ID SP100_HUMAN Reviewed; 879 AA. AC P23497; B4DDX5; B8ZZD8; E7EUA7; E9PH61; F8WFE2; O75450; Q13343; Q8TE34; AC Q96F70; Q96T24; Q96T95; Q9NP33; Q9UE32; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 3. DT 27-MAR-2024, entry version 245. DE RecName: Full=Nuclear autoantigen Sp-100; DE AltName: Full=Nuclear dot-associated Sp100 protein; DE AltName: Full=Speckled 100 kDa; GN Name=SP100; 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] (ISOFORM SP100-A). RC TISSUE=Liver, and Placenta; RX PubMed=2258622; RA Szostecki C., Guldner H.H., Netter H.J., Will H.; RT "Isolation and characterization of cDNA encoding a human nuclear antigen RT predominantly recognized by autoantibodies from patients with primary RT biliary cirrhosis."; RL J. Immunol. 145:4338-4347(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP100-B). RX PubMed=8695863; RA Dent A.L., Yewdell J., Puvion-Dutilleul F., Koken M.H.M., de The H., RA Staudt L.M.; RT "LYSP100-associated nuclear domains (LANDs): description of a new class of RT subnuclear structures and their relationship to PML nuclear bodies."; RL Blood 88:1423-1426(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP100-HMG). RC TISSUE=Mammary cancer; RX PubMed=9636146; DOI=10.1073/pnas.95.13.7316; RA Seeler J.-S., Marchio A., Sitterlin D., Transy C., Dejean A.; RT "Interaction of SP100 with HP1 proteins: a link between the promyelocytic RT leukemia-associated nuclear bodies and the chromatin compartment."; RL Proc. Natl. Acad. Sci. U.S.A. 95:7316-7321(1998). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP100-C), SUBCELLULAR LOCATION RP (ISOFORMS SP100-A; SP100-C AND SP100-HMG), SUMOYLATION WITH SUMO1, AND RP INTERACTION WITH CBX5. RX PubMed=11313457; DOI=10.1128/mcb.21.10.3314-3324.2001; RA Seeler J.-S., Marchio A., Losson R., Desterro J.M.P., Hay R.T., Chambon P., RA Dejean A.; RT "Common properties of nuclear protein SP100 and TIF1alpha chromatin factor: RT role of SUMO modification."; RL Mol. Cell. Biol. 21:3314-3324(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7). RC TISSUE=Kidney, and Urinary bladder; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SP100-A). RC TISSUE=Kidney; 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 [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10. RC TISSUE=Lymphoma; RX PubMed=8810287; DOI=10.1074/jbc.271.41.25253; RA Groetzinger T., Jensen K., Will H.; RT "The interferon (IFN)-stimulated gene Sp100 promoter contains an IFN-gamma RT activation site and an imperfect IFN-stimulated response element which RT mediate type I IFN inducibility."; RL J. Biol. Chem. 271:25253-25260(1996). RN [9] RP INHIBITION OF SUMOYLATION BY HHV-5 (MICROBIAL INFECTION). RX PubMed=10233977; DOI=10.1128/jvi.73.6.5137-5143.1999; RA Mueller S., Dejean A.; RT "Viral immediate-early proteins abrogate the modification by SUMO-1 of PML RT and Sp100 proteins, correlating with nuclear body disruption."; RL J. Virol. 73:5137-5143(1999). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 477-879 (ISOFORMS SP100-B AND RP SP100-HMG), AND PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM RP SPALT-C). RC TISSUE=Cervix carcinoma; RX PubMed=9973607; DOI=10.1242/jcs.112.5.733; RA Guldner H.H., Szostecki C., Schroeder P., Matschl U., Jensen K., RA Lueders C., Will H., Sternsdorf T.; RT "Splice variants of the nuclear dot-associated Sp100 protein contain RT homologies to HMG-1 and a human nuclear phosphoprotein-box motif."; RL J. Cell Sci. 112:733-747(1999). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 699-879 (ISOFORM SP100-HMG). RC TISSUE=Cervix carcinoma; RX PubMed=10766566; DOI=10.1006/geno.1999.6008; RA Rogalla P., Kazmierczak B., Flohr A.M., Hauke S., Bullerdiek J.; RT "Back to the roots of a new exon-the molecular archaeology of a SP100 RT splice variant."; RL Genomics 63:117-122(2000). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 699-879 (ISOFORM SP100-HMG). RX PubMed=11574059; DOI=10.1186/gb-2001-2-9-research0040; RA Devor E.J.; RT "Molecular archeology of an SP100 splice variant revisited: dating the RT retrotranscription and Alu insertion events."; RL Genome Biol. 2:RESEARCH0040.1-RESEARCH0040.6(2001). RN [13] RP SUMOYLATION WITH SUMO1, AND SUBCELLULAR LOCATION. RX PubMed=9412458; DOI=10.1083/jcb.139.7.1621; RA Sternsdorf T., Jensen K., Will H.; RT "Evidence for covalent modification of the nuclear dot-associated proteins RT PML and Sp100 by PIC1/SUMO-1."; RL J. Cell Biol. 139:1621-1634(1997). RN [14] RP SUMOYLATION AT LYS-297, AND HOMODIMERIZATION. RX PubMed=10212234; DOI=10.1074/jbc.274.18.12555; RA Sternsdorf T., Jensen K., Reich B., Will H.; RT "The nuclear dot protein sp100, characterization of domains necessary for RT dimerization, subcellular localization, and modification by small RT ubiquitin-like modifiers."; RL J. Biol. Chem. 274:12555-12566(1999). RN [15] RP INTERACTION WITH NBN. RX PubMed=12470659; DOI=10.1016/s0006-291x(02)02755-9; RA Naka K., Ikeda K., Motoyama N.; RT "Recruitment of NBS1 into PML oncogenic domains via interaction with SP100 RT protein."; RL Biochem. Biophys. Res. Commun. 