ID BRCA1_RAT Reviewed; 1817 AA. AC O54952; P97951; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 177. DE RecName: Full=Breast cancer type 1 susceptibility protein homolog; DE EC=2.3.2.27 {ECO:0000250|UniProtKB:P38398}; DE AltName: Full=RING-type E3 ubiquitin transferase BRCA1 {ECO:0000305}; GN Name=Brca1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; RX PubMed=9892727; DOI=10.1007/s003359900935; RA Bennett L.M., Brownlee H.A., Hagavik S., Wiseman R.W.; RT "Sequence analysis of the rat brca1 homolog and its promoter region."; RL Mamm. Genome 10:19-25(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 8-222. RC STRAIN=Wistar Kyoto; TISSUE=Spleen; RX PubMed=8761410; DOI=10.1093/carcin/17.8.1561; RA Chen K.S., Shepel L.A., Haag J.D., Heil G.M., Gould M.N.; RT "Cloning, genetic mapping and expression studies of the rat Brca1 gene."; RL Carcinogenesis 17:1561-1566(1996). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1589-1817. RX PubMed=11877378; DOI=10.1101/gad.959202; RA Joo W.S., Jeffrey P.D., Cantor S.B., Finnin M.S., Livingston D.M., RA Pavletich N.P.; RT "Structure of the 53BP1 BRCT region bound to p53 and its comparison to the RT Brca1 BRCT structure."; RL Genes Dev. 16:583-593(2002). CC -!- FUNCTION: E3 ubiquitin-protein ligase that specifically mediates the CC formation of 'Lys-6'-linked polyubiquitin chains and plays a central CC role in DNA repair by facilitating cellular responses to DNA damage. It CC is unclear whether it also mediates the formation of other types of CC polyubiquitin chains. The BRCA1-BARD1 heterodimer coordinates a diverse CC range of cellular pathways such as DNA damage repair, ubiquitination CC and transcriptional regulation to maintain genomic stability. Regulates CC centrosomal microtubule nucleation. Required for appropriate cell cycle CC arrests after ionizing irradiation in both the S-phase and the G2 phase CC of the cell cycle. Required for FANCD2 targeting to sites of DNA CC damage. Inhibits lipid synthesis by binding to inactive phosphorylated CC ACACA and preventing its dephosphorylation. Contributes to homologous CC recombination repair (HRR) via its direct interaction with PALB2, fine- CC tunes recombinational repair partly through its modulatory role in the CC PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. CC Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation CC and controls cell cycle G2/M checkpoints on DNA damage via BRCA1- CC mediated ubiquitination of RBBP8. Acts as a transcriptional activator. CC {ECO:0000250|UniProtKB:P38398}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:P38398}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Heterodimer with BARD1. Part of the BRCA1-associated genome CC surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, CC ATM, BLM, PMS2 and the MRE11-RAD50-NBN protein (MRN) complex. This CC association could be a dynamic process changing throughout the cell CC cycle and within subnuclear domains. Component of the BRCA1-A complex, CC at least composed of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, CC BABAM2 and BABAM1/NBA1. Interacts (via the BRCT domains) with ABRAXAS1 CC (phosphorylated form); this is important for recruitment to sites of CC DNA damage. Can form a heterotetramer with two molecules of ABRAXAS1 CC (phosphorylated form). Component of the BRCA1-RBBP8 complex. Interacts CC (via the BRCT domains) with RBBP8 ('Ser-327' phosphorylated form); the CC interaction ubiquitinates RBBP8, regulates CHEK1 activation, and CC involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA CC damage. Associates with RNA polymerase II holoenzyme. Interacts with CC SMC1A, NELFB, DCLRE1C, CLSPN. CHEK1, CHEK2, BAP1, BRCC3, UBXN1 and CC PCLAF. Interacts (via BRCT domains) with BRIP1 (phosphorylated form). CC Interacts with FANCD2 (ubiquitinated form). Interacts with H2AX CC (phosphorylated on 'Ser-140'). Interacts (via the BRCT