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IID50300
UniprotO35923
ProteinBreast cancer type 2 susceptibility protein homolog
GeneBrca2
OrganismRattus norvegicus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
3343
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 2335-3151 Hetero dimer : P60896
 Evidence X-RAY 1iyj B Reference
       Region 1iyj B 2335-2402 disorder
       Region 1iyj B 2403-2627 order
       Region 1iyj B 2628-2644 disorder
       Region 1iyj B 2645-2784 order
       Region 1iyj B 2785-2891 disorder
       Region 1iyj B 2892-3117 order
       Region 1iyj B 3118-3151 disorder
 Evidence X-RAY 1iyj D Reference
       Region 1iyj D 2335-2402 disorder
       Region 1iyj D 2403-2627 order
       Region 1iyj D 2628-2644 disorder
       Region 1iyj D 2645-2784 order
       Region 1iyj D 2785-2891 disorder
       Region 1iyj D 2892-3117 order
       Region 1iyj D 3118-3151 disorder
Seqphosphorylation
    3250-3250 Phosphoserine
    3222-3222 Phosphoserine; by CDK1 and CDK2
    2063-2063 Phosphoserine
    736-736 Phosphoserine
    475-475 Phosphoserine
    70-70 Phosphoserine
 
Prediction
NeProc
Disorder 1-6,40-142,187-195,205-210,215-221,229-607,615-627,632-658,669-672,680-690,729-775,857-864,922-972,1031-1105,1110-1143,1150-1198,1210-1215,1229-1418,1440-1505,1523-1528,1536-1636,1647-1653,1671-1769,1801-1948,1975-2405,2410-2446,2627-2643,2810-2831,2873-2887,3116-3196,3223-3343
Order 7-39,143-186,196-204,211-214,222-228,608-614,628-631,659-668,673-679,691-728,776-856,865-921,973-1030,1106-1109,1144-1149,1199-1209,1216-1228,1419-1439,1506-1522,1529-1535,1637-1646,1654-1670,1770-1800,1949-1974,2406-2409,2447-2626,2644-2809,2832-2872,2888-3115,3197-3222
ProS 1-6,40-111,117-142,187-195,215-221,229-334,339-370,383-399,404-458,481-516,523-592,605-607,615-627,632-658,669-672,680-690,729-753,760-775,864-864,922-944,953-972,1031-1047,1053-1105,1110-1143,1150-1198,1210-1215,1229-1389,1399-1418,1440-1444,1452-1468,1477-1505,1523-1528,1536-1586,1594-1602,1609-1636,1647-1653,1679-1697,1703-1769,1801-1905,1916-1934,1943-1948,1975-2004,2013-2061,2071-2107,2113-2125,2135-2157,2164-2208,2238-2260,2266-2328,2346-2351,2358-2384,2399-2405,2410-2446,2810-2831,2873-2887,3121-3129,3141-3172,3190-3196,3223-3236,3256-3299,3310-3314,3335-3340
AlphaFold
Disorder 1-1094,1096-1097,1099-1102,1104-2040,2043-2043,2046-2409,2504-2504,2625-2647,2810-2823,2886-2891,2909-2910,2946-2952,3014-3014,3038-3039,3056-3060,3113-3343
Order 1095-1095,1098-1098,1103-1103,2041-2042,2044-2045,2410-2503,2505-2624,2648-2809,2824-2885,2892-2908,2911-2945,2953-3013,3015-3037,3040-3055,3061-3112
Pfam Hmmer
PF00634 984-1018 3.6e-10
PF00634 1197-1231 3.9e-12
PF00634 1405-1439 2.5e-14
PF00634 1503-1537 7.5e-14
PF00634 1638-1672 3.1e-08
PF00634 1939-1973 5.4e-13
PF00634 2019-2053 8.1e-10
SEG 103-117 ,185-197 ,2018-2027 ,2730-2740 ,2880-2889 ,3000-3010 ,3204-3216
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