KPCL_HUMAN - dbPTM
KPCL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KPCL_HUMAN
UniProt AC P24723
Protein Name Protein kinase C eta type
Gene Name PRKCH
Organism Homo sapiens (Human).
Sequence Length 683
Subcellular Localization Cytoplasm.
Protein Description Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in the regulation of cell differentiation in keratinocytes and pre-B cell receptor, mediates regulation of epithelial tight junction integrity and foam cell formation, and is required for glioblastoma proliferation and apoptosis prevention in MCF-7 cells. In keratinocytes, binds and activates the tyrosine kinase FYN, which in turn blocks epidermal growth factor receptor (EGFR) signaling and leads to keratinocyte growth arrest and differentiation. Associates with the cyclin CCNE1-CDK2-CDKN1B complex and inhibits CDK2 kinase activity, leading to RB1 dephosphorylation and thereby G1 arrest in keratinocytes. In association with RALA activates actin depolymerization, which is necessary for keratinocyte differentiation. In the pre-B cell receptor signaling, functions downstream of BLNK by up-regulating IRF4, which in turn activates L chain gene rearrangement. Regulates epithelial tight junctions (TJs) by phosphorylating occludin (OCLN) on threonine residues, which is necessary for the assembly and maintenance of TJs. In association with PLD2 and via TLR4 signaling, is involved in lipopolysaccharide (LPS)-induced RGS2 down-regulation and foam cell formation. Upon PMA stimulation, mediates glioblastoma cell proliferation by activating the mTOR pathway, the PI3K/AKT pathway and the ERK1-dependent phosphorylation of ELK1. Involved in the protection of glioblastoma cells from irradiation-induced apoptosis by preventing caspase-9 activation. In camptothecin-treated MCF-7 cells, regulates NF-kappa-B upstream signaling by activating IKBKB, and confers protection against DNA damage-induced apoptosis. Promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria. Phosphorylates ATF2 which promotes its nuclear retention and transcriptional activity and negatively regulates its mitochondrial localization..
Protein Sequence MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTTGASDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNGIGVNSSNRLGIDNFEFIRVLGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP
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
2Phosphorylation------MSSGTMKFN
------CCCCCCEEC		37.1624719451
11PhosphorylationGTMKFNGYLRVRIGE
CCCEECCEEEEEECC		7.7624719451
25PhosphorylationEAVGLQPTRWSLRHS
CCCCCCCCCHHHHHH		31.6330108239
28PhosphorylationGLQPTRWSLRHSLFK
CCCCCCHHHHHHHHH		16.5423898821
32PhosphorylationTRWSLRHSLFKKGHQ
CCHHHHHHHHHHCCC		29.1216973127
35UbiquitinationSLRHSLFKKGHQLLD
HHHHHHHHHCCCCCC		64.2422817900
36UbiquitinationLRHSLFKKGHQLLDP
HHHHHHHHCCCCCCC		55.0522817900
57PhosphorylationDQVRVGQTSTKQKTN
CEEEECCCCCCCCCC		32.2219369195
73UbiquitinationPTYNEEFCANVTDGG
CCCCHHHCCCCCCCC		2.81-
94PhosphorylationFHETPLGYDHFVANC
EECCCCCCCEEHHHC		17.58-
152UbiquitinationLQRDRIFKHFTRKRQ
HHHHHHHHHHHHHHH		35.12-
155PhosphorylationDRIFKHFTRKRQRAM
HHHHHHHHHHHHHHH		34.6921949786
160UbiquitinationHFTRKRQRAMRRRVH
HHHHHHHHHHHHHHH		34.09-
160UbiquitinationHFTRKRQRAMRRRVH
HHHHHHHHHHHHHHH		34.0922505724
176UbiquitinationINGHKFMATYLRQPT
HCCCHHHHHHHCCCC		9.02-
177PhosphorylationNGHKFMATYLRQPTY
CCCHHHHHHHCCCCC		15.9928857561
183PhosphorylationATYLRQPTYCSHCRE
HHHHCCCCCCHHHHH		28.9027251275
202UbiquitinationVFGKQGYQCQVCTCV
HHCCCCCEEEEEEEE		20.28-
214UbiquitinationTCVVHKRCHHLIVTA
EEEEECCCCEEEEEH		2.57-
233PhosphorylationNNINKVDSKIAEQRF
CCHHHHCHHHHHHHH		29.0228857561
