SP100_MOUSE
ID SP100_MOUSE Reviewed; 482 AA.
AC O35892; E9PY02; O35897; O88392; O88395;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=9268632; DOI=10.1006/geno.1997.4834;
RA Weichenhan D., Kunze B., Zacker S., Traut W., Winking H.;
RT "Structure and expression of the murine Sp100 nuclear dot gene.";
RL Genomics 43:298-306(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP GENOMIC ORGANIZATION.
RX PubMed=9678363; DOI=10.1159/000014985;
RA Weichenhan D., Kunze B., Traut W., Winking H.;
RT "Evolution by fusion and amplification: the murine Sp100-rs gene cluster.";
RL Cytogenet. Cell Genet. 80:226-231(1998).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-190; THR-209;
RP THR-313; SER-314; THR-316; SER-318 AND SER-319, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Under certain conditions, it may also act
CC as a corepressor of ETS1 preventing its binding to DNA. Through the
CC regulation of ETS1 it may play a role in angiogenesis, controlling
CC endothelial cell motility and invasion. Through interaction with the
CC MRN complex it may be involved in the regulation of telomeres
CC lengthening. May also regulate TP53-mediated transcription and through
CC CASP8AP2, regulate FAS-mediated apoptosis. May also play a role in
CC infection by viruses through mechanisms that may involve chromatin
CC and/or transcriptional regulation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with members of the HP1 family of
CC nonhistone chromosomal protein, such as CBX5 and CBX3 via the PxVxL
CC motif. Interacts with ETS1; the interaction is direct and modulates
CC ETS1 transcriptional activity. Interacts with the MRN complex which is
CC composed of two heterodimers RAD50/MRE11 associated with a single NBN;
CC recruits the complex to PML-related bodies. Interacts with HIPK2;
CC positively regulates TP53-dependent transcription. Interacts with
CC CASP8AP2; may negatively regulate CASP8AP2 export from the nucleus to
CC the cytoplasm (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00185,
CC ECO:0000255|PROSITE-ProRule:PRU00747}. Nucleus, PML body {ECO:0000250}.
CC Cytoplasm {ECO:0000250}. Note=Accumulates in the cytoplasm upon FAS
CC activation. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O35892-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35892-2; Sequence=VSP_005985;
CC -!- INDUCTION: By interferon.
CC -!- DOMAIN: The HSR domain is important for the nuclear body targeting as
CC well as for the dimerization. {ECO:0000250}.
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.
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 (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Sp100 is a single-copy gene. A related gene,
CC D1LUB1/Sp100-rs, occurs in multiple copies and forms a conspicuous
CC cluster in the chromosome 1. Sp100 and D1LUB1/Sp100-rs are homologous
CC from the promoter up to a position in intron 3, but they differ 3' of
CC that position.
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DR EMBL; U83630; AAC53512.1; -; mRNA.
DR EMBL; U83636; AAC53513.1; -; mRNA.
DR EMBL; AF040242; AAC40172.1; -; Genomic_DNA.
DR EMBL; AF040241; AAC40172.1; JOINED; Genomic_DNA.
DR EMBL; AF038850; AAC40174.1; -; Genomic_DNA.
DR EMBL; AC147806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS83568.1; -. [O35892-1]
DR CCDS; CCDS83569.1; -. [O35892-2]
DR RefSeq; NP_001300641.1; NM_001313712.1. [O35892-1]
DR RefSeq; NP_001300642.1; NM_001313713.1. [O35892-2]
DR AlphaFoldDB; O35892; -.
DR SMR; O35892; -.
DR IntAct; O35892; 1.
DR STRING; 10090.ENSMUSP00000066399; -.
DR iPTMnet; O35892; -.
DR PhosphoSitePlus; O35892; -.
DR SwissPalm; O35892; -.
DR EPD; O35892; -.
DR jPOST; O35892; -.
DR MaxQB; O35892; -.
DR PaxDb; O35892; -.
DR PeptideAtlas; O35892; -.
DR PRIDE; O35892; -.
DR ProteomicsDB; 257544; -. [O35892-1]
DR ProteomicsDB; 257545; -. [O35892-2]
DR Antibodypedia; 1754; 160 antibodies from 26 providers.
DR DNASU; 20684; -.
