ID M3XZK4_MUSPF Unreviewed; 825 AA.
AC M3XZK4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=SP100 nuclear antigen {ECO:0000313|Ensembl:ENSMPUP00000004505.1};
GN Name=SP100 {ECO:0000313|Ensembl:ENSMPUP00000004505.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000004505.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000004505.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AEYP01081289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01081290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01081291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01081292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01081293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3XZK4; -.
DR STRING; 9669.ENSMPUP00000004505; -.
DR Ensembl; ENSMPUT00000004584.1; ENSMPUP00000004505.1; ENSMPUG00000004541.1.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000162212; -.
DR HOGENOM; CLU_015844_1_0_1; -.
DR InParanoid; M3XZK4; -.
DR OMA; AGMWNNT; -.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0030870; C:Mre11 complex; IEA:Ensembl.
DR GO; GO:0016605; C:PML body; IEA:Ensembl.
DR GO; GO:0070087; F:chromo shadow domain binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:Ensembl.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045765; P:regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:1902044; P:regulation of Fas signaling pathway; IEA:Ensembl.
DR GO; GO:0034340; P:response to type I interferon; IEA:Ensembl.
DR GO; GO:0034341; P:response to type II interferon; IEA:Ensembl.
DR GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR CDD; cd15626; PHD_SP110_140; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.10.390.10; SAND domain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR004865; HSR_dom.
DR InterPro; IPR010919; SAND-like_dom_sf.
DR InterPro; IPR000770; SAND_dom.
DR InterPro; IPR043563; Sp110/Sp140/Sp140L-like.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46386:SF1; NUCLEAR AUTOANTIGEN SP-100; 1.
DR PANTHER; PTHR46386; NUCLEAR BODY PROTEIN SP140; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF03172; HSR; 1.
DR Pfam; PF01342; SAND; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00258; SAND; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63763; SAND domain-like; 1.
DR PROSITE; PS51414; HSR; 1.
DR PROSITE; PS50864; SAND; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 8..124
FT /note="HSR"
FT /evidence="ECO:0000259|PROSITE:PS51414"
FT DOMAIN 533..614
FT /note="SAND"
FT /evidence="ECO:0000259|PROSITE:PS50864"
FT DOMAIN 641..687
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 156..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 94479 MW; 6855ECA5138E0310 CRC64;
MADGGSGFST RTSTEDQYND DRLVYETLFK HFKRHKVEIS NAIKKPFPFF ECLRDRELIS
NKMYDDCQDS CRNLVPVPRV AYNVLNELEK TFDLPLLEAL FSEVNRQEYP NLNHIYKSFE
FAIQEKINYQ ESDEEEVDNS PHTQLSIEQG TGENCYRSLT SSCPQSSSDH GTAPSENGPL
ENLCEAEQIN GNRTDTTSDK NDAQEVQQAN EEYAQESEPA ESCEQEPIQV NNRDTREDTP
IPLPCDGKSS PLSNHGIQVN SCSVHLVDIK KEKPFFSSTL NQASDVIVIS SDSEETSDED
KAPEDSMSTL ESGPAKRFAE YLESSEDEGP PRASCFVLRS DTDEEDPVDI GNKSLWGIPK
RKRYSLDNQG NWKRKCVATS GEGISSANYS ELSDTEEPQE SSSSVLRSGS GAEPQGLGSA
KCSCVMCFSE GISRDQGERT ESSQASDIMD TVDIGNNSTS GKHNEKIRRK RRHIHKKNNL
QKDEVLVRRR GRHRIQTLSN RVLWNRGKQK GRKPVITRSL RRGRKRGPRI PRDTRINFYL
LELPVTCGEA KGTLYKEKMI QGTSEKCIQG VDGRWFTLRE FEVEGKYSRS KNWKTSVRCG
GFTLKDLIKK KYLPEPPRRR RRKQTTPEPS KDFFDPYPGN SNICEVCRRP GKLFCCDTCP
KSFHETCHIH HIDVNREPWS CIFCMIKALQ PSQQCHQISE VLQRRMVPEE QLKCEFVLLK
VYCCSKSPFF ASRPHYSNNA SHGPTKLMWL NKIKKKLNKK LYLRVKGFVQ DMCLIFENHR
AFYKDNQKFI KLGFQLEDIF MNTFGNIFAI QEIREHSFQL DPTLS
//
