UniProt ID | KPCE_HUMAN | |
---|---|---|
UniProt AC | Q02156 | |
Protein Name | Protein kinase C epsilon type | |
Gene Name | PRKCE | |
Organism | Homo sapiens (Human). | |
Sequence Length | 737 | |
Subcellular Localization | Cytoplasm . Cytoplasm, cytoskeleton . Cell membrane . Cytoplasm, perinuclear region. Nucleus. Translocated to plasma membrane in epithelial cells stimulated by HGF. Associated with the Golgi at the perinuclear site in pre-passage fibroblasts (By simi | |
Protein Description | Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin-dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell-cell detachment prior to migration. In HeLa cells, contributes to hepatocyte growth factor (HGF)-induced cell migration, and in human corneal epithelial cells, plays a critical role in wound healing after activation by HGF. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin-induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma-aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2). In prostate cancer cells, interacts with and phosphorylates STAT3, which increases DNA-binding and transcriptional activity of STAT3 and seems to be essential for prostate cancer cell invasion. Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1.. | |
Protein Sequence | MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQINQEEFKGFSYFGEDLMP | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
21 | Phosphorylation | EAVSLKPTAWSLRHA EECCCCCCHHHHHHC | 38.89 | 27251275 | |
24 | Phosphorylation | SLKPTAWSLRHAVGP CCCCCHHHHHHCCCC | 17.04 | 24719451 | |
62 | Phosphorylation | ATKQKTNSPAWHDEF CCCCCCCCCCCCHHH | 22.64 | - | |
175 | Phosphorylation | NGHKFMATYLRQPTY CCCCCHHHHHCCCCC | 15.99 | 28857561 | |
181 | Phosphorylation | ATYLRQPTYCSHCRD HHHHCCCCCCHHHHH | 28.90 | 27251275 | |
228 | Phosphorylation | AGLKKQETPDQVGSQ CCCCCCCCCCCCCCC | 29.67 | 17192257 | |
234 | Phosphorylation | ETPDQVGSQRFSVNM CCCCCCCCCCCEECC | 21.23 | 22817900 | |
261 | Phosphorylation | TFCDHCGSLLWGLLR CCCHHHHHHHHHHHH | 26.19 | - | |
286 | Phosphorylation | NVHRRCETNVAPNCG EEHHCCCCCCCCCCC | 38.32 | - | |
309 | Phosphorylation | VLADLGVTPDKITNS HHHHHCCCHHHHCCC | 24.79 | 29255136 | |
314 | Phosphorylation | GVTPDKITNSGQRRK CCCHHHHCCCHHHHH | 29.13 | 18691976 | |
316 | Phosphorylation | TPDKITNSGQRRKKL CHHHHCCCHHHHHEE | 27.87 | 26055452 | |
321 | Ubiquitination | TNSGQRRKKLIAGAE CCCHHHHHEEEECCC | 54.87 | - | |
329 | Phosphorylation | KLIAGAESPQPASGS EEEECCCCCCCCCCC | 28.44 | 29255136 | |
334 | Phosphorylation | AESPQPASGSSPSEE CCCCCCCCCCCCCHH | 45.98 | 29255136 | |
336 | Phosphorylation | SPQPASGSSPSEEDR CCCCCCCCCCCHHHH | 36.26 | 25159151 | |
337 | Phosphorylation | PQPASGSSPSEEDRS CCCCCCCCCCHHHHH | 35.65 | 25159151 | |
339 | Phosphorylation | PASGSSPSEEDRSKS CCCCCCCCHHHHHCC | 56.41 | 25159151 | |
344 | Phosphorylation | SPSEEDRSKSAPTSP CCCHHHHHCCCCCCH | 43.19 | 26657352 | |
346 | Phosphorylation | SEEDRSKSAPTSPCD CHHHHHCCCCCCHHH | 40.50 | 29255136 | |
349 | Phosphorylation | DRSKSAPTSPCDQEI HHHCCCCCCHHHHHH | 45.04 | 26657352 | |
