Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4JGH

Structure of the SOCS2-Elongin BC complex bound to an N-terminal fragment of Cullin5

Functional Information from GO Data
ChainGOidnamespacecontents
A0035556biological_processintracellular signal transduction
B0001222molecular_functiontranscription corepressor binding
B0003713molecular_functiontranscription coactivator activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005667cellular_componenttranscription regulator complex
B0005829cellular_componentcytosol
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
B0044877molecular_functionprotein-containing complex binding
B0045893biological_processpositive regulation of DNA-templated transcription
B0070449cellular_componentelongin complex
B0140958biological_processtarget-directed miRNA degradation
C0006511biological_processubiquitin-dependent protein catabolic process
D0006511biological_processubiquitin-dependent protein catabolic process
D0031625molecular_functionubiquitin protein ligase binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
DSER34

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648
ChainResidueDetails
DTHR210

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
BSER108
BSER111

218500

PDB entries from 2024-04-17

PDB statisticsPDBj update infoContact PDBjnumon