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8QU8

PROTAC-mediated complex of KRAS with VHL/Elongin-B/Elongin-C/Cullin-2/Rbx1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000902biological_processcell morphogenesis
A0001666biological_processresponse to hypoxia
A0003711molecular_functiontranscription elongation factor activity
A0003714molecular_functiontranscription corepressor activity
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006355biological_processregulation of DNA-templated transcription
A0006508biological_processproteolysis
A0008285biological_processnegative regulation of cell population proliferation
A0009968biological_processnegative regulation of signal transduction
A0010468biological_processregulation of gene expression
A0010507biological_processnegative regulation of autophagy
A0010629biological_processnegative regulation of gene expression
A0016567biological_processprotein ubiquitination
A0019899molecular_functionenzyme binding
A0034244biological_processnegative regulation of transcription elongation by RNA polymerase II
A0043066biological_processnegative regulation of apoptotic process
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0045597biological_processpositive regulation of cell differentiation
A0045893biological_processpositive regulation of DNA-templated transcription
A0046426biological_processnegative regulation of receptor signaling pathway via JAK-STAT
A0050821biological_processprotein stabilization
A0060090molecular_functionmolecular adaptor activity
A0071456biological_processcellular response to hypoxia
A0120283molecular_functionprotein serine/threonine kinase binding
A0140297molecular_functionDNA-binding transcription factor binding
A1900037biological_processregulation of cellular response to hypoxia
A1904262biological_processnegative regulation of TORC1 signaling
A1990000biological_processamyloid fibril formation
A1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000151cellular_componentubiquitin ligase complex
B0001222molecular_functiontranscription corepressor binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006351biological_processDNA-templated transcription
B0006367biological_processtranscription initiation at RNA polymerase II promoter
B0006368biological_processtranscription elongation by RNA polymerase II
B0016567biological_processprotein ubiquitination
B0030891cellular_componentVCB complex
B0031462cellular_componentCul2-RING ubiquitin ligase complex
B0031466cellular_componentCul5-RING ubiquitin ligase complex
B0031625molecular_functionubiquitin protein ligase binding
B0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0065003biological_processprotein-containing complex assembly
B0070449cellular_componentelongin complex
B0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
B0140958biological_processtarget-directed miRNA degradation
B1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
B2000104biological_processnegative regulation of DNA-templated DNA replication
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000151cellular_componentubiquitin ligase complex
C0001222molecular_functiontranscription corepressor binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006351biological_processDNA-templated transcription
C0006357biological_processregulation of transcription by RNA polymerase II
C0006367biological_processtranscription initiation at RNA polymerase II promoter
C0006511biological_processubiquitin-dependent protein catabolic process
C0016567biological_processprotein ubiquitination
C0030674molecular_functionprotein-macromolecule adaptor activity
C0031462cellular_componentCul2-RING ubiquitin ligase complex
C0031466cellular_componentCul5-RING ubiquitin ligase complex
C0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
C0070449cellular_componentelongin complex
C0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
C0140958biological_processtarget-directed miRNA degradation
C1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
C2000104biological_processnegative regulation of DNA-templated DNA replication
D0000082biological_processG1/S transition of mitotic cell cycle
D0000122biological_processnegative regulation of transcription by RNA polymerase II
D0004842molecular_functionubiquitin-protein transferase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005730cellular_componentnucleolus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006511biological_processubiquitin-dependent protein catabolic process
D0010498biological_processproteasomal protein catabolic process
D0016567biological_processprotein ubiquitination
D0019005cellular_componentSCF ubiquitin ligase complex
D0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
D0031461cellular_componentcullin-RING ubiquitin ligase complex
D0031462cellular_componentCul2-RING ubiquitin ligase complex
D0031625molecular_functionubiquitin protein ligase binding
D0031981cellular_componentnuclear lumen
D0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
D0072344biological_processrescue of stalled ribosome
D0097193biological_processintrinsic apoptotic signaling pathway
D0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
D0160072molecular_functionubiquitin ligase complex scaffold activity
D0160276biological_processnegative regulation of beige fat cell differentiation
D1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
D2000104biological_processnegative regulation of DNA-templated DNA replication
E0000082biological_processG1/S transition of mitotic cell cycle
E0000122biological_processnegative regulation of transcription by RNA polymerase II
E0000165biological_processMAPK cascade
E0000209biological_processprotein polyubiquitination
E0004842molecular_functionubiquitin-protein transferase activity
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005794cellular_componentGolgi apparatus
E0005813cellular_componentcentrosome
E0005829cellular_componentcytosol
E0006281biological_processDNA repair
E0006283biological_processtranscription-coupled nucleotide-excision repair
E0006289biological_processnucleotide-excision repair
E0006355biological_processregulation of DNA-templated transcription
E0006511biological_processubiquitin-dependent protein catabolic process
E0006513biological_processprotein monoubiquitination
E0006879biological_processintracellular iron ion homeostasis
E0006974biological_processDNA damage response
E0007283biological_processspermatogenesis
E0007346biological_processregulation of mitotic cell cycle
E0008270molecular_functionzinc ion binding
E0008283biological_processcell population proliferation
E0010506biological_processregulation of autophagy
E0010564biological_processregulation of cell cycle process
