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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 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
 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
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. 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