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Nuclear autoantigen Sp-100 (Nuclear dot-associated Sp100 protein) (Speckled 100 kDa)

 SP100_HUMAN             Reviewed;         879 AA.
P23497; B4DDX5; B8ZZD8; E7EUA7; E9PH61; F8WFE2; O75450; Q13343;
Q8TE34; Q96F70; Q96T24; Q96T95; Q9NP33; Q9UE32;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 3.
25-OCT-2017, entry version 204.
RecName: Full=Nuclear autoantigen Sp-100;
AltName: Full=Nuclear dot-associated Sp100 protein;
AltName: Full=Speckled 100 kDa;
Name=SP100;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP100-A).
TISSUE=Liver, and Placenta;
PubMed=2258622;
Szostecki C., Guldner H.H., Netter H.J., Will H.;
"Isolation and characterization of cDNA encoding a human nuclear
antigen predominantly recognized by autoantibodies from patients with
primary biliary cirrhosis.";
J. Immunol. 145:4338-4347(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP100-B).
PubMed=8695863;
Dent A.L., Yewdell J., Puvion-Dutilleul F., Koken M.H.M., de The H.,
Staudt L.M.;
"LYSP100-associated nuclear domains (LANDs): description of a new
class of subnuclear structures and their relationship to PML nuclear
bodies.";
Blood 88:1423-1426(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP100-HMG).
TISSUE=Mammary cancer;
PubMed=9636146; DOI=10.1073/pnas.95.13.7316;
Seeler J.-S., Marchio A., Sitterlin D., Transy C., Dejean A.;
"Interaction of SP100 with HP1 proteins: a link between the
promyelocytic leukemia-associated nuclear bodies and the chromatin
compartment.";
Proc. Natl. Acad. Sci. U.S.A. 95:7316-7321(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP100-C), SUBCELLULAR LOCATION
(ISOFORMS SP100-A; SP100-C AND SP100-HMG), SUMOYLATION WITH SUMO1, AND
INTERACTION WITH CBX5.
PubMed=11313457; DOI=10.1128/MCB.21.10.3314-3324.2001;
Seeler J.-S., Marchio A., Losson R., Desterro J.M.P., Hay R.T.,
Chambon P., Dejean A.;
"Common properties of nuclear protein SP100 and TIF1alpha chromatin
factor: role of SUMO modification.";
Mol. Cell. Biol. 21:3314-3324(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7).
TISSUE=Kidney, and Urinary bladder;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SP100-A).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
TISSUE=Lymphoma;
PubMed=8810287; DOI=10.1074/jbc.271.41.25253;
Groetzinger T., Jensen K., Will H.;
"The interferon (IFN)-stimulated gene Sp100 promoter contains an IFN-
gamma activation site and an imperfect IFN-stimulated response element
which mediate type I IFN inducibility.";
J. Biol. Chem. 271:25253-25260(1996).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 477-879 (ISOFORMS SP100-B AND
SP100-HMG), AND PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM
SPALT-C).
TISSUE=Cervix carcinoma;
PubMed=9973607;
Guldner H.H., Szostecki C., Schroeder P., Matschl U., Jensen K.,
Lueders C., Will H., Sternsdorf T.;
"Splice variants of the nuclear dot-associated Sp100 protein contain
homologies to HMG-1 and a human nuclear phosphoprotein-box motif.";
J. Cell Sci. 112:733-747(1999).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 699-879 (ISOFORM SP100-HMG).
TISSUE=Cervix carcinoma;
PubMed=10766566; DOI=10.1006/geno.1999.6008;
Rogalla P., Kazmierczak B., Flohr A.M., Hauke S., Bullerdiek J.;
"Back to the roots of a new exon-the molecular archaeology of a SP100
splice variant.";
Genomics 63:117-122(2000).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 699-879 (ISOFORM SP100-HMG).
PubMed=11574059; DOI=10.1186/gb-2001-2-9-research0040;
Devor E.J.;
"Molecular archeology of an SP100 splice variant revisited: dating the
retrotranscription and Alu insertion events.";
Genome Biol. 2:RESEARCH0040.1-RESEARCH0040.6(2001).
[12]
SUMOYLATION WITH SUMO1, AND SUBCELLULAR LOCATION.
PubMed=9412458; DOI=10.1083/jcb.139.7.1621;
Sternsdorf T., Jensen K., Will H.;
"Evidence for covalent modification of the nuclear dot-associated
proteins PML and Sp100 by PIC1/SUMO-1.";
J. Cell Biol. 139:1621-1634(1997).
[13]
SUMOYLATION AT LYS-297, AND HOMODIMERIZATION.
PubMed=10212234; DOI=10.1074/jbc.274.18.12555;
Sternsdorf T., Jensen K., Reich B., Will H.;
"The nuclear dot protein sp100, characterization of domains necessary
for dimerization, subcellular localization, and modification by small
ubiquitin-like modifiers.";
J. Biol. Chem. 274:12555-12566(1999).
[14]
INTERACTION WITH NBN.
PubMed=12470659; DOI=10.1016/S0006-291X(02)02755-9;
Naka K., Ikeda K., Motoyama N.;
"Recruitment of NBS1 into PML oncogenic domains via interaction with
SP100 protein.";
Biochem. Biophys. Res. Commun. 299:863-871(2002).
[15]
FUNCTION AS A TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH ETS1, AND
SUBCELLULAR LOCATION.
PubMed=11909962; DOI=10.1128/MCB.22.8.2687-2702.2002;
Wasylyk C., Schlumberger S.E., Criqui-Filipe P., Wasylyk B.;
"Sp100 interacts with ETS-1 and stimulates its transcriptional
activity.";
Mol. Cell. Biol. 22:2687-2702(2002).
[16]
FUNCTION IN TP53-DEPENDENT TRANSCRIPTION, AND INTERACTION WITH HIPK2.
