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IID00518
UniprotQ92990
ProteinGlomulin
GeneGLMN
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
594
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-594 Hetero trimer : IID00059Complex,IID00133Complex
 Evidence X-RAY 4f52 F Reference
       Region 4f52 F 1-19 order
       Region 4f52 F 20-21 disorder
       Region 4f52 F 22-39 order
       Region 4f52 F 40-44 disorder
       Region 4f52 F 45-75 order
       Region 4f52 F 76-80 disorder
       Region 4f52 F 81-161 order
       Region 4f52 F 162-164 disorder
       Region 4f52 F 165-193 order
       Region 4f52 F 194-200 disorder
       Region 4f52 F 201-226 order
       Region 4f52 F 227-233 disorder
       Region 4f52 F 234-259 order
       Region 4f52 F 260-278 disorder
       Region 4f52 F 279-432 order
       Region 4f52 F 433-438 disorder
       Region 4f52 F 439-532 order
       Region 4f52 F 533-549 disorder
       Region 4f52 F 550-583 order
       Region 4f52 F 584-594 disorder
 Evidence X-RAY 4f52 E Reference
       Region 4f52 E 1-17 order
       Region 4f52 E 18-26 disorder
       Region 4f52 E 27-163 order
       Region 4f52 E 164-167 disorder
       Region 4f52 E 168-226 order
       Region 4f52 E 227-234 disorder
       Region 4f52 E 235-258 order
       Region 4f52 E 259-279 disorder
       Region 4f52 E 280-434 order
       Region 4f52 E 435-438 disorder
       Region 4f52 E 439-535 order
       Region 4f52 E 536-549 disorder
       Region 4f52 E 550-583 order
       Region 4f52 E 584-594 disorder
Seqacetylation
    2-2 N-acetylalanine
 
Prediction
NeProc
Disorder 1-4,533-545,584-594
Order 5-532,546-583
ProS 533-545,589-594
AlphaFold
Disorder 77-78,195-197,228-233,253-253,261-280,435-437,530-549,585-594
Order 1-76,79-194,198-227,234-252,254-260,281-434,438-529,550-584
SEG 101-112 ,117-130 ,193-210
Function
Function in SwissProt
Isoform 1
Regulatory component of cullin-RING-based SCF (SKP1-Cullin-F-box protein) E3 ubiquitin-protein ligase complexes (PubMed:22405651, PubMed:22748924). Inhibits E3 ubiquitin ligase activity by binding to RBX1 (via RING domain) and inhibiting its interaction with the E2 ubiquitin-conjugating enzyme CDC34 (PubMed:22405651, PubMed:22748924). Inhibits RBX1-mediated neddylation of CUL1 (PubMed:22405651). Required for normal stability and normal cellular levels of key components of SCF ubiquitin ligase complexes, including FBXW7, RBX1, CUL1, CUL2, CUL3, CUL4A, and thereby contributes to the regulation of CCNE1 and MYC levels (By similarity). Essential for normal development of the vasculature (PubMed:11845407). Contributes to the regulation of RPS6KB1 phosphorylation (PubMed:11571281).