ID Q53F80_HUMAN Unreviewed; 777 AA. AC Q53F80; DT 24-MAY-2005, integrated into UniProtKB/TrEMBL. DT 24-MAY-2005, sequence version 1. DT 29-MAY-2024, entry version 107. DE SubName: Full=BRCA1 associated RING domain 1 variant {ECO:0000313|EMBL:BAD97129.1}; DE Flags: Fragment; 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:BAD97129.1}; RN [1] {ECO:0000313|EMBL:BAD97129.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=8125298; DOI=10.1016/0378-1119(94)90802-8; RA Maruyama K., Sugano S.; RT "Oligo-capping: a simple method to replace the cap structure of eukaryotic RT mRNAs with oligoribonucleotides."; RL Gene 138:171-174(1994). RN [2] {ECO:0000313|EMBL:BAD97129.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=9373149; DOI=10.1016/S0378-1119(97)00411-3; RA Suzuki Y., Yoshitomo K., Maruyama K., Suyama A., Sugano S.; RT "Construction and characterization of a full length-enriched and a 5'-end- RT enriched cDNA library."; RL Gene 200:149-156(1997). RN [3] {ECO:0000313|EMBL:BAD97129.1} RP NUCLEOTIDE SEQUENCE. RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. 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; AK223409; BAD97129.1; -; mRNA. DR AlphaFoldDB; Q53F80; -. DR PeptideAtlas; Q53F80; -. DR GO; GO:0070531; C:BRCA1-A complex; IEA:TreeGrafter. DR GO; GO:0031436; C:BRCA1-BARD1 complex; IEA:TreeGrafter. DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:TreeGrafter. DR GO; GO:0085020; P:protein K6-linked ubiquitination; IEA:TreeGrafter. DR CDD; cd17734; BRCT_Bard1_rpt1; 1. DR CDD; cd17720; BRCT_Bard1_rpt2; 1. DR CDD; cd16496; RING-HC_BARD1; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1. DR Gene3D; 3.40.50.10190; BRCT domain; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR039503; BARD1_Znf-RING. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR24171; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1. DR PANTHER; PTHR24171:SF8; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1. DR Pfam; PF12796; Ank_2; 1. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF14835; zf-RING_6; 1. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 3. DR SMART; SM00292; BRCT; 2. DR SUPFAM; SSF48403; Ankyrin repeat; 1. DR SUPFAM; SSF52113; BRCT domain; 2. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50297; ANK_REP_REGION; 3. DR PROSITE; PS50088; ANK_REPEAT; 3. DR PROSITE; PS50172; BRCT; 2. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 2: Evidence at transcript level; KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE- KW ProRule:PRU00023}; Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00175}. FT DOMAIN 50..86 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT REPEAT 427..459 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 460..492 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 493..525 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT DOMAIN 570..653 FT /note="BRCT" FT /evidence="ECO:0000259|PROSITE:PS50172" FT DOMAIN 667..777 FT /note="BRCT" FT /evidence="ECO:0000259|PROSITE:PS50172" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 167..211 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 356..404 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..15 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 167..183 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 369..404 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAD97129.1" SQ SEQUENCE 777 AA; 86496 MW; 8258990E33CB9341 CRC64; MPDNRQPRNR QPRIRSGNEP RSASAMEPDG RGAWAHSRAA LDRLEKLLRC SRCTNILREP VCLGGCEHIF CSNCVSDYIG TGCPVCYTPA WIQDLKINRQ LDSMIQLCSK LRNLLHDNEL SDLKEDKPRK GLFNDAGNKK NSIKMWFSPR SKKVRYVVSK ASVQTQPAIK KDASAQQDSY EFVSPSPPAD VSERAKKASA RSGKKQKKKT LAEINQKWNL EAEKEDGEFD SKEESKQKLV SFCSQPSVIS SPQINGEIDL LASGSLTESE CFGSLTEVSL PLAEQIESPD TKSRNEVVTP EKVCKNYLTS KKSLPLENNG KRGHHNRLSS PISKRCRTSI LSTSGDFVKQ TVPSENIPLP ECSSPPSCKR KVGGTSGSKN SNMSDEFISL SPGTPPSTLS SSSYRRVMSS PSAMKLLPNM AVKRNHRGET LLHIASIKGD IPSVEYLLQN GSDPNVKDHA GWTPLHEACN HGHLKVVELL LQHKALVNTT GYQNDSPLHD AAKNGHVDIV KLLLSYGASR NAVNIFGLRP VDYTDDESMK SLLLLPEKNE SSSASHCSVM NTGQRRDGPL VLIGSGLSSE QQKMLSGLAV ILKAKKYTEF DSTVTHVVVP GDAVQSTLKC MLGILNGCWI LKFEWVKACL RRKVCEQEEK YEIPEGPRRS RLNREQLLPK LFDGCYFYLW GTFKHHPKDN LIKLVTAGGG QILSRKPKPD SDVTQTINTV AYHARPDSDQ RFCTQYIIYE DLCNYHPERV RQGKVWKAPS SWFIDCVTSF ELLPLDS //