KPCI_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KPCI_MOUSE
• UniProt AC: Q62074
• Protein Name: Protein kinase C iota type
• Gene Name: Prkci
• Organism: Mus musculus (Mouse).
• Sequence Length: 595
• Subcellular Localization: Cytoplasm . Membrane . Endosome . Nucleus . Transported into the endosome through interaction with SQSTM1/p62. After phosphorylation by SRC, transported into the nucleus through interaction with KPNB1. Colocalizes with CDK7 in the cytoplasm and nucle
• Protein Description: Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI3K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis (By similarity). Downstream of PI3K is required for insulin-stimulated glucose transport. Activates RAB4A and promotes its association with KIF3A which is required for the insulin-induced SLC2A4/GLUT4 translocation in adipocytes. Is essential in early embryogenesis and development of differentiating photoreceptors by playing a role in the establishment of epithelial and neuronal polarity..
• Protein Sequence: MPTQRDSSTMSHTVACGGGGDHSHQVRVKAYYRGDIMITHFEPSISFEGLCSEVRDMCSFDNEQPFTMKWIDEEGDPCTVSSQLELEEAFRLYELNKDSELLIHVFPCVPERPGMPCPGEDKSIYRRGARRWRKLYCANGHTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHKKCHKLVTIECGRHSLPPEPMMPMDQTMHPDHTQTVIPYNPSSHESLDQVGEEKEAMNTRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV

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
2	Acetylation	------MPTQRDSST ------CCCCCCCCC	36.92	-
3	Phosphorylation	-----MPTQRDSSTM -----CCCCCCCCCC	34.63	26643407
7	Phosphorylation	-MPTQRDSSTMSHTV -CCCCCCCCCCCCEE	29.87	26643407
8	Phosphorylation	MPTQRDSSTMSHTVA CCCCCCCCCCCCEEE	32.21	26643407
9	Phosphorylation	PTQRDSSTMSHTVAC CCCCCCCCCCCEEEC	27.01	25777480
11	Phosphorylation	QRDSSTMSHTVACGG CCCCCCCCCEEECCC	18.98	26643407
13	Phosphorylation	DSSTMSHTVACGGGG CCCCCCCEEECCCCC	11.51	25777480
23	Phosphorylation	CGGGGDHSHQVRVKA CCCCCCCCCEEEEEE	21.98	25777480
123	Phosphorylation	PCPGEDKSIYRRGAR CCCCCCCCHHHHHHH	36.85	22817900
136	Phosphorylation	ARRWRKLYCANGHTF HHHHEEEEECCCCCE	7.80	-
206	Phosphorylation	PMMPMDQTMHPDHTQ CCCCCCCCCCCCCCC	17.12	-
212	Phosphorylation	QTMHPDHTQTVIPYN CCCCCCCCCCEECCC	33.06	-
221	Phosphorylation	TVIPYNPSSHESLDQ CEECCCCCCCCCHHH	40.46	25338131
225	Phosphorylation	YNPSSHESLDQVGEE CCCCCCCCHHHHHHH	31.64	25338131
243	Ubiquitination	MNTRESGKASSSLGL HHHHHCCCCCHHCCC	55.14	-
245	Phosphorylation	TRESGKASSSLGLQD HHHCCCCCHHCCCCC	24.76	29472430
246	Phosphorylation	RESGKASSSLGLQDF HHCCCCCHHCCCCCH	34.15	26239621
247	Phosphorylation	ESGKASSSLGLQDFD HCCCCCHHCCCCCHH	24.78	26239621
263	Phosphorylation	LRVIGRGSYAKVLLV EEEECCCCCEEEEEE	22.13	25338131
264	Phosphorylation	RVIGRGSYAKVLLVR EEECCCCCEEEEEEE	17.17	29514104
279	Phosphorylation	LKKTDRIYAMKVVKK CCCCCCEEEEEEEEH	11.09	-
333	Phosphorylation	RLFFVIEYVNGGDLM EEEEEEEEECCCCHH	6.52	-
376	Methylation	HERGIIYRDLKLDNV HHCCCEEEEECCCCE	32.17	30988865
379	Ubiquitination	GIIYRDLKLDNVLLD CCEEEEECCCCEEEC	59.07	-
408	Phosphorylation	EGLRPGDTTSTFCGT CCCCCCCCCCCCCCC	28.67	22322096
409	Phosphorylation	GLRPGDTTSTFCGTP CCCCCCCCCCCCCCC	30.43	22322096
410	Phosphorylation	LRPGDTTSTFCGTPN CCCCCCCCCCCCCCC	22.91	22322096
411	Phosphorylation	RPGDTTSTFCGTPNY CCCCCCCCCCCCCCC	22.35	25521595
415	Phosphorylation	TTSTFCGTPNYIAPE CCCCCCCCCCCCCHH	15.00	25159016
418	Phosphorylation	TFCGTPNYIAPEILR CCCCCCCCCCHHHHC	10.32	25777480
543	Phosphorylation	PPFKPNISGEFGLDN CCCCCCCCCCCCCCC	38.62	25619855
553	Phosphorylation	FGLDNFDSQFTNEPV CCCCCCCCCCCCCCC	24.05	25619855
556	Phosphorylation	DNFDSQFTNEPVQLT CCCCCCCCCCCCCCC	30.91	25619855
563	Phosphorylation	TNEPVQLTPDDDDIV CCCCCCCCCCCCHHH	13.95	27087446
590	Phosphorylation	YINPLLMSAEECV-- CCHHHHHCHHHCC--	32.28	-

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
264	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot
279	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot
333	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
411	T	Phosphorylation	Phosphorylation at Thr-411 in the activation loop is not mandatory for activation.	17242355
563	T	Phosphorylation	Phosphorylated at Thr-563 during the initial phase of long term potentiation (By similarity).	21183079

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FRS2_MOUSE	Frs2	physical	10383403
AL3A2_HUMAN	ALDH3A2	physical	26496610
ATP5E_HUMAN	ATP5E	physical	26496610
DYN2_HUMAN	DNM2	physical	26496610
NIPS2_HUMAN	GBAS	physical	26496610
GPC1_HUMAN	GPC1	physical	26496610
L2GL2_HUMAN	LLGL2	physical	26496610
L2GL1_HUMAN	LLGL1	physical	26496610
PYGB_HUMAN	PYGB	physical	26496610
XRCC1_HUMAN	XRCC1	physical	26496610
ZNF3_HUMAN	ZNF3	physical	26496610
NIPS1_HUMAN	NIPSNAP1	physical	26496610
SQSTM_HUMAN	SQSTM1	physical	26496610
MBD4_HUMAN	MBD4	physical	26496610
NGAP_HUMAN	RASAL2	physical	26496610
KEAP1_HUMAN	KEAP1	physical	26496610
RT18B_HUMAN	MRPS18B	physical	26496610
PAR6A_HUMAN	PARD6A	physical	26496610
TM160_HUMAN	TMEM160	physical	26496610
NOL8_HUMAN	NOL8	physical	26496610
LSG1_HUMAN	LSG1	physical	26496610
TM165_HUMAN	TMEM165	physical	26496610
PARD3_HUMAN	PARD3	physical	26496610
RM11_HUMAN	MRPL11	physical	26496610
PRR3_HUMAN	PRR3	physical	26496610
INT14_HUMAN	VWA9	physical	26496610
PAR6B_HUMAN	PARD6B	physical	26496610
CENPV_HUMAN	CENPV	physical	26496610
LAMA1_HUMAN	LAMA1	physical	26496610
TIM23_HUMAN	TIMM23	physical	26496610

Drug and Disease Associations

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