2Y4T

Crystal structure of the human co-chaperone P58(IPK)

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00226	e2y4tA5	A: alpha bundles	X: Chaperone J-domain (From Topology)	H: Chaperone J-domain (From Topology)	T: Chaperone J-domain	F: PF00226	ECOD (1.6)
A	PF00515	e2y4tA6	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: PF00515	ECOD (1.6)
B	PF00226	e2y4tB3	A: alpha bundles	X: Chaperone J-domain (From Topology)	H: Chaperone J-domain (From Topology)	T: Chaperone J-domain	F: PF00226	ECOD (1.6)
B	PF00515	e2y4tB4	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: PF00515	ECOD (1.6)
C	PF00226	e2y4tC3	A: alpha bundles	X: Chaperone J-domain (From Topology)	H: Chaperone J-domain (From Topology)	T: Chaperone J-domain	F: PF00226	ECOD (1.6)
C	PF00515	e2y4tC4	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: PF00515	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.25.40.10	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Tetratricopeptide repeat domain	CATH (4.3.0)
A	1.10.287.110	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	DnaJ domain	CATH (4.3.0)
B	1.25.40.10	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Tetratricopeptide repeat domain	CATH (4.3.0)
B	1.10.287.110	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	DnaJ domain	CATH (4.3.0)
C	1.25.40.10	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Tetratricopeptide repeat domain	CATH (4.3.0)
C	1.10.287.110	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	DnaJ domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF00226	DnaJ domain (DnaJ)	DnaJ domain	DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are conf ...	DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature [2].	Domain
A, B, C	PF13181	Tetratricopeptide repeat (TPR_8)	Tetratricopeptide repeat	-	Repeat
A, B, C	PF00515	Tetratricopeptide repeat (TPR_1)	Tetratricopeptide repeat	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	DNAJ HOMOLOG SUBFAMILY C MEMBER 3	enzyme regulator activity protein kinase inhibitor activity molecular function inhibitor activity molecular function regulator activity enzyme inhibitor activity protein kinase regulator activity kinase inhibitor activity kinase regulator activity protein binding binding misfolded protein binding protein-folding chaperone binding kinase binding enzyme binding enzyme regulator activity protein kinase inhibitor activity molecular function inhibitor activity molecular function regulator activity enzyme inhibitor activity protein kinase regulator activity kinase inhibitor activity kinase regulator activity protein binding binding misfolded protein binding protein-folding chaperone binding kinase binding enzyme binding protein kinase binding	cellular response to stimulus regulation of cellular process response to stimulus organonitrogen compound biosynthetic process positive regulation of translation initiation in response to endoplasmic reticulum stress positive regulation of macromolecule biosynthetic process regulation of primary metabolic process positive regulation of translational initiation in response to stress post-transcriptional regulation of gene expression positive regulation of metabolic process organic substance biosynthetic process positive regulation of macromolecule metabolic process translational initiation positive regulation of translation in response to stress cellular response to stimulus regulation of cellular process response to stimulus organonitrogen compound biosynthetic process positive regulation of translation initiation in response to endoplasmic reticulum stress positive regulation of macromolecule biosynthetic process regulation of primary metabolic process positive regulation of translational initiation in response to stress post-transcriptional regulation of gene expression positive regulation of metabolic process organic substance biosynthetic process positive regulation of macromolecule metabolic process translational initiation positive regulation of translation in response to stress response to endoplasmic reticulum stress positive regulation of translation in response to endoplasmic reticulum stress regulation of biological process regulation of translational initiation cellular metabolic process regulation of protein metabolic process regulation of translation initiation in response to endoplasmic reticulum stress regulation of cellular metabolic process primary metabolic process regulation of gene expression biosynthetic process regulation of macromolecule biosynthetic process metabolic process macromolecule metabolic process positive regulation of translational initiation regulation of metabolic process cellular biosynthetic process positive regulation of protein metabolic process positive regulation of biological process positive regulation of translation positive regulation of cellular metabolic process regulation of translation