptide-disruption assays (TRIB3/USP10); siRNA depletion, viral replication, and mutant M-protein rescue (FEAR, preprint)

    PMID:39653795 PMID:bio_10.1101_2024.08.22.609092

    Open questions at the time
    • FEAR finding is a non-peer-reviewed preprint
    • Whether SSRP1 vs SPT16 drives FEAR chromatin remodeling not separated

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved how SSRP1 partitions between its FACT-bound elongation role, its SPT16-independent repair/replication/homodimer activities, and its many transcription-factor co-activator functions within a single cell.
  • No in vivo measurement of the relative abundance of FACT heterodimer vs SSRP1 homodimer
  • No unified model linking phospho-regulation, dimer state, and functional choice

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140110 transcription regulator activity 4 GO:0003677 DNA binding 3 GO:0042393 histone binding 2 GO:0098772 molecular function regulator activity 2
Localization
GO:0000228 nuclear chromosome 2 GO:0005634 nucleus 1
Pathway
R-HSA-4839726 Chromatin organization 3 R-HSA-73894 DNA Repair 2 R-HSA-74160 Gene expression (Transcription) 2 R-HSA-5357801 Programmed Cell Death 1 R-HSA-69306 DNA Replication 1
Partners
CHD1CSNK2A1RAD54SRFSUPT16HTP63USP10XRCC1
Complex memberships
FACT complex

Evidence

Reading pass · 25 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 FACT complex is a heterodimer of human SPT16 (hSpt16) and SSRP1; it acts as a chromatin-specific transcription elongation factor, interacts with nucleosomes and histone H2A/H2B dimers, and promotes nucleosome disassembly to facilitate transcription elongation through chromatin templates in vitro. FACT activity is abrogated by covalently crosslinking nucleosomal histones. Biochemical purification, in vitro transcription reconstitution on chromatin templates, nucleosome binding assays, crosslinking experiments Nature High 10421373
2001 SSRP1 (as part of FACT, a heterodimer with hSpt16) forms a UV-activated kinase complex with CK2 that selectively phosphorylates p53 at Ser-392 in vitro. FACT alters the substrate specificity of CK2 such that it preferentially phosphorylates p53 over other CK2 substrates including casein. Phosphorylation by this complex enhances p53 transcriptional activity. Biochemical purification of UV-activated kinase complex, in vitro kinase assay, identification of complex components by mass spectrometry/sequencing Molecular cell High 11239457
2002 hSPT16 and SSRP1 interact via non-overlapping domains in vitro and in cells; binding of hSPT16 and SSRP1 to CK2 changes CK2 conformation to specifically target p53 Ser-392 over other substrates. UV irradiation induces assembly of the CK2·hSPT16·SSRP1 complex, increasing specificity of CK2 for p53 at Ser-392. Co-immunoprecipitation, in vitro binding assays, domain mapping, in vitro kinase assay The Journal of biological chemistry Medium 12393879
2001 The FACT complex (SSRP1/Spt16 heterodimer) exhibits affinity and specificity for cisplatin-damaged DNA, binding the major 1,2-d(GpG) intrastrand adduct. The isolated SSRP1 subunit alone fails to form discrete high-affinity complexes with cisplatin-modified DNA, suggesting Spt16 primes SSRP1 for cisplatin-damaged DNA recognition by unveiling its HMG domain. The isolated HMG domain of SSRP1 alone is sufficient for specific binding to cisplatin-damaged DNA. Gel mobility shift assays (EMSA) with cisplatin-damaged DNA, testing FACT complex, isolated SSRP1, and isolated HMG domain The Journal of biological chemistry Medium 11344167
2003 CK2 phosphorylates maize SSRP1 at multiple C-terminal residues including two sites adjacent to the HMG box domain; this phosphorylation induces a conformational change in the HMG box region (detected by circular dichroism) and switches on recognition of UV-damaged DNA by SSRP1 (non-phosphorylated SSRP1 does not discriminate between UV-damaged and control DNA). In vitro kinase assay with CK2α, acetic acid-urea PAGE, mass spectrometry phosphosite mapping, circular dichroism, DNA binding assays with UV-damaged DNA The Journal of biological chemistry Medium 12571244
2005 CK2 phosphorylates SSRP1 at serines 510, 657, and 688 in vitro; phosphorylation inhibits the nonspecific DNA-binding activity of SSRP1 and FACT. Ser-510 is the most critical site for this regulation. SSRP1 is also phosphorylated in cells in response to UV (but not gamma) irradiation. In vitro CK2 kinase assay, peptide array kinase assay, site-directed mutagenesis (S510A/S657A/S688A), EMSA DNA-binding assays, metabolic 32P-labeling in cells The Journal of biological chemistry High 15659405
2002 SSRP1 functions as a co-activator of p63 by direct physical interaction (in vitro and in cells); it binds p63γ through its central domain, and ectopic expression of full-length SSRP1 (but not deletion mutants) enhances p63γ-dependent transcription, G1 arrest, apoptosis, and expression of endogenous p53 target genes. SSRP1 co-occupies p53-responsive elements of MDM2 and p21 promoters with p63γ. Co-immunoprecipitation, in vitro GST pulldown, luciferase reporter assays, chromatin immunoprecipitation (ChIP), cell-based gain/loss-of-function The EMBO journal Medium 12374749
1999 SSRP1 interacts with SRF (serum response factor) through the MADS box of SRF and a basic region of SSRP1 (amino acids 489–542 adjacent to the HMG domain); this interaction dramatically increases the DNA-binding activity of SRF and results in synergistic transcriptional activation of SRF-dependent promoters. SSRP1 itself does not bind the CArG box. Yeast one-hybrid screen, co-immunoprecipitation in mammalian cells, EMSA, luciferase reporter assays, domain mapping The Journal of biological chemistry Medium 10336466
1999 CHD1 interacts in vivo with SSRP1 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 of Drosophila polytene chromosomes. Co-immunoprecipitation (in vivo), immunocytochemistry/immunofluorescence co-localization Chromosoma Medium 10199952
2001 In yeast, the bipartite FACT analog composed of Cdc68 (Spt16), Pob3, and Nhp6 functionally recapitulates the vertebrate FACT complex; Nhp6 (the yeast functional analog of the SSRP1 HMG domain) associates with the CP complex and provides HMG box functions for transcription elongation. An artificial Pob3-Nhp6a fusion protein (mimicking SSRP1) restores both Pob3 and Nhp6a functions. Genetic epistasis (double mutant analysis), 6-azauracil sensitivity, protein fusion complementation, co-immunoprecipitation Molecular and cellular biology Medium 11313475
2003 Ssrp1 homozygous knockout in mice causes embryonic lethality at day 3.5, with preimplantation blastocysts defective for cell outgrowth/survival in vitro. This lethality is p53-independent (crosses with p53-null background do not rescue), establishing nonredundant, essential functions for SSRP1 in early cell viability. Gene targeting in mouse ES cells, germline transmission, embryo outgrowth assays, p53-null genetic background cross Molecular and cellular biology High 12861016
2007 SSRP1 has both SPT16-dependent and SPT16-independent roles in transcription regulation in human cells; approximately 1.3% of assayed genes are co-regulated by both SSRP1 and Spt16, while a distinct subset is regulated by SSRP1 alone. Both SSRP1 and Spt16 are required for progression of elongating RNA Pol II on the egr1 gene. Spotted microarray after siRNA knockdown of SSRP1 or Spt16, chromatin immunoprecipitation for elongating Pol II The Journal of biological chemistry Medium 17209051
