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8PQL

K48-linked ubiquitin chain formation with a cullin-RING E3 ligase and Cdc34: NEDD8-CUL2-RBX1-ELOB/C-FEM1C with trapped UBE2R2-donor UB-acceptor UB-SIL1 peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0010498biological_processproteasomal protein catabolic process
A0016567biological_processprotein ubiquitination
A0019005cellular_componentSCF ubiquitin ligase complex
A0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
A0031461cellular_componentcullin-RING ubiquitin ligase complex
A0031462cellular_componentCul2-RING ubiquitin ligase complex
A0031625molecular_functionubiquitin protein ligase binding
A0031981cellular_componentnuclear lumen
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0072344biological_processrescue of stalled ribosome
A0097193biological_processintrinsic apoptotic signaling pathway
A0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
A0160072molecular_functionubiquitin ligase complex scaffold activity
A0160276biological_processnegative regulation of beige fat cell differentiation
A1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
A2000104biological_processnegative regulation of DNA-templated DNA replication
C0000166molecular_functionnucleotide binding
C0000209biological_processprotein polyubiquitination
C0004842molecular_functionubiquitin-protein transferase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0006511biological_processubiquitin-dependent protein catabolic process
C0006513biological_processprotein monoubiquitination
C0016567biological_processprotein ubiquitination
C0016740molecular_functiontransferase activity
C0061631molecular_functionubiquitin conjugating enzyme activity
C0070936biological_processprotein K48-linked ubiquitination
D0000122biological_processnegative regulation of transcription by RNA polymerase II
D0000151cellular_componentubiquitin ligase complex
D0001222molecular_functiontranscription corepressor binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006357biological_processregulation of transcription by RNA polymerase II
D0006367biological_processtranscription initiation at RNA polymerase II promoter
D0006511biological_processubiquitin-dependent protein catabolic process
D0016567biological_processprotein ubiquitination
D0030674molecular_functionprotein-macromolecule adaptor activity
D0031462cellular_componentCul2-RING ubiquitin ligase complex
D0031466cellular_componentCul5-RING ubiquitin ligase complex
D0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
D0070449cellular_componentelongin complex
D0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
D0140958biological_processtarget-directed miRNA degradation
D1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
D2000104biological_processnegative regulation of DNA-templated DNA replication
E0003723molecular_functionRNA binding
E0003735molecular_functionstructural constituent of ribosome
E0005515molecular_functionprotein binding
E0005615cellular_componentextracellular space
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005741cellular_componentmitochondrial outer membrane
E0005789cellular_componentendoplasmic reticulum membrane
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0010008cellular_componentendosome membrane
E0016567biological_processprotein ubiquitination
E0019941biological_processmodification-dependent protein catabolic process
E0022626cellular_componentcytosolic ribosome
E0030666cellular_componentendocytic vesicle membrane
E0031386molecular_functionprotein tag activity
E0031982cellular_componentvesicle
E0070062cellular_componentextracellular exosome
G0000122biological_processnegative regulation of transcription by RNA polymerase II
G0000151cellular_componentubiquitin ligase complex
G0001222molecular_functiontranscription corepressor binding
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005654cellular_componentnucleoplasm
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0006367biological_processtranscription initiation at RNA polymerase II promoter
G0006368biological_processtranscription elongation by RNA polymerase II
G0016567biological_processprotein ubiquitination
G0030891cellular_componentVCB complex
G0031462cellular_componentCul2-RING ubiquitin ligase complex
G0031466cellular_componentCul5-RING ubiquitin ligase complex
G0031625molecular_functionubiquitin protein ligase binding
G0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
G0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
G0065003biological_processprotein-containing complex assembly
G0070449cellular_componentelongin complex
G0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
G0140958biological_processtarget-directed miRNA degradation
G1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
G2000104biological_processnegative regulation of DNA-templated DNA replication
H0000151cellular_componentubiquitin ligase complex
H0005515molecular_functionprotein binding
H0005654cellular_componentnucleoplasm
H0005737cellular_componentcytoplasm
H0005829cellular_componentcytosol
H0016567biological_processprotein ubiquitination
H0031462cellular_componentCul2-RING ubiquitin ligase complex
H0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
H0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
H1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
K0000082biological_processG1/S transition of mitotic cell cycle
K0000109cellular_componentnucleotide-excision repair complex
K0000122biological_processnegative regulation of transcription by RNA polymerase II
K0000165biological_processMAPK cascade
K0000209biological_processprotein polyubiquitination
K0004842molecular_functionubiquitin-protein transferase activity
K0005515molecular_functionprotein binding
K0005634cellular_componentnucleus
K0005654cellular_componentnucleoplasm
K0005737cellular_componentcytoplasm
K0005794cellular_componentGolgi apparatus
K0005813cellular_componentcentrosome
K0005829cellular_componentcytosol
K0006281biological_processDNA repair
K0006283biological_processtranscription-coupled nucleotide-excision repair
K0006289biological_processnucleotide-excision repair
K0006355biological_processregulation of DNA-templated transcription
