SSRP1_HUMAN
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 03-AUG-2022, entry version 220.
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};
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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 SMR; Q08945; -.
DR BioGRID; 112627; 295.
DR ComplexPortal; CPX-419; FACT complex.
DR CORUM; Q08945; -.
DR DIP; DIP-169N; -.
DR IntAct; Q08945; 97.
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; Q08945; -.
DR PeptideAtlas; Q08945; -.
DR PRIDE; Q08945; -.
DR ProteomicsDB; 58651; -.
DR Antibodypedia; 1060; 360 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 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; SKQPGKC; -.
DR OrthoDB; 915055at2759; -.
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; 771 hits in 1116 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 200 other tissues.
DR ExpressionAtlas; Q08945; baseline and differential.
DR Genevisible; Q08945; HS.
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; IC:ComplexPortal.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:ComplexPortal.
DR GO; GO:1902275; P:regulation of chromatin organization; IDA:CACAO.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 2.30.29.220; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR013719; DUF1747.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR035417; POB3_N.
DR InterPro; IPR000969; SSrcognition.
DR InterPro; IPR024954; SSRP1_dom.
DR InterPro; IPR038167; SSRP1_sf.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF17292; POB3_N; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF03531; SSrecog; 1.
DR PRINTS; PR00887; SSRCOGNITION.
DR SMART; SM00398; HMG; 1.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
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 A-
FT 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 A-
FT 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
