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IID50324
UniprotP97929
ProteinBreast cancer type 2 susceptibility protein homolog
GeneBrca2
OrganismMus musculus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
3329
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 2378-3115 Hetero dimer : P60896
 Evidence X-RAY 1miu A Reference
       Region 1miu A 2378-2398 disorder
       Region 1miu A 2399-2614 order
       Region 1miu A 2615-2636 disorder
       Region 1miu A 2637-2795 order
       Region 1miu A 2796-2807 disorder
       Region 1miu A 2808-3103 order
       Region 1miu A 3104-3115 disorder
 Evidence X-RAY 1mje A Reference
       Region 1mje A 2378-2398 disorder
       Region 1mje A 2399-2614 order
       Region 1mje A 2615-2636 disorder
       Region 1mje A 2637-2792 order
       Region 1mje A 2880-2881 disorder
       Region 1mje A 2882-3109 order
       Region 1mje A 3110-3113 disorder
Seqphosphorylation
    435-435 Phosphoserine
    481-481 Phosphoserine
    735-735 Phosphoserine
    2048-2048 Phosphoserine
    3214-3214 Phosphoserine; by CDK1 and CDK2
    3241-3241 Phosphoserine
 
Prediction
NeProc
Disorder 1-6,42-144,190-198,218-222,233-287,295-627,632-703,709-723,733-810,823-829,839-863,919-972,1031-1191,1227-1372,1377-1410,1415-1421,1429-1478,1522-1649,1656-1760,1769-1949,1959-2438,2618-2635,2801-2819,3107-3329
Order 7-41,145-189,199-205,212-217,223-232,288-294,628-631,704-708,724-732,811-822,830-838,864-918,973-1030,1192-1226,1373-1376,1411-1414,1422-1428,1479-1521,1650-1655,1761-1768,1950-1958,2439-2492,2499-2617,2636-2800,2820-2876,2883-3106
ProS 1-6,42-88,94-108,114-144,190-198,218-222,233-287,295-334,342-400,406-482,489-601,610-627,632-703,709-723,733-753,761-810,823-829,839-852,858-863,919-940,949-972,1031-1056,1064-1071,1077-1191,1234-1372,1377-1410,1415-1421,1429-1433,1438-1457,1463-1478,1522-1533,1540-1589,1595-1649,1665-1760,1769-1897,1904-1918,1927-1949,1964-1971,1985-1989,2007-2046,2061-2071,2077-2092,2099-2124,2130-2193,2199-2211,2226-2228,2238-2314,2340-2343,2351-2375,2385-2438,2801-2819,3110-3120,3148-3162,3184-3230,3248-3291,3312-3329
AlphaFold
Disorder 1-2028,2030-2401,2616-2638,2797-2815,2876-2883,2901-2901,2936-2942,3005-3006,3030-3030,3047-3051,3104-3329
Order 2029-2029,2402-2615,2639-2796,2816-2875,2884-2900,2902-2935,2943-3004,3007-3029,3031-3046,3052-3103
Pfam Hmmer
PF00634 981-1015 1.3e-12
PF00634 1192-1226 1.8e-12
PF00634 1394-1428 7.6e-13
PF00634 1491-1525 7.5e-14
PF00634 1623-1657 1.2e-08
PF00634 1924-1958 8.7e-13
PF00634 2004-2038 7.6e-12
SEG 36-51 ,100-123 ,187-199 ,746-761 ,904-917 ,1239-1252 ,2712-2734 ,2991-3001 ,3197-3208
Function
Function in SwissProt
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.
Biological Process
See also
Diagram with PDB data
BRCA2/RAD51Crystal structure of a RAD51-BRCA2 BRC repeat complex