PubMed=14647468; DOI=10.1038/sj.onc.1207079;
Moeller A., Sirma H., Hofmann T.G., Staege H., Gresko E., Luedi K.S.,
Klimczak E., Droege W., Will H., Schmitz M.L.;
"Sp100 is important for the stimulatory effect of homeodomain-
interacting protein kinase-2 on p53-dependent gene expression.";
Oncogene 22:8731-8737(2003).
[17]
FUNCTION AS A TRANSCRIPTIONAL COREPRESSOR, INTERACTION WITH ETS1, AND
INDUCTION BY INTERFERON ALPHA.
PubMed=15247905; DOI=10.1038/sj.onc.1207891;
Yordy J.S., Li R., Sementchenko V.I., Pei H., Muise-Helmericks R.C.,
Watson D.K.;
"SP100 expression modulates ETS1 transcriptional activity and inhibits
cell invasion.";
Oncogene 23:6654-6665(2004).
[18]
INTERACTION WITH CBX5.
PubMed=15882967; DOI=10.1016/j.bbrc.2005.04.016;
Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III;
"The mammalian heterochromatin protein 1 binds diverse nuclear
proteins through a common motif that targets the chromoshadow
domain.";
Biochem. Biophys. Res. Commun. 331:929-937(2005).
[19]
FUNCTION IN VIRAL INFECTION, AND INTERACTION WITH EBV EBNA-LP.
PubMed=16177824; DOI=10.1038/sj.emboj.7600820;
Ling P.D., Peng R.S., Nakajima A., Yu J.H., Tan J., Moses S.M.,
Yang W.H., Zhao B., Kieff E., Bloch K.D., Bloch D.B.;
"Mediation of Epstein-Barr virus EBNA-LP transcriptional coactivation
by Sp100.";
EMBO J. 24:3565-3575(2005).
[20]
FUNCTION IN TELOMERE SHORTENING, AND INTERACTION WITH MRN COMPLEX.
PubMed=15767676; DOI=10.1128/MCB.25.7.2708-2721.2005;
Jiang W.Q., Zhong Z.H., Henson J.D., Neumann A.A., Chang A.C.,
Reddel R.R.;
"Suppression of alternative lengthening of telomeres by Sp100-mediated
sequestration of the MRE11/RAD50/NBS1 complex.";
Mol. Cell. Biol. 25:2708-2721(2005).
[21]
FUNCTION IN ENDOTHELIAL CELL MIGRATION, AND INDUCTION.
PubMed=15592518; DOI=10.1038/sj.onc.1208245;
Yordy J.S., Moussa O., Pei H., Chaussabel D., Li R., Watson D.K.;
"SP100 inhibits ETS1 activity in primary endothelial cells.";
Oncogene 24:916-931(2005).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-331, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[23]
FUNCTION IN FAS-MEDIATED APOPTOSIS, INTERACTION WITH CASP8AP2, AND
SUBCELLULAR LOCATION.
PubMed=17245429; DOI=10.1038/sj.emboj.7601504;
Milovic-Holm K., Krieghoff E., Jensen K., Will H., Hofmann T.G.;
"FLASH links the CD95 signaling pathway to the cell nucleus and
nuclear bodies.";
EMBO J. 26:391-401(2007).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407; SER-409 AND
SER-410, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-407; SER-409
AND SER-410, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[26]
TUMOR SUPPRESSOR.
PubMed=21118961; DOI=10.1158/0008-5472.CAN-10-1483;
Negorev D.G., Vladimirova O.V., Kossenkov A.V., Nikonova E.V.,
Demarest R.M., Capobianco A.J., Showe M.K., Rauscher F.J. III,
Showe L.C., Maul G.G.;
"Sp100 as a potent tumor suppressor: accelerated senescence and rapid
malignant transformation of human fibroblasts through modulation of an
embryonic stem cell program.";
Cancer Res. 70:9991-10001(2010).
[27]
ERRATUM, AND RETRACTION.
PubMed=23907639; DOI=10.1158/0008-5472.CAN-13-1715;
Negorev D.G., Vladimirova O.V., Kossenkov A.V., Demarest R.M.,
Showe M.K., Rauscher F.J. III, Showe L.C., Nikonova E.V.,
Capobianco A.J.;
Cancer Res. 73:4960-4961(2013).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-362; SER-407;
SER-409 AND SER-410, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[29]
DOMAIN D-BOX MOTIF, AND MUTAGENESIS OF ARG-165 AND LEU-168.
PubMed=22086178; DOI=10.1016/j.bbrc.2011.10.146;
Wang R., Li K.M., Zhou C.H., Xue J.L., Ji C.N., Chen J.Z.;
"Cdc20 mediates D-box-dependent degradation of Sp100.";
Biochem. Biophys. Res. Commun. 415:702-706(2011).
[30]
FUNCTION IN CELL PROLIFERATION.
PubMed=21274506; DOI=10.3892/ijo.2011.927;
Held-Feindt J., Hattermann K., Knerlich-Lukoschus F., Mehdorn H.M.,
Mentlein R.;
"SP100 reduces malignancy of human glioma cells.";
Int. J. Oncol. 38:1023-1030(2011).
[31]
FUNCTION IN VIRAL INFECTION, INTERACTION WITH HHV-5 PROTEIN UL123, AND
INDUCTION BY INTERFERON.