K0006511biological_processubiquitin-dependent protein catabolic process
K0006513biological_processprotein monoubiquitination
K0006879biological_processintracellular iron ion homeostasis
K0006974biological_processDNA damage response
K0007283biological_processspermatogenesis
K0007346biological_processregulation of mitotic cell cycle
K0008270molecular_functionzinc ion binding
K0008283biological_processcell population proliferation
K0010506biological_processregulation of autophagy
K0010564biological_processregulation of cell cycle process
K0010824biological_processregulation of centrosome duplication
K0014033biological_processneural crest cell differentiation
K0016567biological_processprotein ubiquitination
K0016740molecular_functiontransferase activity
K0019005cellular_componentSCF ubiquitin ligase complex
K0019788molecular_functionNEDD8 transferase activity
K0030174biological_processregulation of DNA-templated DNA replication initiation
K0030510biological_processregulation of BMP signaling pathway
K0030891cellular_componentVCB complex
K0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
K0031297biological_processreplication fork processing
K0031461cellular_componentcullin-RING ubiquitin ligase complex
K0031462cellular_componentCul2-RING ubiquitin ligase complex
K0031463cellular_componentCul3-RING ubiquitin ligase complex
K0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
K0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
K0031466cellular_componentCul5-RING ubiquitin ligase complex
K0031467cellular_componentCul7-RING ubiquitin ligase complex
K0031625molecular_functionubiquitin protein ligase binding
K0032006biological_processregulation of TOR signaling
K0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
K0032480biological_processnegative regulation of type I interferon production
K0032814biological_processregulation of natural killer cell activation
K0034450molecular_functionubiquitin-ubiquitin ligase activity
K0034599biological_processcellular response to oxidative stress
K0034644biological_processcellular response to UV
K0040029biological_processepigenetic regulation of gene expression
K0042110biological_processT cell activation
K0042127biological_processregulation of cell population proliferation
K0042752biological_processregulation of circadian rhythm
K0042770biological_processsignal transduction in response to DNA damage
K0042981biological_processregulation of apoptotic process
K0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
K0043124biological_processnegative regulation of canonical NF-kappaB signal transduction
K0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
K0043687biological_processpost-translational protein modification
K0044314biological_processprotein K27-linked ubiquitination
K0044877molecular_functionprotein-containing complex binding
K0045116biological_processprotein neddylation
K0045732biological_processpositive regulation of protein catabolic process
K0045995biological_processregulation of embryonic development
K0046627biological_processnegative regulation of insulin receptor signaling pathway
K0046872molecular_functionmetal ion binding
K0050727biological_processregulation of inflammatory response
K0051298biological_processcentrosome duplication
K0051726biological_processregulation of cell cycle
K0060090molecular_functionmolecular adaptor activity
K0060173biological_processlimb development
K0060271biological_processcilium assembly
K0060964biological_processregulation of miRNA-mediated gene silencing
K0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
K0061630molecular_functionubiquitin protein ligase activity
K0061663molecular_functionNEDD8 ligase activity
K0062197biological_processcellular response to chemical stress
K0070936biological_processprotein K48-linked ubiquitination
K0071230biological_processcellular response to amino acid stimulus
K0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
K0080135biological_processregulation of cellular response to stress
K0090090biological_processnegative regulation of canonical Wnt signaling pathway
K0090734cellular_componentsite of DNA damage
K0097602molecular_functioncullin family protein binding
K0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
K0160240biological_processRNA polymerase II transcription initiation surveillance
K0160276biological_processnegative regulation of beige fat cell differentiation
K1900076biological_processregulation of cellular response to insulin stimulus
K1901524biological_processregulation of mitophagy
K1901525biological_processnegative regulation of mitophagy
K1901987biological_processregulation of cell cycle phase transition
K1902412biological_processregulation of mitotic cytokinesis
K1902499biological_processpositive regulation of protein autoubiquitination
K1902883biological_processnegative regulation of response to oxidative stress
K1904178biological_processnegative regulation of adipose tissue development
K1904263biological_processpositive regulation of TORC1 signaling
K1904415biological_processregulation of xenophagy
K1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
K2000001biological_processregulation of DNA damage checkpoint
K2000036biological_processregulation of stem cell population maintenance
K2000104biological_processnegative regulation of DNA-templated DNA replication
U0003723molecular_functionRNA binding
U0003735molecular_functionstructural constituent of ribosome
U0005515molecular_functionprotein binding
U0005615cellular_componentextracellular space
U0005634cellular_componentnucleus
U0005654cellular_componentnucleoplasm
U0005737cellular_componentcytoplasm
U0005741cellular_componentmitochondrial outer membrane
U0005789cellular_componentendoplasmic reticulum membrane
U0005829cellular_componentcytosol
U0005886cellular_componentplasma membrane
U0010008cellular_componentendosome membrane
U0016567biological_processprotein ubiquitination
U0019941biological_processmodification-dependent protein catabolic process
U0022626cellular_componentcytosolic ribosome
U0030666cellular_componentendocytic vesicle membrane
U0031386molecular_functionprotein tag activity
U0031982cellular_componentvesicle
U0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. WHPNIyen.GdVCIsiL
ChainResidueDetails
CTRP82-LEU97

