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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Protein disulfide-isomerase

UniprotKB/SwissProt ID: PDIA1_HUMAN (P07237)

Gene Name: P4HB

Synonyms: ERBA2L, PDI, PDIA1, PO4DB

Organism: Homo sapiens (Human).

Function: 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.

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Endoplasmic reticulum lumen. Melanosome. Cell membrane; Peripheral membrane protein (Potential). Note=Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacem

PDB :
( If your security settings prevent Jmol from running, please register http://140.138.144.145/ as a safe location in your Java settings. )

Protein disease:
Disease database Database Entry Disease information
OMIM176790PROCOLLAGEN-PROLINE, 2-OXOGLUTARATE-4-DIOXYGENASE, BETA SUBUNIT; P4HB ;;PROLYL 4-HYDROXYLASE
Network with metabolic pathway:
Kegg map ID Pathway Link
map04141Protein processing in endoplasmic reticulum
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR000886
IPR005788
IPR005792
IPR006662
IPR012335
IPR012336
IPR013766

3D Structure Databases:
3D structure databases
EntryMethodResolution (A)ChainPositionsView
1BJX NMR - A136-245Link
1MEK NMR - A18-137Link
1X5C NMR - A368-475Link
2BJX NMR - A136-245Link
2K18 NMR - A135-357Link
3BJ5 X-ray 2.20 A A230-368Link
3UEM X-ray 2.29 A A137-479Link
4EKZ X-ray 2.51 A A18-479Link
4EL1 X-ray 2.88 A A/B18-479Link
4JU5 X-ray 2.28 A A/B135-367Link

The S-nitrosylation sites of PDIA1_HUMAN

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
153YLLVEFYAPW C GHCKALAPEY CEEEEEECCC C HHHHHHHHHH 2.31%HC0522178444-
253YLLVEFYAPW C GHCKALAPEY CEEEEEECCC C HHHHHHHHHH 2.31%HC0516724068-
356VEFYAPWCGH C KALAPEYAKA EEEECCCCHH H HHHHHHHHHH 1.35%HC0222178444-
456VEFYAPWCGH C KALAPEYAKA EEEECCCCHH H HHHHHHHHHH 1.35%HC0216724068-
5312LEFFGLKKEE C PAVRLITLEE HHHCCCCCCC C CEEEEEEECC 2.48%HC0422178444-
6312LEFFGLKKEE C PAVRLITLEE HHHCCCCCCC C CEEEEEEECC 2.48%HC0420140087in vivo
7397NVFVEFYAPW C GHCKQLAPIW CEEEEEECCC C HHHHHHHHHH 2.31%HC0522178444-
8397NVFVEFYAPW C GHCKQLAPIW CEEEEEECCC C HHHHHHHHHH 2.31%HC0516724068-
9400VEFYAPWCGH C KQLAPIWDKL EEEECCCCHH H HHHHHHHHHH 1.50%HC0222178444-
10400VEFYAPWCGH C KQLAPIWDKL EEEECCCCHH H HHHHHHHHHH 1.50%HC0216724068-