DR Ensembl; ENSMUST00000147552; ENSMUSP00000116942; ENSMUSG00000026222. [O35892-2]
DR Ensembl; ENSMUST00000155094; ENSMUSP00000118481; ENSMUSG00000026222. [O35892-1]
DR GeneID; 20684; -.
DR KEGG; mmu:20684; -.
DR UCSC; uc007buf.1; mouse. [O35892-1]
DR CTD; 6672; -.
DR MGI; MGI:109561; Sp100.
DR VEuPathDB; HostDB:ENSMUSG00000026222; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000162129; -.
DR InParanoid; O35892; -.
DR OrthoDB; 377499at2759; -.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR BioGRID-ORCS; 20684; 1 hit in 45 CRISPR screens.
DR ChiTaRS; Sp100; mouse.
DR PRO; PR:O35892; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O35892; protein.
DR Bgee; ENSMUSG00000026222; Expressed in granulocyte and 127 other tissues.
DR ExpressionAtlas; O35892; baseline and differential.
DR Genevisible; O35892; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030870; C:Mre11 complex; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0034399; C:nuclear periphery; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0070087; F:chromo shadow domain binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISO:MGI.
DR GO; GO:0045185; P:maintenance of protein location; ISO:MGI.
DR GO; GO:0043392; P:negative regulation of DNA binding; ISO:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0032897; P:negative regulation of viral transcription; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISS:UniProtKB.
DR GO; GO:1902044; P:regulation of Fas signaling pathway; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR GO; GO:0034341; P:response to interferon-gamma; ISO:MGI.
DR GO; GO:0032526; P:response to retinoic acid; ISO:MGI.
DR GO; GO:0034340; P:response to type I interferon; ISO:MGI.
DR GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
DR Gene3D; 3.10.390.10; -; 1.
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; PF03172; HSR; 1.
DR Pfam; PF01342; SAND; 1.
DR SMART; SM00258; SAND; 1.
DR SUPFAM; SSF63763; SSF63763; 1.
DR PROSITE; PS51414; HSR; 1.
DR PROSITE; PS50864; SAND; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..482
FT /note="Nuclear autoantigen Sp-100"
FT /id="PRO_0000074098"
FT DOMAIN 6..121
FT /note="HSR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00747"
FT DOMAIN 378..459
FT /note="SAND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00185"
FT REGION 136..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 230..243
FT /note="PxVxL motif"
FT COMPBIAS 250..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 209
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 316
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 243
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 312..330
FT /note="DTSDTESSIIIRRRKRTGR -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9268632"
FT /id="VSP_005985"
FT CONFLICT 83
FT /note="E -> D (in Ref. 1; AAC40174)"
FT /evidence="ECO:0000305"
FT CONFLICT 91..92
FT /note="MT -> IP (in Ref. 1; AAC40174)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="R -> K (in Ref. 1; AAC40174)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="G -> E (in Ref. 1; AAC40174)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="G -> R (in Ref. 1; AAC53512/AAC53513)"
FT /evidence="ECO:0000305"
FT CONFLICT 204..206
FT /note="NNR -> ITE (in Ref. 1; AAC40172)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="S -> T (in Ref. 1; AAC53512/AAC53513)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 54727 MW; 4F41E481AE655412 CRC64;
MEGSDGSPRM STEQENTEMH LIECMLKHFK TQKVAISNAI RSTFPFLESL RDHEFITGKM
YEDLLDSCRS LVPVDKVIYR ALEELEKKFD MTVLCELFNE VNMEKYPDLN LIRRSFGCVF
PNELCFQGID GGNPNSQLSL EQGPGASYSQ GSPNGSSLDL SASEGWRSND RRNSNLMQAN
QTENHQLAES PGHLDSCELQ VQLNNRDATP ESCSLLPQNE ERAVQLNYEL QINPCFVQLV
DVKKENSSFS LAGNQQTRAR TNQNEDSEII ELSSGDSDNG ENFSEATTTV PSQPAPAYSR
KPPTLRRDRG GDTSDTESSI IIRRRKRTGR KKRERLGSYL IRNIKIPMKP SWKTAFLARS
ANPSSQRRRK RGPRIPREEN ADFGGAELPV VCGNAQGFLD KEKFKQGIYV RSIRGKTGRL
FTPMDFEIEG NCEKAKNWRQ SIRCKGWTLR ELIQKGVLQD PPRKKKETPR NPRQTRRQVN
AL
