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IID00133
UniprotQ13616
ProteinCullin-1
GeneCUL1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
776
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-776 Hetero trimer : IID00059Complex,IID00089Complex
 Evidence X-RAY 1u6g A Reference
       Region 1u6g A 1-16 disorder
       Region 1u6g A 17-55 order
       Region 1u6g A 56-83 disorder
       Region 1u6g A 84-149 order
       Region 1u6g A 150-153 disorder
       Region 1u6g A 154-213 order
       Region 1u6g A 214-221 disorder
       Region 1u6g A 222-432 order
       Region 1u6g A 433-437 disorder
       Region 1u6g A 438-776 order
Seq 15-776 Hetero pentamer : IID00059Complex,IID00321Complex,P63208
 Evidence X-RAY 1ldk B Reference
       Region 1ldk B 411-776 order
 Evidence X-RAY 1ldk A Reference
       Region 1ldk A 15-55 order
       Region 1ldk A 56-81 disorder
       Region 1ldk A 82-149 order
       Region 1ldk A 150-153 disorder
       Region 1ldk A 154-216 order
       Region 1ldk A 217-224 disorder
       Region 1ldk A 225-410 order
Seq 17-776 Hetero dimer : IID00059Complex
 Evidence X-RAY 1ldj A Reference
       Region 1ldj A 17-55 order
       Region 1ldj A 56-83 disorder
       Region 1ldj A 84-149 order
       Region 1ldj A 150-156 disorder
       Region 1ldj A 157-776 order
Seq 411-690 Hetero trimer : IID00059Complex,IID00518Complex
 Evidence X-RAY 4f52 C Reference
       Region 4f52 C 411-418 disorder
       Region 4f52 C 419-431 order
       Region 4f52 C 432-441 disorder
       Region 4f52 C 442-456 order
       Region 4f52 C 457-460 disorder
       Region 4f52 C 461-494 order
       Region 4f52 C 495-496 disorder
       Region 4f52 C 497-688 order
       Region 4f52 C 689-690 disorder
 Evidence X-RAY 4f52 A Reference
       Region 4f52 A 411-419 disorder
       Region 4f52 A 420-431 order
       Region 4f52 A 432-441 disorder
       Region 4f52 A 442-455 order
       Region 4f52 A 456-457 disorder
       Region 4f52 A 458-689 order
       Region 4f52 A 690-690 disorder
Seq 411-776 Hetero dimer : IID00059Complex
 Evidence X-RAY 3rtr E Reference
       Region 3rtr E 411-417 disorder
       Region 3rtr E 418-776 order
 Evidence X-RAY 3rtr C Reference
       Region 3rtr C 411-418 disorder
       Region 3rtr C 419-432 order
       Region 3rtr C 433-440 disorder
       Region 3rtr C 441-495 order
       Region 3rtr C 496-498 disorder
       Region 3rtr C 499-590 order
       Region 3rtr C 591-602 disorder
       Region 3rtr C 603-614 order
       Region 3rtr C 615-619 disorder
       Region 3rtr C 620-649 order
       Region 3rtr C 650-652 disorder
       Region 3rtr C 653-661 order
       Region 3rtr C 662-663 disorder
       Region 3rtr C 664-670 order
       Region 3rtr C 671-673 disorder
       Region 3rtr C 674-677 order
       Region 3rtr C 678-682 disorder
       Region 3rtr C 683-776 order
 Evidence X-RAY 3rtr A Reference
       Region 3rtr A 411-417 disorder
       Region 3rtr A 418-432 order
       Region 3rtr A 433-438 disorder
       Region 3rtr A 439-776 order
 Evidence X-RAY 3rtr G Reference
       Region 3rtr G 411-416 disorder
       Region 3rtr G 417-776 order
Seq 411-776 Hetero hexamer : IID00059Complex,Q96GG9
 Evidence X-RAY 4p5o C Reference
       Region 4p5o C 411-415 disorder
       Region 4p5o C 416-596 order
       Region 4p5o C 597-599 disorder
       Region 4p5o C 600-610 order
       Region 4p5o C 611-619 disorder
       Region 4p5o C 620-649 order
       Region 4p5o C 650-664 disorder
       Region 4p5o C 665-669 order
       Region 4p5o C 670-681 disorder
       Region 4p5o C 682-776 order
 Evidence X-RAY 4p5o A Reference
       Region 4p5o A 411-415 disorder
       Region 4p5o A 416-612 order
       Region 4p5o A 613-619 disorder
       Region 4p5o A 620-648 order
       Region 4p5o A 649-664 disorder
       Region 4p5o A 665-669 order
       Region 4p5o A 670-680 disorder
       Region 4p5o A 681-776 order
Seq 702-776 Hetero trimer : Q96GG9
 Evidence X-RAY 3tdu D Reference
       Region 3tdu D 702-776 order
 Evidence X-RAY 3tdu C Reference
       Region 3tdu C 702-776 order
Seq 702-776 Hetero trimer : Q96GG9
 Evidence X-RAY 3tdz D Reference
       Region 3tdz D 702-775 order
       Region 3tdz D 776-776 disorder
 Evidence X-RAY 3tdz C Reference
       Region 3tdz C 702-776 order
Seq 702-776 Hetero dimer : Q92564
 Evidence X-RAY 5v89 C Reference
       Region 5v89 C 702-702 disorder
       Region 5v89 C 703-738 order
       Region 5v89 C 739-743 disorder
       Region 5v89 C 744-766 order
       Region 5v89 C 767-768 disorder
       Region 5v89 C 769-776 order
 
Prediction
NeProc
Disorder 1-11,65-78,655-663,687-696
Order 12-57,79-217,224-411,417-654,664-686,697-776
ProS 660-663,696-696
AlphaFold
Disorder 1-15,56-82,215-223,550-550,690-690
Order 16-55,83-214,224-549,551-689,691-776
Pfam Hmmer
PF00888 21-676 5.9e-301
SEG 638-651
Function
Function in SwissProt
Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. SCF complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins (PubMed:27565346). In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and exchange of the substrate recognition component is mediated by TIP120A/CAND1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(BTRC) and/or SCF(FBXW11) direct ubiquitination of CEP68 (PubMed:25704143, PubMed:25503564). SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of CCNE1, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO1) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) directs ubiquitination of TTI1 and TELO2. SCF(FBXO10) directs ubiquitination of BCL2.
Biological Process
See also
Diagram with PDB data
AXIN1/GSK3BCrystal structure of GSK-3/Axin complex bound to phosphorylated N-terminal auto-inhibitory pS9 peptide
REST/CTDSP1Structure of Scp1 D96N bound to REST-pS861/4 peptide