UniProtKB - P07237 (PDIA1_HUMAN)
Protein disulfide-isomerase
P4HB
Functioni
This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307).
3 PublicationsMiscellaneous
Catalytic activityi
- Catalyzes the rearrangement of -S-S- bonds in proteins. EC:5.3.4.1
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 53 | Nucleophile | 1 | |
Sitei | 54 | Contributes to redox potential value | 1 | |
Sitei | 55 | Contributes to redox potential value | 1 | |
Active sitei | 56 | Nucleophile | 1 | |
Sitei | 120 | Lowers pKa of C-terminal Cys of first active site | 1 | |
Active sitei | 397 | NucleophileBy similarity | 1 | |
Sitei | 398 | Contributes to redox potential valueBy similarity | 1 | |
Sitei | 399 | Contributes to redox potential valueBy similarity | 1 | |
Active sitei | 400 | NucleophileBy similarity | 1 | |
Sitei | 461 | Lowers pKa of C-terminal Cys of second active siteBy similarity | 1 |
GO - Molecular functioni
- actin binding Source: ARUK-UCL
- enzyme binding Source: Ensembl
- integrin binding Source: UniProtKB
- procollagen-proline 4-dioxygenase activity Source: ProtInc
- protein disulfide isomerase activity Source: FlyBase
- protein-disulfide reductase activity Source: UniProtKB
- protein heterodimerization activity Source: UniProtKB
- RNA binding Source: UniProtKB
- thiol oxidase activity Source: FlyBase
GO - Biological processi
- cellular response to hypoxia Source: BHF-UCL
- cellular response to interleukin-7 Source: Ensembl
- interleukin-12-mediated signaling pathway Source: Reactome
- interleukin-23-mediated signaling pathway Source: Reactome
- peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: MGI
- positive regulation of cell adhesion Source: ARUK-UCL
- positive regulation of substrate adhesion-dependent cell spreading Source: ARUK-UCL
- positive regulation of viral entry into host cell Source: UniProtKB
- protein folding Source: GO_Central
- protein folding in endoplasmic reticulum Source: FlyBase
- regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
- response to endoplasmic reticulum stress Source: BHF-UCL
Keywordsi
Molecular function | Chaperone, Isomerase |
Enzyme and pathway databases
BRENDAi | 5.3.4.1, 2681 |
PathwayCommonsi | P07237 |
Reactomei | R-HSA-1650814, Collagen biosynthesis and modifying enzymes R-HSA-3299685, Detoxification of Reactive Oxygen Species R-HSA-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) R-HSA-5358346, Hedgehog ligand biogenesis R-HSA-8866423, VLDL assembly R-HSA-8957275, Post-translational protein phosphorylation R-HSA-8963888, Chylomicron assembly R-HSA-8964041, LDL remodeling R-HSA-9020591, Interleukin-12 signaling R-HSA-9020933, Interleukin-23 signaling |
SignaLinki | P07237 |
Names & Taxonomyi
Protein namesi | Recommended name: Protein disulfide-isomerase (EC:5.3.4.1)Short name: PDI Alternative name(s): Cellular thyroid hormone-binding protein Prolyl 4-hydroxylase subunit beta p55 |
Gene namesi | Name:P4HB Synonyms:ERBA2L, PDI, PDIA1, PO4DB |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:8548, P4HB |
MIMi | 176790, gene |
neXtProti | NX_P07237 |
VEuPathDBi | HostDB:ENSG00000185624 |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum 1 Publication
- Endoplasmic reticulum lumen 2 Publications
Plasma membrane
- Cell membrane 1 Publication; Peripheral membrane protein Curated
Other locations
- Melanosome 2 Publications
Note: Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources (Probable). Localizes near CD4-enriched regions on lymphoid cell surfaces (PubMed:11181151). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:10636893). Colocalizes with MTTP in the endoplasmic reticulum (PubMed:23475612).Curated3 Publications
Cytoskeleton
- cytoskeleton Source: ARUK-UCL
Cytosol
- cytosol Source: ARUK-UCL
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
- endoplasmic reticulum chaperone complex Source: Ensembl