PubMed=21880768; DOI=10.1128/JVI.00758-11;
Kim Y.E., Lee J.H., Kim E.T., Shin H.J., Gu S.Y., Seol H.S.,
Ling P.D., Lee C.H., Ahn J.H.;
"Human cytomegalovirus infection causes degradation of Sp100 proteins
that suppress viral gene expression.";
J. Virol. 85:11928-11937(2011).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-171; SER-180;
SER-362; SER-394 AND SER-451, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-157; SER-228;
SER-362; SER-407; SER-409 AND SER-410, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[35]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-306 AND LYS-387, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[36]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-306, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[37]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-306, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-241; LYS-300; LYS-306;
LYS-366 AND LYS-594, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Together with PML, this tumor suppressor is a major
constituent of the PML bodies, a subnuclear organelle involved in
a large number of physiological processes including cell growth,
differentiation and apoptosis. Functions as a transcriptional
coactivator of ETS1 and ETS2 according to PubMed:11909962. Under
certain conditions, it may also act as a corepressor of ETS1
preventing its binding to DNA according to PubMed:15247905.
Through the regulation of ETS1 it may play a role in angiogenesis,
controlling endothelial cell motility and invasion. Through
interaction with the MRN complex it may be involved in the
regulation of telomeres lengthening. May also regulate TP53-
mediated transcription and through CASP8AP2, regulate FAS-mediated
apoptosis. Also plays a role in infection by viruses, including
human cytomegalovirus and Epstein-Barr virus, through mechanisms
that may involve chromatin and/or transcriptional regulation.
{ECO:0000269|PubMed:11909962, ECO:0000269|PubMed:14647468,
ECO:0000269|PubMed:15247905, ECO:0000269|PubMed:15592518,
ECO:0000269|PubMed:15767676, ECO:0000269|PubMed:16177824,
ECO:0000269|PubMed:17245429, ECO:0000269|PubMed:21274506,
ECO:0000269|PubMed:21880768}.
-!- SUBUNIT: Homodimer; isoforms are able to heterodimerize. Interacts
with members of the HP1 family of nonhistone chromosomal protein,
such as CBX5 and CBX3 via the PxVxL motif. Interacts with ETS1;
the interaction is direct and modulates ETS1 transcriptional
activity. Interacts with the MRN complex which is composed of two
heterodimers RAD50/MRE11 associated with a single NBN; recruits
the complex to PML-related bodies. Interacts with HIPK2;
positively regulates TP53-dependent transcription. Interacts with
CASP8AP2; may negatively regulate CASP8AP2 export from the nucleus
to the cytoplasm. Interacts with Epstein-Barr virus EBNA-LP; this
interaction is important for EBNA-LP coactivator activity.
Interacts with human cytomegalovirus/HHV-5 protein UL123; may play
a role in infection by the virus. {ECO:0000269|PubMed:11313457,
ECO:0000269|PubMed:11909962, ECO:0000269|PubMed:12470659,
ECO:0000269|PubMed:14647468, ECO:0000269|PubMed:15247905,
ECO:0000269|PubMed:15767676, ECO:0000269|PubMed:15882967,
ECO:0000269|PubMed:16177824, ECO:0000269|PubMed:17245429,
ECO:0000269|PubMed:21880768}.
-!- INTERACTION:
Q59GP6:-; NbExp=3; IntAct=EBI-751145, EBI-10243413;
P35609:ACTN2; NbExp=5; IntAct=EBI-751145, EBI-77797;
Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-751145, EBI-10187270;
Q9UKL3:CASP8AP2; NbExp=5; IntAct=EBI-751145, EBI-2339650;
P45973:CBX5; NbExp=6; IntAct=EBI-6589365, EBI-78219;
Q9Y6K1:DNMT3A; NbExp=3; IntAct=EBI-751145, EBI-923653;
Q92630:DYRK2; NbExp=3; IntAct=EBI-751145, EBI-749432;
P14921:ETS1; NbExp=4; IntAct=EBI-751145, EBI-913209;
Q8TF65:GIPC2; NbExp=3; IntAct=EBI-751145, EBI-712067;
V9HWG0:HEL25; NbExp=3; IntAct=EBI-751145, EBI-10183977;
Q96JM7:L3MBTL3; NbExp=3; IntAct=EBI-751145, EBI-2686809;
Q14498-3:RBM39; NbExp=3; IntAct=EBI-751145, EBI-6654703;
Q14D33:RTP5; NbExp=3; IntAct=EBI-751145, EBI-10217913;
P63165:SUMO1; NbExp=6; IntAct=EBI-751145, EBI-80140;
P55854:SUMO3; NbExp=2; IntAct=EBI-751145, EBI-474067;
Q9Y228:TRAF3IP3; NbExp=3; IntAct=EBI-751145, EBI-765817;
P03169:UL123 (xeno); NbExp=4; IntAct=EBI-751145, EBI-6691147;
Q96GY0:ZC2HC1A; NbExp=3; IntAct=EBI-751145, EBI-5458880;
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Cytoplasm.
Note=Differences in the subnuclear localization of the different
isoforms seem to exist and may also be cell cycle- and interferon-
dependent. Accumulates in the cytoplasm upon FAS activation.
-!- SUBCELLULAR LOCATION: Isoform Sp100-C: Nucleus
{ECO:0000269|PubMed:11313457}. Note=Forms a reticulate or track-
like nuclear pattern with denser concentrations at the nuclear
lamina and surrounding the nucleoli, a pattern reminiscent of
heterochromatin-rich regions according to PubMed:11313457.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=Sp100-HMG; Synonyms=SP100HMG, SpAlt-HMG;
IsoId=P23497-1; Sequence=Displayed;
Name=Sp100-A; Synonyms=SP100A, SP100;
IsoId=P23497-2; Sequence=VSP_005978, VSP_005979;
Note=Major isoform.;
Name=Sp100-B; Synonyms=SP100B, SpAlt-212;
IsoId=P23497-3; Sequence=VSP_005980, VSP_005981;
Note=Ref.2 (AAC50743) sequence is in conflict in position:
686:M->T. {ECO:0000305};
Name=Sp100-C; Synonyms=SP100C;
IsoId=P23497-4; Sequence=VSP_005984;
Note=Ref.4 (AAK51202) sequence is in conflict in position:
826:M->T. {ECO:0000305};
Name=SpAlt-C;
IsoId=P23497-5; Sequence=VSP_005982, VSP_005983;
Name=6;
IsoId=P23497-6; Sequence=VSP_045869, VSP_045870, VSP_005978,
VSP_005979;
Note=No experimental confirmation available.;
Name=7;
IsoId=P23497-7; Sequence=VSP_045868, VSP_005978, VSP_005979;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Sp100-B is expressed only in
spleen, tonsil, thymus, mature B-cell line and some T-cell line,
but not in brain, liver, muscle or non-lymphoid cell lines.