in response to stress organic substance metabolic process cellular response to stress positive regulation of biosynthetic process response to stress protein metabolic process positive regulation of cellular process regulation of biosynthetic process organonitrogen compound metabolic process regulation of translation in response to endoplasmic reticulum stress biological regulation regulation of macromolecule metabolic process gene expression translation macromolecule biosynthetic process regulation of cellular biosynthetic process positive regulation of gene expression regulation of translation regulation of translational initiation in response to stress cellular process positive regulation of cellular biosynthetic process negative regulation of programmed cell death regulation of apoptotic process negative regulation of biological process regulation of programmed cell death cell death negative regulation of apoptotic process negative regulation of cellular process apoptotic process programmed cell death response to organic substance response to topologically incorrect protein response to chemical response to unfolded protein protein maturation protein folding protein folding in endoplasmic reticulum organonitrogen compound catabolic process catabolic process proteolysis involved in protein catabolic process protein catabolic process macromolecule catabolic process proteolysis organic substance catabolic process cellular response to cold response to abiotic stimulus response to cold response to temperature stimulus regulation of translational initiation by eIF2 alpha phosphorylation negative regulation of cellular metabolic process regulation of phosphate metabolic process phosphate-containing compound metabolic process negative regulation of protein modification process protein modification process phosphorus metabolic process negative regulation of protein metabolic process protein phosphorylation phosphorylation negative regulation of metabolic process eiF2alpha phosphorylation in response to endoplasmic reticulum stress negative regulation of protein phosphorylation macromolecule modification regulation of phosphorus metabolic process regulation of protein modification process regulation of protein phosphorylation negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation negative regulation of phosphate metabolic process negative regulation of macromolecule metabolic process negative regulation of phosphorus metabolic process regulation of phosphorylation negative regulation of phosphorylation biological process involved in interspecies interaction between organisms response to other organism defense response defense response to symbiont response to external stimulus response to biotic stimulus defense response to virus defense response to other organism response to external biotic stimulus response to virus	membrane cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol membrane cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol intracellular organelle endoplasmic reticulum smooth endoplasmic reticulum intracellular membrane-bounded organelle endomembrane system lytic vacuole intracellular vesicle membrane-enclosed lumen cytoplasmic vesicle lumen vacuolar lumen intracellular organelle lumen cytoplasmic vesicle lysosome vesicle lumen azurophil granule vacuole secretory granule lumen azurophil granule lumen organelle lumen secretory granule primary lysosome secretory vesicle endoplasmic reticulum lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR011990	Tetratricopeptide-like helical domain superfamily	Homologous Superfamily
A, B, C	IPR001440	TPR_1	Unknown
A, B, C	IPR001623	DnaJ domain	Domain
A, B, C	IPR019734	Tetratricopeptide repeat	Repeat
A, B, C	IPR036869	Chaperone J-domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C	Pharos: Q13217	juvenile-onset diabetes mellitus-central and peripheral neurodegeneration syndrome peripheral neuropathy prostate cancer diabetes mellitus pituitary cancer psoriasis subependymal giant cell astrocytoma acquired metabolic disease Crohn disease intellectual disability large cell medulloblastoma myopathy ovarian cancer rheumatoid arthritis ulcerative colitis juvenile-onset diabetes mellitus-central and peripheral neurodegeneration syndrome peripheral neuropathy prostate cancer diabetes mellitus pituitary cancer psoriasis subependymal giant cell astrocytoma acquired metabolic disease Crohn disease intellectual disability large cell medulloblastoma myopathy ovarian cancer rheumatoid arthritis ulcerative colitis Alzheimer disease juvenile dermatomyositis malignant ependymoma neurodegenerative disease pancreatic ductal adenocarcinoma Pick disease Prostatic Neoplasms sarcoidosis atypical teratoid rhabdoid tumor glioblastoma malignant glioma osteosarcoma peripheral nervous system disease

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.