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IID00568
 UniprotQ14676
ProteinMediator of DNA damage checkpoint protein 1
GeneMDC1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
2089
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-10,19-138 Hetero dimer :
 Evidence X-RAY 3uot E Reference
       Region 3uot E 1-1 disorder
       Region 3uot E 2-9 order
       Region 3uot E 10-10 disorder
 Evidence X-RAY 3uot D Reference
       Region 3uot D 1-1 disorder
       Region 3uot D 2-9 order
       Region 3uot D 10-10 disorder
 Evidence X-RAY 3unn B Reference
       Region 3unn B 1-8 order
 Evidence X-RAY 3uot B Reference
       Region 3uot B 19-27 disorder
       Region 3uot B 28-134 order
       Region 3uot B 135-138 disorder
 Evidence X-RAY 3uot A Reference
       Region 3uot A 19-135 order
       Region 3uot A 136-138 disorder
 Evidence X-RAY 3unn A Reference
       Region 3unn A 27-133 order
       Region 3unn A 134-138 disorder
Seq 26-138 Homo dimer :
 Evidence X-RAY 3unm B Reference
       Region 3unm B 27-28 disorder
       Region 3unm B 29-134 order
       Region 3unm B 135-138 disorder
 Evidence X-RAY 3unm A Reference
       Region 3unm A 27-28 disorder
       Region 3unm A 29-101 order
       Region 3unm A 102-104 disorder
       Region 3unm A 105-109 order
       Region 3unm A 110-110 disorder
       Region 3unm A 111-133 order
       Region 3unm A 134-138 disorder
 Evidence X-RAY 3un0 B Reference
       Region 3un0 B 26-26 disorder
       Region 3un0 B 27-133 order
       Region 3un0 B 134-138 disorder
 Evidence X-RAY 3un0 A Reference
       Region 3un0 A 26-134 order
       Region 3un0 A 135-138 disorder
 Evidence X-RAY 3umz B Reference
       Region 3umz B 27-28 disorder
       Region 3umz B 29-133 order
       Region 3umz B 134-138 disorder
 Evidence X-RAY 3umz A Reference
       Region 3umz A 27-28 disorder
       Region 3umz A 29-133 order
       Region 3umz A 134-138 disorder
Seq 325-336 Hetero trimer : Q92547
 Evidence X-RAY 3ueo E Reference
       Region 3ueo E 325-325 disorder
       Region 3ueo E 326-335 order
       Region 3ueo E 336-336 disorder
 Evidence X-RAY 3ueo F Reference
       Region 3ueo F 325-327 disorder
       Region 3ueo F 328-335 order
       Region 3ueo F 336-336 disorder
Seq 1883-2089 Hetero dimer : IID00027Complex
 Evidence X-RAY 2azm B Reference
       Region 2azm B 1883-1890 disorder
       Region 2azm B 1891-2085 order
       Region 2azm B 2086-2089 disorder
 Evidence X-RAY 2azm A Reference
       Region 2azm A 1883-1890 disorder
       Region 2azm A 1891-2083 order
       Region 2azm A 2084-2089 disorder
Seq 1884-2089 Homo dimer :
 Evidence X-RAY 2etx B Reference
       Region 2etx B 1884-1890 disorder
       Region 2etx B 1891-2085 order
       Region 2etx B 2086-2089 disorder
 Evidence X-RAY 2etx A Reference
       Region 2etx A 1884-1891 disorder
       Region 2etx A 1892-2085 order
       Region 2etx A 2086-2089 disorder
Seq 1891-2089 Monomer :
 Evidence X-RAY 3k05 B This region binds to a peptide. Reference
       Region 3k05 B 1891-2089 order
 Evidence X-RAY 3k05 A This region binds to a peptide. Reference
       Region 3k05 A 1891-2083 order
       Region 3k05 A 2084-2089 disorder
 Evidence X-RAY 2ado B Reference
       Region 2ado B 1891-2085 order