site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGcqleD
ChainResidueDetails
ULYS-49-ASP-24
ELYS27-ASP52
ELYS103-ASP128
ELYS179-ASP204
ELYS255-ASP280
ELYS331-ASP356
ELYS407-ASP432
ELYS483-ASP508
ELYS559-ASP584
ELYS635-ASP660
ULYS27-ASP52
ULYS103-ASP128
ULYS179-ASP204
ULYS255-ASP280
ULYS331-ASP356
ULYS407-ASP432
ULYS483-ASP508
ULYS559-ASP584

site_idPS01256
Number of Residues28
DetailsCULLIN_1 Cullin family signature. IKkcIevLIDKqYIeRsqasadeYsYvA
ChainResidueDetails
AILE718-ALA745

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues166
DetailsDomain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues15
DetailsRegion: {"description":"Important for ubiquitin transfer","evidences":[{"source":"PubMed","id":"38326650","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"38326650","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8PQL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Interacts with activating enzyme"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Essential for function"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PINK1","evidences":[{"source":"PubMed","id":"24660806","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24751536","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24784582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25527291","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"(Microbial infection) ADP-ribosylthreonine","evidences":[{"source":"PubMed","id":"32330457","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18719106","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"15466860","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752573","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34239127","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues30
DetailsRepeat: {"description":"ANK 2"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues29
DetailsRepeat: {"description":"ANK 3"}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues29
DetailsRepeat: {"description":"ANK 4"}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues29
DetailsRepeat: {"description":"ANK 5"}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues29
DetailsRepeat: {"description":"ANK 6"}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues29
DetailsRepeat: {"description":"ANK 7"}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues34
DetailsRepeat: {"description":"TPR 1"}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues33
DetailsRepeat: {"description":"TPR 2"}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues42
DetailsRepeat: {"description":"ANK 8"}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues29
DetailsRepeat: {"description":"ANK 9"}
ChainResidueDetails

site_idSWS_FT_FI24
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_FI25
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_FI26
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_FI27
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues65
DetailsDomain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62869","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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