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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7Z8V

CAND1-SCF-SKP2 (SKP1deldel) CAND1 engaged SCF rocked

Functional Information from GO Data
ChainGOidnamespacecontents
C0000082biological_processG1/S transition of mitotic cell cycle
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006511biological_processubiquitin-dependent protein catabolic process
C0006513biological_processprotein monoubiquitination
C0006915biological_processapoptotic process
C0008283biological_processcell population proliferation
C0009887biological_processanimal organ morphogenesis
C0016567biological_processprotein ubiquitination
C0019005cellular_componentSCF ubiquitin ligase complex
C0030674molecular_functionprotein-macromolecule adaptor activity
C0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
C0031461cellular_componentcullin-RING ubiquitin ligase complex
C0031625molecular_functionubiquitin protein ligase binding
C0034599biological_processcellular response to oxidative stress
C0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
C0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
C0070936biological_processprotein K48-linked ubiquitination
C0097193biological_processintrinsic apoptotic signaling pathway
C0160072molecular_functionubiquitin ligase complex scaffold activity
C1990452cellular_componentParkin-FBXW7-Cul1 ubiquitin ligase complex
D0000151cellular_componentubiquitin ligase complex
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005794cellular_componentGolgi apparatus
D0005829cellular_componentcytosol
D0010265biological_processSCF complex assembly
D0016020cellular_componentmembrane
D0016567biological_processprotein ubiquitination
D0017025molecular_functionTBP-class protein binding
D0030154biological_processcell differentiation
D0031461cellular_componentcullin-RING ubiquitin ligase complex
D0034774cellular_componentsecretory granule lumen
D0043086biological_processnegative regulation of catalytic activity
D0045893biological_processpositive regulation of DNA-templated transcription
D0045899biological_processpositive regulation of RNA polymerase II transcription preinitiation complex assembly
D0070062cellular_componentextracellular exosome
D1904813cellular_componentficolin-1-rich granule lumen
F0000082biological_processG1/S transition of mitotic cell cycle
F0000086biological_processG2/M transition of mitotic cell cycle
F0000209biological_processprotein polyubiquitination
F0002376biological_processimmune system process
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005730cellular_componentnucleolus
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006511biological_processubiquitin-dependent protein catabolic process
F0016567biological_processprotein ubiquitination
F0019005cellular_componentSCF ubiquitin ligase complex
F0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
F0033148biological_processpositive regulation of intracellular estrogen receptor signaling pathway
F0042802molecular_functionidentical protein binding
F0042981biological_processregulation of apoptotic process
F0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
F0045087biological_processinnate immune response
F0048661biological_processpositive regulation of smooth muscle cell proliferation
F0051607biological_processdefense response to virus
F0051726biological_processregulation of cell cycle
F0070534biological_processprotein K63-linked ubiquitination
F0070936biological_processprotein K48-linked ubiquitination
F0071460biological_processcellular response to cell-matrix adhesion
F1902916biological_processpositive regulation of protein polyubiquitination
F1905168biological_processpositive regulation of double-strand break repair via homologous recombination
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_idPS01256
Number of Residues28
DetailsCULLIN_1 Cullin family signature. IKkcIdiLIEKeYLeRvdgekdtYsYlA
ChainResidueDetails
CILE749-ALA776
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
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)","evidences":[{"source":"PubMed","id":"10597293","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15537541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18805092","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues37
DetailsRepeat: {"description":"HEAT 2"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues36
DetailsRepeat: {"description":"HEAT 3"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues34
DetailsRepeat: {"description":"HEAT 4"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues37
DetailsRepeat: {"description":"HEAT 5"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues37
DetailsRepeat: {"description":"HEAT 6"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues34
DetailsRepeat: {"description":"HEAT 7"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues43
DetailsRepeat: {"description":"HEAT 10"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues39
DetailsRepeat: {"description":"HEAT 11"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues37
DetailsRepeat: {"description":"HEAT 12"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues39
DetailsRepeat: {"description":"HEAT 13"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues37
DetailsRepeat: {"description":"HEAT 14"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues37
DetailsRepeat: {"description":"HEAT 15"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues37
DetailsRepeat: {"description":"HEAT 16"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues39
DetailsRepeat: {"description":"HEAT 17"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues38
DetailsRepeat: {"description":"HEAT 18"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues36
DetailsRepeat: {"description":"HEAT 19"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues37
DetailsRepeat: {"description":"HEAT 20"}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues37
DetailsRepeat: {"description":"HEAT 21"}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues32
DetailsRepeat: {"description":"HEAT 22"}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues37
DetailsRepeat: {"description":"HEAT 23"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues37
DetailsRepeat: {"description":"HEAT 24"}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues54
DetailsRepeat: {"description":"HEAT 25"}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues34
DetailsRepeat: {"description":"HEAT 26"}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues49
DetailsRepeat: {"description":"HEAT 27"}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues45
DetailsZinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI30
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_FI31
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_FI32
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_FI33
Number of Residues25
DetailsRepeat: {"description":"LRR 1","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues27
DetailsRepeat: {"description":"LRR 2","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues24
DetailsRepeat: {"description":"LRR 3","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues22
DetailsRepeat: {"description":"LRR 4","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues26
DetailsRepeat: {"description":"LRR 5","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues22
DetailsRepeat: {"description":"LRR 6","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI39
Number of Residues21
DetailsRepeat: {"description":"LRR 7","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI40
Number of Residues22
DetailsRepeat: {"description":"LRR 8","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI41
Number of Residues19
DetailsRepeat: {"description":"LRR 9","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI42
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI43
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_FI44
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

245011

PDB entries from 2025-11-19

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