299:863-871(2002). RN [16] RP FUNCTION AS A TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH ETS1, AND RP SUBCELLULAR LOCATION. RX PubMed=11909962; DOI=10.1128/mcb.22.8.2687-2702.2002; RA Wasylyk C., Schlumberger S.E., Criqui-Filipe P., Wasylyk B.; RT "Sp100 interacts with ETS-1 and stimulates its transcriptional activity."; RL Mol. Cell. Biol. 22:2687-2702(2002). RN [17] RP FUNCTION IN TP53-DEPENDENT TRANSCRIPTION, AND INTERACTION WITH HIPK2. RX PubMed=14647468; DOI=10.1038/sj.onc.1207079; RA Moeller A., Sirma H., Hofmann T.G., Staege H., Gresko E., Luedi K.S., RA Klimczak E., Droege W., Will H., Schmitz M.L.; RT "Sp100 is important for the stimulatory effect of homeodomain-interacting RT protein kinase-2 on p53-dependent gene expression."; RL Oncogene 22:8731-8737(2003). RN [18] RP FUNCTION AS A TRANSCRIPTIONAL COREPRESSOR, INTERACTION WITH ETS1, AND RP INDUCTION BY INTERFERON ALPHA. RX PubMed=15247905; DOI=10.1038/sj.onc.1207891; RA Yordy J.S., Li R., Sementchenko V.I., Pei H., Muise-Helmericks R.C., RA Watson D.K.; RT "SP100 expression modulates ETS1 transcriptional activity and inhibits cell RT invasion."; RL Oncogene 23:6654-6665(2004). RN [19] RP INTERACTION WITH CBX5. RX PubMed=15882967; DOI=10.1016/j.bbrc.2005.04.016; RA Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III; RT "The mammalian heterochromatin protein 1 binds diverse nuclear proteins RT through a common motif that targets the chromoshadow domain."; RL Biochem. Biophys. Res. Commun. 331:929-937(2005). RN [20] RP FUNCTION, AND INTERACTION WITH EBV EBNA-LP (MICROBIAL INFECTION). RX PubMed=16177824; DOI=10.1038/sj.emboj.7600820; RA Ling P.D., Peng R.S., Nakajima A., Yu J.H., Tan J., Moses S.M., Yang W.H., RA Zhao B., Kieff E., Bloch K.D., Bloch D.B.; RT "Mediation of Epstein-Barr virus EBNA-LP transcriptional coactivation by RT Sp100."; RL EMBO J. 24:3565-3575(2005). RN [21] RP FUNCTION IN TELOMERE SHORTENING, AND INTERACTION WITH MRN COMPLEX. RX PubMed=15767676; DOI=10.1128/mcb.25.7.2708-2721.2005; RA Jiang W.Q., Zhong Z.H., Henson J.D., Neumann A.A., Chang A.C., Reddel R.R.; RT "Suppression of alternative lengthening of telomeres by Sp100-mediated RT sequestration of the MRE11/RAD50/NBS1 complex."; RL Mol. Cell. Biol. 25:2708-2721(2005). RN [22] RP FUNCTION IN ENDOTHELIAL CELL MIGRATION, AND INDUCTION. RX PubMed=15592518; DOI=10.1038/sj.onc.1208245; RA Yordy J.S., Moussa O., Pei H., Chaussabel D., Li R., Watson D.K.; RT "SP100 inhibits ETS1 activity in primary endothelial cells."; RL Oncogene 24:916-931(2005). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-331, AND 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 [24] RP FUNCTION IN FAS-MEDIATED APOPTOSIS, INTERACTION WITH CASP8AP2, AND RP SUBCELLULAR LOCATION. RX PubMed=17245429; DOI=10.1038/sj.emboj.7601504; RA Milovic-Holm K., Krieghoff E., Jensen K., Will H., Hofmann T.G.; RT "FLASH links the CD95 signaling pathway to the cell nucleus and nuclear RT bodies."; RL EMBO J. 26:391-401(2007). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407; SER-409 AND SER-410, AND RP IDENTIFICATION BY MASS 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 [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-407; SER-409 AND RP SER-410, AND IDENTIFICATION BY 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 [27] RP RETRACTED PAPER. RX PubMed=21118961; DOI=10.1158/0008-5472.can-10-1483; RA Negorev D.G., Vladimirova O.V., Kossenkov A.V., Nikonova E.V., RA Demarest R.M., Capobianco A.J., Showe M.K., Rauscher F.J. III, Showe L.C., RA Maul G.G.; RT "Sp100 as a potent tumor suppressor: accelerated senescence and rapid RT malignant transformation of human fibroblasts through modulation of an RT embryonic stem cell program."; RL Cancer Res. 70:9991-10001(2010). RN [28] RP RETRACTION NOTICE OF PUBMED:21118961. RX PubMed=23907639; DOI=10.1158/0008-5472.can-13-1715; RA Negorev D.G., Vladimirova O.V., Kossenkov A.V., Demarest R.M., Showe M.K., RA Rauscher F.J. III, Showe L.C., Nikonova E.V., Capobianco A.J.; RL Cancer Res. 73:4960-4961(2013). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-362; SER-407; RP SER-409 AND SER-410, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 DOMAIN D-BOX MOTIF, AND MUTAGENESIS OF ARG-165 AND LEU-168. RX PubMed=22086178; DOI=10.1016/j.bbrc.2011.10.146; RA Wang R., Li K.M., Zhou C.H., Xue J.L., Ji C.N., Chen J.Z.; RT "Cdc20 mediates D-box-dependent degradation of Sp100."; RL Biochem. Biophys. Res. Commun. 415:702-706(2011). RN [31] RP FUNCTION IN CELL PROLIFERATION. RX PubMed=21274506; DOI=10.3892/ijo.2011.927; RA Held-Feindt J., Hattermann K., Knerlich-Lukoschus F., Mehdorn H.M., RA Mentlein R.; RT "SP100 reduces malignancy of human glioma cells."; RL Int. J. Oncol. 38:1023-1030(2011). RN [32] RP FUNCTION, INTERACTION WITH HHV-5 PROTEIN UL123 (MICROBIAL INFECTION), AND RP INDUCTION BY INTERFERON. RX PubMed=21880768; DOI=10.1128/jvi.00758-11; RA Kim Y.E., Lee J.H., Kim E.T., Shin H.J., Gu S.Y., Seol H.S., Ling P.D., RA Lee C.H., Ahn J.H.; RT "Human cytomegalovirus infection causes degradation of Sp100 proteins that RT suppress viral gene expression."; RL J. Virol. 85:11928-11937(2011). 