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8EI3

Crystal structure of VHL in complex with H313, a Helicon Polypeptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0001222molecular_functiontranscription corepressor binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0006367biological_processtranscription initiation at RNA polymerase II promoter
A0006368biological_processtranscription elongation by RNA polymerase II
A0016567biological_processprotein ubiquitination
A0030891cellular_componentVCB complex
A0031462cellular_componentCul2-RING ubiquitin ligase complex
A0031466cellular_componentCul5-RING ubiquitin ligase complex
A0031625molecular_functionubiquitin protein ligase binding
A0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
A0065003biological_processprotein-containing complex assembly
A0070449cellular_componentelongin complex
A0140958biological_processtarget-directed miRNA degradation
B0006511biological_processubiquitin-dependent protein catabolic process
D0001222molecular_functiontranscription corepressor binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005829cellular_componentcytosol
D0006367biological_processtranscription initiation at RNA polymerase II promoter
D0006368biological_processtranscription elongation by RNA polymerase II
D0016567biological_processprotein ubiquitination
D0030891cellular_componentVCB complex
D0031462cellular_componentCul2-RING ubiquitin ligase complex
D0031466cellular_componentCul5-RING ubiquitin ligase complex
D0031625molecular_functionubiquitin protein ligase binding
D0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
D0065003biological_processprotein-containing complex assembly
D0070449cellular_componentelongin complex
D0140958biological_processtarget-directed miRNA degradation
E0006511biological_processubiquitin-dependent protein catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1
DMET1

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62869
ChainResidueDetails
ATHR84
DTHR84

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62869
ChainResidueDetails
ASER108
ASER111
DSER108
DSER111

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PDB entries from 2024-07-17

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