SP100_HYLLA
ID SP100_HYLLA Reviewed; 242 AA.
AC Q9N1Q5;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Nuclear autoantigen Sp-100;
DE AltName: Full=Nuclear dot-associated Sp100 protein;
DE AltName: Full=Speckled 100 kDa;
DE Flags: Fragment;
GN Name=SP100;
OS Hylobates lar (Common gibbon) (White-handed gibbon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Hylobates.
OX NCBI_TaxID=9580;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
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).
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:PRU00267}. Nucleus, PML body {ECO:0000250}.
CC Cytoplasm {ECO:0000250}. Note=Accumulates in the cytoplasm upon FAS
CC activation. {ECO:0000250}.
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; AF169948; AAF43110.1; -; mRNA.
DR AlphaFoldDB; Q9N1Q5; -.
DR SMR; Q9N1Q5; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
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:0000723; P:telomere maintenance; ISS:UniProtKB.
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; IPR010919; SAND-like_dom_sf.
DR InterPro; IPR000770; SAND_dom.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF09011; HMG_box_2; 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; PS50864; SAND; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN <1..>242
FT /note="Nuclear autoantigen Sp-100"
FT /id="PRO_0000074097"
FT DOMAIN <1..50
FT /note="SAND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00185"
FT DNA_BIND 51..127
FT /note="HMG box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT DNA_BIND 143..211
FT /note="HMG box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 205..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 91..108
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 242
SQ SEQUENCE 242 AA; 28174 MW; 472AE2B4B47CCF22 CRC64;
KKCIQSEDKK WFTPREFEIE GDRRASKNWK LSIRCGGYTL KFLMENKLLP EPPSTRKKRI
LKSHNNTLVD PCAVHKKKNP DASVNLSEFL KKCSEMWKTI FAKEKGKFED MAKADKAHYE
REMKTYIPSK GEKKKKFKDP NAPKRPPLAF FLFCSEYRPK IKGEHPGLSI DDVVKKLAEM
WNNTAAADKQ FYEKKAAKLK EKYKKDIAAD RAKGKPNSAK KRVVKAEKSK KKKEEEEDEV
DE