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=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 [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-171; SER-180; RP SER-362; SER-394 AND SER-451, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [35] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-157; SER-228; RP SER-362; SER-407; SER-409 AND SER-410, AND IDENTIFICATION BY MASS RP 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 [36] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-306 AND LYS-387, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [37] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-306, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [38] RP SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [39] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-306, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [40] RP INTERACTION WITH SUMO1P1/SUMO5, AND SUBCELLULAR LOCATION. RX PubMed=27211601; DOI=10.1038/srep26509; RA Liang Y.C., Lee C.C., Yao Y.L., Lai C.C., Schmitz M.L., Yang W.M.; RT "SUMO5, a novel poly-sumo isoform, regulates pml nuclear bodies."; RL Sci. Rep. 6:26509-26509(2016). RN [41] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-241; LYS-300; LYS-306; LYS-366 RP AND LYS-594, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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: Together with PML, this tumor suppressor is a major CC constituent of the PML bodies, a subnuclear organelle involved in a CC large number of physiological processes including cell growth, CC differentiation and apoptosis. Functions as a transcriptional CC coactivator of ETS1 and ETS2 according to PubMed:11909962. Under CC certain conditions, it may also act as a corepressor of ETS1 preventing CC its binding to DNA according to PubMed:15247905. Through the regulation CC of ETS1 it may play a role in angiogenesis, controlling endothelial CC cell motility and invasion. Through interaction with the MRN complex it CC may be involved in the regulation of telomeres lengthening. May also CC regulate TP53-mediated transcription and through CASP8AP2, regulate CC FAS-mediated apoptosis. Also plays a role in infection by viruses, CC including human cytomegalovirus and Epstein-Barr virus, through CC mechanisms that may involve chromatin and/or transcriptional CC regulation. {ECO:0000269|PubMed:11909962, ECO:0000269|PubMed:14647468, CC ECO:0000269|PubMed:15247905, ECO:0000269|PubMed:15592518, CC ECO:0000269|PubMed:15767676, ECO:0000269|PubMed:16177824, CC ECO:0000269|PubMed:17245429, ECO:0000269|PubMed:21274506, CC ECO:0000269|PubMed:21880768}. CC -!- SUBUNIT: Homodimer; isoforms are able to heterodimerize. Interacts with CC members of the HP1 family of nonhistone chromosomal protein, such as CC CBX5 and CBX3 via the PxVxL motif. Interacts with ETS1; the interaction CC is direct and modulates ETS1 transcriptional activity. Interacts with CC the MRN complex which is composed of two heterodimers RAD50/MRE11 CC associated with a single NBN; recruits the complex to PML-related CC bodies. Interacts with HIPK2; positively regulates TP53-dependent CC transcription. Interacts with CASP8AP2; may negatively regulate CC CASP8AP2 export from the nucleus to the cytoplasm. Interacts with CC SUMO1P1/SUMO5 (PubMed:27211601). {ECO:0000269|PubMed:11313457, CC ECO:0000269|PubMed:11909962, ECO:0000269|PubMed:12470659, CC ECO:0000269|PubMed:14647468, ECO:0000269|PubMed:15247905, CC ECO:0000269|PubMed:15767676, ECO:0000269|PubMed:15882967, CC ECO:0000269|PubMed:17245429, ECO:0000269|PubMed:27211601}. CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus EBNA- CC LP; this interaction is important for EBNA-LP coactivator activity. CC {ECO:0000269|PubMed:16177824}. CC -!- SUBUNIT: (Microbial infection) Interacts with human CC cytomegalovirus/HHV-5 protein UL123; may play a role in infection by CC the virus. {ECO:0000269|PubMed:21880768}. CC -!- INTERACTION: CC P23497; P35609: ACTN2; NbExp=6; IntAct=EBI-751145, EBI-77797; CC P23497; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-751145, EBI-10187270; CC P23497; Q9UKL3: CASP8AP2; NbExp=5; IntAct=EBI-751145, EBI-2339650; CC P23497; Q9Y6K1: DNMT3A; NbExp=3; IntAct=EBI-751145, EBI-923653; CC P23497; Q92630: DYRK2; NbExp=3; IntAct=EBI-751145, EBI-749432; CC P23497; P14921: ETS1; NbExp=4; IntAct=EBI-751145, EBI-913209; CC P23497; Q8TF65: GIPC2; NbExp=4; IntAct=EBI-751145, EBI-712067; CC P23497; V9HWG0: HEL25; NbExp=3; IntAct=EBI-751145, EBI-10183977; CC P23497; Q96JM7: L3MBTL3; NbExp=3; IntAct=EBI-751145, EBI-2686809; CC P23497; Q14498-3: RBM39; NbExp=3; IntAct=EBI-751145, EBI-6654703; CC P23497; Q14D33: RTP5; NbExp=3; IntAct=EBI-751145, EBI-10217913; CC P23497; P63165: SUMO1; NbExp=6; IntAct=EBI-751145, EBI-80140; CC P23497; P55854: SUMO3; NbExp=2; IntAct=EBI-751145, EBI-474067; CC P23497; Q9Y228: TRAF3IP3; NbExp=4; IntAct=EBI-751145, EBI-765817; CC P23497; Q96GY0: ZC2HC1A; NbExp=3; IntAct=EBI-751145, EBI-5458880; CC P23497; Q59GP6; NbExp=3; IntAct=EBI-751145, EBI-10243413; CC P23497; PRO_0000449627 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-751145, EBI-25475877; CC P23497; P03169: UL123; Xeno; NbExp=4; IntAct=EBI-751145, EBI-6691147; CC P23497-2; P35609: ACTN2; NbExp=3; IntAct=EBI-6589365, EBI-77797; CC P23497-2; P83916: CBX1; NbExp=3; IntAct=EBI-6589365, EBI-78129; CC P23497-2; Q13185: CBX3; NbExp=3; IntAct=EBI-6589365, EBI-78176; CC P23497-2; P45973: CBX5; NbExp=7; IntAct=EBI-6589365, EBI-78219; CC P23497-2; Q8TF65: GIPC2; NbExp=3; IntAct=EBI-6589365, EBI-712067; CC P23497-2; Q9BUI4: POLR3C; NbExp=3; IntAct=EBI-6589365, EBI-5452779; CC P23497-2; Q14D33: RTP5; NbExp=3; IntAct=EBI-6589365, EBI-10217913; CC P23497-2; P37840: SNCA; NbExp=3; IntAct=EBI-6589365, EBI-985879; CC P23497-2; P23497-2: SP100; NbExp=5; IntAct=EBI-6589365, EBI-6589365; CC P23497-2; P63165: SUMO1; NbExp=3; IntAct=EBI-6589365, EBI-80140; CC P23497-2; P61956: SUMO2; NbExp=3; IntAct=EBI-6589365, EBI-473220; CC P23497-2; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-6589365, EBI-765817; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25593309}. Nucleus, CC PML body {ECO:0000269|PubMed:27211601}. Nucleus, nuclear body CC {ECO:0000269|PubMed:17245429}. Cytoplasm {ECO:0000269|PubMed:17245429}. CC Note=Differences in the subnuclear localization of the different CC isoforms seem to exist and may also be cell cycle- and interferon- CC dependent. Accumulates in the cytoplasm upon FAS activation. CC {ECO:0000269|PubMed:17245429}. CC -!- SUBCELLULAR LOCATION: [Isoform Sp100-C]: Nucleus CC {ECO:0000269|PubMed:11313457}. Note=Forms a reticulate or track-like CC nuclear pattern with denser concentrations at the nuclear lamina and CC surrounding the nucleoli, a pattern reminiscent of heterochromatin-rich CC regions according to PubMed:11313457. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=Sp100-HMG; Synonyms=SP100HMG, SpAlt-HMG; CC IsoId=P23497-1; Sequence=Displayed; CC Name=Sp100-A; Synonyms=SP100A, SP100; CC IsoId=P23497-2; Sequence=VSP_005978, VSP_005979; CC Name=Sp100-B; Synonyms=SP100B, SpAlt-212; CC IsoId=P23497-3; Sequence=VSP_005980, VSP_005981; CC Name=Sp100-C; Synonyms=SP100C; CC IsoId=P23497-4; Sequence=VSP_005984; CC Name=SpAlt-C; CC IsoId=P23497-5; Sequence=VSP_005982, VSP_005983; CC Name=6; CC IsoId=P23497-6; Sequence=VSP_045869, VSP_045870, VSP_005978, CC VSP_005979; CC Name=7; CC IsoId=P23497-7; Sequence=VSP_045868, VSP_005978, VSP_005979; CC -!- TISSUE SPECIFICITY: Widely expressed. Sp100-B is expressed only in CC spleen, tonsil, thymus, mature B-cell line and some T-cell line, but CC not in brain, liver, muscle or non-lymphoid cell lines. CC -!- INDUCTION: Up-regulated by interferon, retinoic acid, TNF-alpha/TNFA CC and lipopolysaccharide (at protein level). Up-regulated following heat- CC shock. {ECO:0000269|PubMed:15247905, ECO:0000269|PubMed:15592518, CC ECO:0000269|PubMed:21880768}. CC -!- DOMAIN: The HSR domain is important for the nuclear body targeting as CC well as for the dimerization. {ECO:0000269|PubMed:22086178}. CC -!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is CC required for interaction with chromoshadow domains. This motif requires CC additional residues -7, -6, +4 and +5 of the central Val which contact CC the chromoshadow domain. {ECO:0000269|PubMed:22086178}. CC -!- PTM: Sumoylated. Sumoylation depends on a functional nuclear CC localization signal but is not necessary for nuclear import or nuclear CC body targeting. CC -!- PTM: Sumoylated. Sumoylated with SUMO1. Sumoylation depends on a CC functional nuclear localization signal but is not necessary for nuclear CC import or nuclear body targeting. Sumoylation may stabilize the CC interaction with CBX5. CC -!- PTM: (Microbial infection) Immediate early protein IE1 of human CC cytomegalovirus (HHV-5) interferes with the sumoylation of SP100. CC {ECO:0000269|PubMed:10233977}. CC -!- MISCELLANEOUS: The major isoform Sp100-A, has a calculated molecular CC weight of 54 kDa, but exhibits aberrant electrophoretic mobilities, CC with an apparent molecular weight of 100 kDa. CC -!- MISCELLANEOUS: [Isoform Sp100-A]: Major isoform. {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; M60618; AAA35537.1; -; mRNA. DR EMBL; U36501; AAC50743.1; -; mRNA. DR EMBL; AF056322; AAC39790.1; -; mRNA. DR EMBL; AF255565; AAK51202.1; -; mRNA. DR EMBL; AK293373; BAG56886.1; -; mRNA. DR EMBL; AC009949; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC010149; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC011562; AAH11562.1; -; mRNA. DR EMBL; X95472; CAA64744.1; -; Genomic_DNA. DR EMBL; L79986; AAL77441.1; -; mRNA. DR EMBL; L79987; AAL77439.1; -; mRNA. DR EMBL; L79988; AAL77438.1; -; mRNA. DR EMBL; AF076675; AAF39781.1; -; Genomic_DNA. DR EMBL; AF378670; AAK57703.1; -; Genomic_DNA. DR CCDS; CCDS2477.1; -. [P23497-1] DR CCDS; CCDS42832.1; -. [P23497-4] DR CCDS; CCDS56170.1; -. [P23497-3] DR CCDS; CCDS56171.1; -. [P23497-2] DR CCDS; CCDS56172.1; -. [P23497-6] DR CCDS; CCDS56173.1; -. [P23497-7] DR PIR; A37244; A37244. DR RefSeq; NP_001073860.1; NM_001080391.1. [P23497-4] DR RefSeq; NP_001193630.1; NM_001206701.1. [P23497-3] DR RefSeq; NP_001193631.1; NM_001206702.1. [P23497-2] DR RefSeq; NP_001193632.1; NM_001206703.1. [P23497-6] DR RefSeq; NP_001193633.1; NM_001206704.1. [P23497-7] DR