-!- INDUCTION: Up-regulated by interferon, retinoic acid, TNF-
alpha/TNFA and lipopolysaccharide (at protein level). Up-regulated
following heat-shock. {ECO:0000269|PubMed:15247905,
ECO:0000269|PubMed:15592518, ECO:0000269|PubMed:21880768}.
-!- DOMAIN: The HSR domain is important for the nuclear body targeting
as well as for the dimerization. {ECO:0000269|PubMed:22086178}.
-!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
required for interaction with chromoshadow domains. This motif
requires additional residues -7, -6, +4 and +5 of the central Val
which contact the chromoshadow domain.
{ECO:0000269|PubMed:22086178}.
-!- PTM: Sumoylated. Sumoylation depends on a functional nuclear
localization signal but is not necessary for nuclear import or
nuclear body targeting.
-!- PTM: Sumoylated. Sumoylated with SUMO1. Sumoylation depends on a
functional nuclear localization signal but is not necessary for
nuclear import or nuclear body targeting. Sumoylation may
stabilize the interaction with CBX5.
-!- MISCELLANEOUS: The major isoform Sp100-A, has a calculated
molecular weight of 54 kDa, but exhibits aberrant electrophoretic
mobilities, with an apparent molecular weight of 100 kDa.
-----------------------------------------------------------------------
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EMBL; M60618; AAA35537.1; -; mRNA.
EMBL; U36501; AAC50743.1; -; mRNA.
EMBL; AF056322; AAC39790.1; -; mRNA.
EMBL; AF255565; AAK51202.1; -; mRNA.
EMBL; AK293373; BAG56886.1; -; mRNA.
EMBL; AC009949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC010149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC011562; AAH11562.1; -; mRNA.
EMBL; X95472; CAA64744.1; -; Genomic_DNA.
EMBL; L79986; AAL77441.1; -; mRNA.
EMBL; L79987; AAL77439.1; -; mRNA.
EMBL; L79988; AAL77438.1; -; mRNA.
EMBL; AF076675; AAF39781.1; -; Genomic_DNA.
EMBL; AF378670; AAK57703.1; -; Genomic_DNA.
CCDS; CCDS2477.1; -. [P23497-1]
CCDS; CCDS42832.1; -. [P23497-4]
CCDS; CCDS56170.1; -. [P23497-3]
CCDS; CCDS56171.1; -. [P23497-2]
CCDS; CCDS56172.1; -. [P23497-6]
CCDS; CCDS56173.1; -. [P23497-7]
PIR; A37244; A37244.
RefSeq; NP_001073860.1; NM_001080391.1. [P23497-4]
RefSeq; NP_001193630.1; NM_001206701.1. [P23497-3]
RefSeq; NP_001193631.1; NM_001206702.1. [P23497-2]
RefSeq; NP_001193632.1; NM_001206703.1. [P23497-6]
RefSeq; NP_001193633.1; NM_001206704.1. [P23497-7]
RefSeq; NP_003104.2; NM_003113.3. [P23497-1]
UniGene; Hs.369056; -.
PDB; 1H5P; NMR; -; A=595-688.
PDB; 4PTB; X-ray; 1.60 A; A/B=466-508.
PDB; 5FB0; X-ray; 2.70 A; A/C=696-878.
PDB; 5FB1; X-ray; 2.10 A; A=696-875.
PDB; 5PWE; X-ray; 1.69 A; A/B=466-508.
PDB; 5PWF; X-ray; 1.48 A; A/B=466-508.
PDB; 5PWG; X-ray; 1.46 A; A/B=466-508.
PDB; 5PWH; X-ray; 1.50 A; A/B=466-508.
PDB; 5PWI; X-ray; 1.62 A; A/B=466-508.
PDB; 5PWJ; X-ray; 1.89 A; A/B=466-508.
PDB; 5PWK; X-ray; 1.62 A; A/B=466-508.
PDB; 5PWL; X-ray; 1.83 A; A/B=466-508.
PDB; 5PWM; X-ray; 1.54 A; A/B=466-508.
PDB; 5PWN; X-ray; 1.64 A; A/B=466-508.
PDB; 5PWO; X-ray; 1.85 A; A/B=466-508.
PDB; 5PWP; X-ray; 1.51 A; A/B=466-508.
PDB; 5PWQ; X-ray; 1.52 A; A/B=466-508.
PDB; 5PWR; X-ray; 1.46 A; A/B=466-508.
PDB; 5PWS; X-ray; 1.40 A; A/B=466-508.
PDB; 5PWT; X-ray; 1.58 A; A/B=466-508.
PDB; 5PWU; X-ray; 1.44 A; A/B=466-508.
PDB; 5PWV; X-ray; 1.58 A; A/B=466-508.
PDB; 5PWW; X-ray; 1.59 A; A/B=466-508.
PDB; 5PWX; X-ray; 1.69 A; A/B=466-508.
PDB; 5PWY; X-ray; 1.98 A; A/B=466-508.
PDB; 5PWZ; X-ray; 1.62 A; A/B=466-508.
PDB; 5PX0; X-ray; 1.55 A; A/B=466-508.
PDB; 5PX1; X-ray; 1.55 A; A/B=466-508.