       Region 2ado B 2086-2086 disorder
 Evidence X-RAY 2ado A Reference
       Region 2ado A 1891-1891 disorder
       Region 2ado A 1892-2085 order
       Region 2ado A 2086-2086 disorder
Seqphosphorylation
    4-4 Phosphothreonine; by ATM
    108-108 Phosphoserine
    146-146 Phosphothreonine
    168-168 Phosphoserine; by CK2
    176-176 Phosphoserine
    196-196 Phosphoserine; by CK2
    299-299 Phosphoserine
    301-301 Phosphothreonine
    329-329 Phosphoserine; by CK2
    331-331 Phosphothreonine; by CK2
    372-372 Phosphoserine
    376-376 Phosphoserine
    378-378 Phosphothreonine
    394-394 Phosphoserine
    397-397 Phosphoserine
    402-402 Phosphoserine
    404-404 Phosphothreonine
    411-411 Phosphoserine
    449-449 Phosphothreonine
    453-453 Phosphoserine
    455-455 Phosphothreonine
    485-485 Phosphoserine
    495-495 Phosphoserine
    498-498 Phosphoserine
    504-504 Phosphoserine
    505-505 Phosphoserine
    513-513 Phosphoserine
    523-523 Phosphothreonine
    590-590 Phosphoserine
    780-780 Phosphoserine
    793-793 Phosphoserine
    955-955 Phosphoserine
    998-998 Phosphoserine
    1033-1033 Phosphoserine
    1068-1068 Phosphoserine
    1086-1086 Phosphoserine
    1157-1157 Phosphothreonine
    1198-1198 Phosphothreonine
    1235-1235 Phosphoserine
    1239-1239 Phosphothreonine
    1280-1280 Phosphothreonine
    1302-1302 Phosphothreonine
    1399-1399 Phosphoserine
    1400-1400 Phosphoserine
    1403-1403 Phosphothreonine
    1425-1425 Phosphothreonine
    1466-1466 Phosphothreonine
    1548-1548 Phosphothreonine
    1564-1564 Phosphoserine
    1567-1567 Phosphothreonine
    1589-1589 Phosphothreonine
    1604-1604 Phosphoserine
    1608-1608 Phosphothreonine
    1630-1630 Phosphothreonine
    1664-1664 Phosphothreonine
    1671-1671 Phosphothreonine
    1681-1681 Phosphoserine
    1697-1697 Phosphothreonine
    1702-1702 Phosphoserine
    1711-1711 Phosphoserine
    1775-1775 Phosphoserine
    1800-1800 Phosphothreonine
    1820-1820 Phosphoserine
    1858-1858 Phosphothreonine
Seqacetylation
    812-812 N6-acetyllysine
    1402-1402 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-26,137-1894,2084-2089
Order 27-136,1895-2083
ProS 1-10,211-218,253-262,325-332,350-354,376-382,426-430,491-499,666-669,678-682,692-704,719-725,1854-1859
AlphaFold
Disorder 1-28,135-1890,2083-2089
Order 29-134,1891-2082
Pfam Hmmer
PF00498 54-124 1e-10
SEG 12-23 ,298-307 ,457-470 ,602-613 ,983-1001 ,1039-1052 ,1061-1073 ,1299-1318 ,1347-1359 ,1608-1623 ,1908-1924 ,1986-1997
Function
Function in SwissProt
Required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. May serve as a scaffold for the recruitment of DNA repair and signal transduction proteins to discrete foci of DNA damage marked by 'Ser-139' phosphorylation of histone H2AX. Also required for downstream events subsequent to the recruitment of these proteins. These include phosphorylation and activation of the ATM, CHEK1 and CHEK2 kinases, and stabilization of TP53 and apoptosis. ATM and CHEK2 may also be activated independently by a parallel pathway mediated by TP53BP1.
Biological Process
See also
Diagram with PDB data
H2AX/MDC1Crystal structure of the MDC1 brct repeat in complex with the histone tail of gamma-H2AX