ID SSRP1_HUMAN Reviewed; 709 AA. AC Q08945; Q5BJG8; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 229. DE RecName: Full=FACT complex subunit SSRP1; DE AltName: Full=Chromatin-specific transcription elongation factor 80 kDa subunit; DE AltName: Full=Facilitates chromatin transcription complex 80 kDa subunit; DE Short=FACT 80 kDa subunit; DE Short=FACTp80; DE AltName: Full=Facilitates chromatin transcription complex subunit SSRP1; DE AltName: Full=Recombination signal sequence recognition protein 1; DE AltName: Full=Structure-specific recognition protein 1; DE Short=hSSRP1; DE AltName: Full=T160; GN Name=SSRP1; Synonyms=FACT80; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=B-cell; RX PubMed=1372440; DOI=10.1073/pnas.89.6.2307; RA Bruhn S.L., Pil P.M., Essigmann J.M., Housman D.E., Lippard S.J.; RT "Isolation and characterization of human cDNA clones encoding a high RT mobility group box protein that recognizes structural distortions to DNA RT caused by binding of the anticancer agent cisplatin."; RL Proc. Natl. Acad. Sci. U.S.A. 89:2307-2311(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 2-15; 234-241; 252-264; 305-316; 388-396 AND 414-421, RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC TISSUE=Lung carcinoma; RA Bienvenut W.V., Vousden K.H., Lukashchuk N.; RL Submitted (MAR-2008) to UniProtKB. RN [4] RP FUNCTION. RX PubMed=9489704; DOI=10.1016/s0092-8674(00)80903-4; RA Orphanides G., LeRoy G., Chang C.-H., Luse D.S., Reinberg D.; RT "FACT, a factor that facilitates transcript elongation through RT nucleosomes."; RL Cell 92:105-116(1998). RN [5] RP FUNCTION. RX PubMed=9566881; DOI=10.1128/mcb.18.5.2617; RA Dyer M.A., Hayes P.J., Baron M.H.; RT "The HMG domain protein SSRP1/PREIIBF is involved in activation of the RT human embryonic beta-like globin gene."; RL Mol. Cell. Biol. 18:2617-2628(1998). RN [6] RP FUNCTION. RX PubMed=9836642; DOI=10.1126/science.282.5395.1900; RA LeRoy G., Orphanides G., Lane W.S., Reinberg D.; RT "Requirement of RSF and FACT for transcription of chromatin templates in RT vitro."; RL Science 282:1900-1904(1998). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INTERACTION RP WITH SUPT16H. RX PubMed=10421373; DOI=10.1038/22350; RA Orphanides G., Wu W.-H., Lane W.S., Hampsey M., Reinberg D.; RT "The chromatin-specific transcription elongation factor FACT comprises RT human SPT16 and SSRP1 proteins."; RL Nature 400:284-288(1999). RN [8] RP FUNCTION. RX PubMed=10912001; DOI=10.1016/s1097-2765(00)80272-5; RA Wada T., Orphanides G., Hasegawa J., Kim D.-K., Shima D., Yamaguchi Y., RA Fukuda A., Hisatake K., Oh S., Reinberg D., Handa H.; RT "FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation RT and reveals functional differences between P-TEFb and TFIIH."; RL Mol. Cell 5:1067-1072(2000). RN [9] RP DOMAIN. RX PubMed=11344167; DOI=10.1074/jbc.m101208200; RA Yarnell A.T., Oh S., Reinberg D., Lippard S.J.; RT "Interaction of FACT, SSRP1, and the high mobility group (HMG) domain of RT SSRP1 with DNA damaged by the anticancer drug cisplatin."; RL J. Biol. Chem. 276:25736-25741(2001). RN [10] RP FUNCTION, AND INTERACTION WITH SUPT16H; CSNK2A1; CSNK2A2 AND CSNK2B. RX PubMed=11239457; DOI=10.1016/s1097-2765(01)00176-9; RA Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., RA Lozano G., Zhao Y., Lu H.; RT "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, RT and SSRP1."; RL Mol. Cell 7:283-292(2001). RN [11] RP FUNCTION, AND INTERACTION WITH TP63. RX PubMed=12374749; DOI=10.1093/emboj/cdf540; RA Zeng S.X., Dai M.-S., Keller D.M., Lu H.; RT "SSRP1 functions as a co-activator of the transcriptional activator p63."; RL EMBO J. 21:5487-5497(2002). RN [12] RP ERRATUM OF PUBMED:12374749. RA Zeng S.X., Dai M.