PDB; 5PX2; X-ray; 1.43 A; A/B=466-508.
PDB; 5PX3; X-ray; 1.57 A; A/B=466-508.
PDB; 5PX4; X-ray; 1.45 A; A/B=466-508.
PDB; 5PX5; X-ray; 1.74 A; A/B=466-508.
PDB; 5PX6; X-ray; 1.43 A; A/B=466-508.
PDB; 5PX7; X-ray; 1.74 A; A/B=466-508.
PDB; 5PX8; X-ray; 1.71 A; A/B=466-508.
PDB; 5PX9; X-ray; 1.89 A; A/B=466-508.
PDB; 5PXA; X-ray; 1.43 A; A/B=466-508.
PDB; 5PXB; X-ray; 1.46 A; A/B=466-508.
PDB; 5PXC; X-ray; 1.52 A; A/B=466-508.
PDB; 5PXD; X-ray; 1.64 A; A/B=466-508.
PDB; 5PXE; X-ray; 1.55 A; A/B=466-508.
PDB; 5PXF; X-ray; 1.71 A; A/B=466-508.
PDB; 5PXG; X-ray; 1.98 A; A/B=466-508.
PDB; 5PXH; X-ray; 2.25 A; A/B=466-508.
PDB; 5PXI; X-ray; 1.76 A; A/B=466-508.
PDB; 5PXJ; X-ray; 1.68 A; A/B=466-508.
PDB; 5PXK; X-ray; 1.98 A; A/B=466-508.
PDB; 5PXL; X-ray; 1.35 A; A/B=466-508.
PDB; 5PXM; X-ray; 1.59 A; A/B=466-508.
PDB; 5PXN; X-ray; 1.43 A; A/B=466-508.
PDB; 5PXO; X-ray; 1.78 A; A/B=466-508.
PDB; 5PXP; X-ray; 1.86 A; A/B=466-508.
PDB; 5PXQ; X-ray; 1.62 A; A/B=466-508.
PDB; 5PXR; X-ray; 1.81 A; A/B=466-508.
PDB; 5PXS; X-ray; 1.49 A; A/B=466-508.
PDB; 5PXT; X-ray; 1.40 A; A/B=466-508.
PDB; 5PXU; X-ray; 1.76 A; A/B=466-508.
PDB; 5PXV; X-ray; 1.65 A; A/B=466-508.
PDB; 5PXW; X-ray; 2.01 A; A/B=466-508.
PDB; 5PXX; X-ray; 1.57 A; A/B=466-508.
PDB; 5PXY; X-ray; 2.14 A; A/B=466-508.
PDB; 5PXZ; X-ray; 1.65 A; A/B=466-508.
PDB; 5PY0; X-ray; 1.70 A; A/B=466-508.
PDB; 5PY1; X-ray; 1.74 A; A/B=466-508.
PDB; 5PY2; X-ray; 1.62 A; A/B=466-508.
PDB; 5PY3; X-ray; 1.78 A; A/B=466-508.
PDB; 5PY4; X-ray; 1.67 A; A/B=466-508.
PDB; 5PY5; X-ray; 1.44 A; A/B=466-508.
PDB; 5PY6; X-ray; 1.74 A; A/B=466-508.
PDB; 5PY7; X-ray; 1.68 A; A/B=466-508.
PDB; 5PY8; X-ray; 1.66 A; A/B=466-508.
PDB; 5PY9; X-ray; 1.73 A; A/B=466-508.
PDB; 5PYA; X-ray; 1.55 A; A/B=466-508.
PDB; 5PYB; X-ray; 1.74 A; A/B=466-508.
PDB; 5PYC; X-ray; 1.87 A; A/B=466-508.
PDB; 5PYD; X-ray; 2.02 A; A/B=466-508.
PDB; 5PYE; X-ray; 1.81 A; A/B=466-508.
PDB; 5PYF; X-ray; 1.83 A; A/B=466-508.
PDB; 5PYG; X-ray; 1.95 A; A/B=466-508.
PDB; 5PYH; X-ray; 1.74 A; A/B=466-508.
PDB; 5PYI; X-ray; 2.29 A; A/B=466-508.
PDB; 5PYJ; X-ray; 1.97 A; A/B=466-508.
PDB; 5PYK; X-ray; 1.88 A; A/B=466-508.
PDB; 5PYL; X-ray; 1.53 A; A/B=466-508.
PDB; 5PYM; X-ray; 1.70 A; A/B=466-508.
PDB; 5PYN; X-ray; 1.89 A; A/B=466-508.
PDB; 5PYO; X-ray; 1.67 A; A/B=466-508.
PDB; 5PYP; X-ray; 1.63 A; A/B=466-508.
PDB; 5PYQ; X-ray; 1.97 A; A/B=466-508.
PDB; 5PYR; X-ray; 1.94 A; A/B=466-508.
PDB; 5PYS; X-ray; 2.09 A; A/B=466-508.
PDB; 5PYT; X-ray; 2.13 A; A/B=466-508.
PDB; 5PYU; X-ray; 1.74 A; A/B=466-508.
PDB; 5PYV; X-ray; 1.94 A; A/B=466-508.
PDB; 5PYW; X-ray; 1.45 A; A/B=466-508.
PDB; 5PYX; X-ray; 1.57 A; A/B=466-508.
PDB; 5PYY; X-ray; 1.64 A; A/B=466-508.
PDB; 5PYZ; X-ray; 1.59 A; A/B=466-508.
PDB; 5PZ0; X-ray; 2.13 A; A/B=466-508.
PDB; 5PZ1; X-ray; 2.13 A; A/B=466-508.
PDB; 5PZ2; X-ray; 1.88 A; A/B=466-508.
PDB; 5PZ3; X-ray; 1.93 A; A/B=466-508.
PDB; 5PZ4; X-ray; 1.94 A; A/B=466-508.
