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IID00237
UniprotP51587
ProteinBreast cancer type 2 susceptibility protein
GeneBRCA2
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
3418
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 21-39 Hetero dimer : IID00249Complex
 Evidence X-RAY 3eu7 X Reference
       Region 3eu7 X 21-23 disorder
       Region 3eu7 X 24-37 order
       Region 3eu7 X 38-39 disorder
Seq 1517-1551 Hetero tetramer : IID00241Complex
 Evidence X-RAY 1n0w B Reference
       Region 1n0w B 1517-1518 disorder
       Region 1n0w B 1519-1551 order
SeqProS possible 1519-1551 This region is described to be disordered in the free state and be ordered when it binds eith RAD51. (PubMed=22971516) Hetero tetramer : IID00241Complex
       Region 1n0w B 1519-1551 order
Seqphosphorylation
    3387-3387 Phosphothreonine; by CHEK1 and CHEK2
    3319-3319 Phosphoserine
    3291-3291 Phosphoserine; by CDK1 and CDK2
    2095-2095 Phosphoserine
    1970-1970 Phosphoserine
    2035-2035 Phosphothreonine
    755-755 Phosphoserine
    492-492 Phosphoserine
    70-70 Phosphoserine
    445-445 Phosphoserine
 
Prediction
NeProc
Disorder 1-6,42-60,75-83,96-143,197-204,225-230,239-600,605-625,632-679,689-718,738-788,825-854,878-883,936-995,1044-1154,1161-1271,1286-1289,1305-1433,1455-1530,1550-2203,2239-2514,2699-2713,2881-2894,3189-3418
Order 7-41,61-74,84-95,144-196,205-224,231-238,601-604,626-631,680-688,719-737,789-824,855-877,884-935,996-1043,1155-1160,1272-1285,1290-1304,1434-1454,1531-1549,2204-2238,2515-2698,2714-2880,2895-2956,2961-3188
ProS 1-6,42-60,75-83,96-143,197-204,225-230,239-346,351-386,394-408,419-485,499-600,605-611,621-625,632-679,689-718,738-788,825-843,848-854,936-995,1044-1061,1066-1084,1092-1154,1161-1271,1286-1289,1305-1433,1455-1475,1481-1487,1493-1530,1550-1590,1596-1716,1727-1926,1931-1938,1947-1964,1974-2004,2014-2018,2057-2093,2098-2140,2145-2161,2177-2181,2187-2203,2239-2242,2250-2256,2268-2281,2289-2368,2391-2399,2404-2436,2467-2514,2881-2894,3189-3198,3212-3226,3259-3306,3323-3355,3360-3383,3392-3395,3402-3418
Pfam Hmmer
PF00634 1002-1036 6.3e-13
PF00634 1212-1246 1.5e-12
PF00634 1421-1455 4.5e-12
PF00634 1517-1551 1.3e-14
PF00634 1664-1698 3.9e-10
PF00634 1837-1871 2.5e-12
PF00634 1971-2005 3.9e-14
PF00634 2051-2085 1.8e-12
SEG 193-207 ,1741-1753 ,2052-2063 ,2792-2813 ,2844-2860 ,2871-2878 ,3274-3285
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. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180).
Biological Process
Diagram with PDB data
BRCA2/RAD51Crystal structure of a RAD51-BRCA2 BRC repeat complex
See also
Diagram with PDB data
PALB2/BRCA2Crystal Structure of a PALB2 / BRCA2 complex