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 Publications

Miscellaneous

Reduces and may activate fusogenic properties of HIV-1 gp120 surface protein, thereby enabling HIV-1 entry into the cell.

Catalytic activityⁱ

Catalyzes the rearrangement of -S-S- bonds in proteins.

Sites

Feature key	Position(s)	DescriptionActions	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

enzyme binding Source: Ensembl
integrin binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 21670307
peptide disulfide oxidoreductase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 16677074
procollagen-proline 4-dioxygenase activity
Source: ProtInc
Traceable author statementⁱ
- 2846539
protein disulfide isomerase activity
Source: CACAO
Inferred from direct assayⁱ
- 15225124
protein heterodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- 23475612
RNA binding
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 22658674
- 22681889

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell redox homeostasis Source: InterPro
cellular protein metabolic process Source: Reactome
cellular response to hypoxia
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 12095988
chylomicron assembly Source: Reactome
interleukin-12-mediated signaling pathway Source: Reactome
interleukin-23-mediated signaling pathway Source: Reactome
peptidyl-proline hydroxylation to 4-hydroxy-L-proline
Source: MGI
Inferred from direct assayⁱ
- 7753822
positive regulation of viral entry into host cell
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21670307
post-translational protein modification Source: Reactome
protein folding Source: GO_Central
regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 12095988
response to endoplasmic reticulum stress
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 12095988
very-low-density lipoprotein particle assembly Source: Reactome

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Chaperone, Isomerase

Molecular function

Chaperone, Isomerase

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS06845-MONOMER
BRENDAⁱ	5.3.4.1 2681
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-9020591 Interleukin-12 signaling R-HSA-9020933 Interleukin-23 signaling

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	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 17

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000185624.14
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:8548 P4HB
MIMⁱ	176790 gene
neXtProtⁱ	NX_P07237

Keywords - Cellular componentⁱ

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Cole-Carpenter syndrome 1 (CLCRP1)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of Cole-Carpenter syndrome, a disorder characterized by features of osteogenesis imperfecta such as bone deformities and severe bone fragility with frequent fractures, in association with craniosynostosis, ocular proptosis, hydrocephalus, growth failure and distinctive facial features. Craniofacial findings include marked frontal bossing, midface hypoplasia, and micrognathia. Despite the craniosynostosis and hydrocephalus, intellectual development is normal. CLCRP1 inheritance is autosomal dominant.

Keywords - Diseaseⁱ

Craniosynostosis, Disease mutation, Osteogenesis imperfecta

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5034
MalaCards human disease database More...MalaCardsⁱ	P4HB
MIMⁱ	112240 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000185624
PharmGKBⁱ	PA32876

Chemistry databases

ChEMBLⁱ	CHEMBL5422
Drug and drug target database More...DrugBankⁱ	DB03615 Ribostamycin

Polymorphism and mutation 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	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, Phosphoprotein

Proteomic databases

EPDⁱ	P07237
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P07237
PaxDbⁱ	P07237
PeptideAtlas More...PeptideAtlasⁱ	P07237
PRIDEⁱ	P07237
ProteomicsDBⁱ	51976
TopDownProteomicsⁱ	P07237

2D gel databases

DOSAC-COBS 2D-PAGE database More...DOSAC-COBS-2DPAGEⁱ	P07237
USC-OGP 2-DE database More...OGPⁱ	P07237
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	IPI00010796 P07237
SWISS-2DPAGEⁱ	P07237

PTM databases

iPTMnetⁱ	P07237
PhosphoSitePlusⁱ	P07237
SwissPalmⁱ	P07237

Miscellaneous databases

PMAP-CutDBⁱ	P07237

PMAP-CutDBⁱ

P07237

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000185624 Expressed in 235 organ(s), highest expression level in right lobe of liver
CleanExⁱ	HS_P4HB
ExpressionAtlasⁱ	P07237 baseline and differential
Genevisibleⁱ	P07237 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB012463 HPA018884