PDB; 5PZ5; X-ray; 2.64 A; A/B=466-508.
PDB; 5PZ6; X-ray; 1.87 A; A/B=466-508.
PDB; 5PZ7; X-ray; 1.54 A; A/B=466-508.
PDB; 5PZ8; X-ray; 1.52 A; A/B=466-508.
PDB; 5PZ9; X-ray; 2.01 A; A/B=466-508.
PDB; 5PZA; X-ray; 1.59 A; A/B=466-508.
PDB; 5PZB; X-ray; 2.05 A; A/B=466-508.
PDB; 5PZC; X-ray; 1.61 A; A/B=466-508.
PDB; 5PZD; X-ray; 1.74 A; A/B=466-508.
PDB; 5PZE; X-ray; 1.82 A; A/B=466-508.
PDB; 5PZF; X-ray; 1.84 A; A/B=466-508.
PDB; 5PZG; X-ray; 1.88 A; A/B=466-508.
PDB; 5PZH; X-ray; 1.63 A; A/B=466-508.
PDB; 5PZI; X-ray; 1.62 A; A/B=466-508.
PDB; 5PZJ; X-ray; 1.72 A; A/B=466-508.
PDBsum; 1H5P; -.
PDBsum; 4PTB; -.
PDBsum; 5FB0; -.
PDBsum; 5FB1; -.
PDBsum; 5PWE; -.
PDBsum; 5PWF; -.
PDBsum; 5PWG; -.
PDBsum; 5PWH; -.
PDBsum; 5PWI; -.
PDBsum; 5PWJ; -.
PDBsum; 5PWK; -.
PDBsum; 5PWL; -.
PDBsum; 5PWM; -.
PDBsum; 5PWN; -.
PDBsum; 5PWO; -.
PDBsum; 5PWP; -.
PDBsum; 5PWQ; -.
PDBsum; 5PWR; -.
PDBsum; 5PWS; -.
PDBsum; 5PWT; -.
PDBsum; 5PWU; -.
PDBsum; 5PWV; -.
PDBsum; 5PWW; -.
PDBsum; 5PWX; -.
PDBsum; 5PWY; -.
PDBsum; 5PWZ; -.
PDBsum; 5PX0; -.
PDBsum; 5PX1; -.
PDBsum; 5PX2; -.
PDBsum; 5PX3; -.
PDBsum; 5PX4; -.
PDBsum; 5PX5; -.
PDBsum; 5PX6; -.
PDBsum; 5PX7; -.
PDBsum; 5PX8; -.
PDBsum; 5PX9; -.
PDBsum; 5PXA; -.
PDBsum; 5PXB; -.
PDBsum; 5PXC; -.
PDBsum; 5PXD; -.
PDBsum; 5PXE; -.
PDBsum; 5PXF; -.
PDBsum; 5PXG; -.
PDBsum; 5PXH; -.
PDBsum; 5PXI; -.
PDBsum; 5PXJ; -.
PDBsum; 5PXK; -.
PDBsum; 5PXL; -.
PDBsum; 5PXM; -.
PDBsum; 5PXN; -.
PDBsum; 5PXO; -.
PDBsum; 5PXP; -.
PDBsum; 5PXQ; -.
PDBsum; 5PXR; -.
PDBsum; 5PXS; -.
PDBsum; 5PXT; -.
PDBsum; 5PXU; -.
PDBsum; 5PXV; -.
PDBsum; 5PXW; -.
PDBsum; 5PXX; -.
PDBsum; 5PXY; -.
PDBsum; 5PXZ; -.
PDBsum; 5PY0; -.
PDBsum; 5PY1; -.
PDBsum; 5PY2; -.
PDBsum; 5PY3; -.
PDBsum; 5PY4; -.
PDBsum; 5PY5; -.
PDBsum; 5PY6; -.
PDBsum; 5PY7; -.
PDBsum; 5PY8; -.
PDBsum; 5PY9; -.
PDBsum; 5PYA; -.
PDBsum; 5PYB; -.
PDBsum; 5PYC; -.
PDBsum; 5PYD; -.
PDBsum; 5PYE; -.
PDBsum; 5PYF; -.
PDBsum; 5PYG; -.
PDBsum; 5PYH; -.
PDBsum; 5PYI; -.
PDBsum; 5PYJ; -.
PDBsum; 5PYK; -.
PDBsum; 5PYL; -.
PDBsum; 5PYM; -.
PDBsum; 5PYN; -.
PDBsum; 5PYO; -.
PDBsum; 5PYP; -.
PDBsum; 5PYQ; -.
PDBsum; 5PYR; -.
PDBsum; 5PYS; -.
PDBsum; 5PYT; -.
PDBsum; 5PYU; -.
PDBsum; 5PYV; -.
PDBsum; 5PYW; -.
PDBsum; 5PYX; -.
PDBsum; 5PYY; -.
PDBsum; 5PYZ; -.
PDBsum; 5PZ0; -.
PDBsum; 5PZ1; -.
PDBsum; 5PZ2; -.
PDBsum; 5PZ3; -.
PDBsum; 5PZ4; -.
PDBsum; 5PZ5; -.
PDBsum; 5PZ6; -.
PDBsum; 5PZ7; -.
PDBsum; 5PZ8; -.
PDBsum; 5PZ9; -.
PDBsum; 5PZA; -.
PDBsum; 5PZB; -.
PDBsum; 5PZC; -.
PDBsum; 5PZD; -.
PDBsum; 5PZE; -.
PDBsum; 5PZF; -.
PDBsum; 5PZG; -.
PDBsum; 5PZH; -.
PDBsum; 5PZI; -.
PDBsum; 5PZJ; -.
ProteinModelPortal; P23497; -.
SMR; P23497; -.
BioGrid; 112555; 56.
DIP; DIP-5983N; -.