2009 SSRP1 physically interacts with the HR repair protein Rad54 both in vitro and in vivo; SSRP1 inhibits Rad54-promoted branch migration of Holliday junctions in vitro. Knockdown of SSRP1 increases HR frequency and Rad51/H2AX foci, while overexpression reduces HU-induced Rad51 foci, indicating SSRP1 suppresses inappropriate homologous recombination repair. Co-immunoprecipitation (in vivo), in vitro pulldown, branch migration assay with Holliday junctions, hprt recombination assay, immunofluorescence for Rad51/γH2AX foci, siRNA knockdown and overexpression Journal of cellular biochemistry Medium 19639603
2009 SSRP1 (as a FACT subunit) binds the KSHV latent origin replication element and forms a complex with LANA at this origin; siRNA knockdown of SSRP1 significantly reduces the efficiency of LANA-dependent latent DNA replication. Biotinylated DNA pulldown/affinity purification to identify origin-binding proteins, Co-immunoprecipitation, siRNA knockdown with plasmid replication efficiency assay Journal of virology Medium 19710137
2006 SSRP1 is cleaved during apoptosis by caspase 3 and/or caspase 7 at the DQHD450 site, generating a truncated chromatin-associated form of FACT. The N-terminal cleavage product is subsequently degraded via the ubiquitin-proteasome pathway (stabilized by proteasome inhibitors and ubiquitylated in cells). In vitro caspase cleavage assay, site-directed mutagenesis of caspase site, proteasome inhibitor treatment, ubiquitylation assay in cells, cellular fractionation Cell death and differentiation Medium 16498457
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 patch on its surface, but does not bind histones (negative result confirmed by pulldown assay). X-ray crystallography, DNA binding assays, histone pulldown assays Scientific reports High 26687053
2015 FACT components SUPT16H and SSRP1 suppress HIV-1 transcription and promote viral latency; SUPT16H (but not SSRP1) directly interacts with HIV-1 Tat protein, yet both are recruited to the HIV-1 LTR promoter. SUPT16H interferes with association of Cyclin T1 (a P-TEFb subunit) with the Tat-LTR axis. Depletion of either SSRP1 or SUPT16H spontaneously reverses HIV-1 latency. RNAi functional genomic screen, Co-immunoprecipitation, HIV-1 LTR reporter assay, ChIP, latency reversal assays in U1/HIV, J-LAT cells, and primary CD4+ T cell model The Journal of biological chemistry Medium 26378236
2017 SSRP1 is recruited to DNA single-strand break (SSB) sites in a PARP-dependent manner and is retained at damage sites via N-terminal interactions with XRCC1. SSRP1 (but not SPT16) is specifically required for chromatin decondensation and histone H2B exchange at SSB sites, which primes chromatin for efficient SSB repair and cell survival after ionizing radiation or MMS treatment. Live-cell imaging (laser microirradiation recruitment), co-immunoprecipitation, domain mutational analysis, siRNA knockdown with survival assay, histone exchange (FRAP), chromatin decondensation assay Cancer research High 28416484
2018 SSRP1 forms an elongated homodimer in solution (characterized by AUC and SAXS); homodimerization involves the PH2 region, the same surface used for heterodimerization with SPT16, suggesting homo- and heterodimerization are mutually exclusive. SSRP1 homodimerization promotes binding to both histones H2A-H2B and H3-H4 (isothermal titration calorimetry); disruption of homodimerization decreases histone-binding affinity. Analytical ultracentrifugation (AUC), small-angle X-ray scattering (SAXS), isothermal titration calorimetry (ITC), site-directed mutagenesis The Journal of biological chemistry High 29764934
2020 SSRP1 promotes replication origin assembly on somatic chromatin in Xenopus by evicting histone H1 via its N-terminal domain; histone H1 removal derepresses ORC and MCM chromatin binding, enabling efficient replication origin firing. SSRP1 protein decays at mid-blastula transition (MBT), and increased SSRP1 levels delay MBT and accelerate post-MBT cell cycle speed and embryo development. Xenopus laevis egg extract replication assays, chromatin fractionation, siRNA/antibody depletion of SSRP1 and H1, domain mutational analysis, embryo microinjection Nature communications High 32165637
2016 Depletion of SSRP1 in human mesenchymal stem cells decreases expression of osteoblast-specific genes and downregulates Wnt pathway target genes, accompanied by decreased nuclear localization of active β-catenin, identifying a role for SSRP1 in promoting Wnt signaling pathway activity during osteoblast differentiation. siRNA knockdown in human MSCs, RNA-seq, Western blot for active β-catenin nuclear localization, differentiation assays Stem cells Medium 27146025
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 effect. A stapled peptide (SP-A) disrupts the TRIB3/USP10/SSRP1 complex and promotes SSRP1 degradation. Co-immunoprecipitation, ubiquitination assays, in vivo and in vitro interaction studies, peptide disruption assay Oncogene Medium 39653795
1998 SSRP1 (identified as PREIIBF) binds with sequence specificity to a 19-bp positive regulatory element (PRE II) in the human embryonic ε-globin gene promoter, bends the target DNA, and is required for promoter activation in stable erythroid cell lines. This is the first evidence that SSRP1 plays a direct role in transcriptional regulation via sequence-specific DNA binding. cDNA expression cloning, EMSA (gel shift with specific DNA competition), DNA bending assay (circularization), stable transfection reporter assay in erythroid cells Molecular and cellular biology Medium 9566881
2023 SSRP1 maintains mitochondrial oxidative respiration in hepatocellular carcinoma cells by transcriptionally promoting expression of TRAP1 (the mitochondrial HSP90 family member); SSRP1 occupies the TRAP1 promoter (by ChIP), and SSRP1 knockdown decreases TRAP1 mRNA and protein, reduces mitochondrial oxidative respiration, and causes mitochondrial damage. siRNA knockdown, ChIP assay, qRT-PCR, Western blot, mitochondrial respiration assay (Seahorse), rescue experiments Biochemistry and cell biology Medium 37084412
2024 The FACT complex (hSpt16/SSRP1) mediates the FEAR (FACT-ETS-1 Antiviral Response) pathway, remodeling chromatin to activate expression of the antiviral transcription factor ETS-1 to restrict RNA virus (VSV and paramyxovirus) replication. VSV M protein promotes proteasome-dependent degradation of SUMOylated hSpt16 to counter FEAR; this antagonism of SUMOylated Spt16 by viral proteins is a conserved mechanism across DNA and RNA viruses. siRNA depletion of hSpt16/SSRP1, viral replication assays, mutant M protein analysis, genetic rescue experiments bioRxiv (preprint)preprint Medium bio_10.1101_2024.08.22.609092