RefSeq; NP_003104.2; NM_003113.3. [P23497-1] DR PDB; 1H5P; NMR; -; A=595-688. DR PDB; 4PTB; X-ray; 1.60 A; A/B=466-508. DR PDB; 5FB0; X-ray; 2.70 A; A/C=696-878. DR PDB; 5FB1; X-ray; 2.10 A; A=696-875. DR PDB; 5PWE; X-ray; 1.69 A; A/B=466-508. DR PDB; 5PWF; X-ray; 1.48 A; A/B=466-508. DR PDB; 5PWG; X-ray; 1.46 A; A/B=466-508. DR PDB; 5PWH; X-ray; 1.50 A; A/B=466-508. DR PDB; 5PWI; X-ray; 1.62 A; A/B=466-508. DR PDB; 5PWJ; X-ray; 1.89 A; A/B=466-508. DR PDB; 5PWK; X-ray; 1.62 A; A/B=466-508. DR PDB; 5PWL; X-ray; 1.83 A; A/B=466-508. DR PDB; 5PWM; X-ray; 1.54 A; A/B=466-508. DR PDB; 5PWN; X-ray; 1.64 A; A/B=466-508. DR PDB; 5PWO; X-ray; 1.85 A; A/B=466-508. DR PDB; 5PWP; X-ray; 1.51 A; A/B=466-508. DR PDB; 5PWQ; X-ray; 1.52 A; A/B=466-508. DR PDB; 5PWR; X-ray; 1.46 A; A/B=466-508. DR PDB; 5PWS; X-ray; 1.40 A; A/B=466-508. DR PDB; 5PWT; X-ray; 1.58 A; A/B=466-508. DR PDB; 5PWU; X-ray; 1.44 A; A/B=466-508. DR PDB; 5PWV; X-ray; 1.58 A; A/B=466-508. DR PDB; 5PWW; X-ray; 1.59 A; A/B=466-508. DR PDB; 5PWX; X-ray; 1.69 A; A/B=466-508. DR PDB; 5PWY; X-ray; 1.98 A; A/B=466-508. DR PDB; 5PWZ; X-ray; 1.62 A; A/B=466-508. DR PDB; 5PX0; X-ray; 1.55 A; A/B=466-508. DR PDB; 5PX1; X-ray; 1.55 A; A/B=466-508. DR PDB; 5PX2; X-ray; 1.43 A; A/B=466-508. DR PDB; 5PX3; X-ray; 1.57 A; A/B=466-508. DR PDB; 5PX4; X-ray; 1.45 A; A/B=466-508. DR PDB; 5PX5; X-ray; 1.74 A; A/B=466-508. DR PDB; 5PX6; X-ray; 1.43 A; A/B=466-508. DR PDB; 5PX7; X-ray; 1.74 A; A/B=466-508. DR PDB; 5PX8; X-ray; 1.71 A; A/B=466-508. DR PDB; 5PX9; X-ray; 1.89 A; A/B=466-508. DR PDB; 5PXA; X-ray; 1.43 A; A/B=466-508. DR PDB; 5PXB; X-ray; 1.46 A; A/B=466-508. DR PDB; 5PXC; X-ray; 1.52 A; A/B=466-508. DR PDB; 5PXD; X-ray; 1.64 A; A/B=466-508. DR PDB; 5PXE; X-ray; 1.55 A; A/B=466-508. DR PDB; 5PXF; X-ray; 1.71 A; A/B=466-508. DR PDB; 5PXG; X-ray; 1.98 A; A/B=466-508. DR PDB; 5PXH; X-ray; 2.25 A; A/B=466-508. DR PDB; 5PXI; X-ray; 1.76 A; A/B=466-508. DR PDB; 5PXJ; X-ray; 1.68 A; A/B=466-508. DR PDB; 5PXK; X-ray; 1.98 A; A/B=466-508. DR PDB; 5PXL; X-ray; 1.35 A; A/B=466-508. DR PDB; 5PXM; X-ray; 1.59 A; A/B=466-508. DR PDB; 5PXN; X-ray; 1.43 A; A/B=466-508. DR PDB; 5PXO; X-ray; 1.78 A; A/B=466-508. DR PDB; 5PXP; X-ray; 1.86 A; A/B=466-508. DR PDB; 5PXQ; X-ray; 1.62 A; A/B=466-508. DR PDB; 5PXR; X-ray; 1.81 A; A/B=466-508. DR PDB; 5PXS; X-ray; 1.49 A; A/B=466-508. DR PDB; 5PXT; X-ray; 1.40 A; A/B=466-508. DR PDB; 5PXU; X-ray; 1.76 A; A/B=466-508. DR PDB; 5PXV; X-ray; 1.65 A; A/B=466-508. DR PDB; 5PXW; X-ray; 2.01 A; A/B=466-508. DR PDB; 5PXX; X-ray; 1.57 A; A/B=466-508. DR PDB; 5PXY; X-ray; 2.14 A; A/B=466-508. DR PDB; 5PXZ; X-ray; 1.65 A; A/B=466-508. DR PDB; 5PY0; X-ray; 1.70 A; A/B=466-508. DR PDB; 5PY1; X-ray; 1.74 A; A/B=466-508. DR PDB; 5PY2; X-ray; 1.62 A; A/B=466-508. DR PDB; 5PY3; X-ray; 1.78 A; A/B=466-508. DR PDB; 5PY4; X-ray; 1.67 A; A/B=466-508. DR PDB; 5PY5; X-ray; 1.44 A; A/B=466-508. DR PDB; 5PY6; X-ray; 1.74 A; A/B=466-508. DR PDB; 5PY7; X-ray; 1.68 A; A/B=466-508. DR PDB; 5PY8; X-ray; 1.66 A; A/B=466-508. DR PDB; 5PY9; X-ray; 1.73 A; A/B=466-508. DR PDB; 5PYA; X-ray; 1.55 A; A/B=466-508. DR PDB; 5PYB; X-ray; 1.74 A; A/B=466-508. DR PDB; 5PYC; X-ray; 1.87 A; A/B=466-508. DR PDB; 5PYD; X-ray; 2.02 A; A/B=466-508. DR PDB; 5PYE; X-ray; 1.81 A; A/B=466-508. DR PDB; 5PYF; X-ray; 1.83 A; A/B=466-508. DR PDB; 5PYG; X-ray; 1.95 A; A/B=466-508. DR PDB; 5PYH; X-ray; 1.74 A; A/B=466-508. DR PDB; 5PYI; X-ray; 2.29 A; A/B=466-508. DR PDB; 5PYJ; X-ray; 1.97 A; A/B=466-508. DR PDB; 5PYK; X-ray; 1.88 A; A/B=466-508. DR PDB; 5PYL; X-ray; 1.53 A; A/B=466-508. DR PDB; 5PYM; X-ray; 1.70 A; A/B=466-508. DR PDB; 5PYN; X-ray; 1.89 A; A/B=466-508. DR PDB; 5PYO; X-ray; 1.67 A; A/B=466-508. DR PDB; 5PYP; X-ray; 1.63 A; A/B=466-508. DR PDB; 5PYQ; X-ray; 1.97 A; A/B=466-508. DR PDB; 5PYR; X-ray; 1.94 A; A/B=466-508. DR PDB; 5PYS; X-ray; 2.09 A; A/B=466-508. DR PDB; 5PYT; X-ray; 2.13 A; A/B=466-508. DR PDB; 5PYU; X-ray; 1.74 A; A/B=466-508. DR PDB; 5PYV; X-ray; 1.94 A; A/B=466-508. DR PDB; 5PYW; X-ray; 1.45 A; A/B=466-508. DR PDB; 5PYX; X-ray; 1.57 A; A/B=466-508. DR PDB; 5PYY; X-ray; 1.64 A; A/B=466-508. DR PDB; 5PYZ; X-ray; 1.59 A; A/B=466-508. DR PDB; 5PZ0; X-ray; 2.13 A; A/B=466-508. DR PDB; 5PZ1; X-ray; 2.13 A; A/B=466-508. DR PDB; 5PZ2; X-ray; 1.88 A; A/B=466-508. DR PDB; 5PZ3; X-ray; 1.93 A; A/B=466-508. DR PDB; 5PZ4; X-ray; 1.94 A; A/B=466-508. DR PDB; 5PZ5; X-ray; 2.64 A; A/B=466-508. DR PDB; 5PZ6; X-ray; 1.87 A; A/B=466-508. DR PDB; 5PZ7; X-ray; 1.54 A; A/B=466-508. DR PDB; 5PZ8; X-ray; 1.52 A; A/B=466-508. DR PDB; 5PZ9; X-ray; 2.01 A; A/B=466-508. DR PDB; 5PZA; X-ray; 1.59 A; A/B=466-508. DR PDB; 5PZB; X-ray; 2.05 A; A/B=466-508. DR PDB; 5PZC; X-ray; 1.61 A; A/B=466-508. DR PDB; 5PZD; X-ray; 1.74 A; A/B=466-508. DR PDB; 5PZE; X-ray; 1.82 A; A/B=466-508. DR PDB; 5PZF; X-ray; 1.84 A; A/B=466-508. DR PDB; 5PZG; X-ray; 1.88 A; A/B=466-508. DR PDB; 5PZH; X-ray; 1.63 A; A/B=466-508. DR PDB; 5PZI; X-ray; 1.62 A; A/B=466-508. DR PDB; 5PZJ; X-ray; 1.72 A; A/B=466-508. DR PDB; 6G5N; X-ray; 1.76 A; A/B=466-508. DR PDB; 6G5P; X-ray; 1.35 A; A/B=466-508. DR PDBsum; 1H5P; -. DR PDBsum; 4PTB; -. DR PDBsum; 5FB0; -. DR