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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7ONI

Structure of Neddylated CUL5 C-terminal region-RBX2-ARIH2*

Functional Information from GO Data
ChainGOidnamespacecontents
C0000082biological_processG1/S transition of mitotic cell cycle
C0004842molecular_functionubiquitin-protein transferase activity
C0005262molecular_functioncalcium channel activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006511biological_processubiquitin-dependent protein catabolic process
C0007165biological_processsignal transduction
C0010498biological_processproteasomal protein catabolic process
C0016477biological_processcell migration
C0016567biological_processprotein ubiquitination
C0019005cellular_componentSCF ubiquitin ligase complex
C0030335biological_processpositive regulation of cell migration
C0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
C0031461cellular_componentcullin-RING ubiquitin ligase complex
C0031466cellular_componentCul5-RING ubiquitin ligase complex
C0031625molecular_functionubiquitin protein ligase binding
C0038023molecular_functionsignaling receptor activity
C0038026biological_processreelin-mediated signaling pathway
C0038128biological_processERBB2 signaling pathway
C0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
C0051895biological_processnegative regulation of focal adhesion assembly
C0070588biological_processcalcium ion transmembrane transport
C0070979biological_processprotein K11-linked ubiquitination
C0090734cellular_componentsite of DNA damage
C0097193biological_processintrinsic apoptotic signaling pathway
C0120184biological_processnegative regulation of focal adhesion disassembly
C0160072molecular_functionubiquitin ligase complex scaffold activity
C2001222biological_processregulation of neuron migration
H0000151cellular_componentubiquitin ligase complex
H0000209biological_processprotein polyubiquitination
H0004842molecular_functionubiquitin-protein transferase activity
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005737cellular_componentcytoplasm
H0006511biological_processubiquitin-dependent protein catabolic process
H0008270molecular_functionzinc ion binding
H0016567biological_processprotein ubiquitination
H0016740molecular_functiontransferase activity
H0031466cellular_componentCul5-RING ubiquitin ligase complex
H0031624molecular_functionubiquitin conjugating enzyme binding
H0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
H0046872molecular_functionmetal ion binding
H0048588biological_processdevelopmental cell growth
H0061630molecular_functionubiquitin protein ligase activity
H0070534biological_processprotein K63-linked ubiquitination
H0070936biological_processprotein K48-linked ubiquitination
H0071425biological_processhematopoietic stem cell proliferation
H1903955biological_processobsolete positive regulation of protein targeting to mitochondrion
N0005515molecular_functionprotein binding
N0005634cellular_componentnucleus
N0005654cellular_componentnucleoplasm
N0005737cellular_componentcytoplasm
N0005829cellular_componentcytosol
N0006508biological_processproteolysis
N0006511biological_processubiquitin-dependent protein catabolic process
N0009653biological_processanatomical structure morphogenesis
N0016567biological_processprotein ubiquitination
N0019941biological_processmodification-dependent protein catabolic process
N0030162biological_processregulation of proteolysis
N0031386molecular_functionprotein tag activity
N0031625molecular_functionubiquitin protein ligase binding
N0036211biological_processprotein modification process
N0045116biological_processprotein neddylation
N0070062cellular_componentextracellular exosome
N0072757biological_processcellular response to camptothecin
N0098794cellular_componentpostsynapse
N0098978cellular_componentglutamatergic synapse
N0150052biological_processregulation of postsynapse assembly
R0005507molecular_functioncopper ion binding
R0005515molecular_functionprotein binding
R0005634cellular_componentnucleus
R0005654cellular_componentnucleoplasm
R0005737cellular_componentcytoplasm
R0005829cellular_componentcytosol
R0006511biological_processubiquitin-dependent protein catabolic process
R0008270molecular_functionzinc ion binding
R0016567biological_processprotein ubiquitination
R0016740molecular_functiontransferase activity
R0019788molecular_functionNEDD8 transferase activity
R0030335biological_processpositive regulation of cell migration
R0030968biological_processendoplasmic reticulum unfolded protein response
R0031466cellular_componentCul5-RING ubiquitin ligase complex
R0035556biological_processintracellular signal transduction
R0038026biological_processreelin-mediated signaling pathway
R0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
R0043687biological_processpost-translational protein modification
R0045116biological_processprotein neddylation
R0046872molecular_functionmetal ion binding
R0051775biological_processresponse to redox state
R0051895biological_processnegative regulation of focal adhesion assembly
R0061630molecular_functionubiquitin protein ligase activity
R0061663molecular_functionNEDD8 ligase activity
R0070979biological_processprotein K11-linked ubiquitination
R0097602molecular_functioncullin family protein binding
R0120184biological_processnegative regulation of focal adhesion disassembly
R2001222biological_processregulation of neuron migration
Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KerVeEkegIPpqqQrLIYsGkqmnD
ChainResidueDetails
NLYS27-ASP52
site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CkHdFCwmCL
ChainResidueDetails
HCYS318-LEU327
site_idPS01256
Number of Residues28
DetailsCULLIN_1 Cullin family signature. IKeqIewLIEHkYIrRdesdintFiYmA
ChainResidueDetails
CILE753-ALA780
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues61
DetailsDomain: {"description":"Cullin neddylation","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)","evidences":[{"source":"PubMed","id":"18805092","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33268465","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34518685","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7ONI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues49
DetailsZinc finger: {"description":"RING-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues62
DetailsZinc finger: {"description":"IBR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues47
DetailsRegion: {"description":"UBA-like","evidences":[{"source":"UniProtKB","id":"Q9Y4X5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34518685","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7OD1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7ONI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34518685","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7OD1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues42
DetailsZinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34518685","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7ONI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsRegion: {"description":"Interaction with UBE1C","evidences":[{"source":"PubMed","id":"14690597","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsSite: {"description":"Interaction with UBE1C","evidences":[{"source":"PubMed","id":"14690597","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"(Microbial infection) Deamidated glutamine","evidences":[{"source":"PubMed","id":"20688984","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21903097","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23175788","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23589306","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26632597","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P29595","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)","evidences":[{"source":"PubMed","id":"38316879","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

250359

PDB entries from 2026-03-11

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