GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

HUMAN:PDIA1

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) P4HB (synonyms: ERBA2L, PDI, PDIA1, PO4DB)
Protein Name(s) Protein disulfide-isomerase

PDI Cellular thyroid hormone-binding protein Prolyl 4-hydroxylase subunit beta p55

External Links
UniProt P07237
EMBL X05130
J02783
M22806
M22803
M22804
M22805
AK315631
CH471099
BC010859
BC029617
BC071892
S37207
X07077
CCDS CCDS11787.1
PIR A31913
RefSeq NP_000909.2
UniGene Hs.464336
PDB 1BJX
1MEK
1X5C
2BJX
2K18
3BJ5
3UEM
4EKZ
4EL1
4JU5
PDBsum 1BJX
1MEK
1X5C
2BJX
2K18
3BJ5
3UEM
4EKZ
4EL1
4JU5
ProteinModelPortal P07237
SMR P07237
BioGrid 111073
IntAct P07237
MINT MINT-4999403
STRING 9606.ENSP00000327801
BindingDB P07237
ChEMBL CHEMBL2364681
PhosphoSite P07237
DMDM 2507460
DOSAC-COBS-2DPAGE P07237
OGP P07237
REPRODUCTION-2DPAGE IPI00010796
P07237
SWISS-2DPAGE P07237
MaxQB P07237
PaxDb P07237
PeptideAtlas P07237
PRIDE P07237
DNASU 5034
Ensembl ENST00000331483
GeneID 5034
KEGG hsa:5034
UCSC uc002kbn.1
CTD 5034
GeneCards GC17M079801
HGNC HGNC:8548
HPA CAB012463
HPA018884
MIM 176790
neXtProt NX_P07237
PharmGKB PA32876
eggNOG COG0526
GeneTree ENSGT00760000119201
HOGENOM HOG000162459
HOVERGEN HBG005920
InParanoid P07237
KO K09580
OMA YRDHENI
OrthoDB EOG7VHSX1
PhylomeDB P07237
TreeFam TF106381
BRENDA 5.3.4.1
Reactome REACT_121139
REACT_172715
REACT_228111
REACT_6841
ChiTaRS P4HB
EvolutionaryTrace P07237
GeneWiki P4HB
GenomeRNAi 5034
NextBio 19398
PMAP-CutDB P07237
PRO PR:P07237
Proteomes UP000005640
Bgee P07237
CleanEx HS_P4HB
ExpressionAtlas P07237
Genevestigator P07237
GO GO:0005783
GO:0005788
GO:0005793
GO:0005576
GO:0070062
GO:0005925
GO:0042470
GO:0005886
GO:0016222
GO:0044822
GO:0004656
GO:0003756
GO:0045454
GO:0071456
GO:0030198
GO:0042157
GO:0018401
GO:0006457
GO:1902175
GO:0034976
GO:0044281
Gene3D 3.40.30.10
InterPro IPR005788
IPR005792
IPR012336
IPR017937
IPR013766
Pfam PF00085
SUPFAM SSF52833
TIGRFAMs TIGR01130
TIGR01126
PROSITE PS00014
PS00194
PS51352

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0003756

protein disulfide isomerase activity

PMID:15225124[1]

ECO:0000314

F

Figure 8 shows the Oxydoreductase activity of PDI using ricin.

complete
CACAO 4181

GO:0015036

disulfide oxidoreductase activity

PMID:9013867[2]

ECO:0000314

F

Figure 6 (lane 2 and 3). CTA get reduced in the presence of PDI (lane 3). Lane 2 is without PDI.

complete
CACAO 4602

GO:0006457

protein folding

PMID:11694508[3]

ECO:0000314

P

Figure 1 shows increased refolding of proinsulin in cells with PDI in comparison to those lacking PDI.

complete
CACAO 4892

enables

GO:0005178

integrin binding

PMID:21670307[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P05106

F

Seeded From UniProt

complete

involved_in

GO:0046598

positive regulation of viral entry into host cell

PMID:21670307[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0009897

external side of plasma membrane

PMID:21670307[4]

ECO:0000314

direct assay evidence used in manual assertion

C

part_of:(CL:0000546)

Seeded From UniProt

complete

enables

GO:0046982

protein heterodimerization activity

PMID:23475612[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

PMID:23475612[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003756

protein disulfide isomerase activity

PMID:15225124[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005925

focal adhesion

PMID:21423176[6]

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[7]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0001831)

Seeded From UniProt

complete

involved_in

GO:1902175

regulation of oxidative stress-induced intrinsic apoptotic signaling pathway

PMID:12095988[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071456

cellular response to hypoxia

PMID:12095988[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034976

response to endoplasmic reticulum stress

PMID:12095988[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

PMID:12095988[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0015037

peptide disulfide oxidoreductase activity

PMID:16677074[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

PMID:22681889[10]

ECO:0007005

high throughput direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

PMID:22658674[11]

ECO:0007005

high throughput direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005793

endoplasmic reticulum-Golgi intermediate compartment

PMID:15308636[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

PMID:14718574[13]

ECO:0000303

author statement without traceable support used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0034976

response to endoplasmic reticulum stress

PMID:21873635[14]

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:0009897

external side of plasma membrane

PMID:21873635[14]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:97464
PANTHER:PTN000432883
UniProtKB:P07237

