Structure of PDB 2c2l Chain D Binding Site BS01

Receptor Information
>2c2l Chain D (length=281) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLK
MQQPEQALADCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYS
LAKEQRLNFGDDIPSALRIAKKKRWNSIEERRIHQESELHSYLTRLIAAE
RERELEECQRNHEGHEDDGHIRAQQACIEAKHDKYMADMDELFSQVDEKR
KKRDIPDYLCGKISFELMREPCITPSGITYDRKDIEEHLQRVGHFNPVTR
SPLTQEQLIPNLAMKEVIDAFISENGWVEDY
Ligand information
Receptor-Ligand Complex Structure
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PDB2c2l Chaperoned Ubiquitylation-Crystal Structures of the Chip U Box E3 Ubiquitin Ligase and a Chip-Ubc13-Uev1A Complex
Resolution3.3 Å
Binding residue
(original residue number in PDB)		Y50 N66 L69 K96 F99 N131 F132
Binding residue
(residue number reindexed from 1)		Y27 N43 L46 K73 F76 N108 F109
Enzymatic activity
Enzyme Commision number 2.3.2.27: RING-type E3 ubiquitin transferase.
Gene Ontology
Molecular Function
GO:0001664 G protein-coupled receptor binding
GO:0004842 ubiquitin-protein transferase activity
GO:0005515 protein binding
GO:0016740 transferase activity
GO:0019899 enzyme binding
GO:0019900 kinase binding
GO:0030544 Hsp70 protein binding
GO:0030674 protein-macromolecule adaptor activity
GO:0030911 TPR domain binding
GO:0031072 heat shock protein binding
GO:0031625 ubiquitin protein ligase binding
GO:0034450 ubiquitin-ubiquitin ligase activity
GO:0042803 protein homodimerization activity
GO:0046332 SMAD binding
GO:0051087 protein-folding chaperone binding
GO:0051787 misfolded protein binding
GO:0051879 Hsp90 protein binding
GO:0061630 ubiquitin protein ligase activity
GO:0070412 R-SMAD binding
Biological Process
GO:0000165 MAPK cascade
GO:0000209 protein polyubiquitination
GO:0002931 response to ischemia
GO:0006281 DNA repair
GO:0006457 protein folding
GO:0006511 ubiquitin-dependent protein catabolic process
GO:0006513 protein monoubiquitination
GO:0006515 protein quality control for misfolded or incompletely synthesized proteins
GO:0016567 protein ubiquitination
GO:0030512 negative regulation of transforming growth factor beta receptor signaling pathway
GO:0030968 endoplasmic reticulum unfolded protein response
GO:0031398 positive regulation of protein ubiquitination
GO:0031647 regulation of protein stability
GO:0031943 regulation of glucocorticoid metabolic process
GO:0032091 negative regulation of protein binding
GO:0032436 positive regulation of proteasomal ubiquitin-dependent protein catabolic process
GO:0034392 negative regulation of smooth muscle cell apoptotic process
GO:0034393 positive regulation of smooth muscle cell apoptotic process
GO:0034605 cellular response to heat
GO:0035359 negative regulation of peroxisome proliferator activated receptor signaling pathway
GO:0036503 ERAD pathway
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0045862 positive regulation of proteolysis
GO:0050821 protein stabilization
GO:0051443 positive regulation of ubiquitin-protein transferase activity
GO:0051604 protein maturation
GO:0051865 protein autoubiquitination
GO:0061684 chaperone-mediated autophagy
GO:0070534 protein K63-linked ubiquitination
GO:0071218 cellular response to misfolded protein
GO:0071456 cellular response to hypoxia
GO:0090035 positive regulation of chaperone-mediated protein complex assembly
GO:1901526 positive regulation of mitophagy
GO:1904294 positive regulation of ERAD pathway
Cellular Component
GO:0000151 ubiquitin ligase complex
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005783 endoplasmic reticulum
GO:0005829 cytosol
GO:0030018 Z disc
GO:0031371 ubiquitin conjugating enzyme complex
GO:0042405 nuclear inclusion body
GO:0101031 protein folding chaperone complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2c2l, PDBe:2c2l, PDBj:2c2l
PDBsum2c2l
PubMed16307917
UniProtQ9WUD1|CHIP_MOUSE E3 ubiquitin-protein ligase CHIP (Gene Name=Stub1)

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