Structure of PDB 2c2l Chain C

Receptor sequence

>2c2lC (length=281) Species: 10090 (Mus musculus) [Search protein sequence]

SPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLK
MQQPEQALADCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYS
LAKEQRLNFGDDIPSALRIAKKKRWNSIEERRIHQESELHSYLTRLIAAE
RERELEECQRNHEGHEDDGHIRAQQACIEAKHDKYMADMDELFSQVDEKR
KKRDIPDYLCGKISFELMREPCITPSGITYDRKDIEEHLQRVGHFNPVTR
SPLTQEQLIPNLAMKEVIDAFISENGWVEDY

3D structure

PDB

2c2l Chaperoned Ubiquitylation-Crystal Structures of the Chip U Box E3 Ubiquitin Ligase and a Chip-Ubc13-Uev1A Complex

Chain

Resolution

3.3 Å

3D
structure

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Enzymatic activity

Enzyme Commision number

2.3.2.27: RING-type E3 ubiquitin transferase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	peptide	C	F38 Y50 N66 L69 K73 K96 F99 N131 F132 D135	F15 Y27 N43 L46 K50 K73 F76 N108 F109 D112

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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:2c2l, PDBe:2c2l, PDBj:2c2l
PDBsum	2c2l
PubMed	16307917
UniProt	Q9WUD1\|CHIP_MOUSE E3 ubiquitin-protein ligase CHIP (Gene Name=Stub1)

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