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- Table of Contents
Facts about Protein disulfide-isomerase.
May therefore cause structural modifications of exofacial proteins. Within the cell, seems to form/rearrange disulfide bonds of nascent proteins.
Human | |
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Gene Name: | P4HB |
Uniprot: | P07237 |
Entrez: | 5034 |
Belongs to: |
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protein disulfide isomerase family |
Cellular thyroid hormone-binding protein; collagen prolyl 4-hydroxylase beta; DSI; ERBA2L; GIT; glutathione-insulin transhydrogenase; P4HB; P4Hbeta; p55; PDI; PDIA1; PDIA1procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), betapolypeptide (protein disulfide isomerase-associated 1); PDIEC 5.3.4.1; PHDB; PO4DB; PO4HB; procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), betapolypeptide; PROHB; PROHBprocollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), betapolypeptide (protein disulfide isomerase; thyroid hormone binding protein p5
Mass (kDA):
57.116 kDA
Human | |
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Location: | 17q25.3 |
Sequence: | 17; NC_000017.11 (81843159..81860535, complement) |
Endoplasmic reticulum. Endoplasmic reticulum lumen. Melanosome. Cell membrane; Peripheral membrane protein. 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).
PMID: 3034602 by Pihlajaniemi T., et al. Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene.
PMID: 3611107 by Cheng S.-Y., et al. The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum.
*More publications can be found for each product on its corresponding product page