234UbiquitinationNINKVDSKIAEQRFG
CHHHHCHHHHHHHHC		41.2829967540
241UbiquitinationKIAEQRFGINIPHKF
HHHHHHHCCCCCCCC		17.7722505724
242UbiquitinationIAEQRFGINIPHKFS
HHHHHHCCCCCCCCE		3.7722505724
243UbiquitinationAEQRFGINIPHKFSI
HHHHHCCCCCCCCEE		41.96-
249PhosphorylationINIPHKFSIHNYKVP
CCCCCCCEECCCCCC		27.9527251275
264PhosphorylationTFCDHCGSLLWGIMR
CCCHHHHHHHHHHHH		26.1930631047
305PhosphorylationNAVELAKTLAGMGLQ
CHHHHHHHHHCCCCC		19.0823403867
317PhosphorylationGLQPGNISPTSKLVS
CCCCCCCCCHHHHHC		26.5623401153
319PhosphorylationQPGNISPTSKLVSRS
CCCCCCCHHHHHCHH		31.5330278072
320PhosphorylationPGNISPTSKLVSRST
CCCCCCHHHHHCHHH		27.6330631047
320UbiquitinationPGNISPTSKLVSRST
CCCCCCHHHHHCHHH		27.63-
321UbiquitinationGNISPTSKLVSRSTL
CCCCCHHHHHCHHHH		56.2222505724
324PhosphorylationSPTSKLVSRSTLRRQ
CCHHHHHCHHHHHHC		30.8323401153
326PhosphorylationTSKLVSRSTLRRQGK
HHHHHCHHHHHHCCC		25.0423401153
327PhosphorylationSKLVSRSTLRRQGKE
HHHHCHHHHHHCCCC		24.1523401153
337UbiquitinationRQGKESSKEGNGIGV
HCCCCCCCCCCCCCC		78.06-
363UbiquitinationEFIRVLGKGSFGKVM
EEEEEECCCCCCEEE		47.42-
365PhosphorylationIRVLGKGSFGKVMLA
EEEECCCCCCEEEEE		34.0227067055
375UbiquitinationKVMLARVKETGDLYA
EEEEEEEECCCCEEE		43.9629967540
381PhosphorylationVKETGDLYAVKVLKK
EECCCCEEEEEEECC		17.6825839225
384UbiquitinationTGDLYAVKVLKKDVI
CCCEEEEEEECCCEE		33.4129967540
388UbiquitinationYAVKVLKKDVILQDD
EEEEEECCCEECCCC		53.7329967540
404UbiquitinationVECTMTEKRILSLAR
EEEEECHHHHHHHHH		35.26-
430UbiquitinationFQTPDRLFFVMEFVN
CCCCCEEEEEEEEEC		4.52-
454UbiquitinationKSRRFDEARARFYAA
HHCCHHHHHHHHHHH		16.5722505724
454UbiquitinationKSRRFDEARARFYAA
HHCCHHHHHHHHHHH		16.57-
481UbiquitinationGIIYRDLKLDNVLLD
CCCCCCCCCCCEEEC		59.0729967540
494UbiquitinationLDHEGHCKLADFGMC
ECCCCCEEECCCCCC		40.8229967540
513PhosphorylationCNGVTTATFCGTPDY
CCCCCHHCCCCCCCC		19.8422817900
517PhosphorylationTTATFCGTPDYIAPE
CHHCCCCCCCCCCHH		17.73-
520PhosphorylationTFCGTPDYIAPEILQ
CCCCCCCCCCHHHHH		10.5322817900
535UbiquitinationEMLYGPAVDWWAMGV
HHHHCHHHHHHHHHH		7.7222505724
536UbiquitinationMLYGPAVDWWAMGVL
HHHCHHHHHHHHHHH		36.9922505724
591UbiquitinationILKSFMTKNPTMRLG
HHHHHHCCCCCCCCC		49.49-
599PhosphorylationNPTMRLGSLTQGGEH
CCCCCCCCCCCCCCE		32.60-
601PhosphorylationTMRLGSLTQGGEHAI
CCCCCCCCCCCCEEE		27.19-
615UbiquitinationILRHPFFKEIDWAQL
ECCCCCHHCCCHHHC		54.8922505724
637PhosphorylationPFRPRIKSREDVSNF
CCCCCCCCHHHHHCC		38.2325849741
642PhosphorylationIKSREDVSNFDPDFI
CCCHHHHHCCCHHHH		44.0628348404
656PhosphorylationIKEEPVLTPIDEGHL
HCCCCCCCCCCCCCC		20.5930266825
675PhosphorylationQDEFRNFSYVSPELQ
HHHCCCCCCCCCCCC		28.3330266825
676PhosphorylationDEFRNFSYVSPELQP
HHCCCCCCCCCCCCC		10.7828102081
678PhosphorylationFRNFSYVSPELQP--
CCCCCCCCCCCCC--		12.3930266825
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
28SPhosphorylationKinasePRKCHP24723
GPS
32SPhosphorylationKinasePRKCHP24723
GPS
513TPhosphorylationKinasePDPK1O15530
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KPCL_HUMAN !!
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 KPCL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARCH_HUMANZBTB8OSphysical
20936779
NF2L2_HUMANNFE2L2physical
19920073
KPCL_HUMANPRKCHphysical
19920073
VHL_HUMANVHLphysical
10491320
GSK3A_HUMANGSK3Aphysical
11884598
BANP_HUMANBANPphysical
25416956
AKP13_HUMANAKAP13physical
15383279
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
601367Ischemic stroke (ISCHSTR)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KPCL_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; SER-317 AND SER-675,AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317 AND SER-320, ANDMASS SPECTROMETRY.

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