Entry sw: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   05-OCT-2016, entry version 72.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hylobatidae; 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
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/MRE11A
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:PRU00267}. Nucleus,
CC       PML body {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Accumulates
CC       in the cytoplasm upon FAS activation. {ECO:0000250}.
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   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Contains 2 HMG box DNA-binding domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC   -!- SIMILARITY: Contains 1 SAND domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00185}.
DR   EMBL; AF169948; AAF43110.1; -; mRNA.
DR   ProteinModelPortal; Q9N1Q5; -.
DR   PRIDE; Q9N1Q5; -.
DR   HOVERGEN; HBG009000; -.
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:0006954; P:inflammatory response; IEA:InterPro.
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   Gene3D; 1.10.30.10; -; 2.
DR   Gene3D; 3.10.390.10; -; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR031076; HMGB1.
DR   InterPro; IPR000770; SAND_dom.
DR   InterPro; IPR010919; SAND_dom-like.
DR   PANTHER; PTHR13711:SF157; PTHR13711:SF157; 1.
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       Nuclear autoantigen Sp-100.
FT                                /FTId=PRO_0000074097.
FT   DOMAIN       <1     50       SAND. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00185}.
FT   DNA_BIND     51    127       HMG box 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00267}.
FT   DNA_BIND    143    211       HMG box 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00267}.
FT   MOTIF        91    108       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   COMPBIAS     76    242       Asp/Glu/Lys-rich.
FT   NON_TER       1      1
FT   NON_TER     242    242
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         1     50       ismart:SAND [T]
FT   MYHIT        50    127       iprf:HMG_BOX_2 [T]
FT   MYHIT         1     49       ipfam:SAND [T]
FT   MYHIT        59    128       ismart:HMG [T]
FT   MYHIT       143    211       iprf:HMG_BOX_2 [T]
FT   MYHIT         1     50       iprf:SAND [T]
FT   MYHIT        74    126       ipfam:HMG_box_2 [T]
FT   MYHIT       143    208       ipfam:HMG_box [T]
FT   MYHIT       142    212       ismart:HMG [T]
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
//