-S., Keller D.M., Lu H.; RL EMBO J. 23:1679-1679(2004). RN [13] RP INTERACTION WITH SUPT16H; CSNK2A1; CSNK2A2 AND CSNK2B, AND PHOSPHORYLATION. RX PubMed=12393879; DOI=10.1074/jbc.m209820200; RA Keller D.M., Lu H.; RT "p53 serine 392 phosphorylation increases after UV through induction of the RT assembly of the CK2.hSPT16.SSRP1 complex."; RL J. Biol. Chem. 277:50206-50213(2002). RN [14] RP AUTOANTIBODIES. RX PubMed=11824977; RA Santoro P., De Andrea M., Migliaretti G., Trapani C., Landolfo S., RA Gariglio M.; RT "High prevalence of autoantibodies against the nuclear high mobility group RT (HMG) protein SSRP1 in sera from patients with systemic lupus RT erythematosus, but not other rheumatic diseases."; RL J. Rheumatol. 29:90-93(2002). RN [15] RP FUNCTION. RX PubMed=12934006; DOI=10.1126/science.1085703; RA Belotserkovskaya R., Oh S., Bondarenko V.A., Orphanides G., Studitsky V.M., RA Reinberg D.; RT "FACT facilitates transcription-dependent nucleosome alteration."; RL Science 301:1090-1093(2003). RN [16] RP INTERACTION WITH NEK9. RX PubMed=14660563; DOI=10.1074/jbc.m311477200; RA Tan B.C.-M., Lee S.-C.; RT "Nek9, a novel FACT-associated protein, modulates interphase progression."; RL J. Biol. Chem. 279:9321-9330(2004). RN [17] RP SUMOYLATION. RX PubMed=15561718; DOI=10.1074/jbc.m411718200; RA Gocke C.B., Yu H., Kang J.; RT "Systematic identification and analysis of mammalian small ubiquitin-like RT modifier substrates."; RL J. Biol. Chem. 280:5004-5012(2005). RN [18] RP PHOSPHORYLATION AT SER-510; SER-657 AND SER-688, AND MUTAGENESIS OF RP SER-510; SER-657 AND SER-688. RX PubMed=15659405; DOI=10.1074/jbc.m413944200; RA Li Y., Keller D.M., Scott J.D., Lu H.; RT "CK2 phosphorylates SSRP1 and inhibits its DNA-binding activity."; RL J. Biol. Chem. 280:11869-11875(2005). RN [19] RP FUNCTION. RX PubMed=16713563; DOI=10.1016/j.cell.2006.04.029; RA Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., Reinberg D.; RT "Histone H2B monoubiquitination functions cooperatively with FACT to RT regulate elongation by RNA polymerase II."; RL Cell 125:703-717(2006). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [21] RP CLEAVAGE SITE, UBIQUITINATION, AND MUTAGENESIS OF ASP-450. RX PubMed=16498457; DOI=10.1038/sj.cdd.4401878; RA Landais I., Lee H., Lu H.; RT "Coupling caspase cleavage and ubiquitin-proteasome-dependent degradation RT of SSRP1 during apoptosis."; RL Cell Death Differ. 13:1866-1878(2006). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170; SER-437; SER-444; RP SER-667; SER-668; SER-671; SER-672 AND SER-673, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [25] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [26] RP INTERACTION WITH FYTTD1. RX PubMed=19836239; DOI=10.1016/j.cub.2009.09.041; RA Hautbergue G.M., Hung M.L., Walsh M.J., Snijders A.P., Chang C.T., RA Jones R., Ponting C.P., Dickman M.J., Wilson S.A.; RT "UIF, a new mRNA export adaptor that works together with REF/ALY, requires RT FACT for recruitment to mRNA."; RL Curr. Biol. 19:1918-1924(2009). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [28] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233 AND LYS-413, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170 AND SER-444, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [30] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444; SER-657; SER-667; RP SER-668 AND SER-671, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [32] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=22002106; DOI=10.1074/mcp.m111.013680; RA Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.; RT "Systematic analysis of protein pools, isoforms, and modifications RT affecting turnover and subcellular localization."; RL Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012). RN [33] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [34] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [35] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444; SER-659 AND SER-667, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [36] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444 AND SER-471, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [37] RP SUBUNIT. RX PubMed=27499292; DOI=10.1016/j.molcel.2016.06.023; RA Roulland Y., Ouararhni K., Naidenov M., Ramos L., Shuaib M., Syed