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IID00588
 UniprotQ9NS91
ProteinE3 ubiquitin-protein ligase RAD18
GeneRAD18
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
495
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-99 Homo dimer :
 Evidence X-RAY 2y43 A Reference
       Region 2y43 A 1-7 disorder
       Region 2y43 A 8-95 order
       Region 2y43 A 96-99 disorder
 Evidence X-RAY 2y43 B Reference
       Region 2y43 B 1-6 disorder
       Region 2y43 B 7-94 order
       Region 2y43 B 95-99 disorder
Seq 198-227 Hetero dimer : P0CG48
 Evidence NMR 2mre B Reference
       Region 2mre B 198-227 order
Seq 198-227 Monomer :
 Evidence NMR 2mrf A Reference
       Region 2mrf A 198-227 order
Seq 198-240 Hetero dimer : P0CG47
 Evidence NMR 5vf0 B Reference
       Region 5vf0 B 198-240 order
       Region 5vf0 B 232-240 high_rmsd
Seq 340-366 Hetero dimer : IID00558Complex
 Evidence X-RAY 2ybf B Reference
       Region 2ybf B 340-340 disorder
       Region 2ybf B 341-361 order
       Region 2ybf B 362-366 disorder
Seqdisorder 341-366
 Evidence NMR Reference
       Region 341-366 disorder
SeqProS verified 341-361 Hetero dimer : IID00558Complex
       Region 2ybf B 341-361 order
       Region 341-366 disorder
Seqphosphorylation
    158-158 Phosphoserine
    99-99 Phosphoserine
    103-103 Phosphoserine
    118-118 Phosphothreonine
    122-122 Phosphoserine
    125-125 Phosphoserine
    142-142 Phosphoserine
    164-164 Phosphoserine
    322-322 Phosphoserine
    471-471 Phosphoserine
    483-483 Phosphoserine
Seqacetylation
    1-1 N-acetylmethionine
 
Prediction
NeProc
Disorder 1-5,99-240,312-495
Order 6-98,241-311
ProS 1-5,110-123,132-137,148-156,164-170,179-186,192-226,236-240,327-360,414-418,448-451,463-476,482-486,492-495
AlphaFold
Disorder 1-7,99-199,227-238,319-322,366-454,456-495
Order 8-98,200-226,239-318,323-365,455-455
Pfam Hmmer
PF00097 25-63 0.00014
PF02037 248-282 1.5e-12
SEG 99-110 ,224-236 ,250-261 ,432-444
Function
Function in SwissProt
E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity.