| IED ID | IndEnz0002014594 |
| Enzyme Type ID | protease014594 |
| Protein Name |
Breast cancer type 2 susceptibility protein homolog Fanconi anemia group D1 protein homolog |
| Gene Name | Brca2 Fancd1 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MTVEYKRRPTFWEIFKARCSTADLGPISLNWFEELFSEAPPYNTEHPEESEYKPQGHEPQLFKTPQRNPSYHQFASTPIMFKEQSQTLPLDQSPFKELGNVVANSKRKHHSKKKARKDPVVDVASLPLKACPSESPCTPRCTQVAPQRRKPVVSGSLFYTPKLEETPKHISESLGVEVDPDMSWTSSLATPPTLSSTVLIARDEEAHRNAFPADSPASLKSYFSNHNESLKKNDRFIPSVSDSENKSQQEAFSQGLEKMLGDSSSKINRFRDCLRKPIPNVLEDGETAVDTSGEDSFSLCFPKRRTRNLQKTRMGKMKKKIFSETRTDGLSEEARGQADDKNSFALEIEPRDSEPLDPSVTNQKPLYSQSGDISSEAGQCSDSIWSQPDPSGLNGTQTRKIPLLHISFHKQSILEDFIDMKKEGTGSITFPHISSLPEPEKMFSEETLVDKEHEGQHLESLEDSISGKQMVSGTSQTACLSPSIRKSIVKMREPLEETLDTVFSDSMTSSAFTEELDASAGGLEIHTACSQREDSLCPSSVDTGSWPTTLTDTSATVKNAGLITTLKNKRRKFIYSVSDDASHQGKKLQTQRQSELTNLSAPFEASAFEVPFPFTNVDSGIPDSSIKRSNLPNDPEEPSLSLTNSFVTAASKEISYIHALISQDLNDKEAILSEEKPQPYTALEADFLSCLPERSCENDQKSPKVSDRKEKVLVSACRPSGRLAAAVQLSSISFDSQENPLGSHNVTSTLKLTPSPKTPLSKPVVVSRGKMCKMPEKLQCKSCKDNIELSKNIPLGVNEMCVLSENSETPELLPPLEYITEVSSSVKSQFNQNTKIAVVQKDQKDSTFISEVTVHMNSEELFPEKENNFAFQVTNESNKPNIGSTVEFQEEDLSHAKGHSLKNSPMTVDRDLDDEQAGQVLITEDSDSLAVVHDCTKKSRNTIEQHQKGTADKDFKSNSSLYLKSDGNNDYLDKWSEFLDPLMNHKLGGSFRTASNKEIKLSEDNVKKSKMFFKDIEEQYPTSLDCIDTVSTLQLANKKRLSEPHTFDLKSGTTVSTQCHSQSSVSHEDTHTAPQMLSSKQDFHSSHNLTPSQKAEITELSTILEESGSQFEFTQFKNPSHIAQNNTSAVLGNQMAVVRTASEEWKDVDLHLPLNPSSVGQIDHNKKFECLVGVKQSSSHLLEDTCNQNTSCFLPIKEMEFGGFCSALGTKLSVSNEALRKAMKLFSDIENISEEPSTKVGPRGFSSCAHHDSVASVFKIKKQNTDKSFDEKSSKCQVTVQNNKEMTTCILVDENPENYVKNIKQDNNYTGSQRNAYKLENSDVSKSSTSGTVYINKGDSDLPFAAEKGNKYPESCTQYVREENAQIKESVSDLTCLEVMKAEETCHMKSSDKEQLPSDKMEQNMKEFNISFQTASGKNIRVSKESLNKSVNILDQETEDLTVTSDSLNSKILCGINKDKMHISCHKKSINIKKVFEEHFPIGTVSQLPALQQYPEYEIESIKEPTLLSFHTASGKKVKIMQESLDKVKNLFDETQYVRKTTNFGHQESKPLKDREDYKERLTLAYEKIEVTASKCEEMQNFVSKQTEMLPQQNDHMYRQTENLTSNGSSPKVHGNIENKIEKNPRICCICQSSYFVTEDSALACYTGDSRKTCVGESSLSKGKKWLREQSDKLGTRNTIEIQCVKEHTEDFAGNALYEHSLVIIRTEIDTSHVSENQASTLFSDPNVCHSYLSHSSFCHHDDMHNDSGYFLKDKIDSDVQPDMKNTEGNAIFPKISATKEIKLHPQTVNEECVQKLETNASPYANKNIAIDSAMLDLRNCKVGSPVFITTHSQETVRMKEIFTDNCSKIVEQNRESKPDTCQTSCHKALDNSEDFICPSSSGDVCINSPMAIFYPQSEQILQHNQSVSGLKKAATPPVSLETWDTCKSIRGSPQEVHPSRTYGFFSTASGKAVQVSDASLEKARQVFSEIDGDAKQLASMVSLEGNEKSHHSVKRESSVVHNTHGVLSLRKTLPGNVSSFVFSGFSTAGGKLVTVSESALHKVKGMLEEFDLIRTEHTLQHSPTPEDVSKIPPQPCLESRTPEYSVSSKLQKTYNDKSRSPSNYKESGSSGNTQSLEVSPQLSQMERKQETQSVLGTKVSQRKTNILEKKQNLPQNIKIESNKMETFSDVSMKTNVGEYYSKEPENYFETEAVEIAKAFMEDDELTDSEQTHAKCSLFACPQNEALLNSRTRKRGGMAGVAVGQPPIKRSLLNEFDRIIESKGKSLTPSKSTPDGTIKDRRLFTHHMSLEPVTCGPFCSSKERQETQSPHVTSPAQGLQSKEHPSRHSAVGKSSSNPTVSALRSERTRHSVSDKSTKVFVPPFKVKSRFHRDEHFDSKNVNLEGKNQKSADGVSEDGNDSDFPQFNKDLMSSLQNARDLQDIRIKNKERHHLCPQPGSLYLTKSSTLPRISLQAAVGDSVPSACSPKQLYMYGVSKACISVNSKNAEYFQFAIEDHFGKEALCAGKGFRLADGGWLIPSDDGKAGKEEFYRALCDTPGVDPKLISSVWVSNHYRWIVWKLAAMEFAFPKEFANRCLNPERVLLQLKYRYDVEIDNSSRSALKKILERDDTAAKTLVLCVSDIISLSTNVSETSGSKASSEDSNKVDTIELTDGWYAVKAQLDPPLLALVKSGRLTVGQKIITQGAELVGSPDACAPLEAPDSLRLKISANSTRPARWHSKLGFFHDPRPFPLPLSSLFSDGGNVGCVDVIVQRVYPLQWVEKTVSGSYIFRNEREEEKEALRFAEAQQKKLEALFTKVHTELKEHEEDIAQRRVLSRALTRQQVHALQDGAELYAAVQDASDPEHLETCFSEEQLRALNNYRQMLSDKKQARIQSEFRKALEAAEKEEGLSRDVSTVWKLRVTSYKKREKSALLSIWRPSSDLPSLLTEGQRYRIYHLSVSKSKNKFEWPSIQLTATKRTQYQQLPVSSETLLQLYQPRELLPFSKLSDPAFQPPCSEVDVVGVVVSVVKPIGLAPLVYLSDECLHLLVVKFGIDLNEDIKPRVLIAASNLQWRPESTSRVPTLFAGNFSVFSASPKEAHFQERVTNMKHAIENIDTFYKEAEKKLIQVLKGDSPKWSTPNKDPTREPYPASTCSASDLASGGQLPRSSPTDQQSYRSPLSCCTPTGKSTPLAHSAWMAAKSCSGENEIEDPKTCRKKRALDLLSRLPLPPPLSPVCTFVSPAAQKAFQPPRSCGTKYPTPLKKEGPSSPWSRAPFQKASGVSLLDCDSVADEELALLSTQALVPHSVGGSEQVFPSDSTRTEGPSASTEARPANRSKRESLRDCRDDSDGKLAAETVPDYS |
| Enzyme Length | 3343 |
| Uniprot Accession Number | O35923 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and SEM1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability, independently of its known role in homologous recombination (By similarity). {ECO:0000250|UniProtKB:P51587, ECO:0000250|UniProtKB:P97929}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (30); Chain (1); Compositional bias (6); Helix (19); Modified residue (6); Motif (1); Region (14); Repeat (8); Turn (9) |
| Keywords | 3D-structure;Cell cycle;Cytoplasm;Cytoskeleton;DNA damage;DNA recombination;DNA repair;DNA-binding;Nucleus;Phosphoprotein;Reference proteome;Repeat;Tumor suppressor;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51587}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P51587}. |
| Modified Residue | MOD_RES 70; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P51587; MOD_RES 475; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P51587; MOD_RES 736; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P51587; MOD_RES 2063; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P51587; MOD_RES 3222; /note=Phosphoserine; by CDK1 and CDK2; /evidence=ECO:0000250|UniProtKB:P51587; MOD_RES 3250; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P51587 |
| Post Translational Modification | PTM: Phosphorylated by ATM upon irradiation-induced DNA damage. Phosphorylation by CHEK1 and CHEK2 regulates interaction with RAD51. Phosphorylation at Ser-3222 by CDK1 and CDK2 is low in S phase when recombination is active, but increases as cells progress towards mitosis; this phosphorylation prevents homologous recombination-dependent repair during S phase and G2 by inhibiting RAD51 binding. {ECO:0000250|UniProtKB:P51587}.; PTM: Ubiquitinated in the absence of DNA damage; this does not lead to proteasomal degradation. In contrast, ubiquitination in response to DNA damage leads to proteasomal degradation. {ECO:0000250|UniProtKB:P51587}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1IYJ; |
| Mapped Pubmed ID | 12754522; 14583453; 16273225; 16964288; 20890790; 21748659; 25861310; |
| Motif | MOTIF 2612..2628; /note=Nuclear export signal; masked by interaction with SEM1; /evidence=ECO:0000250|UniProtKB:P51587 |
| Gene Encoded By | |
| Mass | 372,216 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |