ID Q15156_HUMAN Unreviewed; 797 AA. AC Q15156; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 164. DE SubName: Full=PML-RAR protein {ECO:0000313|EMBL:AAA60126.1}; GN Name=PML-RAR {ECO:0000313|EMBL:AAA60126.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAA60126.1}; RN [1] {ECO:0000313|EMBL:AAA60126.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=1652368; DOI=10.1016/0092-8674(91)90112-C; RA Kakizuka A., Miller W.H. Jr., Umenono K., Warrell R.P. Jr., Frankel S.R., RA Murty V.V., Dmitrovsky E., Evans R.M.; RT "Chromosomal translocation t(15;17) in human acute promyelocytic leukemia RT fuses RAR alpha with a novel putative transcription factor, PML."; RL Cell 66:663-674(1991). CC -!- INTERACTION: CC Q15156; O75530: EED; NbExp=2; IntAct=EBI-867256, EBI-923794; CC Q15156; Q15910: EZH2; NbExp=8; IntAct=EBI-867256, EBI-530054; CC Q15156; P25445: FAS; NbExp=6; IntAct=EBI-867256, EBI-494743; CC Q15156; Q9UIS9: MBD1; NbExp=4; IntAct=EBI-867256, EBI-867196; CC Q15156; Q9Y618: NCOR2; NbExp=2; IntAct=EBI-867256, EBI-80830; CC Q15156; Q9UPP1-2: PHF8; NbExp=6; IntAct=EBI-867256, EBI-6601215; CC Q15156; P17947: SPI1; NbExp=20; IntAct=EBI-867256, EBI-2293548; CC Q15156; Q15022: SUZ12; NbExp=6; IntAct=EBI-867256, EBI-1264675; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU004334}. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 CC subfamily. {ECO:0000256|ARBA:ARBA00008092}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M73779; AAA60126.1; -; mRNA. DR PIR; C40045; C40045. DR AlphaFoldDB; Q15156; -. DR SMR; Q15156; -. DR IntAct; Q15156; 10. DR MaxQB; Q15156; -. DR PeptideAtlas; Q15156; -. DR ChiTaRS; PRAM1; human. DR GO; GO:0031264; C:death-inducing signaling complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt. DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB. DR GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IEA:InterPro. DR CDD; cd19804; Bbox1_TRIM19_C-V; 1. DR CDD; cd19770; Bbox2_TRIM19_C-V; 1. DR CDD; cd06964; NR_DBD_RAR; 1. DR CDD; cd06937; NR_LBD_RAR; 1. DR CDD; cd16579; RING-HC_PML_C-V; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1. DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR035500; NHR-like_dom_sf. DR InterPro; IPR047159; NR_DBD_RAR. DR InterPro; IPR047158; NR_LBD_RAR. DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd. DR InterPro; IPR001723; Nuclear_hrmn_rcpt. DR InterPro; IPR021978; PML-like_CC. DR InterPro; IPR003078; Retinoic_acid_rcpt. DR InterPro; IPR000315; Znf_B-box. DR InterPro; IPR001628; Znf_hrmn_rcpt. DR InterPro; IPR013088; Znf_NHR/GATA. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR24085; NUCLEAR HORMONE RECEPTOR; 1. DR PANTHER; PTHR24085:SF8; RETINOIC ACID RECEPTOR ALPHA; 1. DR Pfam; PF12126; DUF3583; 1. DR Pfam; PF00104; Hormone_recep; 1. DR Pfam; PF00643; zf-B_box; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR01292; RETNOICACIDR. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR SMART; SM00336; BBOX; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00184; RING; 1. DR SMART; SM00399; ZnF_C4; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS51843; NR_LBD; 1. DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1. DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1. DR PROSITE; PS50119; ZF_BBOX; 2. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 1: Evidence at protein level; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004334}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU004334}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004334}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004334}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, KW ECO:0000256|RuleBase:RU004334}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, KW ECO:0000256|RuleBase:RU004334}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004334}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00024}. FT DOMAIN 57..92 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT DOMAIN 124..166 FT /note="B box-type" FT /evidence="ECO:0000259|PROSITE:PS50119" FT DOMAIN 184..222 FT /note="B box-type" FT /evidence="ECO:0000259|PROSITE:PS50119" FT DOMAIN 420..495 FT /note="Nuclear receptor" FT /evidence="ECO:0000259|PROSITE:PS51030" FT DOMAIN 518..752 FT /note="NR LBD" FT /evidence="ECO:0000259|PROSITE:PS51843" FT REGION 1..48 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 754..797 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..42 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 782..797 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 797 AA; 89282 MW; 8C16B6E85CBDD214 CRC64; MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKAIETQS SSSEEIVPSP PSPPPLPRIY KPCFVCQDKS SGYHYGVSAC EGCKGFFRRS IQKNMVYTCH RDKNCIINKV TRNRCQYCRL QKCFEVGMSK ESVRNDRNKK KKEVPKPECS ESYTLTPEVG ELIEKVRKAH QETFPALCQL GKYTTNNSSE QRVSLDIDLW DKFSELSTKC IIKTVEFAKQ LPGFTTLTIA DQITLLKAAC LDILILRICT RYTPEQDTMT FSDGLTLNRT QMHNAGFGPL TDLVFAFANQ LLPLEMDDAE TGLLSAICLI CGDRQDLEQP DRVDMLQEPL LEALKVYVRK RRPSRPHMFP KMLMKITDLR SISAKGAERV ITLKMEIPGS MPPLIQEMLE NSEGLDTLSG QPGGGGRDGG GLAPPPGSCS PSLSPSSNRS SPATHSP //