E0010824biological_processregulation of centrosome duplication
E0014033biological_processneural crest cell differentiation
E0016567biological_processprotein ubiquitination
E0016740molecular_functiontransferase activity
E0019005cellular_componentSCF ubiquitin ligase complex
E0019788molecular_functionNEDD8 transferase activity
E0030174biological_processregulation of DNA-templated DNA replication initiation
E0030510biological_processregulation of BMP signaling pathway
E0030891cellular_componentVCB complex
E0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
E0031297biological_processreplication fork processing
E0031461cellular_componentcullin-RING ubiquitin ligase complex
E0031462cellular_componentCul2-RING ubiquitin ligase complex
E0031463cellular_componentCul3-RING ubiquitin ligase complex
E0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
E0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
E0031466cellular_componentCul5-RING ubiquitin ligase complex
E0031467cellular_componentCul7-RING ubiquitin ligase complex
E0031625molecular_functionubiquitin protein ligase binding
E0032006biological_processregulation of TOR signaling
E0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
E0032480biological_processnegative regulation of type I interferon production
E0032814biological_processregulation of natural killer cell activation
E0034450molecular_functionubiquitin-ubiquitin ligase activity
E0034599biological_processcellular response to oxidative stress
E0034644biological_processcellular response to UV
E0040029biological_processepigenetic regulation of gene expression
E0042110biological_processT cell activation
E0042127biological_processregulation of cell population proliferation
E0042752biological_processregulation of circadian rhythm
E0042770biological_processsignal transduction in response to DNA damage
E0042981biological_processregulation of apoptotic process
E0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
E0043124biological_processnegative regulation of canonical NF-kappaB signal transduction
E0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
E0043687biological_processpost-translational protein modification
E0044314biological_processprotein K27-linked ubiquitination
E0044877molecular_functionprotein-containing complex binding
E0045116biological_processprotein neddylation
E0045732biological_processpositive regulation of protein catabolic process
E0045995biological_processregulation of embryonic development
E0046627biological_processnegative regulation of insulin receptor signaling pathway
E0046872molecular_functionmetal ion binding
E0050727biological_processregulation of inflammatory response
E0051298biological_processcentrosome duplication
E0051726biological_processregulation of cell cycle
E0060090molecular_functionmolecular adaptor activity
E0060173biological_processlimb development
E0060271biological_processcilium assembly
E0060964biological_processregulation of miRNA-mediated gene silencing
E0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
E0061630molecular_functionubiquitin protein ligase activity
E0061663molecular_functionNEDD8 ligase activity
E0062197biological_processcellular response to chemical stress
E0070936biological_processprotein K48-linked ubiquitination
E0071230biological_processcellular response to amino acid stimulus
E0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
E0080135biological_processregulation of cellular response to stress
E0090090biological_processnegative regulation of canonical Wnt signaling pathway
E0090734cellular_componentsite of DNA damage
E0097602molecular_functioncullin family protein binding
E0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
E0160240biological_processRNA polymerase II transcription initiation surveillance
E0160276biological_processnegative regulation of beige fat cell differentiation
E1900076biological_processregulation of cellular response to insulin stimulus
E1901524biological_processregulation of mitophagy
E1901525biological_processnegative regulation of mitophagy
E1901987biological_processregulation of cell cycle phase transition
E1902412biological_processregulation of mitotic cytokinesis
E1902499biological_processpositive regulation of protein autoubiquitination
E1902883biological_processnegative regulation of response to oxidative stress
E1904178biological_processnegative regulation of adipose tissue development
E1904263biological_processpositive regulation of TORC1 signaling
E1904415biological_processregulation of xenophagy
E1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
E2000001biological_processregulation of DNA damage checkpoint
E2000036biological_processregulation of stem cell population maintenance
E2000104biological_processnegative regulation of DNA-templated DNA replication
F0003924molecular_functionGTPase activity
F0005525molecular_functionGTP binding
F0007165biological_processsignal transduction
F0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS01256
Number of Residues28
DetailsCULLIN_1 Cullin family signature. IKkcIevLIDKqYIeRsqasadeYsYvA
ChainResidueDetails
DILE718-ALA745

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues55
DetailsRegion: {"description":"Involved in binding to CCT complex"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsRegion: {"description":"Interaction with Elongin BC complex"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62869","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues60
DetailsDomain: {"description":"Cullin neddylation","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)","evidences":[{"source":"PubMed","id":"10092517","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10597293","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues45
DetailsZinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
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_FI10
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_FI11
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_FI12
Number of Residues8
DetailsMotif: {"description":"Effector region"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22431598","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22566140","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34380736","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"35522713","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine; in GTPase KRas; alternate","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"N-acetylthreonine; in GTPase KRas, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues1
DetailsGlycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL","evidences":[{"source":"PubMed","id":"19744486","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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