PDBsum; 5FB1; -. DR PDBsum; 5PWE; -. DR PDBsum; 5PWF; -. DR PDBsum; 5PWG; -. DR PDBsum; 5PWH; -. DR PDBsum; 5PWI; -. DR PDBsum; 5PWJ; -. DR PDBsum; 5PWK; -. DR PDBsum; 5PWL; -. DR PDBsum; 5PWM; -. DR PDBsum; 5PWN; -. DR PDBsum; 5PWO; -. DR PDBsum; 5PWP; -. DR PDBsum; 5PWQ; -. DR PDBsum; 5PWR; -. DR PDBsum; 5PWS; -. DR PDBsum; 5PWT; -. DR PDBsum; 5PWU; -. DR PDBsum; 5PWV; -. DR PDBsum; 5PWW; -. DR PDBsum; 5PWX; -. DR PDBsum; 5PWY; -. DR PDBsum; 5PWZ; -. DR PDBsum; 5PX0; -. DR PDBsum; 5PX1; -. DR PDBsum; 5PX2; -. DR PDBsum; 5PX3; -. DR PDBsum; 5PX4; -. DR PDBsum; 5PX5; -. DR PDBsum; 5PX6; -. DR PDBsum; 5PX7; -. DR PDBsum; 5PX8; -. DR PDBsum; 5PX9; -. DR PDBsum; 5PXA; -. DR PDBsum; 5PXB; -. DR PDBsum; 5PXC; -. DR PDBsum; 5PXD; -. DR PDBsum; 5PXE; -. DR PDBsum; 5PXF; -. DR PDBsum; 5PXG; -. DR PDBsum; 5PXH; -. DR PDBsum; 5PXI; -. DR PDBsum; 5PXJ; -. DR PDBsum; 5PXK; -. DR PDBsum; 5PXL; -. DR PDBsum; 5PXM; -. DR PDBsum; 5PXN; -. DR PDBsum; 5PXO; -. DR PDBsum; 5PXP; -. DR PDBsum; 5PXQ; -. DR PDBsum; 5PXR; -. DR PDBsum; 5PXS; -. DR PDBsum; 5PXT; -. DR PDBsum; 5PXU; -. DR PDBsum; 5PXV; -. DR PDBsum; 5PXW; -. DR PDBsum; 5PXX; -. DR PDBsum; 5PXY; -. DR PDBsum; 5PXZ; -. DR PDBsum; 5PY0; -. DR PDBsum; 5PY1; -. DR PDBsum; 5PY2; -. DR PDBsum; 5PY3; -. DR PDBsum; 5PY4; -. DR PDBsum; 5PY5; -. DR PDBsum; 5PY6; -. DR PDBsum; 5PY7; -. DR PDBsum; 5PY8; -. DR PDBsum; 5PY9; -. DR PDBsum; 5PYA; -. DR PDBsum; 5PYB; -. DR PDBsum; 5PYC; -. DR PDBsum; 5PYD; -. DR PDBsum; 5PYE; -. DR PDBsum; 5PYF; -. DR PDBsum; 5PYG; -. DR PDBsum; 5PYH; -. DR PDBsum; 5PYI; -. DR PDBsum; 5PYJ; -. DR PDBsum; 5PYK; -. DR PDBsum; 5PYL; -. DR PDBsum; 5PYM; -. DR PDBsum; 5PYN; -. DR PDBsum; 5PYO; -. DR PDBsum; 5PYP; -. DR PDBsum; 5PYQ; -. DR PDBsum; 5PYR; -. DR PDBsum; 5PYS; -. DR PDBsum; 5PYT; -. DR PDBsum; 5PYU; -. DR PDBsum; 5PYV; -. DR PDBsum; 5PYW; -. DR PDBsum; 5PYX; -. DR PDBsum; 5PYY; -. DR PDBsum; 5PYZ; -. DR PDBsum; 5PZ0; -. DR PDBsum; 5PZ1; -. DR PDBsum; 5PZ2; -. DR PDBsum; 5PZ3; -. DR PDBsum; 5PZ4; -. DR PDBsum; 5PZ5; -. DR PDBsum; 5PZ6; -. DR PDBsum; 5PZ7; -. DR PDBsum; 5PZ8; -. DR PDBsum; 5PZ9; -. DR PDBsum; 5PZA; -. DR PDBsum; 5PZB; -. DR PDBsum; 5PZC; -. DR PDBsum; 5PZD; -. DR PDBsum; 5PZE; -. DR PDBsum; 5PZF; -. DR PDBsum; 5PZG; -. DR PDBsum; 5PZH; -. DR PDBsum; 5PZI; -. DR PDBsum; 5PZJ; -. DR PDBsum; 6G5N; -. DR PDBsum; 6G5P; -. DR AlphaFoldDB; P23497; -. DR SMR; P23497; -. DR BioGRID; 112555; 211. DR DIP; DIP-5983N; -. DR IntAct; P23497; 93. DR MINT; P23497; -. DR STRING; 9606.ENSP00000343023; -. DR GlyCosmos; P23497; 3 sites, 2 glycans. DR GlyGen; P23497; 3 sites, 2 O-linked glycans (3 sites). DR iPTMnet; P23497; -. DR PhosphoSitePlus; P23497; -. DR SwissPalm; P23497; -. DR BioMuta; SP100; -. DR DMDM; 13878931; -. DR EPD; P23497; -. DR jPOST; P23497; -. DR MassIVE; P23497; -. DR MaxQB; P23497; -. DR PaxDb; 9606-ENSP00000343023; -. DR PeptideAtlas; P23497; -. DR ProteomicsDB; 18390; -. DR ProteomicsDB; 32155; -. DR ProteomicsDB; 54115; -. [P23497-1] DR ProteomicsDB; 54116; -. [P23497-2] DR ProteomicsDB; 54117; -. [P23497-3] DR ProteomicsDB; 54118; -. [P23497-4] DR ProteomicsDB; 54119; -. [P23497-5] DR ProteomicsDB; 7363; -. DR Pumba; P23497; -. DR Antibodypedia; 20190; 333 antibodies from 32 providers. DR DNASU; 6672; -. DR Ensembl; ENST00000264052.9; ENSP00000264052.5; ENSG00000067066.17. [P23497-1] DR Ensembl; ENST00000340126.9; ENSP00000343023.4; ENSG00000067066.17. [P23497-4] DR Ensembl; ENST00000409112.5; ENSP00000386427.1; ENSG00000067066.17. [P23497-3] DR Ensembl; ENST00000409341.5; ENSP00000386404.1; ENSG00000067066.17. [P23497-2] DR Ensembl; ENST00000409897.5; ENSP00000386998.1; ENSG00000067066.17. [P23497-7] DR Ensembl; ENST00000427101.6; ENSP00000399389.2; ENSG00000067066.17. [P23497-6] DR GeneID; 6672; -. DR KEGG; hsa:6672; -. DR MANE-Select; ENST00000340126.9; ENSP00000343023.4; NM_001080391.2; NP_001073860.1. [P23497-4] DR UCSC; uc002vqq.3; human. [P23497-1] DR AGR; HGNC:11206; -. DR CTD; 6672; -. DR DisGeNET; 6672; -. DR GeneCards; SP100; -. DR HGNC; HGNC:11206; SP100. DR HPA; ENSG00000067066; Tissue enhanced (bone). DR MIM; 604585; gene. DR neXtProt; NX_P23497; -. DR OpenTargets; ENSG00000067066; -. DR PharmGKB; PA36043; -. DR VEuPathDB; HostDB:ENSG00000067066; -. DR eggNOG; KOG2177; Eukaryota. DR GeneTree; ENSGT00940000162212; -. DR HOGENOM; CLU_015844_0_0_1; -. DR InParanoid; P23497; -. DR OMA; AGMWNNT; -. DR OrthoDB; 38708at2759; -. DR PhylomeDB; P23497; -. DR TreeFam; TF335091; -. DR PathwayCommons; P23497; -. DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR SignaLink; P23497; -. DR SIGNOR; P23497; -. DR BioGRID-ORCS; 6672; 11 hits in 1190 CRISPR screens. DR ChiTaRS; SP100; human. DR EvolutionaryTrace; P23497; -. DR GenomeRNAi; 6672; -. DR Pharos; P23497; Tbio. DR PRO; PR:P23497; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P23497; Protein. DR Bgee; ENSG00000067066; Expressed in calcaneal tendon and 201 other cell types or tissues. DR ExpressionAtlas; P23497; baseline and differential. DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0034399; C:nuclear periphery; IDA:BHF-UCL. DR GO; GO:0005730; C:nucleolus; IDA:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0016605; C:PML body; IDA:BHF-UCL. DR GO; GO:0070087; F:chromo shadow domain binding; IPI:BHF-UCL. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0019900; F:kinase binding; IPI:BHF-UCL. DR GO; GO:0046983; F:protein dimerization activity; IPI:BHF-UCL. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IDA:BHF-UCL. DR GO; GO:0045185; P:maintenance of protein location; IDA:BHF-UCL. DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:BHF-UCL. DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:BHF-UCL. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-UCL. DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IMP:UniProtKB. DR GO; GO:0046826; P:negative regulation of protein export from nucleus; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0032897; P:negative regulation of viral transcription; IDA:BHF-UCL. DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0045765; P:regulation of angiogenesis; IMP:UniProtKB. DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:UniProtKB. DR GO; GO:1902044; P:regulation of Fas signaling pathway; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0034097; P:response to cytokine; IDA:BHF-UCL. DR GO; GO:0032526; P:response to retinoic acid; IDA:BHF-UCL. DR GO; GO:0034340; P:response to type I interferon; IDA:BHF-UCL. DR GO; GO:0034341; P:response to type II interferon; IDA:BHF-UCL. DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IC:BHF-UCL. DR GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB. DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; IC:BHF-UCL. DR GO; GO:0060333; P:type II interferon-mediated signaling pathway; IC:BHF-UCL. DR CDD; cd21978; HMG-box_HMGB_rpt1; 1. DR CDD; cd21979; HMG-box_HMGB_rpt2; 1. DR Gene3D; 1.10.30.10; High mobility group box domain; 2. DR Gene3D; 3.10.390.10; SAND domain-like; 1. DR InterPro; IPR009071; HMG_box_dom. DR InterPro; IPR036910; HMG_box_dom_sf. DR InterPro; IPR004865; HSR_dom. DR InterPro; IPR010919; SAND-like_dom_sf. DR InterPro; IPR000770; SAND_dom. DR InterPro; IPR043563; Sp110/Sp140/Sp140L-like. DR PANTHER; PTHR46386:SF1; NUCLEAR AUTOANTIGEN SP-100; 1. DR PANTHER; PTHR46386; NUCLEAR BODY PROTEIN SP140; 1. DR Pfam; PF00505; HMG_box; 1. DR Pfam; PF09011; HMG_box_2; 1. DR Pfam; PF03172; HSR; 1. DR Pfam; PF01342; SAND; 1. DR PRINTS; PR00886; HIGHMOBLTY12. DR SMART; SM00398; HMG; 2. DR SMART; SM00258; SAND; 1. DR SUPFAM; SSF47095; HMG-box; 2. DR SUPFAM; SSF63763; SAND domain-like; 1. DR PROSITE; PS50118; HMG_BOX_2; 2. DR PROSITE; PS51414; HSR; 1. DR PROSITE; PS50864; SAND; 1. DR Genevisible; P23497; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm; KW DNA-binding; Host-virus interaction; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..879 FT /note="Nuclear autoantigen Sp-100" FT /id="PRO_0000074096" FT DOMAIN 33..149 FT /note="HSR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00747" FT DOMAIN 595..676 FT /note="SAND" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00185" FT DNA_BIND 677..753 FT /note="HMG box 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT DNA_BIND 769..837 FT /note="HMG box 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT REGION 154..245 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 333..478 FT /note="Sufficient to mediate interaction with ETS1" FT REGION 345..386 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 401..596 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 835..879 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 165..168 FT /note="D-box; recognition signal for CDC20-mediated FT degradation" FT MOTIF 284..297 FT /note="PxVxL motif" FT MOTIF 536..553 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOTIF 568..592 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOTIF 717..734 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 154..168 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 169..200 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 211..226 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 227..245 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 432..446 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 454..485 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 502..521 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 529..590 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 846..862 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 863..879 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 18 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:24275569" FT MOD_RES 157 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 171 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 180 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 228 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 331 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 362 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 394 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 407 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 409 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 410 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 451 