SP100_HUMAN
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 03-AUG-2022, entry version 236.
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 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 [39]
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 [40]
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. Nucleus, PML body
CC {ECO:0000269|PubMed:27211601}. Cytoplasm. Note=Differences in the
CC subnuclear localization of the different isoforms seem to exist and may
CC also be cell cycle- and interferon-dependent. Accumulates in the
CC cytoplasm upon FAS activation.
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}.
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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; 209.
DR DIP; DIP-5983N; -.
DR IntAct; P23497; 93.
DR MINT; P23497; -.
DR STRING; 9606.ENSP00000343023; -.
DR GlyGen; P23497; 3 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; P23497; -.
DR PhosphoSitePlus; P23497; -.
DR BioMuta; SP100; -.
DR DMDM; 13878931; -.
DR EPD; P23497; -.
DR jPOST; P23497; -.
DR MassIVE; P23497; -.
DR MaxQB; P23497; -.
DR PaxDb; P23497; -.
DR PeptideAtlas; P23497; -.
DR PRIDE; 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 Antibodypedia; 20190; 313 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 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 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 BioGRID-ORCS; 6672; 10 hits in 1113 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 199 other tissues.
DR ExpressionAtlas; P23497; baseline and differential.
DR Genevisible; P23497; HS.
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:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:BHF-UCL.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IC: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: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:0045892; P:negative regulation of transcription, DNA-templated; 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:0045893; P:positive regulation of transcription, DNA-templated; IMP: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:0034341; P:response to interferon-gamma; 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: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 signaling pathway; IC:BHF-UCL.
DR Gene3D; 1.10.30.10; -; 2.
DR Gene3D; 3.10.390.10; -; 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.
DR PANTHER; PTHR46386; PTHR46386; 2.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF09011; HMG_box_2; 1.
DR Pfam; PF03172; HSR; 1.
DR Pfam; PF01342; SAND; 1.
DR SMART; SM00398; HMG; 2.
DR SMART; SM00258; SAND; 1.
DR SUPFAM; SSF47095; SSF47095; 2.
DR SUPFAM; SSF63763; SSF63763; 1.
DR PROSITE; PS50118; HMG_BOX_2; 2.
DR PROSITE; PS51414; HSR; 1.
DR PROSITE; PS50864; SAND; 1.
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