- endoplasmic reticulum lumen Source: Reactome
- procollagen-proline 4-dioxygenase complex Source: MGI
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
- extracellular region Source: UniProtKB
Plasma Membrane
- external side of plasma membrane Source: UniProtKB
Other locations
- endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
- focal adhesion Source: UniProtKB
- lamellipodium Source: ARUK-UCL
- melanosome Source: UniProtKB-SubCell
- protein-containing complex Source: ARUK-UCL
Keywords - Cellular componenti
Cell membrane, Endoplasmic reticulum, MembranePathology & Biotechi
Involvement in diseasei
Cole-Carpenter syndrome 1 (CLCRP1)1 Publication
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_073440 | 393 | Y → C in CLCRP1; impairs ability to act as a disulfide isomerase enzyme. 1 PublicationCorresponds to variant dbSNP:rs786204843EnsemblClinVar. | 1 |
Keywords - Diseasei
Craniosynostosis, Disease variant, Osteogenesis imperfectaOrganism-specific databases
DisGeNETi | 5034 |
MalaCardsi | P4HB |
MIMi | 112240, phenotype |
OpenTargetsi | ENSG00000185624 |
Orphaneti | 2050, Cole-Carpenter syndrome 216796, Osteogenesis imperfecta type 1 |
PharmGKBi | PA32876 |
Miscellaneous databases
Pharosi | P07237, Tbio |
Chemistry databases
ChEMBLi | CHEMBL5422 |
DrugBanki | DB11638, Artenimol DB09130, Copper DB03615, Ribostamycin DB01593, Zinc DB14487, Zinc acetate DB14533, Zinc chloride DB14548, Zinc sulfate, unspecified form |
Genetic variation databases
BioMutai | P4HB |
DMDMi | 2507460 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 17 | Combined sources4 PublicationsAdd BLAST | 17 | |
ChainiPRO_0000034195 | 18 – 508 | Protein disulfide-isomeraseAdd BLAST | 491 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 53 ↔ 56 | Redox-activePROSITE-ProRule annotation1 Publication | ||
Modified residuei | 200 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 222 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 271 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 357 | Phosphoserine; by FAM20C1 Publication | 1 | |
Disulfide bondi | 397 ↔ 400 | Redox-activePROSITE-ProRule annotation |
Keywords - PTMi
Acetylation, Disulfide bond, PhosphoproteinProteomic databases
EPDi | P07237 |
jPOSTi | P07237 |
MassIVEi | P07237 |
MaxQBi | P07237 |
PaxDbi | P07237 |
PeptideAtlasi | P07237 |
PRIDEi | P07237 |
ProteomicsDBi | 51976 |
TopDownProteomicsi | P07237 |
2D gel databases
DOSAC-COBS-2DPAGEi | P07237 |
OGPi | P07237 |
REPRODUCTION-2DPAGEi | IPI00010796 P07237 |
SWISS-2DPAGEi | P07237 |
PTM databases
GlyGeni | P07237, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | P07237 |
MetOSitei | P07237 |
PhosphoSitePlusi | P07237 |
SwissPalmi | P07237 |
Expressioni
Gene expression databases
Bgeei | ENSG00000185624, Expressed in stromal cell of endometrium and 245 other tissues |
ExpressionAtlasi | P07237, baseline and differential |
Genevisiblei | P07237, HS |
Organism-specific databases
HPAi | ENSG00000185624, Tissue enhanced (liver, pancreas) |
Interactioni
Subunit structurei
Heterodimer; heterodimerizes with the protein microsomal triglyceride transfer MTTP (PubMed:23475612, PubMed:26224785, PubMed:16478722). Homodimer. Monomers and homotetramers may also occur.
Interacts with P4HA2, forming a heterotetramer consisting of 2 alpha subunits (P4HA2) and 2 beta (P4HB), where P4HB plays the role of a structural subunit; this tetramer catalyzes the formation of 4-hydroxyproline in collagen (PubMed:7753822). Also constitutes the structural subunit of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity (By similarity). Binds UBQLN1 (PubMed:12095988).
Interacts with ERO1B (PubMed:11707400). Binds to CD4, and upon HIV-1 binding to the cell membrane, is part of a P4HB/PDI-CD4-CXCR4-gp120 complex.
Interacts with ILDR2 (By similarity).
