Entry sw:SP100_PANTR

ID   SP100_PANTR             Reviewed;         215 AA.
AC   Q9N1Q7;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   05-OCT-2016, entry version 78.
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   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598;
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: Phosphorylated. {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   -!- 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; AF169946; AAF43108.1; -; mRNA.
DR   UniGene; Ptr.6635; -.
DR   ProteinModelPortal; Q9N1Q7; -.
DR   PRIDE; Q9N1Q7; -.
DR   HOGENOM; HOG000197861; -.
DR   HOVERGEN; HBG009000; -.
DR   InParanoid; Q9N1Q7; -.
DR   Proteomes; UP000002277; Unplaced.
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   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; Complete proteome; Cytoplasm; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN        <1   >215       Nuclear autoantigen Sp-100.
FT                                /FTId=PRO_0000074100.
FT   DOMAIN       <1     31       SAND. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00185}.
FT   DNA_BIND     32    108       HMG box 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00267}.
FT   DNA_BIND    124    192       HMG box 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00267}.
FT   MOTIF        72     89       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   COMPBIAS     57    215       Asp/Glu/Lys-rich.
FT   NON_TER       1      1
FT   NON_TER     215    215
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         2     30       ipfam:SAND [T]
FT   MYHIT        53    107       ipfam:HMG_box_2 [T]
FT   MYHIT        37    109       ismart:HMG [T]
FT   MYHIT       124    192       iprf:HMG_BOX_2 [T]
FT   MYHIT        31    108       iprf:HMG_BOX_2 [T]
FT   MYHIT       123    193       ismart:HMG [T]
FT   MYHIT       124    190       ipfam:HMG_box [T]
FT   MYHIT         1     31       iprf:SAND [T]
SQ   SEQUENCE   215 AA;  24766 MW;  A639D7FE601B5B73 CRC64;
     EGDRGASKNW KLSIRCGGYT LKVLTENKFL PEPPSTRKKR ILESHNNTLV DPCEEHKKKN
     PDASVKFSEF LKKRSEMWKT IFAKEKGKFE DMAKADKAHY EREMKTYIPP KGEKKKKFKD
     PNAPKRPPLA FFLFCSEYRP KIKGEHPGLS IDDVVKKLAG MWNNTAASDK QFYEKKAAKL
     KEKYKKDIAA CRAKGKPNSA TKRVVKAEKS KKKKE
//