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9RP9

Crystal structure of mouse pVHL-ElonginB-ElonginC complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000151cellular_componentubiquitin ligase complex
A0001525biological_processangiogenesis
A0001666biological_processresponse to hypoxia
A0003309biological_processtype B pancreatic cell differentiation
A0003310biological_processpancreatic A cell differentiation
A0003711molecular_functiontranscription elongation factor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005886cellular_componentplasma membrane
A0005929cellular_componentcilium
A0006355biological_processregulation of DNA-templated transcription
A0006582biological_processmelanin metabolic process
A0008285biological_processnegative regulation of cell population proliferation
A0009968biological_processnegative regulation of signal transduction
A0010468biological_processregulation of gene expression
A0010498biological_processproteasomal protein catabolic process
A0010507biological_processnegative regulation of autophagy
A0010629biological_processnegative regulation of gene expression
A0014069cellular_componentpostsynaptic density
A0015031biological_processprotein transport
A0015630cellular_componentmicrotubule cytoskeleton
A0016567biological_processprotein ubiquitination
A0019899molecular_functionenzyme binding
A0030163biological_processprotein catabolic process
A0030182biological_processneuron differentiation
A0030198biological_processextracellular matrix organization
A0030891cellular_componentVCB complex
A0031462cellular_componentCul2-RING ubiquitin ligase complex
A0032880biological_processregulation of protein localization
A0034244biological_processnegative regulation of transcription elongation by RNA polymerase II
A0042069biological_processregulation of catecholamine metabolic process
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0043534biological_processblood vessel endothelial cell migration
A0044877molecular_functionprotein-containing complex binding
A0045471biological_processresponse to ethanol
A0045602biological_processnegative regulation of endothelial cell differentiation
A0045893biological_processpositive regulation of DNA-templated transcription
A0046426biological_processnegative regulation of receptor signaling pathway via JAK-STAT
A0048069biological_processeye pigmentation
A0048593biological_processcamera-type eye morphogenesis
A0048877biological_processhomeostasis of number of retina cells
A0050679biological_processpositive regulation of epithelial cell proliferation
A0060090molecular_functionmolecular adaptor activity
A0061072biological_processiris morphogenesis
A0061073biological_processciliary body morphogenesis
A0070243biological_processregulation of thymocyte apoptotic process
A0070244biological_processnegative regulation of thymocyte apoptotic process
A0097542cellular_componentciliary tip
A0098978cellular_componentglutamatergic synapse
A0099175biological_processregulation of postsynapse organization
A0120283molecular_functionprotein serine/threonine kinase binding
A0140252biological_processregulation protein catabolic process at postsynapse
A0140297molecular_functionDNA-binding transcription factor binding
A1900037biological_processregulation of cellular response to hypoxia
A1902072biological_processnegative regulation of hypoxia-inducible factor-1alpha signaling pathway
A1904262biological_processnegative regulation of TORC1 signaling
A1990000biological_processamyloid fibril formation
A1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
A2001233biological_processregulation of apoptotic signaling pathway
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues78
DetailsDomain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"Q15370","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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