Entry euk: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   10-MAY-2017, entry version 126.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   GENOMIC ORGANIZATION.
RX   PubMed=9678363;
RA   Weichenhan D., Kunze B., Traut W., Winking H.;
RT   "Evolution by fusion and amplification: the murine Sp100-rs gene
RT   cluster.";
RL   Cytogenet. Cell Genet. 80:226-231(1998).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, AND IDENTIFICATION
RP   BY 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
RP   MASS 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
RT   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
CC       a 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
CC       also act as a corepressor of ETS1 preventing its binding to DNA.
CC       Through the regulation of ETS1 it may play a role in angiogenesis,
CC       controlling endothelial cell motility and invasion. Through
CC       interaction with the MRN complex it may be involved in the
CC       regulation of telomeres lengthening. May also regulate TP53-
CC       mediated transcription and through CASP8AP2, regulate FAS-mediated
CC       apoptosis. May also play a role in infection by viruses through
CC       mechanisms that may involve chromatin and/or transcriptional
CC       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
CC       PxVxL motif. Interacts with ETS1; the interaction is direct and
CC       modulates ETS1 transcriptional activity. Interacts with the MRN
CC       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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00185, ECO:0000255|PROSITE-ProRule:PRU00747}. Nucleus,
CC       PML body {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Accumulates
CC       in the cytoplasm upon FAS 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
CC       as 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
CC       requires additional residues -7, -6, +4 and +5 of the central Val
CC       which contact the chromoshadow domain.
CC   -!- PTM: Sumoylated. Sumoylated with SUMO1. Sumoylation depends on a
CC       functional nuclear localization signal but is not necessary for
CC       nuclear import or nuclear body targeting. Sumoylation may
CC       stabilize the interaction with CBX5 (By similarity).
CC       {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
CC       homologous from the promoter up to a position in intron 3, but
CC       they differ 3' of 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   UniGene; Mm.290906; -.
DR   UniGene; Mm.486514; -.
DR   ProteinModelPortal; O35892; -.
DR   SMR; O35892; -.
DR   STRING; 10090.ENSMUSP00000066399; -.
DR   iPTMnet; O35892; -.
DR   PhosphoSitePlus; O35892; -.
DR   EPD; O35892; -.
DR   MaxQB; O35892; -.
DR   PaxDb; O35892; -.
DR   PeptideAtlas; O35892; -.
DR   PRIDE; O35892; -.
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   eggNOG; KOG2177; Eukaryota.
DR   eggNOG; ENOG4111G04; LUCA.
DR   GeneTree; ENSGT00510000046835; -.
DR   HOGENOM; HOG000089984; -.
DR   HOVERGEN; HBG062077; -.
DR   InParanoid; O35892; -.
DR   KO; K15413; -.
DR   ChiTaRS; Sp100; mouse.
DR   PRO; PR:O35892; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000026222; -.
DR   CleanEx; MM_SP100; -.
DR   ExpressionAtlas; O35892; baseline and differential.
DR   Genevisible; O35892; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0016605; C:PML body; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR004865; HSR_dom.
DR   InterPro; IPR000770; SAND_dom.
DR   InterPro; IPR010919; SAND_dom-like.
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; Complete proteome; Cytoplasm; DNA-binding;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN         1    482       Nuclear autoantigen Sp-100.
FT                                /FTId=PRO_0000074098.
FT   DOMAIN        6    121       HSR. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00747}.
FT   DOMAIN      378    459       SAND. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00185}.
FT   MOTIF       230    243       PxVxL motif.
FT   MOD_RES     174    174       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     190    190       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     209    209       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     313    313       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     314    314       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     316    316       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     318    318       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     319    319       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CROSSLNK    243    243       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
FT   VAR_SEQ     312    330       DTSDTESSIIIRRRKRTGR -> G (in isoform 2).
FT                                {ECO:0000303|PubMed:9268632}.
FT                                /FTId=VSP_005985.
FT   CONFLICT     83     83       E -> D (in Ref. 1; AAC40174).
FT                                {ECO:0000305}.
FT   CONFLICT     91     92       MT -> IP (in Ref. 1; AAC40174).
FT                                {ECO:0000305}.
FT   CONFLICT    114    114       R -> K (in Ref. 1; AAC40174).
FT                                {ECO:0000305}.
FT   CONFLICT    117    117       G -> E (in Ref. 1; AAC40174).
FT                                {ECO:0000305}.
FT   CONFLICT    131    131       G -> R (in Ref. 1; AAC53512/AAC53513).
FT                                {ECO:0000305}.
FT   CONFLICT    204    206       NNR -> ITE (in Ref. 1; AAC40172).
FT                                {ECO:0000305}.
FT   CONFLICT    441    441       S -> T (in Ref. 1; AAC53512/AAC53513).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         6    121       iprf:HSR [T]
FT   MYHIT       378    459       iprf:SAND [T]
FT   MYHIT        23    117       ipfam:HSR [T]
FT   MYHIT       384    458       ipfam:SAND [T]
FT   MYHIT       386    459       ismart:SAND [T]
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
//