HUMAN:PDIA3

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	PDIA3 (synonyms: ERP57, ERP60, GRP58)
Protein Name(s)	Protein disulfide-isomerase A3 58 kDa glucose-regulated protein 58 kDa microsomal protein p58 Disulfide isomerase ER-60 Endoplasmic reticulum resident protein 57 ER protein 57 ERp57 Endoplasmic reticulum resident protein 60 ER protein 60 ERp60
External Links
UniProt	P30101
EMBL	D16234 U42068 Z49835 U75885 U75875 U75876 U75877 U75878 U75879 U75880 U75881 U75882 U75883 U75884 D83485 BC014433 BC036000 BC071878
CCDS	CCDS10101.1
PIR	JC5704 S55507 S63994 S68363
RefSeq	NP_005304.3
UniGene	Hs.591095
PDB	2ALB 2DMM 2H8L 3F8U
PDBsum	2ALB 2DMM 2H8L 3F8U
ProteinModelPortal	P30101
SMR	P30101
BioGrid	109180
DIP	DIP-29132N
IntAct	P30101
MINT	MINT-5000005
STRING	9606.ENSP00000300289
PhosphoSite	P30101
DMDM	2507461
DOSAC-COBS-2DPAGE	P30101
REPRODUCTION-2DPAGE	P30101
SWISS-2DPAGE	P30101
UCD-2DPAGE	P30101
MaxQB	P30101
PaxDb	P30101
PRIDE	P30101
DNASU	2923
Ensembl	ENST00000300289
GeneID	2923
KEGG	hsa:2923
UCSC	uc001zsu.3
CTD	2923
GeneCards	GC15P044038
HGNC	HGNC:4606
HPA	CAB011199 CAB015181 HPA002645 HPA003230
MIM	602046
neXtProt	NX_P30101
PharmGKB	PA29000
eggNOG	COG0526
HOGENOM	HOG000162459
HOVERGEN	HBG005920
InParanoid	P30101
KO	K08056
OMA	RFAHTNS
OrthoDB	EOG7VHSX1
PhylomeDB	P30101
TreeFam	TF106382
BRENDA	5.3.4.1
Reactome	REACT_111178 REACT_23810 REACT_75795
ChiTaRS	PDIA3
EvolutionaryTrace	P30101
GenomeRNAi	2923
NextBio	11593
PRO	PR:P30101
Proteomes	UP000005640
Bgee	P30101
CleanEx	HS_PDIA3
ExpressionAtlas	P30101
Genevestigator	P30101
GO	GO:0009986 GO:0005783 GO:0005788 GO:0070062 GO:0005925 GO:0042470 GO:0005634 GO:0005790 GO:0004197 GO:0004629 GO:0044822 GO:0003756 GO:0042590 GO:0002479 GO:0002474 GO:0045454 GO:0044267 GO:2001238 GO:0043687 GO:0006457 GO:0006606 GO:0018279 GO:0006621 GO:0006508 GO:0034976 GO:0007165
Gene3D	3.40.30.10
InterPro	IPR005788 IPR005792 IPR012336 IPR017937 IPR013766
Pfam	PF00085
SUPFAM	SSF52833
TIGRFAMs	TIGR01130 TIGR01126
PROSITE	PS00194 PS51352