domains) with CC ACACA (phosphorylated form); the interaction prevents dephosphorylation CC of ACACA. Part of a BRCA complex containing BRCA1, BRCA2 and PALB2. CC Interacts directly with PALB2; the interaction is essential for its CC function in HRR. Interacts directly with BRCA2; the interaction occurs CC only in the presence of PALB2 which serves as the bridging protein. CC Interacts (via the BRCT domains) with LMO4; the interaction represses CC the transcriptional activity of BRCA1. Interacts (via the BRCT domains) CC with CCAR2 (via N-terminus); the interaction represses the CC transcriptional activator activity of BRCA1 (By similarity). Interacts CC with EXD2 (By similarity). Interacts (via C-terminus) with DHX9; this CC interaction is direct and links BRCA1 to the RNA polymerase II CC holoenzyme (By similarity). Interacts with DNA helicase ZGRF1; the CC interaction is increased following DNA damage induction (By CC similarity). {ECO:0000250|UniProtKB:P38398}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38398}. CC Chromosome {ECO:0000250|UniProtKB:P48754}. Cytoplasm CC {ECO:0000250|UniProtKB:P38398}. Note=Localizes at sites of DNA damage CC at double-strand breaks (DSBs); recruitment to DNA damage sites is CC mediated by the BRCA1-A complex. Translocated to the cytoplasm during CC UV-induced apoptosis. {ECO:0000250|UniProtKB:P38398}. CC -!- DOMAIN: The BRCT domains recognize and bind phosphorylated pSXXF motif CC on proteins. The interaction with the phosphorylated pSXXF motif of CC ABRAXAS1, recruits BRCA1 at DNA damage sites. CC {ECO:0000250|UniProtKB:P38398}. CC -!- DOMAIN: The RING-type zinc finger domain interacts with BAP1. CC {ECO:0000250|UniProtKB:P38398}. CC -!- PTM: Phosphorylated in response to IR, UV, and various stimuli that CC cause checkpoint activation, probably by ATM or ATR. Phosphorylation at CC Ser-975 by CHEK2 regulates mitotic spindle assembly. Phosphorylation by CC AURKA regulates centrosomal microtubule nucleation. CC {ECO:0000250|UniProtKB:P38398}. CC -!- PTM: Autoubiquitinated, undergoes 'Lys-6'-linked polyubiquitination. CC 'Lys-6'-linked polyubiquitination does not promote degradation. CC {ECO:0000250|UniProtKB:P38398}. 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; AF036760; AAC36493.1; -; mRNA. DR EMBL; S82504; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; S82502; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U60523; AAB40387.1; -; mRNA. DR EMBL; S82500; AAB37501.1; -; Genomic_DNA. DR RefSeq; NP_036646.1; NM_012514.1. DR PDB; 1L0B; X-ray; 2.30 A; A=1589-1817. DR PDBsum; 1L0B; -. DR SMR; O54952; -. DR STRING; 10116.ENSRNOP00000072366; -. DR iPTMnet; O54952; -. DR PhosphoSitePlus; O54952; -. DR PaxDb; 10116-ENSRNOP00000028109; -. DR GeneID; 497672; -. DR KEGG; rno:497672; -. DR UCSC; RGD:2218; rat. DR AGR; RGD:2218; -. DR CTD; 672; -. DR RGD; 2218; Brca1. DR eggNOG; KOG4362; Eukaryota. DR InParanoid; O54952; -. DR OrthoDB; 5405431at2759; -. DR PhylomeDB; O54952; -. DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins. DR Reactome; R-RNO-5685938; HDR through Single Strand Annealing (SSA). DR Reactome; R-RNO-5685942; HDR through Homologous Recombination (HRR). DR Reactome; R-RNO-5689901; Metalloprotease DUBs. DR Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. DR Reactome; R-RNO-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates. DR Reactome; R-RNO-5693571; Nonhomologous End-Joining (NHEJ). DR Reactome; R-RNO-5693579; Homologous DNA Pairing and Strand Exchange. DR Reactome; R-RNO-5693607; Processing of DNA double-strand break ends. DR Reactome; R-RNO-5693616; Presynaptic phase of homologous DNA pairing and strand exchange. DR Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-RNO-69473; G2/M DNA damage checkpoint. DR UniPathway; UPA00143; -. DR EvolutionaryTrace; O54952; -. DR PRO; PR:O54952; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0070531; C:BRCA1-A