dbPTM

KPCI_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KPCI_RAT
UniProt AC	F1M7Y5
Protein Name	Protein kinase C iota type
Gene Name	Prkci
Organism	Rattus norvegicus (Rat).
Sequence Length	596
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. 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 (By similarity)..
Protein Sequence	MPTQRDSSTMSHTVACGGGGDHSHQVRVKAYYRGDIMITHFEPSISFEGLCSEVRDMCSFDNEQPFTMKWIDEEGDPCTVSSQLELEEAFRLYELNKDSELLIHVFPCVPERPGMPCPGEDKSIYRRGARRWRKLYCANGHTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHKKCHKLVTIECGRHSLPPEPMMPMDQSSMHPDHTQTVIPYNPSSHESLDQVGEEKEAMNTRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV

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	-
7	Phosphorylation	-MPTQRDSSTMSHTV -CCCCCCCCCCCCEE	29.87	25575281
8	Phosphorylation	MPTQRDSSTMSHTVA CCCCCCCCCCCCEEE	32.21	25575281
9	Phosphorylation	PTQRDSSTMSHTVAC CCCCCCCCCCCEEEC	27.01	25575281
11	Phosphorylation	QRDSSTMSHTVACGG CCCCCCCCCEEECCC	18.98	25575281
13	Phosphorylation	DSSTMSHTVACGGGG CCCCCCCEEECCCCC	11.51	25575281
136	Phosphorylation	ARRWRKLYCANGHTF HHHHEEEEECCCCCE	7.80	-
246	Phosphorylation	TRESGKASSSLGLQD HHHCCCCCHHCCCCC	24.76	22108457
247	Phosphorylation	RESGKASSSLGLQDF HHCCCCCHHCCCCCH	34.15	28432305
248	Phosphorylation	ESGKASSSLGLQDFD HCCCCCHHCCCCCHH	24.78	23984901
264	Phosphorylation	LRVIGRGSYAKVLLV EEEECCCCCEEEEEE	22.13	-
265	Phosphorylation	RVIGRGSYAKVLLVR EEECCCCCEEEEEEE	17.17	11891849
280	Phosphorylation	LKKTDRIYAMKVVKK CCCCCCEEEEEEEEH	11.09	-
334	Phosphorylation	RLFFVIEYVNGGDLM EEEEEEEEECCCCHH	6.52	-
409	Phosphorylation	EGLRPGDTTSTFCGT CCCCCCCCCCCCCCC	28.67	27097102
410	Phosphorylation	GLRPGDTTSTFCGTP CCCCCCCCCCCCCCC	30.43	27097102
411	Phosphorylation	LRPGDTTSTFCGTPN CCCCCCCCCCCCCCC	22.91	27097102
412	Phosphorylation	RPGDTTSTFCGTPNY CCCCCCCCCCCCCCC	22.35	21738781
416	Phosphorylation	TTSTFCGTPNYIAPE CCCCCCCCCCCCCHH	15.00	23984901
488	Acetylation	IPRSLSVKAASVLKS CCCCHHHHHHHHHHH	34.55	22902405
544	Phosphorylation	PPFKPNISGEFGLDN CCCCCCCCCCCCCCC	38.62	21630457
564	Phosphorylation	TNEPVQLTPDDDDIV CCCCCCCCCCCCHHH	13.95	27097102

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
265	Y	Phosphorylation	Kinase	SRC	P12931	PSP
265	Y	Phosphorylation	Kinase	SRC	Q9WUD9	Uniprot
280	Y	Phosphorylation	Kinase	SRC	P12931	PSP
280	Y	Phosphorylation	Kinase	SRC	Q9WUD9	Uniprot
334	Y	Phosphorylation	Kinase	SRC	P12931	PSP
334	Y	Phosphorylation	Kinase	SRC	Q9WUD9	Uniprot
412	T	Phosphorylation	Kinase	PDPK1	O55173	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
412	T	Phosphorylation	27498875
Phosphorylation at Thr-412 in the activation loop is not mandatory for activation (By similarity).
564	T	Phosphorylation	22673903
Phosphorylated at Thr-564 during the initial phase of long term potentiation.

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 KPCI_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
KPCI_RAT	Prkci	physical	11463795
MBP_RAT	Mbp	physical	11500922

Drug and Disease Associations

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

Regulatory Network of KPCI_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphorylation of tyrosine 256 facilitates nuclear import ofatypical protein kinase C."; White W.O., Seibenhener M.L., Wooten M.W.; J. Cell. Biochem. 85:42-53(2002). Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-265, AND MUTAGENESIS OFTYR-265.	11891849 [Abstract]

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