S.H., RA Lone I.N., Boopathi R., Fontaine E., Papai G., Tachiwana H., Gautier T., RA Skoufias D., Padmanabhan K., Bednar J., Kurumizaka H., Schultz P., RA Angelov D., Hamiche A., Dimitrov S.; RT "The flexible ends of CENP-A nucleosome are required for mitotic RT fidelity."; RL Mol. Cell 63:674-685(2016). RN [38] RP INTERACTION WITH HERPES SIMPLEX VIRUS 1 PROTEIN ICP22. RX PubMed=28611249; DOI=10.1128/mbio.00745-17; RA Fox H.L., Dembowski J.A., DeLuca N.A.; RT "A Herpesviral Immediate Early Protein Promotes Transcription Elongation of RT Viral Transcripts."; RL MBio 8:0-0(2017). RN [39] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-90; LYS-296 AND LYS-364, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). CC -!- FUNCTION: Component of the FACT complex, a general chromatin factor CC that acts to reorganize nucleosomes. The FACT complex is involved in CC multiple processes that require DNA as a template such as mRNA CC elongation, DNA replication and DNA repair. During transcription CC elongation the FACT complex acts as a histone chaperone that both CC destabilizes and restores nucleosomal structure. It facilitates the CC passage of RNA polymerase II and transcription by promoting the CC dissociation of one histone H2A-H2B dimer from the nucleosome, then CC subsequently promotes the reestablishment of the nucleosome following CC the passage of RNA polymerase II. The FACT complex is probably also CC involved in phosphorylation of 'Ser-392' of p53/TP53 via its CC association with CK2 (casein kinase II). Binds specifically to double- CC stranded DNA and at low levels to DNA modified by the antitumor agent CC cisplatin. May potentiate cisplatin-induced cell death by blocking CC replication and repair of modified DNA. Also acts as a transcriptional CC coactivator for p63/TP63. {ECO:0000269|PubMed:10912001, CC ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:12374749, CC ECO:0000269|PubMed:12934006, ECO:0000269|PubMed:16713563, CC ECO:0000269|PubMed:9489704, ECO:0000269|PubMed:9566881, CC ECO:0000269|PubMed:9836642}. CC -!- SUBUNIT: Interacts with MYOG (via C-terminal region) (By similarity). CC Component of the FACT complex, a stable heterodimer of SSRP1 and CC SUPT16H (PubMed:10421373). Also a component of a CK2-SPT16-SSRP1 CC complex which forms following UV irradiation, composed of SSRP1, CC SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B (PubMed:11239457, CC PubMed:12393879). Binds to histone H3-H4 tetramers, but not to intact CC nucleosomes. Identified in a centromere complex containing histones CC H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, CC SUPT16H, SSRP1 and RSF1 (PubMed:27499292). Interacts with isoform gamma CC of TP63 (PubMed:12374749). Interacts with FYTTD1/UIF (PubMed:19836239). CC Interacts with SRF (By similarity). Interacts with NEK9 CC (PubMed:14660563). {ECO:0000250|UniProtKB:Q04931, CC ECO:0000250|UniProtKB:Q08943, ECO:0000269|PubMed:10421373, CC ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:12374749, CC ECO:0000269|PubMed:12393879, ECO:0000269|PubMed:14660563, CC ECO:0000269|PubMed:19836239, ECO:0000269|PubMed:27499292}. CC -!- SUBUNIT: (Microbial infection) Interacts with Herpes simplex virus 1 CC (HHV-1) protein ICP22; this interaction relocalizes the FACT complex to CC viral genomes in infected cells. {ECO:0000269|PubMed:28611249}. CC -!- INTERACTION: CC Q08945; P68400: CSNK2A1; NbExp=3; IntAct=EBI-353771, EBI-347804; CC Q08945; P49736: MCM2; NbExp=3; IntAct=EBI-353771, EBI-374819; CC Q08945; P33991: MCM4; NbExp=6; IntAct=EBI-353771, EBI-374938; CC Q08945; Q14566: MCM6; NbExp=3; IntAct=EBI-353771, EBI-374900; CC Q08945; P33993: MCM7; NbExp=2; IntAct=EBI-353771, EBI-355924; CC Q08945; Q9Y5B9: SUPT16H; NbExp=6; IntAct=EBI-353771, EBI-1046849; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10421373, CC ECO:0000269|PubMed:22002106}. Nucleus, nucleolus CC {ECO:0000269|PubMed:22002106}. Chromosome CC {ECO:0000269|PubMed:10421373}. Note=Colocalizes with RNA polymerase II CC on chromatin. Recruited to actively transcribed loci. CC {ECO:0000250|UniProtKB:Q05344}. CC -!