IntAct; P23497; 38.
MINT; MINT-1188807; -.
STRING; 9606.ENSP00000343023; -.
iPTMnet; P23497; -.
PhosphoSitePlus; P23497; -.
BioMuta; SP100; -.
DMDM; 13878931; -.
EPD; P23497; -.
MaxQB; P23497; -.
PaxDb; P23497; -.
PeptideAtlas; P23497; -.
PRIDE; P23497; -.
Ensembl; ENST00000264052; ENSP00000264052; ENSG00000067066. [P23497-1]
Ensembl; ENST00000340126; ENSP00000343023; ENSG00000067066. [P23497-4]
Ensembl; ENST00000409112; ENSP00000386427; ENSG00000067066. [P23497-3]
Ensembl; ENST00000409341; ENSP00000386404; ENSG00000067066. [P23497-2]
Ensembl; ENST00000409897; ENSP00000386998; ENSG00000067066. [P23497-7]
Ensembl; ENST00000427101; ENSP00000399389; ENSG00000067066. [P23497-6]
GeneID; 6672; -.
KEGG; hsa:6672; -.
UCSC; uc002vqq.3; human. [P23497-1]
CTD; 6672; -.
DisGeNET; 6672; -.
EuPathDB; HostDB:ENSG00000067066.16; -.
GeneCards; SP100; -.
HGNC; HGNC:11206; SP100.
HPA; HPA016707; -.
HPA; HPA017384; -.
MIM; 604585; gene.
neXtProt; NX_P23497; -.
OpenTargets; ENSG00000067066; -.
PharmGKB; PA36043; -.
eggNOG; KOG2177; Eukaryota.
eggNOG; ENOG4111G04; LUCA.
GeneTree; ENSGT00510000046835; -.
HOGENOM; HOG000089984; -.
HOVERGEN; HBG057632; -.
InParanoid; P23497; -.
KO; K15413; -.
OMA; AGRETPC; -.
OrthoDB; EOG091G01MN; -.
PhylomeDB; P23497; -.
TreeFam; TF335091; -.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-877300; Interferon gamma signaling.
ChiTaRS; SP100; human.
EvolutionaryTrace; P23497; -.
GenomeRNAi; 6672; -.
PRO; PR:P23497; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000067066; -.
CleanEx; HS_SP100; -.
ExpressionAtlas; P23497; baseline and differential.
Genevisible; P23497; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0034399; C:nuclear periphery; IDA:BHF-UCL.
GO; GO:0005730; C:nucleolus; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0016605; C:PML body; IDA:BHF-UCL.
GO; GO:0070087; F:chromo shadow domain binding; IPI:BHF-UCL.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019900; F:kinase binding; IPI:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; IDA:BHF-UCL.
GO; GO:0003714; F:transcription corepressor activity; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:BHF-UCL.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0045185; P:maintenance of protein location; IDA:BHF-UCL.
GO; GO:0051271; P:negative regulation of cellular component movement; IMP:BHF-UCL.
GO; GO:0043392; P:negative regulation of DNA binding; IDA:BHF-UCL.
GO; GO:0010596; P:negative regulation of endothelial cell migration; IMP:UniProtKB.
GO; GO:0046826; P:negative regulation of protein export from nucleus; IMP:UniProtKB.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0032897; P:negative regulation of viral transcription; IDA:BHF-UCL.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0045765; P:regulation of angiogenesis; IMP:UniProtKB.
GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:UniProtKB.
GO; GO:1902044; P:regulation of Fas signaling pathway; IMP:UniProtKB.
GO; GO:0034097; P:response to cytokine; IDA:BHF-UCL.
GO; GO:0034341; P:response to interferon-gamma; IDA:BHF-UCL.
GO; GO:0032526; P:response to retinoic acid; IDA:BHF-UCL.
GO; GO:0034340; P:response to type I interferon; IDA:BHF-UCL.
GO; GO:0048384; P:retinoic acid receptor signaling pathway; IC:BHF-UCL.
GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0060337; P:type I interferon signaling pathway; IC:BHF-UCL.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.10.30.10; -; 2.
Gene3D; 3.10.390.10; -; 1.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR036910; HMG_box_dom_sf.
InterPro; IPR004865; HSR_dom.
InterPro; IPR000770; SAND_dom.
InterPro; IPR010919; SAND_dom-like.
Pfam; PF00505; HMG_box; 1.
Pfam; PF09011; HMG_box_2; 1.
Pfam; PF03172; HSR; 1.
Pfam; PF01342; SAND; 1.
SMART; SM00398; HMG; 2.
SMART; SM00258; SAND; 1.
SUPFAM; SSF47095; SSF47095; 2.
SUPFAM; SSF63763; SSF63763; 1.
PROSITE; PS50118; HMG_BOX_2; 2.
PROSITE; PS51414; HSR; 1.
PROSITE; PS50864; SAND; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Cytoplasm; DNA-binding; Host-virus interaction;
Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transcription; Transcription regulation;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 879 Nuclear autoantigen Sp-100.
/FTId=PRO_0000074096.
DOMAIN 33 149 HSR. {ECO:0000255|PROSITE-
ProRule:PRU00747}.
DOMAIN 595 676 SAND. {ECO:0000255|PROSITE-
ProRule:PRU00185}.
DNA_BIND 677 753 HMG box 1. {ECO:0000255|PROSITE-
ProRule:PRU00267}.
DNA_BIND 769 837 HMG box 2. {ECO:0000255|PROSITE-
ProRule:PRU00267}.
REGION 333 478 Sufficient to mediate interaction with
ETS1.
MOTIF 165 168 D-box; recognition signal for CDC20-
mediated degradation.
MOTIF 284 297 PxVxL motif.
MOTIF 536 553 Nuclear localization signal.
{ECO:0000255}.
MOTIF 568 592 Nuclear localization signal.
