Search Keyword:


Search option:


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 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
 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
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. 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).
Biological Process
See also
Diagram with PDB data
BRCA2/RAD51Crystal structure of a RAD51-BRCA2 BRC repeat complex