SP100_MUSCR
ID SP100_MUSCR Reviewed; 482 AA.
AC O35893; O35894; O35895; O35896; O35974; Q9QWH0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 25-MAY-2022, entry version 88.
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 caroli (Ryukyu mouse) (Ricefield mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10089;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC 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).
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=4;
CC Name=1;
CC IsoId=O35893-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35893-2; Sequence=VSP_005988;
CC Name=3;
CC IsoId=O35893-3; Sequence=VSP_005986, VSP_005987;
CC Name=4;
CC IsoId=O35893-4; Sequence=VSP_005989, VSP_005990;
CC -!- INDUCTION: By interferon.
CC -!- DOMAIN: The HSR domain is important for the nuclear body targeting as
CC well as for the dimerization.
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 -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; U83629; AAC53506.1; -; mRNA.
DR EMBL; U83631; AAC53507.1; -; mRNA.
DR EMBL; U83632; AAC53508.1; -; mRNA.
DR EMBL; U83633; AAC53509.1; -; mRNA.
DR EMBL; U83634; AAC53510.1; -; mRNA.
DR EMBL; U83635; AAC53511.1; -; mRNA.
DR EMBL; U83654; AAC12948.1; -; Genomic_DNA.
DR EMBL; U83638; AAC12948.1; JOINED; Genomic_DNA.
DR EMBL; U83639; AAC12948.1; JOINED; Genomic_DNA.
DR EMBL; U83640; AAC12948.1; JOINED; Genomic_DNA.
DR EMBL; U83642; AAC12948.1; JOINED; Genomic_DNA.
DR EMBL; U83643; AAC12948.1; JOINED; Genomic_DNA.
DR EMBL; U83644; AAC12948.1; JOINED; Genomic_DNA.
DR EMBL; U83645; AAC12948.1; JOINED; Genomic_DNA.
DR EMBL; U83646; AAC12948.1; JOINED; Genomic_DNA.
DR EMBL; U83647; AAC12948.1; JOINED; Genomic_DNA.
DR EMBL; U83648; AAC12948.1; JOINED; Genomic_DNA.
DR EMBL; U83649; AAC12948.1; JOINED; Genomic_DNA.
DR EMBL; U83650; AAC12948.1; JOINED; Genomic_DNA.
DR EMBL; U83651; AAC12948.1; JOINED; Genomic_DNA.
DR EMBL; U83652; AAC12948.1; JOINED; Genomic_DNA.
DR EMBL; U83653; AAC12948.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; O35893; -.
DR SMR; O35893; -.
DR MGI; MGI:109561; Sp100.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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: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: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 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..482
FT /note="Nuclear autoantigen Sp-100"
FT /id="PRO_0000074099"
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 131..171
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..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 230..243
FT /note="PxVxL motif"
FT MOTIF 309..326
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 250..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35892"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35892"
FT MOD_RES 209
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35892"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35892"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35892"
FT MOD_RES 316
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35892"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35892"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35892"
FT CROSSLNK 243
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 222..225
FT /note="RAVQ -> SNYC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9268632"
FT /id="VSP_005986"
FT VAR_SEQ 226..482
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9268632"
FT /id="VSP_005987"
FT VAR_SEQ 269..302
FT /note="VIELSSGDSDDGENFSEATTTIPSQPAPAYSRTP -> NSAVGILMMERTSQ
FT KLQPQSPPSQRLHIPEHLQH (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9268632"
FT /id="VSP_005989"
FT VAR_SEQ 303..482
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9268632"
FT /id="VSP_005990"
FT VAR_SEQ 312..330
FT /note="DTSDTESSIIIRRRKRTGR -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9268632"
FT /id="VSP_005988"
FT CONFLICT 61
FT /note="Y -> H (in Ref. 1; AAC53509)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="I -> V (in Ref. 1; AAC53509)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="K -> R (in Ref. 1; AAC53508)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="N -> D (in Ref. 1; AAC53510)"
FT /evidence="ECO:0000305"
FT CONFLICT 118..119
FT /note="CV -> L (in Ref. 1; AAC53511)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="N -> D (in Ref. 1; AAC53508)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="Q -> P (in Ref. 1; AAC53511)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="Q -> R (in Ref. 1; AAC53509)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="A -> V (in Ref. 1; AAC12948/AAC53506)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="A -> V (in Ref. 1; AAC12948/AAC53506/AAC53509)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="V -> S (in Ref. 1; AAC12948/AAC53506)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="K -> Q (in Ref. 1; AAC12948/AAC53506)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="N -> T (in Ref. 1; AAC12948/AAC53506)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 55168 MW; 7A9B40576CE98686 CRC64;
MEDSNASPRM STEHENTEMH PFEYMFKHFK TQKVAISNAI RSTFPFLESL RDREFITGKM
YEDLIDSCRS LVPVDKVIYK ALDELEKKFD VTVLWELFNE VNMEKYPDLN PIRRSFECVF
PNELSFQGID RGNPNSQLSL EQGPSASYSQ GSLNGSSLDL SSSEGWRSND RRNSNLMQAN
QTENHQLAES PGHLDSCELQ VQLNNGDATP ESYSLLPQHE ERAVQLNNEF QINPCFVQLI
DVKKENSSFS LAGNQQTRAR TNQNEDSEVI ELSSGDSDDG ENFSEATTTI PSQPAPAYSR
TPPTLRTDRR GDTSDTESSI IIRRRKRTGR KKRERLGSYL IRNIKIPMKT SWKTAVLARS
ANTSSQRRRK RGPRIPREEN ADFGGAELPA VCGNVQGFLN KEKFKQGIYV RSIRSETGRL
FTPMDFEIEG NCEKAKNWRQ TIRCKGWTLR ELIQKGVLQD PPRKKKENPR NPRQMKRQVN
AL
