Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7Z8B

Structure of CRL7FBXW8 reveals coupling with CUL1-RBX1/ROC1 for multi-cullin-RING E3-catalyzed ubiquitin ligation

Functional Information from GO Data
ChainGOidnamespacecontents
C0000226biological_processmicrotubule cytoskeleton organization
C0000281biological_processmitotic cytokinesis
C0001570biological_processvasculogenesis
C0001837biological_processepithelial to mesenchymal transition
C0001890biological_processplacenta development
C0005515molecular_functionprotein binding
C0005680cellular_componentanaphase-promoting complex
C0005737cellular_componentcytoplasm
C0005794cellular_componentGolgi apparatus
C0005813cellular_componentcentrosome
C0005829cellular_componentcytosol
C0006508biological_processproteolysis
C0006511biological_processubiquitin-dependent protein catabolic process
C0007030biological_processGolgi organization
C0007088biological_processregulation of mitotic nuclear division
C0016567biological_processprotein ubiquitination
C0031461cellular_componentcullin-RING ubiquitin ligase complex
C0031467cellular_componentCul7-RING ubiquitin ligase complex
C0031625molecular_functionubiquitin protein ligase binding
C0046627biological_processnegative regulation of insulin receptor signaling pathway
C0048471cellular_componentperinuclear region of cytoplasm
C0050775biological_processpositive regulation of dendrite morphogenesis
C0160072molecular_functionubiquitin ligase complex scaffold activity
C1990393cellular_component3M complex
F0005515molecular_functionprotein binding
F0005737cellular_componentcytoplasm
F0005794cellular_componentGolgi apparatus
F0005814cellular_componentcentriole
F0005829cellular_componentcytosol
F0006511biological_processubiquitin-dependent protein catabolic process
F0007030biological_processGolgi organization
F0008283biological_processcell population proliferation
F0016567biological_processprotein ubiquitination
F0019005cellular_componentSCF ubiquitin ligase complex
F0031467cellular_componentCul7-RING ubiquitin ligase complex
F0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
F0036064cellular_componentciliary basal body
F0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
F0046627biological_processnegative regulation of insulin receptor signaling pathway
F0048471cellular_componentperinuclear region of cytoplasm
F0050775biological_processpositive regulation of dendrite morphogenesis
F0060271biological_processcilium assembly
F0060716biological_processlabyrinthine layer blood vessel development
F1990393cellular_component3M complex
F1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
R0000165biological_processMAPK cascade
R0000209biological_processprotein polyubiquitination
R0004842molecular_functionubiquitin-protein transferase activity
R0005515molecular_functionprotein binding
R0005634cellular_componentnucleus
R0005654cellular_componentnucleoplasm
R0005737cellular_componentcytoplasm
R0005813cellular_componentcentrosome
R0005829cellular_componentcytosol
R0006281biological_processDNA repair
R0006283biological_processtranscription-coupled nucleotide-excision repair
R0006511biological_processubiquitin-dependent protein catabolic process
R0006513biological_processprotein monoubiquitination
R0006974biological_processDNA damage response
R0007283biological_processspermatogenesis
R0008270molecular_functionzinc ion binding
R0016567biological_processprotein ubiquitination
R0016740molecular_functiontransferase activity
R0019005cellular_componentSCF ubiquitin ligase complex
R0019788molecular_functionNEDD8 transferase activity
R0030163biological_processprotein catabolic process
R0030891cellular_componentVCB complex
R0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
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
R0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
R0032480biological_processnegative regulation of type I interferon production
R0034450molecular_functionubiquitin-ubiquitin ligase activity
R0034599biological_processcellular response to oxidative stress
R0034644biological_processcellular response to UV
R0042110biological_processT cell activation
R0042770biological_processsignal transduction in response to DNA damage
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
R0046627biological_processnegative regulation of insulin receptor signaling pathway
R0046872molecular_functionmetal ion binding
R0060090molecular_functionmolecular adaptor activity
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
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
R1901525biological_processnegative regulation of mitophagy
R1902499biological_processpositive regulation of protein autoubiquitination
R1902883biological_processnegative regulation of response to oxidative stress
R1904263biological_processpositive regulation of TORC1 signaling
S0000209biological_processprotein polyubiquitination
S0005515molecular_functionprotein binding
S0005634cellular_componentnucleus
S0005654cellular_componentnucleoplasm
S0005737cellular_componentcytoplasm
S0005813cellular_componentcentrosome
S0005829cellular_componentcytosol
S0006338biological_processchromatin remodeling
S0006511biological_processubiquitin-dependent protein catabolic process
S0006513biological_processprotein monoubiquitination
S0008013molecular_functionbeta-catenin binding
S0016567biological_processprotein ubiquitination
S0019005cellular_componentSCF ubiquitin ligase complex
S0019904molecular_functionprotein domain specific binding
S0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
S0031467cellular_componentCul7-RING ubiquitin ligase complex
S0031519cellular_componentPcG protein complex
S0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
S0051457biological_processmaintenance of protein location in nucleus
S0070936biological_processprotein K48-linked ubiquitination
S0097602molecular_functioncullin family protein binding
S0140677molecular_functionmolecular function activator activity
S0160072molecular_functionubiquitin ligase complex scaffold activity
S1990444molecular_functionF-box domain binding
S1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
S1990757molecular_functionubiquitin ligase activator activity
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. AVAAyeDgFLNIWDL
ChainResidueDetails
FALA272-LEU286
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues49
DetailsRepeat: {"description":"WD 1","evidences":[{"source":"PubMed","id":"35982156","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7Z8B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues40
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"PubMed","id":"35982156","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7Z8B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues40
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"PubMed","id":"35982156","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7Z8B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues42
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"PubMed","id":"35982156","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7Z8B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues45
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"PubMed","id":"35982156","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7Z8B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues45
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"PubMed","id":"35982156","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7Z8B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues37
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"PubMed","id":"35982156","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7Z8B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues45
DetailsZinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
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_FI11
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_FI12
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_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

PDB statisticsPDBj update infoContact PDBjnumon