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4F8C

Structure of the Cif:Nedd8 complex - Yersinia pseudotuberculosis Cycle Inhibiting Factor in complex with human Nedd8

Functional Information from GO Data
ChainGOidnamespacecontents
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006357biological_processregulation of transcription by RNA polymerase II
B0006508biological_processproteolysis
B0006511biological_processubiquitin-dependent protein catabolic process
B0008104biological_processprotein localization
B0009653biological_processanatomical structure morphogenesis
B0016567biological_processprotein ubiquitination
B0019941biological_processmodification-dependent protein catabolic process
B0030162biological_processregulation of proteolysis
B0031386molecular_functionprotein tag activity
B0031625molecular_functionubiquitin protein ligase binding
B0036211biological_processprotein modification process
B0045116biological_processprotein neddylation
B0070062cellular_componentextracellular exosome
B0072757biological_processcellular response to camptothecin
B0098794cellular_componentpostsynapse
B0098978cellular_componentglutamatergic synapse
B0150052biological_processregulation of postsynapse assembly
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006357biological_processregulation of transcription by RNA polymerase II
D0006508biological_processproteolysis
D0006511biological_processubiquitin-dependent protein catabolic process
D0008104biological_processprotein localization
D0009653biological_processanatomical structure morphogenesis
D0016567biological_processprotein ubiquitination
D0019941biological_processmodification-dependent protein catabolic process
D0030162biological_processregulation of proteolysis
D0031386molecular_functionprotein tag activity
D0031625molecular_functionubiquitin protein ligase binding
D0036211biological_processprotein modification process
D0045116biological_processprotein neddylation
D0070062cellular_componentextracellular exosome
D0072757biological_processcellular response to camptothecin
D0098794cellular_componentpostsynapse
D0098978cellular_componentglutamatergic synapse
D0150052biological_processregulation of postsynapse assembly
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 301
ChainResidue
ALEU57
AASN60
AVAL61
ASER108
ASER109
AARG111
AHOH510

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
AILE235
AASP236
AHIS239
AILE240
AHIS226
AGLY229

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO C 301
ChainResidue
CTHR225
CHIS226
CILE235
CASP236
CHIS239
CILE240

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO C 302
ChainResidue
CLEU57
CASN60
CVAL61
CSER108
CARG111
CHOH530

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KerVeEkegIPpqqQrLIYsGkqmnD
ChainResidueDetails
BLYS27-ASP52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"19308257","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22691497","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"Q63KH5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsRegion: {"description":"Interaction with UBE1C","evidences":[{"source":"PubMed","id":"14690597","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Interaction with UBE1C","evidences":[{"source":"PubMed","id":"14690597","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
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_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P29595","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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