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9PVH

Human Cullin-4 in complex with CAND2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0000109cellular_componentnucleotide-excision repair complex
A0001701biological_processin utero embryonic development
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0006289biological_processnucleotide-excision repair
A0006974biological_processDNA damage response
A0007283biological_processspermatogenesis
A0008283biological_processcell population proliferation
A0010506biological_processregulation of autophagy
A0016567biological_processprotein ubiquitination
A0030174biological_processregulation of DNA-templated DNA replication initiation
A0031297biological_processreplication fork processing
A0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
A0031625molecular_functionubiquitin protein ligase binding
A0032502biological_processdevelopmental process
A0032814biological_processregulation of natural killer cell activation
A0034644biological_processcellular response to UV
A0040029biological_processepigenetic regulation of gene expression
A0042110biological_processT cell activation
A0042127biological_processregulation of cell population proliferation
A0042254biological_processribosome biogenesis
A0042981biological_processregulation of apoptotic process
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0045732biological_processpositive regulation of protein catabolic process
A0045995biological_processregulation of embryonic development
A0051246biological_processregulation of protein metabolic process
A0060964biological_processregulation of miRNA-mediated gene silencing
A0061630molecular_functionubiquitin protein ligase activity
A0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
A0080135biological_processregulation of cellular response to stress
A0097193biological_processintrinsic apoptotic signaling pathway
A0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
A0160072molecular_functionubiquitin ligase complex scaffold activity
A1901987biological_processregulation of cell cycle phase transition
A1902412biological_processregulation of mitotic cytokinesis
A1904178biological_processnegative regulation of adipose tissue development
A2000036biological_processregulation of stem cell population maintenance
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005829cellular_componentcytosol
C0010265biological_processSCF complex assembly
C0016567biological_processprotein ubiquitination
C0045893biological_processpositive regulation of DNA-templated transcription
Functional Information from PROSITE/UniProt
site_idPS01256
Number of Residues28
DetailsCULLIN_1 Cullin family signature. LKkrIesLIDRdYMeRdkdnpnqYhYvA
ChainResidueDetails
ALEU732-ALA759

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":"38316879","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues37
DetailsRepeat: {"description":"HEAT 1"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues37
DetailsRepeat: {"description":"HEAT 2"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues38
DetailsRepeat: {"description":"HEAT 4"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues37
DetailsRepeat: {"description":"HEAT 5"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues36
DetailsRepeat: {"description":"HEAT 6"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues37
DetailsRepeat: {"description":"HEAT 7"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues37
DetailsRepeat: {"description":"HEAT 10"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues37
DetailsRepeat: {"description":"HEAT 11"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues39
DetailsRepeat: {"description":"HEAT 12"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues37
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 Residues39
DetailsRepeat: {"description":"HEAT 16"}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues37
DetailsRepeat: {"description":"HEAT 18"}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues35
DetailsRepeat: {"description":"HEAT 19"}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues33
DetailsRepeat: {"description":"HEAT 20"}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues36
DetailsRepeat: {"description":"HEAT 21"}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues37
DetailsRepeat: {"description":"HEAT 22"}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues36
DetailsRepeat: {"description":"HEAT 23"}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues36
DetailsRepeat: {"description":"HEAT 24"}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues37
DetailsRepeat: {"description":"HEAT 25"}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Ramsay A.","Leung H.Y."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}}]}
ChainResidueDetails

257179

PDB entries from 2026-07-29

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