350 | Phosphorylation | RSKSAPTSPCDQEIK HHCCCCCCHHHHHHH | 23.59 | 25159151 | |
368 | Phosphorylation | NNIRKALSFDNRGEE HHHHHHHCCCCCCCC | 35.10 | 30266825 | |
380 | Phosphorylation | GEEHRAASSPDGQLM CCCCCCCCCCCCCCC | 41.23 | 18691976 | |
381 | Phosphorylation | EEHRAASSPDGQLMS CCCCCCCCCCCCCCC | 23.45 | 25159151 | |
388 | Phosphorylation | SPDGQLMSPGENGEV CCCCCCCCCCCCCCC | 38.04 | 17192257 | |
416 | Ubiquitination | NFIKVLGKGSFGKVM CEEEEECCCCCCCHH | 47.42 | - | |
418 | Phosphorylation | IKVLGKGSFGKVMLA EEEECCCCCCCHHHH | 34.02 | 28348404 | |
421 | Acetylation | LGKGSFGKVMLAELK ECCCCCCCHHHHHHC | 23.59 | 19820911 | |
430 | Acetylation | MLAELKGKDEVYAVK HHHHHCCCCCEEEEE | 49.48 | 19820921 | |
434 | Phosphorylation | LKGKDEVYAVKVLKK HCCCCCEEEEEEEEC | 12.02 | - | |
566 | Phosphorylation | LNGVTTTTFCGTPDY CCCCCCCCCCCCCCC | 18.16 | 22817900 | |
573 | Phosphorylation | TFCGTPDYIAPEILQ CCCCCCCCCCHHHHH | 10.53 | 17561374 | |
636 | Phosphorylation | WLSKEAVSILKAFMT HCCHHHHHHHHHHHC | 29.29 | 24719451 | |
679 | Ubiquitination | DWVLLEQKKIKPPFK CEEEECCCCCCCCCC | 47.28 | - | |
703 | Phosphorylation | NNFDQDFTREEPVLT CCCCCCCCCCCCHHH | 45.52 | 23403867 | |
710 | Phosphorylation | TREEPVLTLVDEAIV CCCCCHHHHHHHHHH | 25.60 | 19664994 | |
729 | Phosphorylation | QEEFKGFSYFGEDLM HHHHCCCCCCCCCCC | 28.37 | 15949469 | |
730 | Phosphorylation | EEFKGFSYFGEDLMP HHHCCCCCCCCCCCC | 17.22 | 23403867 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
234 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
234 | S | Phosphorylation | Kinase | PRKCE | Q02156 | GPS |
316 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
316 | S | Phosphorylation | Kinase | PRKCE | Q02156 | GPS |
346 | S | Phosphorylation | Kinase | GSK3B | P49841 | PSP |
350 | S | Phosphorylation | Kinase | P38B | Q15759 | PSP |
350 | S | Phosphorylation | Kinase | P38A | Q16539 | PSP |
368 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
368 | S | Phosphorylation | Kinase | PRKCE | Q02156 | GPS |
566 | T | Phosphorylation | Kinase | MTOR | P42345 | PSP |
566 | T | Phosphorylation | Kinase | PDK1 | Q15118 | GPS |
566 | T | Phosphorylation | Kinase | PDK1 | O15530 | PSP |
710 | T | Phosphorylation | Kinase | MTOR | P42345 | PSP |
729 | S | Phosphorylation | Kinase | PRKCE | Q02156 | GPS |
729 | S | Phosphorylation | Kinase | MTOR | P42345 | PSP |
- | K | Ubiquitination | E3 ubiquitin ligase | TRIM41 | Q8WV44 | PMID:17893151 |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of KPCE_HUMAN !! |
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Phosphorylation | |
Reference | PubMed |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-309 AND SER-316, ANDMASS SPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-228; THR-309; SER-316;SER-329; SER-339; SER-346; SER-350; SER-368; THR-710 AND SER-729, ANDMASS SPECTROMETRY. | |
"Regulation of novel protein kinase C epsilon by phosphorylation."; Cenni V., Doeppler H., Sonnenburg E.D., Maraldi N., Newton A.C.,Toker A.; Biochem. J. 363:537-545(2002). Cited for: PHOSPHORYLATION AT THR-566 AND SER-729, AND MUTAGENESIS OF LYS-437;THR-566; THR-710 AND SER-729. |