By similarity6 PublicationsBinary interactionsi
P07237
GO - Molecular functioni
- actin binding Source: ARUK-UCL
- enzyme binding Source: Ensembl
- integrin binding Source: UniProtKB
- protein heterodimerization activity Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 111073, 319 interactors |
CORUMi | P07237 |
DIPi | DIP-32979N |
IntActi | P07237, 175 interactors |
MINTi | P07237 |
STRINGi | 9606.ENSP00000327801 |
Chemistry databases
BindingDBi | P07237 |
Miscellaneous databases
RNActi | P07237, protein |
Structurei
Secondary structure
3D structure databases
BMRBi | P07237 |
SMRi | P07237 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P07237 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 18 – 134 | Thioredoxin 1PROSITE-ProRule annotationAdd BLAST | 117 | |
Domaini | 349 – 475 | Thioredoxin 2PROSITE-ProRule annotationAdd BLAST | 127 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 471 – 508 | DisorderedSequence analysisAdd BLAST | 38 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 505 – 508 | Prevents secretion from ER | 4 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 476 – 508 | Acidic residuesSequence analysisAdd BLAST | 33 |
Sequence similaritiesi
Keywords - Domaini
Redox-active center, Repeat, SignalPhylogenomic databases
eggNOGi | KOG0190, Eukaryota |
GeneTreei | ENSGT00940000157351 |
InParanoidi | P07237 |
OMAi | IEKYVDP |
OrthoDBi | 462118at2759 |
PhylomeDBi | P07237 |
TreeFami | TF106381 |
Family and domain databases
DisProti | DP02637 |
InterProi | View protein in InterPro IPR005788, Disulphide_isomerase IPR005792, Prot_disulphide_isomerase IPR036249, Thioredoxin-like_sf IPR017937, Thioredoxin_CS IPR013766, Thioredoxin_domain |
Pfami | View protein in Pfam PF00085, Thioredoxin, 2 hits |
SUPFAMi | SSF52833, SSF52833, 4 hits |
TIGRFAMsi | TIGR01130, ER_PDI_fam, 1 hit TIGR01126, pdi_dom, 2 hits |
PROSITEi | View protein in PROSITE PS00014, ER_TARGET, 1 hit PS00194, THIOREDOXIN_1, 2 hits PS51352, THIOREDOXIN_2, 2 hits |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 31 potential isoforms that are computationally mapped.Show allAlign All
10 20 30 40 50
MLRRALLCLA VAALVRADAP EEEDHVLVLR KSNFAEALAA HKYLLVEFYA
60 70 80 90 100
PWCGHCKALA PEYAKAAGKL KAEGSEIRLA KVDATEESDL AQQYGVRGYP
110 120 130 140 150
TIKFFRNGDT ASPKEYTAGR EADDIVNWLK KRTGPAATTL PDGAAAESLV
160 170 180 190 200
ESSEVAVIGF FKDVESDSAK QFLQAAEAID DIPFGITSNS DVFSKYQLDK
210 220 230 240 250
DGVVLFKKFD EGRNNFEGEV TKENLLDFIK HNQLPLVIEF TEQTAPKIFG
260 270 280 290 300
GEIKTHILLF LPKSVSDYDG KLSNFKTAAE SFKGKILFIF IDSDHTDNQR
310 320 330 340 350
ILEFFGLKKE ECPAVRLITL EEEMTKYKPE SEELTAERIT EFCHRFLEGK
360 370 380 390 400
IKPHLMSQEL PEDWDKQPVK VLVGKNFEDV AFDEKKNVFV EFYAPWCGHC
410 420 430 440 450
KQLAPIWDKL GETYKDHENI VIAKMDSTAN EVEAVKVHSF PTLKFFPASA
460 470 480 490 500
DRTVIDYNGE RTLDGFKKFL ESGGQDGAGD DDDLEDLEEA EEPDMEEDDD
QKAVKDEL
Computationally mapped potential isoform sequencesi
There are 31 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A7P0T8J3 | A0A7P0T8J3_HUMAN | Protein disulfide-isomerase | P4HB | 488 | Annotation score: | ||
A0A7P0T8X1 | A0A7P0T8X1_HUMAN | Protein disulfide-isomerase | P4HB | 479 | Annotation score: | ||
A0A7P0T9U6 | A0A7P0T9U6_HUMAN | Protein disulfide-isomerase | P4HB | 486 | Annotation score: | ||
A0A7P0TA35 | A0A7P0TA35_HUMAN | Protein disulfide-isomerase | P4HB | 542 | Annotation score: | ||
A0A7P0TB26 | A0A7P0TB26_HUMAN | Protein disulfide-isomerase | P4HB | 533 | Annotation score: | ||
I3L3P5 | I3L3P5_HUMAN | Protein disulfide-isomerase | P4HB | 472 | Annotation score: | ||
A0A7P0T9K9 | A0A7P0T9K9_HUMAN | Protein disulfide-isomerase | P4HB | 439 | Annotation score: | ||