Source papers

Stage 0 corpus · 50 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 462 10421373
2001 A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1. Molecular cell 254 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
2003 Protein kinase CK2 phosphorylates the high mobility group domain protein SSRP1, inducing the recognition of UV-damaged DNA. The Journal of biological chemistry 58 12571244
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 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 45 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
2015 Crystal Structure of Human SSRP1 Middle Domain Reveals a Role in DNA Binding. Scientific reports 34 26687053
2009 A role for SSRP1 in recombination-mediated DNA damage response. Journal of cellular biochemistry 34 19639603
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
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 32 40514727
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
2009 Involvement of SSRP1 in latent replication of Kaposi's sarcoma-associated herpesvirus. Journal of virology 25 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 21 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 20 35844005
2020 SSRP1-mediated histone H1 eviction promotes replication origin assembly and accelerated development. Nature communications 17 32165637
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
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
2018 Structure-specific recognition protein-1 (SSRP1) is an elongated homodimer that binds histones. The Journal of biological chemistry 14 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
2024 Pseudokinase TRIB3 stabilizes SSRP1 via USP10-mediated deubiquitination to promote multiple myeloma progression. Oncogene 5 39653795
2022 The Current Status of SSRP1 in Cancer: Tribulation and Road Ahead. Journal of healthcare engineering 5 35463672
2025 A Novel ceRNA Axis LOC121818100/Novel-miR-400/SSRP1 Regulated Muscle Growth and Injury Repair in Sheep. Journal of cachexia, sarcopenia and muscle 3 40468947
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
2026 Arachidonic acid analog AACOCF3 suppresses cPLA2-negative NSCLC cell proliferation by targeting SSRP1 to activate the IFNα/β pathway. Biochemical pharmacology 1 41544858
2024 Evolution of the chromatin remodeling complex FACT: Functional analysis of SSRP1 and SPT16 in early anther development. International journal of biological macromolecules 1 39615716
1997 Characterisation of bovine structure-specific recognition protein 1 (SSRP1) cDNA. Biochemistry and molecular biology international 1 9385438
2024 Retraction: SSRP1 Promotes Colorectal Cancer Progression and is Negatively Regulated by miR-28-5p. Journal of cellular and molecular medicine 0 39267240
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

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