KPCL_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KPCL_RAT
• UniProt AC: Q64617
• Protein Name: Protein kinase C eta type
• Gene Name: Prkch
• Organism: Rattus norvegicus (Rat).
• 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 (By similarity)..
• Protein Sequence: MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCTNVSDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTAGTSDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQVNGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDAKIAEQRFGINIPHKFNVHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLISRSTLRRQGKEGSKEGNGIGVNSSSRFGIDNFEFIRVLGKGSFGKVMLARIKETGELYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHEKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHEILRHPFFKEIDWVQLNHRQLEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP

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
28	Phosphorylation	GLQPTRWSLRHSLFK CCCCCCHHHHHHHHH	16.54	-
32	Phosphorylation	TRWSLRHSLFKKGHQ CCHHHHHHHHHHCCC	29.12	-
177	Phosphorylation	NGHKFMATYLRQPTY CCCHHHHHHHCCCCC	15.99	18295358
178	Phosphorylation	GHKFMATYLRQPTYC CCHHHHHHHCCCCCC	7.14	18295358
317	Phosphorylation	GLQPGNISPTSKLIS CCCCCCCCCHHHHHC	26.56	22673903
319	Phosphorylation	QPGNISPTSKLISRS CCCCCCCHHHHHCHH	31.53	22673903
320	Phosphorylation	PGNISPTSKLISRST CCCCCCHHHHHCHHH	28.93	22673903
365	Phosphorylation	IRVLGKGSFGKVMLA EEEECCCCCCCEEEE	34.02	23984901
381	Phosphorylation	IKETGELYAVKVLKK HHHHCCEEEEEEEEC	12.68	-
513	Phosphorylation	CNGVTTATFCGTPDY CCCCCHHCCCCCCCC	19.84	-
520	Phosphorylation	TFCGTPDYIAPEILQ CCCCCCCCCCHHHHH	10.53	9326592
656	Phosphorylation	IKEEPVLTPIDEGHL HCCCCCCCCCCCCCC	20.59	29779826
675	Phosphorylation	QDEFRNFSYVSPELQ HHHCCCCCCCCCCCC	28.33	22673903
678	Phosphorylation	FRNFSYVSPELQP-- CCCCCCCCCCCCC--	12.39	30181290

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
513	T	Phosphorylation	Kinase	PDPK1	O55173	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KPCL_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of KPCL_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of KPCL_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.