{ECO:0000255}.
MOTIF 717 734 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 3 6 Poly-Gly.
COMPBIAS 156 164 Poly-Glu.
COMPBIAS 759 764 Poly-Lys.
COMPBIAS 854 859 Poly-Lys.
COMPBIAS 860 868 Poly-Glu.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:24275569}.
MOD_RES 157 157 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 171 171 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 180 180 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 228 228 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 331 331 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 407 407 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 451 451 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 241 241 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 297 297 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:10212234}.
CROSSLNK 300 300 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 306 306 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 366 366 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 387 387 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 594 594 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 36 MAGGGGDLSTRRLNECISPVANEMNHLPAHSHDLQR -> M
(in isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045868.
VAR_SEQ 11 35 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045869.
VAR_SEQ 428 430 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045870.
VAR_SEQ 449 472 RFSSSDFSDLSNGEELQETCSSSL -> LKKKKKKKQCHPQ
PQPQRGLLEQS (in isoform SpAlt-C).
{ECO:0000305}.
/FTId=VSP_005982.
VAR_SEQ 473 879 Missing (in isoform SpAlt-C).
{ECO:0000305}.
/FTId=VSP_005983.
VAR_SEQ 478 480 SQP -> KED (in isoform Sp100-A, isoform 6
and isoform 7).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2258622}.
/FTId=VSP_005978.
VAR_SEQ 481 879 Missing (in isoform Sp100-A, isoform 6
and isoform 7).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2258622}.
/FTId=VSP_005979.
VAR_SEQ 685 688 RILE -> VMIK (in isoform Sp100-B).
{ECO:0000303|PubMed:8695863}.
/FTId=VSP_005980.
VAR_SEQ 689 879 Missing (in isoform Sp100-B).
{ECO:0000303|PubMed:8695863}.
/FTId=VSP_005981.
VAR_SEQ 699 879 EEHKKKNPDASVKFSEFLKKCSETWKTIFAKEKGKFEDMAK
ADKAHYEREMKTYIPPKGEKKKKFKDPNAPKRPPLAFFLFC
SEYRPKIKGEHPGLSIDDVVKKLAGMWNNTAAADKQFYEKK
AAKLKEKYKKDIAAYRAKGKPNSAKKRVVKAEKSKKKKEEE
EDEEDEQEEENEEDDDK -> PENSNICEVCNKWGRLFCCD
TCPRSFHEHCHIPSVEANKNPWSCIFCRIKTIQERCPESQS
GHQESEVLMRQMLPEEQLKCEFLLLKVYCDSKSCFFASEPY
YNREGSQGPQKPMWLNKVKTSLNEQMYTRVEGFVQDMRLIF
HNHKEFYREDKFTRLGIQVQDIFEKNFRNIFAIQETSKNII
MFI (in isoform Sp100-C).
{ECO:0000303|PubMed:11313457}.
/FTId=VSP_005984.
VARIANT 433 433 M -> V (in dbSNP:rs12724).
/FTId=VAR_005621.
VARIANT 471 471 S -> P.
/FTId=VAR_005622.
VARIANT 699 699 E -> G (in dbSNP:rs34700604).
/FTId=VAR_034510.
MUTAGEN 165 165 R->A: Prevents CDC20-mediated
degradation; when associated with Ala-
168. {ECO:0000269|PubMed:22086178}.
MUTAGEN 168 168 L->A: Prevents CDC20-mediated
degradation; when associated with Ala-
165. {ECO:0000269|PubMed:22086178}.
CONFLICT 47 47 R -> M (in Ref. 5; BAG56886).
{ECO:0000305}.
CONFLICT 247 247 S -> P (in Ref. 5; BAG56886).
{ECO:0000305}.
CONFLICT 402 402 Q -> H (in Ref. 5; BAG56886).
{ECO:0000305}.
CONFLICT 651 651 A -> R (in Ref. 9; AAL77438/AAL77439).
{ECO:0000305}.
HELIX 600 602 {ECO:0000244|PDB:1H5P}.
STRAND 603 609 {ECO:0000244|PDB:1H5P}.
STRAND 612 617 {ECO:0000244|PDB:1H5P}.
HELIX 618 621 {ECO:0000244|PDB:1H5P}.
HELIX 624 626 {ECO:0000244|PDB:1H5P}.
STRAND 630 632 {ECO:0000244|PDB:1H5P}.
TURN 633 635 {ECO:0000244|PDB:1H5P}.
STRAND 636 638 {ECO:0000244|PDB:1H5P}.
HELIX 640 647 {ECO:0000244|PDB:1H5P}.
HELIX 655 658 {ECO:0000244|PDB:1H5P}.
HELIX 666 672 {ECO:0000244|PDB:1H5P}.
STRAND 673 675 {ECO:0000244|PDB:1H5P}.
STRAND 703 705 {ECO:0000244|PDB:5FB1}.
TURN 706 708 {ECO:0000244|PDB:5FB1}.
STRAND 712 716 {ECO:0000244|PDB:5FB1}.
STRAND 718 721 {ECO:0000244|PDB:5FB1}.
STRAND 723 725 {ECO:0000244|PDB:5FB1}.
TURN 726 728 {ECO:0000244|PDB:5FB1}.
STRAND 729 731 {ECO:0000244|PDB:5FB1}.
HELIX 743 753 {ECO:0000244|PDB:5FB1}.
HELIX 763 768 {ECO:0000244|PDB:5FB1}.
HELIX 773 787 {ECO:0000244|PDB:5FB1}.
HELIX 790 795 {ECO:0000244|PDB:5FB1}.
HELIX 812 820 {ECO:0000244|PDB:5FB1}.
HELIX 827 839 {ECO:0000244|PDB:5FB1}.
HELIX 848 868 {ECO:0000244|PDB:5FB1}.
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


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