HPAⁱ

CAB012463
HPA018884

Interactionⁱ

Subunit structureⁱ

Heterodimer; heterodimerizes with the protein microsomal triglyceride transfer MTTP (PubMed:23475612, PubMed:26224785). Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and 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.By similarity4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
ERO1A	Q96HE7	2	EBI-395883,EBI-2564539
HM13	Q8TCT9	3	EBI-395883,EBI-347472
PRDX4	Q13162	2	EBI-395883,EBI-2211957
TAP1	Q03518	4	EBI-395883,EBI-747259

GO - Molecular functionⁱ

enzyme binding Source: Ensembl
integrin binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 21670307
protein heterodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- 23475612

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	111073, 145 interactors
CORUMⁱ	P07237
Database of interacting proteins More...DIPⁱ	DIP-32979N
IntActⁱ	P07237, 93 interactors
Molecular INTeraction database More...MINTⁱ	P07237
STRINGⁱ	9606.ENSP00000327801

Chemistry databases

BindingDBⁱ

P07237

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	21 – 23	Combined sources	3
Beta strandⁱ	26 – 28	Combined sources	3
Turnⁱ	31 – 33	Combined sources	3
Helixⁱ	34 – 40	Combined sources	7
Beta strandⁱ	42 – 49	Combined sources	8
Helixⁱ	54 – 72	Combined sources	19
Beta strandⁱ	78 – 83	Combined sources	6
Turnⁱ	84 – 86	Combined sources	3
Helixⁱ	88 – 93	Combined sources	6
Beta strandⁱ	101 – 106	Combined sources	6
Beta strandⁱ	110 – 112	Combined sources	3
Beta strandⁱ	114 – 116	Combined sources	3
Helixⁱ	122 – 132	Combined sources	11
Beta strandⁱ	137 – 139	Combined sources	3
Helixⁱ	143 – 151	Combined sources	9
Beta strandⁱ	153 – 160	Combined sources	8
Turnⁱ	162 – 165	Combined sources	4
Helixⁱ	167 – 178	Combined sources	12
Beta strandⁱ	180 – 182	Combined sources	3
Beta strandⁱ	184 – 187	Combined sources	4
Helixⁱ	190 – 195	Combined sources	6
Beta strandⁱ	199 – 209	Combined sources	11
Beta strandⁱ	212 – 215	Combined sources	4
Helixⁱ	222 – 232	Combined sources	11
Beta strandⁱ	237 – 239	Combined sources	3
Turnⁱ	242 – 244	Combined sources	3
Helixⁱ	245 – 249	Combined sources	5
Beta strandⁱ	250 – 252	Combined sources	3
Beta strandⁱ	255 – 260	Combined sources	6
Beta strandⁱ	265 – 267	Combined sources	3
Helixⁱ	268 – 280	Combined sources	13
Turnⁱ	281 – 285	Combined sources	5
Beta strandⁱ	287 – 291	Combined sources	5
Helixⁱ	296 – 298	Combined sources	3
Helixⁱ	299 – 304	Combined sources	6
Helixⁱ	309 – 311	Combined sources	3
Beta strandⁱ	313 – 319	Combined sources	7
Beta strandⁱ	321 – 323	Combined sources	3
Beta strandⁱ	325 – 327	Combined sources	3
Beta strandⁱ	330 – 332	Combined sources	3
Helixⁱ	336 – 347	Combined sources	12
Beta strandⁱ	353 – 355	Combined sources	3
Helixⁱ	362 – 364	Combined sources	3
Beta strandⁱ	367 – 372	Combined sources	6
Turnⁱ	374 – 376	Combined sources	3
Helixⁱ	377 – 381	Combined sources	5
Beta strandⁱ	387 – 393	Combined sources	7
Helixⁱ	398 – 413	Combined sources	16
Turnⁱ	414 – 416	Combined sources	3
Beta strandⁱ	418 – 426	Combined sources	9
Turnⁱ	427 – 429	Combined sources	3
Beta strandⁱ	439 – 446	Combined sources	8
Beta strandⁱ	448 – 451	Combined sources	4
Helixⁱ	463 – 470	Combined sources	8
Turnⁱ	471 – 473	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P07237
SMRⁱ	P07237
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P07237

