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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8IJ1

Protomer 1 and 2 of the asymmetry trimer of the Cul2-Rbx1-EloBC-FEM1B ubiquitin ligase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0010498biological_processproteasomal protein catabolic process
A0016567biological_processprotein ubiquitination
A0019005cellular_componentSCF ubiquitin ligase complex
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
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0072344biological_processrescue of stalled ribosome
A0097193biological_processintrinsic apoptotic signaling pathway
A0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
A0160072molecular_functionubiquitin ligase complex scaffold activity
A0160276biological_processnegative regulation of beige fat cell differentiation
A1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
A2000104biological_processnegative regulation of DNA-templated DNA replication
B0006368biological_processtranscription elongation by RNA polymerase II
B0030891cellular_componentVCB complex
B0070449cellular_componentelongin complex
C0006511biological_processubiquitin-dependent protein catabolic process
D0000151cellular_componentubiquitin ligase complex
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
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
F0000082biological_processG1/S transition of mitotic cell cycle
F0000122biological_processnegative regulation of transcription by RNA polymerase II
F0004842molecular_functionubiquitin-protein transferase activity
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005730cellular_componentnucleolus
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006511biological_processubiquitin-dependent protein catabolic process
F0010498biological_processproteasomal protein catabolic process
F0016567biological_processprotein ubiquitination
F0019005cellular_componentSCF ubiquitin ligase complex
F0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
F0031461cellular_componentcullin-RING ubiquitin ligase complex
F0031462cellular_componentCul2-RING ubiquitin ligase complex
F0031625molecular_functionubiquitin protein ligase binding
F0031981cellular_componentnuclear lumen
F0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
F0072344biological_processrescue of stalled ribosome
F0097193biological_processintrinsic apoptotic signaling pathway
F0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
F0160072molecular_functionubiquitin ligase complex scaffold activity
F0160276biological_processnegative regulation of beige fat cell differentiation
F1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
F2000104biological_processnegative regulation of DNA-templated DNA replication
G0006368biological_processtranscription elongation by RNA polymerase II
G0030891cellular_componentVCB complex
G0070449cellular_componentelongin complex
H0006511biological_processubiquitin-dependent protein catabolic process
I0000151cellular_componentubiquitin ligase complex
I0005123molecular_functiondeath receptor binding
I0005515molecular_functionprotein binding
I0005634cellular_componentnucleus
I0005654cellular_componentnucleoplasm
I0005737cellular_componentcytoplasm
I0005739cellular_componentmitochondrion
I0005829cellular_componentcytosol
I0006915biological_processapoptotic process
I0016567biological_processprotein ubiquitination
I0031462cellular_componentCul2-RING ubiquitin ligase complex
I0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
I0046872molecular_functionmetal ion binding
I0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
I1902041biological_processregulation of extrinsic apoptotic signaling pathway via death domain receptors
I1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
I2000001biological_processregulation of DNA damage checkpoint
R0000082biological_processG1/S transition of mitotic cell cycle
R0000122biological_processnegative regulation of transcription by RNA polymerase II
R0000165biological_processMAPK cascade
R0000209biological_processprotein polyubiquitination
R0004842molecular_functionubiquitin-protein transferase activity
R0005515molecular_functionprotein binding
R0005634cellular_componentnucleus
R0005654cellular_componentnucleoplasm
R0005737cellular_componentcytoplasm
R0005794cellular_componentGolgi apparatus
R0005813cellular_componentcentrosome
R0005829cellular_componentcytosol
R0006281biological_processDNA repair
R0006283biological_processtranscription-coupled nucleotide-excision repair
R0006289biological_processnucleotide-excision repair
R0006355biological_processregulation of DNA-templated transcription
R0006511biological_processubiquitin-dependent protein catabolic process
R0006513biological_processprotein monoubiquitination
R0006879biological_processintracellular iron ion homeostasis
R0006974biological_processDNA damage response
R0007283biological_processspermatogenesis
R0007346biological_processregulation of mitotic cell cycle
R0008270molecular_functionzinc ion binding
R0008283biological_processcell population proliferation
R0010506biological_processregulation of autophagy
R0010564biological_processregulation of cell cycle process
R0010824biological_processregulation of centrosome duplication
R0014033biological_processneural crest cell differentiation
R0016567biological_processprotein ubiquitination
R0016740molecular_functiontransferase activity
R0019005cellular_componentSCF ubiquitin ligase complex
R0019788molecular_functionNEDD8 transferase activity
R0030174biological_processregulation of DNA-templated DNA replication initiation
R0030510biological_processregulation of BMP signaling pathway
R0030891cellular_componentVCB complex
R0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
R0031297biological_processreplication fork processing
R0031461cellular_componentcullin-RING ubiquitin ligase complex
R0031462cellular_componentCul2-RING ubiquitin ligase complex
R0031463cellular_componentCul3-RING ubiquitin ligase complex
R0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
R0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
R0031466cellular_componentCul5-RING ubiquitin ligase complex
R0031467cellular_componentCul7-RING ubiquitin ligase complex
R0031625molecular_functionubiquitin protein ligase binding
R0032006biological_processregulation of TOR signaling
R0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
R0032480biological_processnegative regulation of type I interferon production
R0032814biological_processregulation of natural killer cell activation
R0034450molecular_functionubiquitin-ubiquitin ligase activity
R0034599biological_processcellular response to oxidative stress