- DOMAIN: The HMG box DNA-binding domain mediates DNA-binding. It has CC both affinity and specificity for DNA damaged globally with cisplatin. CC {ECO:0000269|PubMed:11344167}. CC -!- PTM: Phosphorylated by CK2 following UV but not gamma irradiation. CC Phosphorylation inhibits its DNA-binding activity. CC {ECO:0000269|PubMed:12393879, ECO:0000269|PubMed:15659405}. CC -!- PTM: Ubiquitinated. Polyubiquitinated following caspase cleavage CC resulting in degradation of the N-terminal ubiquitinated part of the CC cleaved protein. {ECO:0000269|PubMed:16498457}. CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}. CC -!- MISCELLANEOUS: Autoantibodies against SSRP1 are present in sera from CC patients with systemic lupus erythematosus, but not other rheumatic CC diseases. CC -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH91486.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M86737; AAA58660.1; -; mRNA. DR EMBL; BC005116; AAH05116.1; -; mRNA. DR EMBL; BC091486; AAH91486.1; ALT_SEQ; mRNA. DR CCDS; CCDS7952.1; -. DR PIR; A41976; A41976. DR RefSeq; NP_003137.1; NM_003146.2. DR PDB; 4IFS; X-ray; 1.93 A; A=196-430. DR PDB; 5UMR; X-ray; 1.50 A; A=1-100. DR PDB; 5UMS; X-ray; 1.57 A; A=174-437. DR PDB; 5VWE; NMR; -; A=551-617. DR PDB; 6L1E; X-ray; 2.09 A; A=196-430. DR PDB; 6L1R; X-ray; 1.80 A; A=1-100. DR PDB; 6L34; X-ray; 2.00 A; A=548-615. DR PDB; 6UPK; EM; 4.90 A; H=1-640. DR PDB; 6UPL; EM; 7.40 A; H=1-640. DR PDBsum; 4IFS; -. DR PDBsum; 5UMR; -. DR PDBsum; 5UMS; -. DR PDBsum; 5VWE; -. DR PDBsum; 6L1E; -. DR PDBsum; 6L1R; -. DR PDBsum; 6L34; -. DR PDBsum; 6UPK; -. DR PDBsum; 6UPL; -. DR AlphaFoldDB; Q08945; -. DR EMDB; EMD-20840; -. DR EMDB; EMD-20841; -. DR SMR; Q08945; -. DR BioGRID; 112627; 667. DR ComplexPortal; CPX-419; FACT complex. DR CORUM; Q08945; -. DR DIP; DIP-169N; -. DR IntAct; Q08945; 108. DR MINT; Q08945; -. DR STRING; 9606.ENSP00000278412; -. DR GlyGen; Q08945; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q08945; -. DR MetOSite; Q08945; -. DR PhosphoSitePlus; Q08945; -. DR SwissPalm; Q08945; -. DR BioMuta; SSRP1; -. DR EPD; Q08945; -. DR jPOST; Q08945; -. DR MassIVE; Q08945; -. DR MaxQB; Q08945; -. DR PaxDb; 9606-ENSP00000278412; -. DR PeptideAtlas; Q08945; -. DR ProteomicsDB; 58651; -. DR Pumba; Q08945; -. DR Antibodypedia; 1060; 389 antibodies from 34 providers. DR DNASU; 6749; -. DR Ensembl; ENST00000278412.7; ENSP00000278412.2; ENSG00000149136.9. DR GeneID; 6749; -. DR KEGG; hsa:6749; -. DR MANE-Select; ENST00000278412.7; ENSP00000278412.2; NM_003146.3; NP_003137.1. DR UCSC; uc001njt.3; human. DR AGR; HGNC:11327; -. DR CTD; 6749; -. DR DisGeNET; 6749; -. DR GeneCards; SSRP1; -. DR HGNC; HGNC:11327; SSRP1. DR HPA; ENSG00000149136; Low tissue specificity. DR MIM; 604328; gene. DR neXtProt; NX_Q08945; -. DR OpenTargets; ENSG00000149136; -. DR PharmGKB; PA36151; -. DR VEuPathDB; HostDB:ENSG00000149136; -. DR eggNOG; KOG0526; Eukaryota. DR GeneTree; ENSGT00940000157117; -. DR HOGENOM; CLU_017374_2_1_1; -. DR InParanoid; Q08945; -. DR OMA; KQPGKCK; -. DR OrthoDB; 5488575at2759; -. DR PhylomeDB; Q08945; -. DR TreeFam; TF315228; -. DR PathwayCommons; Q08945; -. DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat. DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat. DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation. DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery. DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript. DR Reactome; R-HSA-167287; HIV elongation arrest and recovery. DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation. DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes. DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation. DR SignaLink; Q08945; -. DR SIGNOR; Q08945; -. DR BioGRID-ORCS; 6749; 804 hits in 1200 CRISPR screens. DR ChiTaRS; SSRP1; human. DR GeneWiki; Structure_specific_recognition_protein_1; -. DR GenomeRNAi; 6749; -. DR Pharos; Q08945; Tbio. DR PRO; PR:Q08945; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q08945; Protein. DR Bgee; ENSG00000149136; Expressed in ventricular zone and 202 other cell types or tissues. DR ExpressionAtlas; Q08945; baseline and differential. DR GO; GO:0035101; C:FACT complex; IPI:ComplexPortal. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0042393; F:histone binding; IBA:GO_Central. DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0006334; P:nucleosome assembly; NAS:ComplexPortal. DR GO; GO:0006337; P:nucleosome disassembly; IDA:ComplexPortal. DR GO; GO:1902275; P:regulation of chromatin organization; IDA:CACAO. DR CDD; cd21994; HMG-box_SSRP1-like; 1. DR CDD; cd13230; PH1_SSRP1-like; 1. DR CDD; cd13231; PH2_SSRP1-like; 1. DR Gene3D; 2.30.29.150; -; 1. DR Gene3D; 1.10.30.10; High mobility group box domain; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2. DR Gene3D; 2.30.29.220; Structure-specific recognition protein (SSRP1); 1. DR InterPro; IPR009071; HMG_box_dom. DR InterPro; IPR036910; HMG_box_dom_sf. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR013719; RTT106/SPT16-like_middle_dom. DR InterPro; IPR048993; SSRP1-like_PH1. DR InterPro; IPR000969; SSRP1/POB3. DR InterPro; IPR035417; SSRP1/POB3_N. DR InterPro; IPR048985; SSRP1_C. DR InterPro; IPR024954; SSRP1_DD. DR InterPro; IPR038167; SSRP1_sf. DR PANTHER; PTHR45849; FACT COMPLEX SUBUNIT SSRP1; 1. DR PANTHER; PTHR45849:SF1; FACT COMPLEX SUBUNIT SSRP1; 1. DR Pfam; PF00505; HMG_box; 1. DR Pfam; PF21103; PH1_SSRP1-like; 1. DR Pfam; PF17292; POB3_N; 1. DR Pfam; PF08512; Rttp106-like_middle; 1. DR Pfam; PF03531; SSrecog; 1. DR Pfam; PF21092; SSRP1_C; 1. DR PRINTS; PR00887; SSRCOGNITION. DR SMART; SM00398; HMG; 1. DR SMART; SM01287; Rtt106; 1. DR SUPFAM; SSF47095; HMG-box; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. DR Genevisible; Q08945; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromosome; Direct protein sequencing; KW DNA damage; DNA repair; DNA replication; DNA-binding; KW Host-virus interaction; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..709 FT /note="FACT complex subunit SSRP1" FT /id="PRO_0000048606" FT DNA_BIND 547..615 FT /note="HMG box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT REGION 458..709 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 470..495 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 519..536 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 583..623 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 624..638 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 642..662 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 663..691 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 450..451 FT /note="Cleavage; by caspase-3 and/or caspase-7" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 170 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 233 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 413 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 437 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 441 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q08943" FT MOD_RES 444 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 452 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q08943" FT MOD_RES 471 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 510 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000305|PubMed:15659405" FT MOD_RES 542 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q08943" FT MOD_RES 657 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15659405, FT ECO:0007744|PubMed:21406692" FT MOD_RES 659 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 667 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 668 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 671 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 672 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 673 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 688 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000305|PubMed:15659405" FT