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

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	505 – 508	Prevents secretion from ER		4

Sequence similaritiesⁱ

Belongs to the protein disulfide isomerase family.Curated

Keywords - Domainⁱ

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGⁱ	KOG0190 Eukaryota COG0526 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00860000133691
HOGENOMⁱ	HOG000162459
HOVERGENⁱ	HBG005920
InParanoidⁱ	P07237
KEGG Orthology (KO) More...KOⁱ	K09580
OMAⁱ	QYGVRGY
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G08WM
PhylomeDBⁱ	P07237
TreeFamⁱ	TF106381

Family and domain databases

InterProⁱ	View protein in InterPro IPR005788 Disulphide_isomerase IPR005792 Prot_disulphide_isomerase IPR036249 Thioredoxin-like_sf IPR017937 Thioredoxin_CS IPR013766 Thioredoxin_domain
Pfam protein domain database More...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

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 11 potential isoforms that are computationally mapped.Show all Align All

P07237-1 [UniParc]FASTA Add to basket

« Hide

        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

Length:508

Mass (Da):57,116

Last modified:November 1, 1997 - v3

Checksum:ⁱ906CE6D9900B8FCE

GO

Computationally mapped potential isoform sequencesⁱ

There are 11 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name	Protein names	Gene names	Length	Annotation

	H7BZ94	H7BZ94_HUMAN	Protein disulfide-isomerase Protein disulfide-isomerase	P4HB	464	Annotation score:
	I3NI03	I3NI03_HUMAN	Protein disulfide-isomerase Protein disulfide-isomerase	P4HB	166	Annotation score:
	I3L0S0	I3L0S0_HUMAN	Protein disulfide-isomerase Protein disulfide-isomerase	P4HB	148	Annotation score:
	I3L3U6	I3L3U6_HUMAN	Protein disulfide-isomerase Protein disulfide-isomerase	P4HB	188	Annotation score:
	H0Y3Z3	H0Y3Z3_HUMAN	Protein disulfide-isomerase Protein disulfide-isomerase	P4HB	274	Annotation score:
	I3L514	I3L514_HUMAN	Protein disulfide-isomerase Protein disulfide-isomerase	P4HB	106	Annotation score:
	I3L3P5	I3L3P5_HUMAN	Protein disulfide-isomerase Protein disulfide-isomerase	P4HB	156	Annotation score:
	I3L398	I3L398_HUMAN	Protein disulfide-isomerase Protein disulfide-isomerase	P4HB	200	Annotation score:
	I3L312	I3L312_HUMAN	Protein disulfide-isomerase Protein disulfide-isomerase	P4HB	208	Annotation score:
	I3L1Y5	I3L1Y5_HUMAN	Protein disulfide-isomerase Protein disulfide-isomerase	P4HB	54	Annotation score:
There is more potential isoformShow all

Experimental Info

Feature key	Position(s)	DescriptionActions	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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS11787.1
PIRⁱ	A31913 ISHUSS
NCBI Reference Sequences More...RefSeqⁱ	NP_000909.2, NM_000918.3
UniGeneⁱ	Hs.464336

Genome annotation databases

Ensemblⁱ	ENST00000331483; ENSP00000327801; ENSG00000185624
GeneIDⁱ	5034
KEGGⁱ	hsa:5034
UCSC genome browser More...UCSCⁱ	uc002kbn.2 human

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P07237	Protein disulfide-isomerase		HUMAN		508	UniRef100_P07237
Procollagen-proline, 2-oxoglutarate 4-dioxygenase (Proline 4-hydroxylase), beta polypeptide, isoform CRA_b		HUMAN		185