complex; ISO:RGD. DR GO; GO:0070532; C:BRCA1-B complex; ISO:RGD. DR GO; GO:0031436; C:BRCA1-BARD1 complex; ISS:UniProtKB. DR GO; GO:0070533; C:BRCA1-C complex; ISO:RGD. DR GO; GO:0005694; C:chromosome; ISS:UniProtKB. DR GO; GO:0000793; C:condensed chromosome; ISO:RGD. DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:1990391; C:DNA repair complex; ISO:RGD. DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; ISO:RGD. DR GO; GO:0000800; C:lateral element; ISO:RGD. DR GO; GO:0001673; C:male germ cell nucleus; ISO:RGD. DR GO; GO:0005759; C:mitochondrial matrix; IDA:RGD. DR GO; GO:0000152; C:nuclear ubiquitin ligase complex; ISO:RGD. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0032991; C:protein-containing complex; ISO:RGD. DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD. DR GO; GO:0001741; C:XY body; ISO:RGD. DR GO; GO:0003682; F:chromatin binding; IDA:RGD. DR GO; GO:0003684; F:damaged DNA binding; ISO:RGD. DR GO; GO:0001216; F:DNA-binding transcription activator activity; ISO:RGD. DR GO; GO:0019899; F:enzyme binding; ISO:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0002039; F:p53 binding; ISO:RGD. DR GO; GO:0003723; F:RNA binding; ISO:RGD. DR GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD. DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071681; P:cellular response to indole-3-methanol; ISO:RGD. DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:RGD. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:RGD. DR GO; GO:0007098; P:centrosome cycle; ISO:RGD. DR GO; GO:0043009; P:chordate embryonic development; ISO:RGD. DR GO; GO:0007059; P:chromosome segregation; ISO:RGD. DR GO; GO:0006974; P:DNA damage response; ISO:RGD. DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IBA:GO_Central. DR GO; GO:0006302; P:double-strand break repair; ISO:RGD. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:RGD. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD. DR GO; GO:0051179; P:localization; ISO:RGD. DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISO:RGD. DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; ISO:RGD. DR GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:RGD. DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD. DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISS:UniProtKB. DR GO; GO:0044027; P:negative regulation of gene expression via CpG island methylation; ISO:RGD. DR GO; GO:0035067; P:negative regulation of histone acetylation; IBA:GO_Central. DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; ISO:RGD. DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:RGD. DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD. DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:RGD. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD. DR GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:RGD. DR GO; GO:0006301; P:postreplication repair; ISO:RGD. DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB. DR GO; GO:0085020; P:protein K6-linked ubiquitination; ISS:UniProtKB. DR GO; GO:0000209; P:protein polyubiquitination; ISO:RGD. DR GO; GO:0016567; P:protein ubiquitination; ISO:RGD. DR GO; GO:0060816; P:random inactivation of X chromosome; ISO:RGD. DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0032355; P:response to estradiol; IEP:RGD. DR GO; GO:0010212; P:response to ionizing radiation; ISO:RGD. DR GO; GO:0033993; P:response to lipid; IEP:RGD. DR GO; GO:0007584; P:response to nutrient; IEP:RGD. DR GO; GO:0010033; P:response to organic substance; IEP:RGD. DR CDD; cd17735; BRCT_BRCA1_rpt1; 1. DR CDD; cd17721; BRCT_BRCA1_rpt2; 1. DR CDD; cd16498; RING-HC_BRCA1; 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 IDEAL; IID50304; -. DR InterPro; IPR011364; BRCA1. DR InterPro; IPR031099; BRCA1-associated. DR InterPro; IPR025994; BRCA1_serine_dom. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR018957; Znf_C3HC4_RING-type. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR13763:SF0; BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN; 1. DR PANTHER; PTHR13763; BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN BRCA1; 1. DR Pfam; PF00533; BRCT; 2. DR Pfam; PF12820; BRCT_assoc; 1. DR Pfam; PF00097; zf-C3HC4; 1. DR PIRSF; PIRSF001734; BRCA1; 1. DR PRINTS; PR00493; BRSTCANCERI. DR SMART; SM00292; BRCT; 2. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF52113; BRCT domain; 2. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50172; BRCT; 2. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Cell cycle; Chromosome; Cytoplasm; KW DNA damage; DNA recombination; DNA repair; DNA-binding; KW Fatty acid biosynthesis; Fatty acid metabolism; Isopeptide bond; KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Transferase; Tumor suppressor; Ubl conjugation; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..1817 FT /note="Breast cancer type 1 susceptibility protein homolog" FT /id="PRO_0000055835" FT DOMAIN 1588..1682 FT /note="BRCT 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT DOMAIN 1701..1800 FT /note="BRCT 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT ZN_FING 24..65 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT REGION 313..347 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 529..560 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 617..768 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 875..907 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 959..982 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1145..1180 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1259..1290 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1354..1381 FT /note="Interaction with PALB2" FT /evidence="ECO:0000250" FT REGION 1373..1534 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 497..503 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 529..557 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 626..655 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 659..690 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 752..768 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 889..904 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 959..979 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1145..1163 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1259..1280 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1406..1431 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1456..1488 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P38398" FT MOD_RES 114 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38398" FT MOD_RES 393 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38398" FT MOD_RES 686 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38398" FT MOD_RES 706 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48754" FT MOD_RES 717 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48754" FT MOD_RES 975 FT /note="Phosphoserine; by CHEK2" FT /evidence="ECO:0000250|UniProtKB:P38398" FT MOD_RES 1153 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38398" FT MOD_RES 1155 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38398" FT MOD_RES 1181 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38398" FT MOD_RES 1242 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38398" FT MOD_RES 1298 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38398" FT MOD_RES 1304 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38398" FT MOD_RES 1344 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38398" FT MOD_RES 1351 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P38398" FT MOD_RES 1380 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38398" FT MOD_RES 1414 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38398" FT MOD_RES 1482 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38398" FT CROSSLNK 109 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P38398" FT CROSSLNK 299 