I3L4M2 | I3L4M2_HUMAN | Protein disulfide-isomerase | P4HB | 537 | Annotation score: | ||
A0A7P0TA71 | A0A7P0TA71_HUMAN | Protein disulfide-isomerase | P4HB | 557 | Annotation score: | ||
A0A7P0TA97 | A0A7P0TA97_HUMAN | Protein disulfide-isomerase | P4HB | 479 | Annotation score: | ||
There are more potential isoformsShow all |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 10 – 11 | AV → PW in CAA28775 (PubMed:3034602).Curated | 2 | |
Sequence conflicti | 21 | E → D AA sequence (PubMed:9399589).Curated | 1 | |
Sequence conflicti | 24 | D → V AA sequence (PubMed:9399589).Curated | 1 | |
Sequence conflicti | 44 – 45 | LL → PP in CAA28775 (PubMed:3034602).Curated | 2 | |
Sequence conflicti | 49 | Y → H in CAA28775 (PubMed:3034602).Curated | 1 | |
Sequence conflicti | 141 | P → R in AAA61169 (PubMed:3611107).Curated | 1 | |
Sequence conflicti | 360 – 362 | LPE → RAG in AAA61169 (PubMed:3611107).Curated | 3 | |
Sequence conflicti | 372 | L → P in AAA61169 (PubMed:3611107).Curated | 1 | |
Sequence conflicti | 439 | S → G in CAA28775 (PubMed:3034602).Curated | 1 | |
Sequence conflicti | 444 | K → G in CAA28775 (PubMed:3034602).Curated | 1 | |
Sequence conflicti | 460 | E → Q in CAA30112 (PubMed:3342239).Curated | 1 | |
Sequence conflicti | 481 | D → V in CAA28775 (PubMed:3034602).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_073440 | 393 | Y → C in CLCRP1; impairs ability to act as a disulfide isomerase enzyme. 1 PublicationCorresponds to variant dbSNP:rs786204843EnsemblClinVar. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X05130 mRNA Translation: CAA28775.1 J02783 mRNA Translation: AAA61169.1 M22806 , M22803, M22804, M22805 Genomic DNA Translation: AAC13652.1 AK315631 mRNA Translation: BAG37999.1 CH471099 Genomic DNA Translation: EAW89690.1 BC010859 mRNA Translation: AAH10859.1 BC029617 mRNA Translation: AAH29617.1 BC071892 mRNA Translation: AAH71892.1 S37207 Genomic DNA Translation: AAB22262.2 X07077 mRNA Translation: CAA30112.1 |
CCDSi | CCDS11787.1 |
PIRi | A31913, ISHUSS |
RefSeqi | NP_000909.2, NM_000918.3 |
Genome annotation databases
Ensembli | ENST00000331483; ENSP00000327801; ENSG00000185624 |
GeneIDi | 5034 |
KEGGi | hsa:5034 |
MANE-Selecti | ENST00000331483.9; ENSP00000327801.4; NM_000918.4; NP_000909.2 |
UCSCi | uc002kbn.2, human |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X05130 mRNA Translation: CAA28775.1 J02783 mRNA Translation: AAA61169.1 M22806 , M22803, M22804, M22805 Genomic DNA Translation: AAC13652.1 AK315631 mRNA Translation: BAG37999.1 CH471099 Genomic DNA Translation: EAW89690.1 BC010859 mRNA Translation: AAH10859.1 BC029617 mRNA Translation: AAH29617.1 BC071892 mRNA Translation: AAH71892.1 S37207 Genomic DNA Translation: AAB22262.2 X07077 mRNA Translation: CAA30112.1 |
CCDSi | CCDS11787.1 |
PIRi | A31913, ISHUSS |
RefSeqi | NP_000909.2, NM_000918.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BJX | NMR | - | A | 136-245 | [»] | |
1MEK | NMR | - | A | 18-137 | [»] | |
1X5C | NMR | - | A | 368-475 | [»] | |
2BJX | NMR | - | A | 136-245 | [»] | |
2K18 | NMR | - | A | 135-357 | [»] | |
3BJ5 | X-ray | 2.20 | A | 230-368 | [»] | |
3UEM | X-ray | 2.29 | A | 137-479 | [»] | |
4EKZ | X-ray | 2.51 | A | 18-479 | [»] | |
4EL1 | X-ray | 2.88 | A/B | 18-479 | [»] | |
4JU5 | X-ray | 2.28 | A/B | 135-367 | [»] | |
6I7S | X-ray | 2.50 | A/B | 18-508 | [»] | |
BMRBi | P07237 | |||||
SMRi | P07237 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 111073, 319 interactors |
CORUMi | P07237 |
DIPi | DIP-32979N |
IntActi | P07237, 175 interactors |
MINTi | P07237 |
STRINGi | 9606.ENSP00000327801 |
Chemistry databases
BindingDBi | P07237 |
ChEMBLi | CHEMBL5422 |