Protein	Similar proteins		Species	Score	Length	Source
P07237	Protein disulfide-isomerase		MACFU		510	UniRef90_P07237
Protein disulfide-isomerase		PONAB		508
Protein disulfide-isomerase		HUMAN		508
Protein disulfide-isomerase		CALJA		510
Protein disulfide-isomerase		MACNE		510
+22

Protein	Similar proteins		Species	Score	Length	Source
P07237	Protein disulfide-isomerase		MACFU		510	UniRef50_P07237
Protein disulfide-isomerase		PONAB		508
Protein disulfide-isomerase		CHICK		515
Protein disulfide-isomerase		BOVIN		510
Protein disulfide-isomerase		CRIGR		509
+365

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
UniGeneⁱ	Hs.464336

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	[»]
ProteinModelPortalⁱ	P07237
SMRⁱ	P07237
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	111073, 145 interactors
CORUMⁱ	P07237
DIPⁱ	DIP-32979N
IntActⁱ	P07237, 93 interactors
MINTⁱ	P07237
STRINGⁱ	9606.ENSP00000327801

Chemistry databases

BindingDBⁱ	P07237
ChEMBLⁱ	CHEMBL5422
DrugBankⁱ	DB03615 Ribostamycin

PTM databases

iPTMnetⁱ	P07237
PhosphoSitePlusⁱ	P07237
SwissPalmⁱ	P07237

Polymorphism and mutation 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
MaxQBⁱ	P07237
PaxDbⁱ	P07237
PeptideAtlasⁱ	P07237
PRIDEⁱ	P07237
ProteomicsDBⁱ	51976
TopDownProteomicsⁱ	P07237

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	5034
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000331483; ENSP00000327801; ENSG00000185624
GeneIDⁱ	5034
KEGGⁱ	hsa:5034
UCSCⁱ	uc002kbn.2 human

Organism-specific databases

CTDⁱ	5034
DisGeNETⁱ	5034
EuPathDBⁱ	HostDB:ENSG00000185624.14
GeneCardsⁱ	P4HB
HGNCⁱ	HGNC:8548 P4HB
HPAⁱ	CAB012463 HPA018884
MalaCardsⁱ	P4HB
MIMⁱ	112240 phenotype 176790 gene
neXtProtⁱ	NX_P07237
OpenTargetsⁱ	ENSG00000185624
PharmGKBⁱ	PA32876
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0190 Eukaryota COG0526 LUCA
GeneTreeⁱ	ENSGT00860000133691
HOGENOMⁱ	HOG000162459
HOVERGENⁱ	HBG005920
InParanoidⁱ	P07237
KOⁱ	K09580
OMAⁱ	QYGVRGY
OrthoDBⁱ	EOG091G08WM
PhylomeDBⁱ	P07237
TreeFamⁱ	TF106381

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS06845-MONOMER
BRENDAⁱ	5.3.4.1 2681
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-9020591 Interleukin-12 signaling R-HSA-9020933 Interleukin-23 signaling

Miscellaneous databases

ChiTaRSⁱ	P4HB human
EvolutionaryTraceⁱ	P07237
GeneWikiⁱ	P4HB
GenomeRNAiⁱ	5034
PMAP-CutDBⁱ	P07237
Protein Ontology More...PROⁱ	PR:P07237
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000185624 Expressed in 235 organ(s), highest expression level in right lobe of liver
CleanExⁱ	HS_P4HB
ExpressionAtlasⁱ	P07237 baseline and differential
Genevisibleⁱ	P07237 HS

Family and domain databases

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
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PDIA1_HUMAN
Accessionⁱ	P07237Primary (citable) accession number: P07237 Secondary accession number(s): B2RDQ2 , P30037, P32079, Q15205, Q6LDE5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
	Last sequence update:	November 1, 1997
	Last modified:	October 10, 2018
	This is version 238 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human chromosome 17
Human chromosome 17: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations

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UniProtKB - P07237 (PDIA1_HUMAN)

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Protein disulfide-isomerase

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