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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8JE2

Cryo-EM structure of neddylated Cul2-Rbx1-EloBC-FEM1B complexed with FNIP1-FLCN

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0010498biological_processproteasomal protein catabolic process
A0016567biological_processprotein ubiquitination
A0019005cellular_componentSCF ubiquitin ligase complex
A0030163biological_processprotein catabolic process
A0030674molecular_functionprotein-macromolecule adaptor activity
A0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
A0031461cellular_componentcullin-RING ubiquitin ligase complex
A0031462cellular_componentCul2-RING ubiquitin ligase complex
A0031625molecular_functionubiquitin protein ligase binding
A0031981cellular_componentnuclear lumen
A0097193biological_processintrinsic apoptotic signaling pathway
A0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
A0160072molecular_functionubiquitin ligase complex scaffold activity
B0006368biological_processtranscription elongation by RNA polymerase II
B0030891cellular_componentVCB complex
B0070449cellular_componentelongin complex
C0006511biological_processubiquitin-dependent protein catabolic process
D0000151cellular_componentubiquitin ligase complex
D0002070biological_processepithelial cell maturation
D0005123molecular_functiondeath receptor binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005829cellular_componentcytosol
D0006915biological_processapoptotic process
D0016567biological_processprotein ubiquitination
D0031462cellular_componentCul2-RING ubiquitin ligase complex
D0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
D0046872molecular_functionmetal ion binding
D0051438biological_processregulation of ubiquitin-protein transferase activity
D0060442biological_processbranching involved in prostate gland morphogenesis
D0060743biological_processepithelial cell maturation involved in prostate gland development
D0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
D1902041biological_processregulation of extrinsic apoptotic signaling pathway via death domain receptors
D1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
D2000001biological_processregulation of DNA damage checkpoint
H0000122biological_processnegative regulation of transcription by RNA polymerase II
H0001783biological_processB cell apoptotic process
H0002327biological_processimmature B cell differentiation
H0002904biological_processpositive regulation of B cell apoptotic process
H0005515molecular_functionprotein binding
H0005737cellular_componentcytoplasm
H0005764cellular_componentlysosome
H0005765cellular_componentlysosomal membrane
H0005829cellular_componentcytosol
H0007040biological_processlysosome organization
H0008047molecular_functionenzyme activator activity
H0008285biological_processnegative regulation of cell population proliferation
H0009267biological_processcellular response to starvation
H0016020cellular_componentmembrane
H0019899molecular_functionenzyme binding
H0030183biological_processB cell differentiation
H0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
H0031334biological_processpositive regulation of protein-containing complex assembly
H0031648biological_processprotein destabilization
H0031669biological_processcellular response to nutrient levels
H0031929biological_processTOR signaling
H0032007biological_processnegative regulation of TOR signaling
H0032008biological_processpositive regulation of TOR signaling
H0038202biological_processTORC1 signaling
H0042030molecular_functionATPase inhibitor activity
H0046872molecular_functionmetal ion binding
H0051087molecular_functionprotein-folding chaperone binding
H1900181biological_processnegative regulation of protein localization to nucleus
H1904263biological_processpositive regulation of TORC1 signaling
H1905672biological_processnegative regulation of lysosome organization
H2000973biological_processregulation of pro-B cell differentiation
Functional Information from PROSITE/UniProt
site_idPS01256
Number of Residues28
DetailsCULLIN_1 Cullin family signature. IKkcIevLIDKqYIeRsqasadeYsYvA
ChainResidueDetails
AILE718-ALA745
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62869","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues29
DetailsRepeat: {"description":"ANK 4"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues29
DetailsRepeat: {"description":"ANK 5"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues30
DetailsRepeat: {"description":"ANK 6"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues33
DetailsRepeat: {"description":"TPR"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues37
DetailsRepeat: {"description":"ANK 8"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9Z2G0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsSite: {"description":"Cleavage; by a caspase-3-like protease","evidences":[{"source":"PubMed","id":"10542291","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsRegion: {"description":"KY-finger","evidences":[{"source":"UniProtKB","id":"Q68FD7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues7
DetailsMotif: {"description":"Cys degron","evidences":[{"source":"UniProtKB","id":"Q68FD7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q68FD7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-07-09

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