DrugBanki | DB11638, Artenimol DB09130, Copper DB03615, Ribostamycin DB01593, Zinc DB14487, Zinc acetate DB14533, Zinc chloride DB14548, Zinc sulfate, unspecified form |
PTM databases
GlyGeni | P07237, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | P07237 |
MetOSitei | P07237 |
PhosphoSitePlusi | P07237 |
SwissPalmi | P07237 |
Genetic variation databases
BioMutai | P4HB |
DMDMi | 2507460 |
2D gel databases
DOSAC-COBS-2DPAGEi | P07237 |
OGPi | P07237 |
REPRODUCTION-2DPAGEi | IPI00010796 P07237 |
SWISS-2DPAGEi | P07237 |
Proteomic databases
EPDi | P07237 |
jPOSTi | P07237 |
MassIVEi | P07237 |
MaxQBi | P07237 |
PaxDbi | P07237 |
PeptideAtlasi | P07237 |
PRIDEi | P07237 |
ProteomicsDBi | 51976 |
TopDownProteomicsi | P07237 |
Protocols and materials databases
Antibodypediai | 3250, 555 antibodies from 43 providers |
DNASUi | 5034 |
Genome annotation databases
Ensembli | ENST00000331483; ENSP00000327801; ENSG00000185624 |
GeneIDi | 5034 |
KEGGi | hsa:5034 |
MANE-Selecti | ENST00000331483.9; ENSP00000327801.4; NM_000918.4; NP_000909.2 |
UCSCi | uc002kbn.2, human |
Organism-specific databases
CTDi | 5034 |
DisGeNETi | 5034 |
GeneCardsi | P4HB |
HGNCi | HGNC:8548, P4HB |
HPAi | ENSG00000185624, Tissue enhanced (liver, pancreas) |
MalaCardsi | P4HB |
MIMi | 112240, phenotype 176790, gene |
neXtProti | NX_P07237 |
OpenTargetsi | ENSG00000185624 |
Orphaneti | 2050, Cole-Carpenter syndrome 216796, Osteogenesis imperfecta type 1 |
PharmGKBi | PA32876 |
VEuPathDBi | HostDB:ENSG00000185624 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0190, Eukaryota |
GeneTreei | ENSGT00940000157351 |
InParanoidi | P07237 |
OMAi | IEKYVDP |
OrthoDBi | 462118at2759 |
PhylomeDBi | P07237 |
TreeFami | TF106381 |
Enzyme and pathway databases
BRENDAi | 5.3.4.1, 2681 |
PathwayCommonsi | P07237 |
Reactomei | R-HSA-1650814, Collagen biosynthesis and modifying enzymes R-HSA-3299685, Detoxification of Reactive Oxygen Species R-HSA-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) R-HSA-5358346, Hedgehog ligand biogenesis R-HSA-8866423, VLDL assembly R-HSA-8957275, Post-translational protein phosphorylation R-HSA-8963888, Chylomicron assembly R-HSA-8964041, LDL remodeling R-HSA-9020591, Interleukin-12 signaling R-HSA-9020933, Interleukin-23 signaling |
SignaLinki | P07237 |
Miscellaneous databases
BioGRID-ORCSi | 5034, 23 hits in 1059 CRISPR screens |
ChiTaRSi | P4HB, human |
EvolutionaryTracei | P07237 |
GeneWikii | P4HB |
GenomeRNAii | 5034 |
Pharosi | P07237, Tbio |
PROi | PR:P07237 |
RNActi | P07237, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000185624, Expressed in stromal cell of endometrium and 245 other tissues |
ExpressionAtlasi | P07237, baseline and differential |
Genevisiblei | P07237, HS |
Family and domain databases
DisProti | DP02637 |
InterProi | View protein in InterPro IPR005788, Disulphide_isomerase IPR005792, Prot_disulphide_isomerase IPR036249, Thioredoxin-like_sf IPR017937, Thioredoxin_CS IPR013766, Thioredoxin_domain |
Pfami | View protein in Pfam PF00085, Thioredoxin, 2 hits |
SUPFAMi | SSF52833, SSF52833, 4 hits |
TIGRFAMsi | TIGR01130, ER_PDI_fam, 1 hit TIGR01126, pdi_dom, 2 hits |
PROSITEi | View protein in PROSITE PS00014, ER_TARGET, 1 hit PS00194, THIOREDOXIN_1, 2 hits PS51352, THIOREDOXIN_2, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | PDIA1_HUMAN | |
Accessioni | P07237Primary (citable) accession number: P07237 Secondary accession number(s): B2RDQ2 Q6LDE5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1988 |
Last sequence update: | November 1, 1997 | |
Last modified: | February 23, 2022 | |
This is version 259 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 17
Human chromosome 17: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families