Search Results
Overview
| Uniprot ID | P13667 |
|---|---|
| Protein Name | Protein disulfide-isomerase A4 |
| Gene Name | PDIA4 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 111 | IANILKDKDPPIPVA |
| 119 | DPPIPVAKIDATSAS |
| 141 | VSGYPTIKILKKGQA |
| 145 | PTIKILKKGQAVDYE |
| 163 | TQEEIVAKVREVSQP |
| 211 | PWCGHCKKLAPEYEK |
| 221 | PEYEKAAKELSKRSP |
| 234 | SPPIPLAKVDATAET |
| 245 | TAETDLAKRFDVSGY |
| 272 | DYNGPREKYGIVDYM |
| 294 | SKEILTLKQVQEFLK |
| 335 | NNLREDYKFHHTFST |
| 346 | TFSTEIAKFLKVSQG |
| 349 | TEIAKFLKVSQGQLV |
| 362 | LVVMQPEKFQSKYEP |
| 366 | QPEKFQSKYEPRSHM |
| 386 | STQDSAIKDFVLKYA |
| 401 | LPLVGHRKVSNDAKR |
| 437 | ATQFWRSKVLEVAKD |
| 485 | ILDESGKKFAMEPEE |
| 506 | REFVTAFKKGKLKPV |
| 509 | VTAFKKGKLKPVIKS |
| 515 | GKLKPVIKSQPVPKN |
| 521 | IKSQPVPKNNKGPVK |
| 524 | QPVPKNNKGPVKVVV |
| 528 | KNNKGPVKVVVGKTF |
| 533 | PVKVVVGKTFDSIVM |
| 543 | DSIVMDPKKDVLIEF |
| 544 | SIVMDPKKDVLIEFY |
| 570 | PVYNSLAKKYKGQKG |
| 576 | AKKYKGQKGLVIAKM |
| 582 | QKGLVIAKMDATAND |
| 611 | YFAPSGDKKNPVKFE |
| 616 | GDKKNPVKFEGGDRD |
| 629 | RDLEHLSKFIEEHAT |
| 637 | FIEEHATKLSRTKEE |
Function
No function data available.
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0009986 | cell surface |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005788 | endoplasmic reticulum lumen |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0042470 | melanosome |
| Molecular Function | GO:0003756 | protein disulfide isomerase activity |
| Molecular Function | GO:0015035 | protein-disulfide reductase activity |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0006457 | protein folding |
| Biological Process | GO:0009306 | protein secretion |
| Biological Process | GO:0034976 | response to endoplasmic reticulum stress |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.