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0042824	MHC class I peptide loading complex	PMID:21263072^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0042824	MHC class I peptide loading complex	PMID:17947644^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:21423176^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001831)	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21630459^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000019)	Seeded From UniProt	complete
enables	GO:0015037	peptide disulfide oxidoreductase activity	PMID:16677074^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:19995400^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:23826168^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0034976	response to endoplasmic reticulum stress	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000432607 TAIR:locus:2082712 TAIR:locus:2204670 UniProtKB:P07237 UniProtKB:Q9XI01	P		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95834 PANTHER:PTN001448745 RGD:68430 UniProtKB:P30101	C		Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000432607 SGD:S000000548 SGD:S000002926 UniProtKB:C0H4Y6	P		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0014002 MGI:MGI:104864 MGI:MGI:95834 MGI:MGI:97464 PANTHER:PTN000432607 RGD:68430 TAIR:locus:2014681 TAIR:locus:2018134 TAIR:locus:2082712 TAIR:locus:2093447 TAIR:locus:2204670 UniProtKB:P07237 UniProtKB:P30101 UniProtKB:Q9FF55 UniProtKB:Q9XI01 WB:WBGene00003963	C		Seeded From UniProt	complete
enables	GO:0003756	protein disulfide isomerase activity	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1919080 PANTHER:PTN000432607 RGD:3244 RGD:619835 SGD:S000000548 SGD:S000002926 TAIR:locus:2204670 UniProtKB:C0H4Y6 UniProtKB:O48949 UniProtKB:P07237 UniProtKB:Q4WH99 WB:WBGene00003962 WB:WBGene00003963 WB:WBGene00003964	F		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:19995400^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16905107^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P30101	F		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004197	P		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0015036	P		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0015037	P		Seeded From UniProt	complete
involved_in	GO:2001238	positive regulation of extrinsic apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27773 ensembl:ENSMUSP00000028683	P		Seeded From UniProt	complete
involved_in	GO:0098761	cellular response to interleukin-7	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27773 ensembl:ENSMUSP00000028683	P		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27773 ensembl:ENSMUSP00000028683	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27773 ensembl:ENSMUSP00000028683	C		Seeded From UniProt	complete
enables	GO:0003756	protein disulfide isomerase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005792	F		Seeded From UniProt	complete
enables	GO:0016853	isomerase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005788	F		Seeded From UniProt	complete
involved_in	GO:0045454	cell redox homeostasis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013766 InterPro:IPR017937	P		Seeded From UniProt	complete
enables	GO:0003756	protein disulfide isomerase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:5.3.4.1	F		Seeded From UniProt	complete
enables	GO:0015036	disulfide oxidoreductase activity	PMID:22013210^[12]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034975	protein folding in endoplasmic reticulum	PMID:22013210^[12]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004629	phospholipase C activity	PMID:3398923^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:9399589^[14]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003756	protein disulfide isomerase activity	PMID:8624847^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:16130169^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0055038	recycling endosome membrane	Reactome:R-HSA-8863973	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0045335	phagocytic vesicle	Reactome:R-HSA-8863973	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	Reactome:R-HSA-532668	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005788	endoplasmic reticulum lumen	Reactome:R-HSA-983161 Reactome:R-HSA-983146 Reactome:R-HSA-983142 Reactome:R-HSA-901047 Reactome:R-HSA-8951499 Reactome:R-HSA-548890	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002479	antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent	Reactome:R-HSA-1236974	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0002474	antigen processing and presentation of peptide antigen via MHC class I	Reactome:R-HSA-983169	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0016853	isomerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0413	F		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256 UniProtKB-SubCell:SL-0095	C		Seeded From UniProt	complete
part_of	GO:0042470	melanosome	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0161	C		Seeded From UniProt	complete
part_of	GO:0005788	endoplasmic reticulum lumen	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0096	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Rizvi, SM et al. (2011) Distinct functions for the glycans of tapasin and heavy chains in the assembly of MHC class I molecules. J. Immunol. 186 2309-20 PubMed GONUTS page
↑ Rufer, E et al. (2007) Molecular architecture of the TAP-associated MHC class I peptide-loading complex. J. Immunol. 179 5717-27 PubMed GONUTS page
↑ Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page
↑ Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
↑ de Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page
↑ Alanen, HI et al. () pH dependence of the peptide thiol-disulfide oxidase activity of six members of the human protein disulfide isomerase family. Antioxid. Redox Signal. 8 283-91 PubMed GONUTS page
↑ ^7.0 ^7.1 Holbrook, LM et al. (2010) Platelets release novel thiol isomerase enzymes which are recruited to the cell surface following activation. Br. J. Haematol. 148 627-37 PubMed GONUTS page
↑ Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
↑ Marques, PI et al. (2013) SERPINA2 is a novel gene with a divergent function from SERPINA1. PLoS ONE 8 e66889 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Kozlov, G et al. (2006) Crystal structure of the bb' domains of the protein disulfide isomerase ERp57. Structure 14 1331-9 PubMed GONUTS page
↑ ^12.0 ^12.1 Hetz, C et al. (2011) The unfolded protein response: integrating stress signals through the stress sensor IRE1α. Physiol. Rev. 91 1219-43 PubMed GONUTS page
↑ Bennett, CF et al. (1988) Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C. Nature 334 268-70 PubMed GONUTS page
↑ Urade, R et al. (1997) Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu (QEDL) motifs of microsomal ER-60 protease. J. Biochem. 122 834-42 PubMed GONUTS page
↑ Charnock-Jones, DS et al. (1996) Cloning, expression and genomic organization of human placental protein disulfide isomerase (previously identified as phospholipase C alpha). Int. J. Biochem. Cell Biol. 28 81-9 PubMed GONUTS page
↑ Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

[PMID:21263072-1] Rizvi, SM et al. (2011) Distinct functions for the glycans of tapasin and heavy chains in the assembly of MHC class I molecules. J. Immunol. 186 2309-20 PubMed GONUTS page

[PMID:17947644-2] Rufer, E et al. (2007) Molecular architecture of the TAP-associated MHC class I peptide-loading complex. J. Immunol. 179 5717-27 PubMed GONUTS page

[PMID:21423176-3] Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page

[PMID:19199708-4] Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page

[PMID:21630459-5] Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page

[PMID:16677074-6] Alanen, HI et al. () pH dependence of the peptide thiol-disulfide oxidase activity of six members of the human protein disulfide isomerase family. Antioxid. Redox Signal. 8 283-91 PubMed GONUTS page

[PMID:19995400-7] 7.0 ^7.1 Holbrook, LM et al. (2010) Platelets release novel thiol isomerase enzymes which are recruited to the cell surface following activation. Br. J. Haematol. 148 627-37 PubMed GONUTS page

[PMID:22658674-8] Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page

[PMID:23826168-9] Marques, PI et al. (2013) SERPINA2 is a novel gene with a divergent function from SERPINA1. PLoS ONE 8 e66889 PubMed GONUTS page

[PMID:21873635-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:16905107-11] Kozlov, G et al. (2006) Crystal structure of the bb' domains of the protein disulfide isomerase ERp57. Structure 14 1331-9 PubMed GONUTS page

[PMID:22013210-12] 12.0 ^12.1 Hetz, C et al. (2011) The unfolded protein response: integrating stress signals through the stress sensor IRE1α. Physiol. Rev. 91 1219-43 PubMed GONUTS page

[PMID:3398923-13] Bennett, CF et al. (1988) Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C. Nature 334 268-70 PubMed GONUTS page

[PMID:9399589-14] Urade, R et al. (1997) Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu (QEDL) motifs of microsomal ER-60 protease. J. Biochem. 122 834-42 PubMed GONUTS page

[PMID:8624847-15] Charnock-Jones, DS et al. (1996) Cloning, expression and genomic organization of human placental protein disulfide isomerase (previously identified as phospholipase C alpha). Int. J. Biochem. Cell Biol. 28 81-9 PubMed GONUTS page

[PMID:16130169-16] Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

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HUMAN:PDIA3

Contents

Annotations

Notes

References

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