KPCL_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KPCL_MOUSE
• UniProt AC: P23298
• Protein Name: Protein kinase C eta type
• Gene Name: Prkch
• Organism: Mus musculus (Mouse).
• Sequence Length: 683
• Subcellular Localization: Cytoplasm . Associates with cell membrane during keratinocytes differentiation.
• 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: MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTAGTSDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQVNGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDAKIAEQRFGINIPHKFNVHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLISRSTLRRQGKEGSKEGNGIGVNSSSRFGIDNFEFIRVLGKGSFGKVMLARIKETGELYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHEKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHEILRHPFFKEIDWAQLNHRQLEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQL

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
25	Phosphorylation	EAVGLQPTRWSLRHS CCCCCCCCCHHHHHH	31.63	22817900
28	Phosphorylation	GLQPTRWSLRHSLFK CCCCCCHHHHHHHHH	16.54	25266776
32	Phosphorylation	TRWSLRHSLFKKGHQ CCHHHHHHHHHHCCC	29.12	25266776
35	Acetylation	SLRHSLFKKGHQLLD HHHHHHHHHCCCCCC	64.24	19857259
44	Phosphorylation	GHQLLDPYLTVSVDQ CCCCCCCCEEEEECE	18.05	23140645
46	Phosphorylation	QLLDPYLTVSVDQVR CCCCCCEEEEECEEE	12.61	23140645
48	Phosphorylation	LDPYLTVSVDQVRVG CCCCEEEEECEEEEC	18.10	23140645
57	Phosphorylation	DQVRVGQTSTKQKTN CEEEECCCCCCCCCC	32.22	23140645
58	Phosphorylation	QVRVGQTSTKQKTNK EEEECCCCCCCCCCC	26.22	23140645
59	Phosphorylation	VRVGQTSTKQKTNKP EEECCCCCCCCCCCC	40.66	23140645
305	Phosphorylation	NAVELAKTLAGMGLQ CHHHHHHHHHCCCCC	19.08	28833060
317	Phosphorylation	GLQPGNISPTSKLIS CCCCCCCCCHHHHHC	26.56	25521595
319	Phosphorylation	QPGNISPTSKLISRS CCCCCCCHHHHHCHH	31.53	28833060
320	Phosphorylation	PGNISPTSKLISRST CCCCCCHHHHHCHHH	28.93	28833060
324	Phosphorylation	SPTSKLISRSTLRRQ CCHHHHHCHHHHHHC	30.52	-
326	Phosphorylation	TSKLISRSTLRRQGK HHHHHCHHHHHHCCC	25.63	-
478	Methylation	HEKGIIYRDLKLDNV HHCCCCCCCCCCCCE	32.17	30988859
513	Phosphorylation	CNGVTTATFCGTPDY CCCCCHHCCCCCCCC	19.84	22817900
637	Phosphorylation	PFRPRIKSREDVSNF CCCCCCCCHHHHHCC	38.23	23375375
642	Phosphorylation	IKSREDVSNFDPDFI CCCHHHHHCCCHHHH	44.06	28285833
656	Phosphorylation	IKEEPVLTPIDEGHL HCCCCCCCCCCCCCC	20.59	27180971
675	Phosphorylation	QDEFRNFSYVSPELQ HHHCCCCCCCCCCCC	28.33	22322096
676	Phosphorylation	DEFRNFSYVSPELQL HHCCCCCCCCCCCCC	10.78	28833060
678	Phosphorylation	FRNFSYVSPELQL-- CCCCCCCCCCCCC--	12.39	28833060

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	Q9Z2A0	Uniprot
642	S	Phosphorylation	Kinase	MTOR	Q9JLN9	PSP

Functions of PTM Sites

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

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_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of KPCL_MOUSE !!

Drug and Disease Associations

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