R0034644biological_processcellular response to UV
R0040029biological_processepigenetic regulation of gene expression
R0042110biological_processT cell activation
R0042127biological_processregulation of cell population proliferation
R0042752biological_processregulation of circadian rhythm
R0042770biological_processsignal transduction in response to DNA damage
R0042981biological_processregulation of apoptotic process
R0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
R0043124biological_processnegative regulation of canonical NF-kappaB signal transduction
R0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
R0043687biological_processpost-translational protein modification
R0044314biological_processprotein K27-linked ubiquitination
R0044877molecular_functionprotein-containing complex binding
R0045116biological_processprotein neddylation
R0045732biological_processpositive regulation of protein catabolic process
R0045995biological_processregulation of embryonic development
R0046627biological_processnegative regulation of insulin receptor signaling pathway
R0046872molecular_functionmetal ion binding
R0050727biological_processregulation of inflammatory response
R0051298biological_processcentrosome duplication
R0051726biological_processregulation of cell cycle
R0060090molecular_functionmolecular adaptor activity
R0060173biological_processlimb development
R0060271biological_processcilium assembly
R0060964biological_processregulation of miRNA-mediated gene silencing
R0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
R0061630molecular_functionubiquitin protein ligase activity
R0061663molecular_functionNEDD8 ligase activity
R0062197biological_processcellular response to chemical stress
R0070936biological_processprotein K48-linked ubiquitination
R0071230biological_processcellular response to amino acid stimulus
R0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
R0080135biological_processregulation of cellular response to stress
R0090090biological_processnegative regulation of canonical Wnt signaling pathway
R0090734cellular_componentsite of DNA damage
R0097602molecular_functioncullin family protein binding
R0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
R0160240biological_processRNA polymerase II transcription initiation surveillance
R0160276biological_processnegative regulation of beige fat cell differentiation
R1900076biological_processregulation of cellular response to insulin stimulus
R1901524biological_processregulation of mitophagy
R1901525biological_processnegative regulation of mitophagy
R1901987biological_processregulation of cell cycle phase transition
R1902412biological_processregulation of mitotic cytokinesis
R1902499biological_processpositive regulation of protein autoubiquitination
R1902883biological_processnegative regulation of response to oxidative stress
R1904178biological_processnegative regulation of adipose tissue development
R1904263biological_processpositive regulation of TORC1 signaling
R1904415biological_processregulation of xenophagy
R1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
R2000001biological_processregulation of DNA damage checkpoint
R2000036biological_processregulation of stem cell population maintenance
R2000104biological_processnegative regulation of DNA-templated DNA replication
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 Residues60
DetailsDomain: {"description":"Cullin neddylation","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)","evidences":[{"source":"PubMed","id":"10092517","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10597293","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11961546","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38605244","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LDK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U6G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HYE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DPL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RTR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4P5O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8Q7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8RHZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11961546","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38605244","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LDK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U6G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HYE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DPL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RTR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4P5O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7Z8B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8Q7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8RHZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11961546","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38605244","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LDK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U6G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HYE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RTR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4P5O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8Q7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8RHZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
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_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62869","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues58
DetailsRepeat: {"description":"ANK 1"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues58
DetailsRepeat: {"description":"ANK 2"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues58
DetailsRepeat: {"description":"ANK 3"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues58
DetailsRepeat: {"description":"ANK 4"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues58
DetailsRepeat: {"description":"ANK 5"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues60
DetailsRepeat: {"description":"ANK 6"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues66
DetailsRepeat: {"description":"TPR"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues88
DetailsRepeat: {"description":"ANK 7"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues74
DetailsRepeat: {"description":"ANK 8"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9Z2G0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsSite: {"description":"Cleavage; by a caspase-3-like protease","evidences":[{"source":"PubMed","id":"10542291","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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