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 241 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 297 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:10212234" FT CROSSLNK 300 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 306 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 366 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 387 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447" FT CROSSLNK 594 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..36 FT /note="MAGGGGDLSTRRLNECISPVANEMNHLPAHSHDLQR -> M (in FT isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045868" FT VAR_SEQ 11..35 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045869" FT VAR_SEQ 428..430 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045870" FT VAR_SEQ 449..472 FT /note="RFSSSDFSDLSNGEELQETCSSSL -> LKKKKKKKQCHPQPQPQRGLLEQS FT (in isoform SpAlt-C)" FT /evidence="ECO:0000305" FT /id="VSP_005982" FT VAR_SEQ 473..879 FT /note="Missing (in isoform SpAlt-C)" FT /evidence="ECO:0000305" FT /id="VSP_005983" FT VAR_SEQ 478..480 FT /note="SQP -> KED (in isoform Sp100-A, isoform 6 and FT isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:2258622" FT /id="VSP_005978" FT VAR_SEQ 481..879 FT /note="Missing (in isoform Sp100-A, isoform 6 and isoform FT 7)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:2258622" FT /id="VSP_005979" FT VAR_SEQ 685..688 FT /note="RILE -> VMIK (in isoform Sp100-B)" FT /evidence="ECO:0000303|PubMed:8695863" FT /id="VSP_005980" FT VAR_SEQ 689..879 FT /note="Missing (in isoform Sp100-B)" FT /evidence="ECO:0000303|PubMed:8695863" FT /id="VSP_005981" FT VAR_SEQ 699..879 FT /note="EEHKKKNPDASVKFSEFLKKCSETWKTIFAKEKGKFEDMAKADKAHYEREMK FT TYIPPKGEKKKKFKDPNAPKRPPLAFFLFCSEYRPKIKGEHPGLSIDDVVKKLAGMWNN FT TAAADKQFYEKKAAKLKEKYKKDIAAYRAKGKPNSAKKRVVKAEKSKKKKEEEEDEEDE FT QEEENEEDDDK -> PENSNICEVCNKWGRLFCCDTCPRSFHEHCHIPSVEANKNPWSC FT IFCRIKTIQERCPESQSGHQESEVLMRQMLPEEQLKCEFLLLKVYCDSKSCFFASEPYY FT NREGSQGPQKPMWLNKVKTSLNEQMYTRVEGFVQDMRLIFHNHKEFYREDKFTRLGIQV FT QDIFEKNFRNIFAIQETSKNIIMFI (in isoform Sp100-C)" FT /evidence="ECO:0000303|PubMed:11313457" FT /id="VSP_005984" FT VARIANT 433 FT /note="M -> V (in dbSNP:rs12724)" FT /id="VAR_005621" FT VARIANT 471 FT /note="S -> P" FT /id="VAR_005622" FT VARIANT 699 FT /note="E -> G (in dbSNP:rs34700604)" FT /id="VAR_034510" FT MUTAGEN 165 FT /note="R->A: Prevents CDC20-mediated degradation; when FT associated with Ala-168." FT /evidence="ECO:0000269|PubMed:22086178" FT MUTAGEN 168 FT /note="L->A: Prevents CDC20-mediated degradation; when FT associated with Ala-165." FT /evidence="ECO:0000269|PubMed:22086178" FT CONFLICT 47 FT /note="R -> M (in Ref. 5; BAG56886)" FT /evidence="ECO:0000305" FT CONFLICT 247 FT /note="S -> P (in Ref. 5; BAG56886)" FT /evidence="ECO:0000305" FT CONFLICT 402 FT /note="Q -> H (in Ref. 5; BAG56886)" FT /evidence="ECO:0000305" FT CONFLICT 651 FT /note="A -> R (in Ref. 10; AAL77438/AAL77439)" FT /evidence="ECO:0000305" FT STRAND 466..469 FT /evidence="ECO:0007829|PDB:5PXL" FT STRAND 471..473 FT /evidence="ECO:0007829|PDB:5PXL" FT TURN 474..476 FT /evidence="ECO:0007829|PDB:5PXL" FT STRAND 477..479 FT /evidence="ECO:0007829|PDB:5PXL" FT HELIX 491..498 FT /evidence="ECO:0007829|PDB:5PXL" FT HELIX 499..502 FT /evidence="ECO:0007829|PDB:5PXL" FT HELIX 600..602 FT /evidence="ECO:0007829|PDB:1H5P" FT STRAND 603..609 FT /evidence="ECO:0007829|PDB:1H5P" FT STRAND 612..617 FT /evidence="ECO:0007829|PDB:1H5P" FT HELIX 618..621 FT /evidence="ECO:0007829|PDB:1H5P" FT HELIX 624..626 FT /evidence="ECO:0007829|PDB:1H5P" FT STRAND 630..632 FT /evidence="ECO:0007829|PDB:1H5P" FT TURN 633..635 FT /evidence="ECO:0007829|PDB:1H5P" FT STRAND 636..638 FT /evidence="ECO:0007829|PDB:1H5P" FT HELIX 640..647 FT /evidence="ECO:0007829|PDB:1H5P" FT HELIX 655..658 FT /evidence="ECO:0007829|PDB:1H5P" FT HELIX 666..672 FT /evidence="ECO:0007829|PDB:1H5P" FT STRAND 673..675 FT /evidence="ECO:0007829|PDB:1H5P" FT CONFLICT P23497-3:686 FT /note="M -> T (in Ref. 2; AAC50743)" FT /evidence="ECO:0000305" FT CONFLICT P23497-4:826 FT /note="M -> T (in Ref. 4; AAK51202)" FT /evidence="ECO:0000305" SQ SEQUENCE 879 AA; 100417 MW; CA55547DE21B2A10 CRC64; MAGGGGDLST RRLNECISPV ANEMNHLPAH SHDLQRMFTE DQGVDDRLLY DIVFKHFKRN KVEISNAIKK TFPFLEGLRD RDLITNKMFE DSQDSCRNLV PVQRVVYNVL SELEKTFNLP VLEALFSDVN MQEYPDLIHI YKGFENVIHD KLPLQESEEE EREERSGLQL SLEQGTGENS FRSLTWPPSG SPSHAGTTPP ENGLSEHPCE TEQINAKRKD TTSDKDDSLG SQQTNEQCAQ KAEPTESCEQ IAVQVNNGDA GREMPCPLPC DEESPEAELH NHGIQINSCS VRLVDIKKEK PFSNSKVECQ AQARTHHNQA SDIIVISSED SEGSTDVDEP LEVFISAPRS EPVINNDNPL ESNDEKEGQE ATCSRPQIVP EPMDFRKLST FRESFKKRVI GQDHDFSESS EEEAPAEASS GALRSKHGEK APMTSRSTST WRIPSRKRRF SSSDFSDLSN GEELQETCSS SLRRGSGSQP QEPENKKCSC VMCFPKGVPR SQEARTESSQ ASDMMDTMDV ENNSTLEKHS GKRRKKRRHR SKVNGLQRGR KKDRPRKHLT LNNKVQKKRW QQRGRKANTR PLKRRRKRGP RIPKDENINF KQSELPVTCG EVKGTLYKER FKQGTSKKCI QSEDKKWFTP REFEIEGDRG ASKNWKLSIR CGGYTLKVLM ENKFLPEPPS TRKKRILESH NNTLVDPCEE HKKKNPDASV KFSEFLKKCS ETWKTIFAKE KGKFEDMAKA DKAHYEREMK TYIPPKGEKK KKFKDPNAPK RPPLAFFLFC SEYRPKIKGE HPGLSIDDVV KKLAGMWNNT AAADKQFYEK KAAKLKEKYK KDIAAYRAKG KPNSAKKRVV KAEKSKKKKE EEEDEEDEQE EENEEDDDK //