CROSSLNK 90 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 296 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 364 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 225 FT /note="L -> V (in dbSNP:rs768436)" FT /id="VAR_052495" FT VARIANT 458 FT /note="E -> Q (in dbSNP:rs11540304)" FT /id="VAR_052496" FT MUTAGEN 450 FT /note="D->A: Abolishes cleavage by caspase." FT /evidence="ECO:0000269|PubMed:16498457" FT MUTAGEN 510 FT /note="S->A: Unable to bind DNA; when associated with A-657 FT and A-688." FT /evidence="ECO:0000269|PubMed:15659405" FT MUTAGEN 657 FT /note="S->A: Unable to bind DNA; when associated with A-510 FT and A-688. Still able to bind DNA; when associated with FT A-688." FT /evidence="ECO:0000269|PubMed:15659405" FT MUTAGEN 688 FT /note="S->A: Unable to bind DNA; when associated with A-510 FT and A-657. Still able to bind DNA; when associated with FT A-657." FT /evidence="ECO:0000269|PubMed:15659405" FT STRAND 3..14 FT /evidence="ECO:0007829|PDB:5UMR" FT STRAND 17..34 FT /evidence="ECO:0007829|PDB:5UMR" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:5UMR" FT STRAND 40..44 FT /evidence="ECO:0007829|PDB:5UMR" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:5UMR" FT STRAND 48..55 FT /evidence="ECO:0007829|PDB:5UMR" FT STRAND 57..66 FT /evidence="ECO:0007829|PDB:5UMR" FT STRAND 71..77 FT /evidence="ECO:0007829|PDB:5UMR" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:5UMR" FT HELIX 82..92 FT /evidence="ECO:0007829|PDB:5UMR" FT STRAND 198..209 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 212..218 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 220..229 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 231..235 FT /evidence="ECO:0007829|PDB:5UMS" FT HELIX 236..238 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 239..246 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 250..265 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 268..278 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 282..286 FT /evidence="ECO:0007829|PDB:5UMS" FT HELIX 291..298 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 304..309 FT /evidence="ECO:0007829|PDB:5UMS" FT HELIX 310..321 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 322..324 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 335..337 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 339..345 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 348..354 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 356..365 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 367..370 FT /evidence="ECO:0007829|PDB:5UMS" FT HELIX 371..373 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 374..381 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 383..385 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 388..395 FT /evidence="ECO:0007829|PDB:5UMS" FT STRAND 400..407 FT /evidence="ECO:0007829|PDB:5UMS" FT HELIX 408..410 FT /evidence="ECO:0007829|PDB:5UMS" FT HELIX 411..420 FT /evidence="ECO:0007829|PDB:5UMS" FT HELIX 549..568 FT /evidence="ECO:0007829|PDB:6L34" FT HELIX 574..587 FT /evidence="ECO:0007829|PDB:6L34" FT HELIX 590..614 FT /evidence="ECO:0007829|PDB:6L34" SQ SEQUENCE 709 AA; 81075 MW; 4E7EE3735EB41082 CRC64; MAETLEFNDV YQEVKGSMND GRLRLSRQGI IFKNSKTGKV DNIQAGELTE GIWRRVALGH GLKLLTKNGH VYKYDGFRES EFEKLSDFFK THYRLELMEK DLCVKGWNWG TVKFGGQLLS FDIGDQPVFE IPLSNVSQCT TGKNEVTLEF HQNDDAEVSL MEVRFYVPPT QEDGVDPVEA FAQNVLSKAD VIQATGDAIC IFRELQCLTP RGRYDIRIYP TFLHLHGKTF DYKIPYTTVL RLFLLPHKDQ RQMFFVISLD PPIKQGQTRY HFLILLFSKD EDISLTLNMN EEEVEKRFEG RLTKNMSGSL YEMVSRVMKA LVNRKITVPG NFQGHSGAQC ITCSYKASSG LLYPLERGFI YVHKPPVHIR FDEISFVNFA RGTTTTRSFD FEIETKQGTQ YTFSSIEREE YGKLFDFVNA KKLNIKNRGL KEGMNPSYDE YADSDEDQHD AYLERMKEEG KIREENANDS SDDSGEETDE SFNPGEEEED VAEEFDSNAS ASSSSNEGDS DRDEKKRKQL KKAKMAKDRK SRKKPVEVKK GKDPNAPKRP MSAYMLWLNA SREKIKSDHP GISITDLSKK AGEIWKGMSK EKKEEWDRKA EDARRDYEKA MKEYEGGRGE SSKRDKSKKK KKVKVKMEKK STPSRGSSSK SSSRQLSESF KSKEFVSSDE SSSGENKSKK KRRRSEDSEE EELASTPPSS EDSASGSDE //