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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8BYL

Cryo-EM structure of SKP1-SKP2-CKS1 from the SCFSKP2 E3 ligase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0000209biological_processprotein polyubiquitination
A0000785cellular_componentchromatin
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0006338biological_processchromatin remodeling
A0006355biological_processregulation of DNA-templated transcription
A0006511biological_processubiquitin-dependent protein catabolic process
A0006879biological_processintracellular iron ion homeostasis
A0007346biological_processregulation of mitotic cell cycle
A0008013molecular_functionbeta-catenin binding
A0010564biological_processregulation of cell cycle process
A0010824biological_processregulation of centrosome duplication
A0014033biological_processneural crest cell differentiation
A0016567biological_processprotein ubiquitination
A0019005cellular_componentSCF ubiquitin ligase complex
A0019904molecular_functionprotein domain specific binding
A0030510biological_processregulation of BMP signaling pathway
A0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
A0031467cellular_componentCul7-RING ubiquitin ligase complex
A0031507biological_processheterochromatin formation
A0031519cellular_componentPcG protein complex
A0032006biological_processregulation of TOR signaling
A0042752biological_processregulation of circadian rhythm
A0042981biological_processregulation of apoptotic process
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0045892biological_processnegative regulation of DNA-templated transcription
A0050727biological_processregulation of inflammatory response
A0051124biological_processsynaptic assembly at neuromuscular junction
A0051298biological_processcentrosome duplication
A0051457biological_processmaintenance of protein location in nucleus
A0051726biological_processregulation of cell cycle
A0060173biological_processlimb development
A0060271biological_processcilium assembly
A0070936biological_processprotein K48-linked ubiquitination
A0097602molecular_functioncullin family protein binding
A0140677molecular_functionmolecular function activator activity
A0160072molecular_functionubiquitin ligase complex scaffold activity
A1901524biological_processregulation of mitophagy
A1904415biological_processregulation of xenophagy
A1990444molecular_functionF-box domain binding
A1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
A1990757molecular_functionubiquitin ligase activator activity
A2000001biological_processregulation of DNA damage checkpoint
B0000082biological_processG1/S transition of mitotic cell cycle
B0002376biological_processimmune system process
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006511biological_processubiquitin-dependent protein catabolic process
B0016567biological_processprotein ubiquitination
B0019005cellular_componentSCF ubiquitin ligase complex
B0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
B0042802molecular_functionidentical protein binding
B0042981biological_processregulation of apoptotic process
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0045087biological_processinnate immune response
B0051607biological_processdefense response to virus
B0070534biological_processprotein K63-linked ubiquitination
B0070936biological_processprotein K48-linked ubiquitination
B1905168biological_processpositive regulation of double-strand break repair via homologous recombination
B1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
C0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
C0005515molecular_functionprotein binding
C0005654cellular_componentnucleoplasm
C0007346biological_processregulation of mitotic cell cycle
C0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
C0019005cellular_componentSCF ubiquitin ligase complex
C0019901molecular_functionprotein kinase binding
C0042393molecular_functionhistone binding
C0043130molecular_functionubiquitin binding
C0051301biological_processcell division
C0061575molecular_functioncyclin-dependent protein serine/threonine kinase activator activity
D0000079biological_processregulation of cyclin-dependent protein serine/threonine kinase activity
D0000082biological_processG1/S transition of mitotic cell cycle
D0004860molecular_functionprotein kinase inhibitor activity
D0004861molecular_functioncyclin-dependent protein serine/threonine kinase inhibitor activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005768cellular_componentendosome
D0005829cellular_componentcytosol
D0007165biological_processsignal transduction
D0007507biological_processheart development
D0008285biological_processnegative regulation of cell population proliferation
D0012501biological_processprogrammed cell death
D0019901molecular_functionprotein kinase binding
D0019903molecular_functionprotein phosphatase binding
D0019914molecular_functioncyclin-dependent protein kinase regulator activity
D0030308biological_processnegative regulation of cell growth
D0030330biological_processDNA damage response, signal transduction by p53 class mediator
D0030332molecular_functioncyclin binding
D0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
D0031625molecular_functionubiquitin protein ligase binding
D0044877molecular_functionprotein-containing complex binding
D0045732biological_processpositive regulation of protein catabolic process
D0045740biological_processpositive regulation of DNA replication
D0045926biological_processnegative regulation of growth
D0045930biological_processnegative regulation of mitotic cell cycle
D0048102biological_processautophagic cell death
D0050680biological_processnegative regulation of epithelial cell proliferation
D0051087molecular_functionprotein-folding chaperone binding
D0051168biological_processnuclear export
D0051726biological_processregulation of cell cycle
D0060090molecular_functionmolecular adaptor activity
D0071285biological_processcellular response to lithium ion
D0090398biological_processcellular senescence
D0140678molecular_functionmolecular function inhibitor activity
D1901990biological_processregulation of mitotic cell cycle phase transition
D1902806biological_processregulation of cell cycle G1/S phase transition
D1904706biological_processnegative regulation of vascular associated smooth muscle cell proliferation
D1905179biological_processnegative regulation of cardiac muscle tissue regeneration
D1990757molecular_functionubiquitin ligase activator activity
D2000045biological_processregulation of G1/S transition of mitotic cell cycle
Functional Information from PROSITE/UniProt
site_idPS00944
Number of Residues19
DetailsCKS_1 Cyclin-dependent kinases regulatory subunits signature 1. YSdKYdDEeFEYRHVmLPK
ChainResidueDetails
CTYR3008-LYS3026
site_idPS00945
Number of Residues11
DetailsCKS_2 Cyclin-dependent kinases regulatory subunits signature 2. HePEpHILLFR
ChainResidueDetails
CHIS3060-ARG3070
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI2
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_FI3
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
site_idSWS_FT_FI4
Number of Residues46
DetailsDomain: {"description":"F-box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00080","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues25
DetailsRepeat: {"description":"LRR 1","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues27
DetailsRepeat: {"description":"LRR 2","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues24
DetailsRepeat: {"description":"LRR 3","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues22
DetailsRepeat: {"description":"LRR 4","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues26
DetailsRepeat: {"description":"LRR 5","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues22
DetailsRepeat: {"description":"LRR 6","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues21
DetailsRepeat: {"description":"LRR 7","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues22
DetailsRepeat: {"description":"LRR 8","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues19
DetailsRepeat: {"description":"LRR 9","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues21
DetailsRepeat: {"description":"LRR 10","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues22
DetailsRegion: {"description":"Mediates interaction with IFI27","evidences":[{"source":"PubMed","id":"27194766","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
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_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKB/AKT1, CDK1 and CDK2","evidences":[{"source":"PubMed","id":"10323868","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12042314","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16209941","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23478441","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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