KPCE_HUMAN - dbPTM
KPCE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
21PhosphorylationEAVSLKPTAWSLRHA
EECCCCCCHHHHHHC
38.8927251275
24PhosphorylationSLKPTAWSLRHAVGP
CCCCCHHHHHHCCCC
17.0424719451
62PhosphorylationATKQKTNSPAWHDEF
CCCCCCCCCCCCHHH
22.64-
175PhosphorylationNGHKFMATYLRQPTY
CCCCCHHHHHCCCCC
15.9928857561
181PhosphorylationATYLRQPTYCSHCRD
HHHHCCCCCCHHHHH
28.9027251275
228PhosphorylationAGLKKQETPDQVGSQ
CCCCCCCCCCCCCCC
29.6717192257
234PhosphorylationETPDQVGSQRFSVNM
CCCCCCCCCCCEECC
21.2322817900
261PhosphorylationTFCDHCGSLLWGLLR
CCCHHHHHHHHHHHH
26.19-
286PhosphorylationNVHRRCETNVAPNCG
EEHHCCCCCCCCCCC
38.32-
309PhosphorylationVLADLGVTPDKITNS
HHHHHCCCHHHHCCC
24.7929255136
314PhosphorylationGVTPDKITNSGQRRK
CCCHHHHCCCHHHHH
29.1318691976
316PhosphorylationTPDKITNSGQRRKKL
CHHHHCCCHHHHHEE
27.8726055452
321UbiquitinationTNSGQRRKKLIAGAE
CCCHHHHHEEEECCC
54.87-
329PhosphorylationKLIAGAESPQPASGS
EEEECCCCCCCCCCC
28.4429255136
334PhosphorylationAESPQPASGSSPSEE
CCCCCCCCCCCCCHH
45.9829255136
336PhosphorylationSPQPASGSSPSEEDR
CCCCCCCCCCCHHHH
36.2625159151
337PhosphorylationPQPASGSSPSEEDRS
CCCCCCCCCCHHHHH
35.6525159151
339PhosphorylationPASGSSPSEEDRSKS
CCCCCCCCHHHHHCC
56.4125159151
344PhosphorylationSPSEEDRSKSAPTSP
CCCHHHHHCCCCCCH
43.1926657352
346PhosphorylationSEEDRSKSAPTSPCD
CHHHHHCCCCCCHHH
40.5029255136
349PhosphorylationDRSKSAPTSPCDQEI
HHHCCCCCCHHHHHH
45.0426657352
350PhosphorylationRSKSAPTSPCDQEIK
HHCCCCCCHHHHHHH
23.5925159151
368PhosphorylationNNIRKALSFDNRGEE
HHHHHHHCCCCCCCC
35.1030266825
380PhosphorylationGEEHRAASSPDGQLM
CCCCCCCCCCCCCCC
41.2318691976
381PhosphorylationEEHRAASSPDGQLMS
CCCCCCCCCCCCCCC
23.4525159151
388PhosphorylationSPDGQLMSPGENGEV
CCCCCCCCCCCCCCC
38.0417192257
416UbiquitinationNFIKVLGKGSFGKVM
CEEEEECCCCCCCHH
47.42-
418PhosphorylationIKVLGKGSFGKVMLA
EEEECCCCCCCHHHH
34.0228348404
421AcetylationLGKGSFGKVMLAELK
ECCCCCCCHHHHHHC
23.5919820911
430AcetylationMLAELKGKDEVYAVK
HHHHHCCCCCEEEEE
49.4819820921
434PhosphorylationLKGKDEVYAVKVLKK
HCCCCCEEEEEEEEC
12.02-
566PhosphorylationLNGVTTTTFCGTPDY
CCCCCCCCCCCCCCC
18.1622817900
573PhosphorylationTFCGTPDYIAPEILQ
CCCCCCCCCCHHHHH
10.5317561374
636PhosphorylationWLSKEAVSILKAFMT
HCCHHHHHHHHHHHC
29.2924719451
679UbiquitinationDWVLLEQKKIKPPFK
CEEEECCCCCCCCCC
47.28-
703PhosphorylationNNFDQDFTREEPVLT
CCCCCCCCCCCCHHH
45.5223403867
710PhosphorylationTREEPVLTLVDEAIV
CCCCCHHHHHHHHHH
25.6019664994
729PhosphorylationQEEFKGFSYFGEDLM
HHHHCCCCCCCCCCC
28.3715949469
730PhosphorylationEEFKGFSYFGEDLMP
HHHCCCCCCCCCCCC
17.2223403867

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
234SPhosphorylationKinasePRKCAP17252
GPS
234SPhosphorylationKinasePRKCEQ02156
GPS
316SPhosphorylationKinasePRKCAP17252
GPS
316SPhosphorylationKinasePRKCEQ02156
GPS
346SPhosphorylationKinaseGSK3BP49841
PSP
350SPhosphorylationKinaseP38BQ15759
PSP
350SPhosphorylationKinaseP38AQ16539
PSP
368SPhosphorylationKinasePRKCAP17252
GPS
368SPhosphorylationKinasePRKCEQ02156
GPS
566TPhosphorylationKinaseMTORP42345
PSP
566TPhosphorylationKinasePDK1Q15118
GPS
566TPhosphorylationKinasePDK1O15530
PSP
710TPhosphorylationKinaseMTORP42345
PSP
729SPhosphorylationKinasePRKCEQ02156
GPS
729SPhosphorylationKinaseMTORP42345
PSP
-KUbiquitinationE3 ubiquitin ligaseTRIM41Q8WV44
PMID:17893151

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
346SPhosphorylation

19662078
350SPhosphorylation

11964154
368SPhosphorylation

23186163
566TPhosphorylation

11964154
729SPhosphorylation

11964154

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRP3_HUMANRASGRP3physical
15213298
DCE2_HUMANGAD2physical
15147202
DCE1_HUMANGAD1physical
15147202
ADAP1_HUMANADAP1physical
12893243
VDAC1_HUMANVDAC1physical
12663490
ADT1_HUMANSLC25A4physical
12663490
HXK2_HUMANHK2physical
12663490
CFTR_HUMANCFTRphysical
11956211
RACK1_HUMANGNB2L1physical
11956211
GNA12_HUMANGNA12physical
8824244
GNA13_HUMANGNA13physical
8824244
MYH9_HUMANMYH9physical
11897493
COPB2_HUMANCOPB2physical
11897493
K2C1_HUMANKRT1physical
11897493
ACTS_HUMANACTA1physical
11897493
1433Z_HUMANYWHAZphysical
11950841
TIAM1_HUMANTIAM1physical
10212259
PK3CB_HUMANPIK3CBphysical
9822674
DESP_HUMANDSPphysical
20936779
STAT1_HUMANSTAT1physical
20353823
HS90B_HUMANHSP90AB1physical
20353823
KPCE_HUMANPRKCEphysical
19920073
KAT5_HUMANKAT5physical
17851107
H11_HUMANHIST1H1Aphysical
16314418
IBTK_HUMANIBTKphysical
21482705
MARK2_HUMANMARK2physical
19011111
PP14A_HUMANPPP1R14Aphysical
15003508
IKKB_HUMANIKBKBphysical
23123196
MARCS_MOUSEMarcksphysical
7588787
ITB2_HUMANITGB2physical
11700305
ATF2_HUMANATF2physical
22304920
KS6B2_HUMANRPS6KB2physical
16810323
BRAF_HUMANBRAFphysical
16810323
ELAV1_HUMANELAVL1physical
17392515
NUMB_HUMANNUMBphysical
17203073
KEAP1_HUMANKEAP1physical
24127568
ZBT16_HUMANZBTB16physical
25178676
NANOG_HUMANNANOGphysical
23708658
BAD_HUMANBADphysical
20179209
BCL6_HUMANBCL6physical
25245533
IL32_HUMANIL32physical
25245533
HS90A_HUMANHSP90AA1physical
20558438
TOM20_HUMANTOMM20physical
20558438

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D09671 Sotrastaurin (USAN/INN)
D09718 Sotrastaurin acetate (USAN)
DrugBank
DB00675Tamoxifen
Regulatory Network of KPCE_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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