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PDIA1 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. 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. Binds UBQLN1. Binds to CD4, and upon HIV-1 binding to the cell membrane, is part of a P4HB/PDI-CD4-CXCR4-gp120 complex. Belongs to the protein disulfide isomerase family. Note: This description may include information from UniProtKB.
Protein type: EC; Endoplasmic reticulum; Isomerase; Nuclear receptor co-regulator; Oxidoreductase
Chromosomal Location of Human Ortholog: 17q25.3
Cellular Component: endoplasmic reticulum; endoplasmic reticulum lumen; ER-Golgi intermediate compartment; external side of plasma membrane; extracellular matrix; focal adhesion
Molecular Function: integrin binding; peptide disulfide oxidoreductase activity; procollagen-proline 4-dioxygenase activity; protein binding; protein disulfide isomerase activity; protein heterodimerization activity; RNA binding
Biological Process: cellular protein metabolic process; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; positive regulation of virion penetration into host cell; post-translational protein modification; protein folding
Disease: Cole-carpenter Syndrome 1
Reference #:  P07237 (UniProtKB)
Alt. Names/Synonyms: Cellular thyroid hormone-binding protein; collagen prolyl 4-hydroxylase beta; DSI; ERBA2L; GIT; glutathione-insulin transhydrogenase; P4HB; P4Hbeta; p55; PDI; PDIA1; PHDB; PO4DB; PO4HB; procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide; PROHB; Prolyl 4-hydroxylase subunit beta; prolyl 4-hydroxylase, beta polypeptide; protein disulfide isomerase family A, member 1; protein disulfide isomerase-associated 1; protein disulfide isomerase/oxidoreductase; Protein disulfide-isomerase; protocollagen hydroxylase; thyroid hormone-binding protein p55; v-erb-a avian erythroblastic leukemia viral oncogene homolog 2-like
Gene Symbols: P4HB
Molecular weight: 57,116 Da
Basal Isoelectric point: 4.76  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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