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9O7E

CHIP E3 ligase dimer in intermediate state bound to 2 Fab H1

Functional Information from GO Data
ChainGOidnamespacecontents
B0000151cellular_componentubiquitin ligase complex
B0000165biological_processMAPK cascade
B0000209biological_processprotein polyubiquitination
B0001664molecular_functionG protein-coupled receptor binding
B0002931biological_processresponse to ischemia
B0004842molecular_functionubiquitin-protein transferase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0006511biological_processubiquitin-dependent protein catabolic process
B0006513biological_processprotein monoubiquitination
B0006515biological_processprotein quality control for misfolded or incompletely synthesized proteins
B0007165biological_processsignal transduction
B0010614biological_processnegative regulation of cardiac muscle hypertrophy
B0016567biological_processprotein ubiquitination
B0019899molecular_functionenzyme binding
B0019900molecular_functionkinase binding
B0030018cellular_componentZ disc
B0030163biological_processprotein catabolic process
B0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
B0030544molecular_functionHsp70 protein binding
B0030674molecular_functionprotein-macromolecule adaptor activity
B0030911molecular_functionTPR domain binding
B0030968biological_processendoplasmic reticulum unfolded protein response
B0031072molecular_functionheat shock protein binding
B0031371cellular_componentubiquitin conjugating enzyme complex
B0031398biological_processpositive regulation of protein ubiquitination
B0031625molecular_functionubiquitin protein ligase binding
B0031647biological_processregulation of protein stability
B0031943biological_processregulation of glucocorticoid metabolic process
B0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
B0033554biological_processcellular response to stress
B0034392biological_processnegative regulation of smooth muscle cell apoptotic process
B0034393biological_processpositive regulation of smooth muscle cell apoptotic process
B0034450molecular_functionubiquitin-ubiquitin ligase activity
B0034605biological_processcellular response to heat
B0035359biological_processnegative regulation of peroxisome proliferator activated receptor signaling pathway
B0036503biological_processERAD pathway
B0038128biological_processERBB2 signaling pathway
B0042405cellular_componentnuclear inclusion body
B0042803molecular_functionprotein homodimerization activity
B0043066biological_processnegative regulation of apoptotic process
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0045862biological_processpositive regulation of proteolysis
B0046332molecular_functionSMAD binding
B0048156molecular_functiontau protein binding
B0050821biological_processprotein stabilization
B0051087molecular_functionprotein-folding chaperone binding
B0051787molecular_functionmisfolded protein binding
B0051865biological_processprotein autoubiquitination
B0051879molecular_functionHsp90 protein binding
B0061630molecular_functionubiquitin protein ligase activity
B0061684biological_processchaperone-mediated autophagy
B0070412molecular_functionR-SMAD binding
B0070534biological_processprotein K63-linked ubiquitination
B0071218biological_processcellular response to misfolded protein
B0071456biological_processcellular response to hypoxia
B0090035biological_processpositive regulation of chaperone-mediated protein complex assembly
B0101031cellular_componentprotein folding chaperone complex
B1901526biological_processpositive regulation of mitophagy
B1904294biological_processpositive regulation of ERAD pathway
B1904694biological_processnegative regulation of vascular associated smooth muscle contraction
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YSCQVTH
ChainResidueDetails
FTYR211-HIS217
ETYR209-HIS215

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues148
DetailsDomain: {"description":"U-box"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues108
DetailsRegion: {"description":"Required for interaction with and ubiquitination of MYOCD","evidences":[{"source":"UniProtKB","id":"A6HD62","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues320
DetailsRegion: {"description":"Required for ubiquitination of FOXO1","evidences":[{"source":"PubMed","id":"19483080","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues108
DetailsRegion: {"description":"Required for interaction with FOXO1","evidences":[{"source":"PubMed","id":"19483080","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"18042044","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues33
DetailsRepeat: {"description":"TPR 1"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues33
DetailsRepeat: {"description":"TPR 2"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues32
DetailsRepeat: {"description":"TPR 3"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues99
DetailsRegion: {"description":"Required for interaction with MAPK7","evidences":[{"source":"PubMed","id":"20724525","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2026-07-22

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