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HUMAN:PDIA1
Contents
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 |
ECO:0000314 |
F |
Figure 8 shows the Oxydoreductase activity of PDI using ricin. |
complete | |||||
GO:0015036 |
disulfide oxidoreductase activity |
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 | |||||
GO:0006457 |
protein folding |
ECO:0000314 |
P |
Figure 1 shows increased refolding of proinsulin in cells with PDI in comparison to those lacking PDI. |
complete | |||||
enables |
GO:0005178 |
integrin binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0046598 |
positive regulation of viral entry into host cell |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0009897 |
external side of plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
part_of:(CL:0000546) |
Seeded From UniProt |
complete | ||
enables |
GO:0046982 |
protein heterodimerization activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005783 |
endoplasmic reticulum |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0003756 |
protein disulfide isomerase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005925 |
focal adhesion |
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 |
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 |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0071456 |
cellular response to hypoxia |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0034976 |
response to endoplasmic reticulum stress |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0005783 |
endoplasmic reticulum |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0015037 |
peptide disulfide oxidoreductase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003723 |
RNA binding |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003723 |
RNA binding |
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 |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005576 |
extracellular region |
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 |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000432607 |
P |
Seeded From UniProt |
complete | ||
part_of |
GO:0009897 |
external side of plasma membrane |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
MGI:MGI:97464 |
C |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006457 |
protein folding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000432607 |
P |
Seeded From UniProt |
complete | ||
part_of |
GO:0005783 |
endoplasmic reticulum |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
FB:FBgn0014002 |
C |
Seeded From UniProt |
complete | ||
enables |
GO:0003756 |
protein disulfide isomerase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
MGI:MGI:1919080 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0003756 |
protein disulfide isomerase activity |
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 |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0016222 |
procollagen-proline 4-dioxygenase complex |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005783 |
endoplasmic reticulum |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
contributes_to |
GO:0004656 |
procollagen-proline 4-dioxygenase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005783 |
endoplasmic reticulum |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
involved_in |
GO:0055114 |
oxidation-reduction process |
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 |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P04785 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0019899 |
enzyme binding |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P04785 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0003756 |
protein disulfide isomerase activity |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P04785 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0098761 |
cellular response to interleukin-7 |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P09103 |
P |
Seeded From UniProt |
complete | ||
part_of |
GO:0034663 |
endoplasmic reticulum chaperone complex |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P09103 |
C |
Seeded From UniProt |
complete | ||
part_of |
GO:0009897 |
external side of plasma membrane |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P09103 |
C |
Seeded From UniProt |
complete | ||
part_of |
GO:0005783 |
endoplasmic reticulum |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P09103 |
C |
Seeded From UniProt |
complete | ||
enables |
GO:0005178 |
integrin binding |
ECO:0000265 |
sequence orthology evidence used in automatic assertion |
UniProtKB:P09103 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0003756 |
protein disulfide isomerase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016853 |
isomerase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0045454 |
cell redox homeostasis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0003756 |
protein disulfide isomerase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005783 |
endoplasmic reticulum |
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 |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003756 |
protein disulfide isomerase activity |
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 |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
|
C |
Seeded From UniProt |
complete | |
part_of |
GO:0005886 |
plasma membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0016853 |
isomerase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005783 |
endoplasmic reticulum |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0016020 |
membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005788 |
endoplasmic reticulum lumen |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0042470 |
melanosome |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 4.0 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
- ↑ 5.0 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
- ↑ 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
- ↑ 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
- ↑ 14.0 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
- ↑ 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
- ↑ 16.0 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
- ↑ 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
- ↑ 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
- ↑ 19.0 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
c
e
- GO:0005793 ! endoplasmic reticulum-Golgi intermediate compartment
- GO:0005783 ! endoplasmic reticulum
- GO:0034663 ! endoplasmic reticulum chaperone complex
- GO:0005788 ! endoplasmic reticulum lumen
- GO:0019899 ! enzyme binding
- Euarchontoglires
- Eukaryota
- Euteleostomi
- Eutheria
- GO:0009897 ! external side of plasma membrane
- GO:0005576 ! extracellular region
- GO:0070062 ! extracellular exosome
i
p
- GO:0015037 ! peptide disulfide oxidoreductase activity
- GO:0018401 ! peptidyl-proline hydroxylation to 4-hydroxy-L-proline
- GO:0005886 ! plasma membrane
- GO:0046598 ! positive regulation of viral entry into host cell
- GO:0043687 ! post-translational protein modification
- Primates
- GO:0016222 ! procollagen-proline 4-dioxygenase complex
- GO:0004656 ! procollagen-proline 4-dioxygenase activity
- GO:0003756 ! protein disulfide isomerase activity
- GO:0006457 ! protein folding
- GO:0046982 ! protein heterodimerization activity
r