C

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

PMID:21873635[14]

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[14]

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[14]

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

enables

GO:0003756

protein disulfide isomerase activity

PMID:15720785[15]

ECO:0000269

experimental evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0018401

peptidyl-proline hydroxylation to 4-hydroxy-L-proline

PMID:7753822[16]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0016222

procollagen-proline 4-dioxygenase complex

PMID:7753822[16]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

PMID:23152784[17]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

contributes_to

GO:0004656

procollagen-proline 4-dioxygenase activity

PMID:7753822[16]

ECO:0000314

direct assay evidence used in manual assertion

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: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

enables

GO:0046982

protein heterodimerization activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P04785
ensembl:ENSRNOP00000051841

F

Seeded From UniProt

complete

enables

GO:0019899

enzyme binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P04785
ensembl:ENSRNOP00000051841

F

Seeded From UniProt

complete

enables

GO:0003756

protein disulfide isomerase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P04785
ensembl:ENSRNOP00000051841

F

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:P09103
ensembl:ENSMUSP00000026122

P

Seeded From UniProt

complete

part_of

GO:0034663

endoplasmic reticulum chaperone complex

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P09103
ensembl:ENSMUSP00000026122

C

Seeded From UniProt

complete

part_of

GO:0009897

external side of plasma membrane

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P09103
ensembl:ENSMUSP00000026122

C

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P09103
ensembl:ENSMUSP00000026122

C

Seeded From UniProt

complete

enables

GO:0005178

integrin binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P09103
ensembl:ENSMUSP00000026122

F

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

part_of

GO:0005783

endoplasmic reticulum

PMID:3034602[18]

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004656

procollagen-proline 4-dioxygenase activity

PMID:2846539[19]

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:2846539[19]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0044267

cellular protein metabolic process

Reactome:R-HSA-392499

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043687

post-translational protein modification

Reactome:R-HSA-597592

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0038155

interleukin-23-mediated signaling pathway

Reactome:R-HSA-9020933

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0035722

interleukin-12-mediated signaling pathway

Reactome:R-HSA-9020591

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034379

very-low-density lipoprotein particle assembly

Reactome:R-HSA-8866423

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034378

chylomicron assembly

Reactome:R-HSA-8963888

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-8952289
Reactome:R-HSA-8950456
Reactome:R-HSA-8950183
Reactome:R-HSA-8950113
Reactome:R-HSA-8948234
Reactome:R-HSA-8866329
Reactome:R-HSA-5358340
Reactome:R-HSA-5358336
Reactome:R-HSA-3341296
Reactome:R-HSA-2002460
Reactome:R-HSA-174786
Reactome:R-HSA-1650808

ECO:0000304

author statement supported by traceable reference used in manual assertion












C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0039

C

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:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

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

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

Notes

References

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

  1. 1.0 1.1 Spooner, RA et al. (2004) Protein disulphide-isomerase reduces ricin to its A and B chains in the endoplasmic reticulum. Biochem. J. 383 285-93 PubMed GONUTS page
  2. Majoul, I et al. (1997) Reduction of protein disulfide bonds in an oxidizing environment. The disulfide bridge of cholera toxin A-subunit is reduced in the endoplasmic reticulum. FEBS Lett. 401 104-8 PubMed GONUTS page
  3. Winter, J et al. (2002) Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin. J. Biol. Chem. 277 310-7 PubMed GONUTS page
  4. 4.0 4.1 4.2 Bi, S et al. (2011) Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry. Proc. Natl. Acad. Sci. U.S.A. 108 10650-5 PubMed GONUTS page
  5. 5.0 5.1 Khatun, I et al. (2013) Loss of both phospholipid and triglyceride transfer activities of microsomal triglyceride transfer protein in abetalipoproteinemia. J. Lipid Res. 54 1541-9 PubMed GONUTS page
  6. 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
  7. 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
  8. 8.0 8.1 8.2 8.3 Ko, HS et al. (2002) Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death. J. Biol. Chem. 277 35386-92 PubMed GONUTS page
  9. 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
  10. Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
  11. Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
  12. Breuza, L et al. (2004) Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46. J. Biol. Chem. 279 47242-53 PubMed GONUTS page
  13. Anderson, NL et al. (2004) The human plasma proteome: a nonredundant list developed by combination of four separate sources. Mol. Cell Proteomics 3 311-26 PubMed GONUTS page
  14. 14.0 14.1 14.2 14.3 14.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  15. Alloza, I & Vandenbroeck, K (2005) The metallopeptide antibiotic bacitracin inhibits interleukin-12 alphabeta and beta2 secretion. J. Pharm. Pharmacol. 57 213-8 PubMed GONUTS page
  16. 16.0 16.1 16.2 Helaakoski, T et al. (1995) Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit. Proc. Natl. Acad. Sci. U.S.A. 92 4427-31 PubMed GONUTS page
  17. Zhang, Y et al. (2012) Transcriptional regulation of the Ufm1 conjugation system in response to disturbance of the endoplasmic reticulum homeostasis and inhibition of vesicle trafficking. PLoS ONE 7 e48587 PubMed GONUTS page
  18. Pihlajaniemi, T et al. (1987) Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J. 6 643-9 PubMed GONUTS page
  19. 19.0 19.1 Tasanen, K et al. (1988) Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase. J. Biol. Chem. 263 16218-24 PubMed GONUTS page