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P38398" FT CROSSLNK 337 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P38398" FT CROSSLNK 457 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P38398" FT CROSSLNK 513 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P38398" FT CROSSLNK 578 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P38398" FT CROSSLNK 1049 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P38398" FT CONFLICT 38 FT /note="Q -> K (in Ref. 2; AAB40387/AAB37501)" FT /evidence="ECO:0000305" FT CONFLICT 192 FT /note="A -> M (in Ref. 2; AAB40387/AAB37501)" FT /evidence="ECO:0000305" FT STRAND 1597..1602 FT /evidence="ECO:0007829|PDB:1L0B" FT HELIX 1605..1617 FT /evidence="ECO:0007829|PDB:1L0B" FT STRAND 1632..1635 FT /evidence="ECO:0007829|PDB:1L0B" FT STRAND 1641..1643 FT /evidence="ECO:0007829|PDB:1L0B" FT HELIX 1647..1654 FT /evidence="ECO:0007829|PDB:1L0B" FT STRAND 1658..1661 FT /evidence="ECO:0007829|PDB:1L0B" FT HELIX 1663..1669 FT /evidence="ECO:0007829|PDB:1L0B" FT TURN 1670..1672 FT /evidence="ECO:0007829|PDB:1L0B" FT HELIX 1678..1680 FT /evidence="ECO:0007829|PDB:1L0B" FT TURN 1686..1688 FT /evidence="ECO:0007829|PDB:1L0B" FT STRAND 1690..1692 FT /evidence="ECO:0007829|PDB:1L0B" FT HELIX 1694..1701 FT /evidence="ECO:0007829|PDB:1L0B" FT STRAND 1710..1713 FT /evidence="ECO:0007829|PDB:1L0B" FT STRAND 1718..1720 FT /evidence="ECO:0007829|PDB:1L0B" FT HELIX 1722..1731 FT /evidence="ECO:0007829|PDB:1L0B" FT STRAND 1735..1737 FT /evidence="ECO:0007829|PDB:1L0B" FT STRAND 1739..1741 FT /evidence="ECO:0007829|PDB:1L0B" FT HELIX 1743..1745 FT /evidence="ECO:0007829|PDB:1L0B" FT STRAND 1752..1755 FT /evidence="ECO:0007829|PDB:1L0B" FT STRAND 1777..1779 FT /evidence="ECO:0007829|PDB:1L0B" FT HELIX 1781..1788 FT /evidence="ECO:0007829|PDB:1L0B" FT HELIX 1795..1798 FT /evidence="ECO:0007829|PDB:1L0B" SQ SEQUENCE 1817 AA; 199879 MW; C0B4760F0E349A01 CRC64; MDLSAVRIQE VQNVLHAMQK ILECPICLEL IKEPVSTQCD HIFCKFCMLK LLNQKKGPSQ CPLCKNEITK RSLQGSARFS QLVEELLKII DAFELDTGMQ CANGFSFSKK KNSSSELLNE DASIIQSVGY RNRVKKLQQI ESGSATLKDS LSVQLSNLGI VRSMKKNRQT QPQNKSVYIA LESDSSEERV NAPDGCSVRD QELFQIAPGG AGDEGKLNSA KKAACDFSEG IRNIEHHQCS DKDLNPTENH ATERHPEKCP RISVANVHVE PCGTDARASS LQRGTRSLLF TEDRLDAEKA EFCDRSKQSG AAVSQQSRWA DSKETCNGRP VPRTEGKADP NVDSLCGRKQ WNHPKSLCPE NSGATTDVPW ITLNSSIQKV NEWFSRTGEM LTSDNASDRR PASNAEAAVV LEVSNEVDGC FSSSKKIDLV APDPDNAVMC TSGRDFSKPV ENIINDKIFG KTYQRKGSRP HLNHVTEIIG TFTTEPQIIQ EQPFTNKLKR KRSTCLHPED FIKKADLTVV QRISENLNQG TDQMEPNDQA MSITSNGQEN RATGNDLQRG RNAHPIESLR KEPAFTAKAK SISNSISDLE VELNVHSSKA PKKNRLRRKS TRCVLPLEPI SRNPSPPTCA ELQIESCGSS EETKKNNSNQ TPAGHIREPQ LIEDTEPAAD AKKNEPNEHI RKRSASDAFP EEKLMNKAGL LTSCSSPRKP QGPVNPSPER KGIEQLEMCQ MPDNNKELGD LVLGGEPSGK PTEPSEESTS VSLVPDTDYD TQNSVSILEA NTVRYARTGS VQCMTQFVAS ENPKELVHGS NNAGSGSECF KHPLRHELNH NQETIEMEDS ELDTQYLQNT FQVSKRQSFA LFSKLRSPQK DCTLVGARSV PSREPSPKVT SRGEQKERQG QEESEISHVQ AVTVTVGLPV PCQEGKPGAV TMCADVSRLC PSSHYRSCEN GLNTTDKSGI SQNSHFRQSV SPLRSSIKTD NRKTLTEGRF EKHTERGMGN ETAVQSTIHT ISLNNRGDAC LEASSGSVIE VHSTGENVQG QLDRNRGPKV NTVSLLDSTQ PGVSKQSAPV SDKYLEIKQE SKAVSADFSP CLFSDHLEKP MRSDKTFQVC SETPDDLLDD VEIQENASFG EGGITEKSAI FNGSVLRRES SRSPSPVTHA SKSRSLHRGS RKLEFSEESD STEDEDLPCF QHLLSRVSST PELTRCSSVV TQRVPEKAKG TQAPRKSSIS DCNNEVILGE ASQEYQFSED AKCSGSMFSS QHSAALGSPA NALSQDPDFN PPSKQRRHQA ENEEAFLSDK ELISDHEDMA ACLEEASDQE EDSIIPDSVA SGYESEANLS EDCSQSDILT TQQRATMKDN LIKLQQEMAQ LEAVLEQHGS QPSGHPPCLP ADPCALEDLP DPEQNRSGTA ILTSKNINEN PVSQNPKRAC DDKSQPQPPD GLPSGDKESG MRRPSPFKSP LTSSRCSARG HSRSLQNRNS TSQEELLQPA XLEKSCEPHN LTGRSCLPRQ DLEGTPYPES GIRLVSSRDP DSESPKVSAL VCTAPASTSA LKISQGQVAG SCRSPAAGGA DTAVVEIVSK IKPEVTSPKE RAERDISMVV SGLTPKEVMI VQKFAEKYRL ALTDVITEET THVIIKTDAE FVCERTLKYF LGIAGGKWIV SYSWVIKSIQ ERKLLSVHEF EVKGDVVTGS NHQGPRRSRE SQEKLFEGLQ IYCCEPFTNM PKDELERMLQ LCGASVVKEL PLLTRDTGAH PIVLVQPSAW TEDNDCPDIG QLCKGRLVMW DWVLDSISVY RCRDLDAYLV QNITCGRDGS EPQDSND //