Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Protein kinase C iota type  

UniProtKB / Swiss-Prot ID :  KPCI_HUMAN

Gene Name (Synonyms) : 
PRKCI, DXS1179E  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Membrane. Endosome. Nucleus. Note=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 nucleus. 

Protein Function :  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 (PI(3)K) 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. 

Protein Sequence MPTQRDSSTMSHTVAGGGSGDHSHQVRVKAYYRGDIMITHFEPSISFEGLCNEVRDMCSFDNEQLFTMKW...
Predicted Secondary Structure CCCCCCCCCCCCCCEEEEEEEEECCCEEEEEECCCCCHHHHHHHHHHHHCCCCCCCEEEEEECCCCCCEE...
Protein Variant
LocationDescription
118P -> L (in a metastatic melanoma sample;somatic mutation).
130R -> C. VAR_042323
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
3Phosphothreonine--MPTQRDS
--CCCCCCC
34.63HPRD
Link-
3Phosphothreonine--MPTQRDS
--CCCCCCC
34.63Phosphositeplus
Link-
7PhosphoserineTQRDSSTMS
CCCCCCCCC
29.87HPRD
Link-
7PhosphoserineTQRDSSTMS
CCCCCCCCC
29.87Phosphositeplus
Link-
8PhosphoserineQRDSSTMSH
CCCCCCCCC
32.21HPRD
Link-
8PhosphoserineQRDSSTMSH
CCCCCCCCC
32.21Phosphositeplus
Link-
9PhosphothreonineRDSSTMSHT
CCCCCCCCC
27.01HPRD
Link-
9PhosphothreonineRDSSTMSHT
CCCCCCCCC
27.01Phosphositeplus
Link-
11PhosphoserineSSTMSHTVA
CCCCCCCCE
18.98HPRD
Link-
11PhosphoserineSSTMSHTVA
CCCCCCCCE
18.98Phosphositeplus
Link-
13PhosphothreonineTMSHTVAGG
CCCCCCEEE
12.54HPRD
Link-
13PhosphothreonineTMSHTVAGG
CCCCCCEEE
12.54Phosphositeplus
Link-
19PhosphoserineAGGGSGDHS
EEEEEEEEE
44.30HPRD
Link
19PhosphoserineAGGGSGDHS
EEEEEEEEE
44.30Phosphositeplus
Link
44PhosphoserineHFEPSISFE
HHHHHHHHH
24.54Phosphositeplus
Link
46PhosphoserineEPSISFEGL
HHHHHHHHC
22.91Phosphositeplus
Link
136PhosphotyrosineWRKLYCANG
CEEEEEECC
7.80Phosphositeplus
Link-
222PhosphoserinePYNPSSHES
CCCCCCCCC
40.46Phosphositeplus
Link-
223PhosphoserineYNPSSHESL
CCCCCCCCC
32.31Phosphositeplus
Link-
226PhosphoserineSSHESLDQV
CCCCCCCCC
31.64Phosphositeplus
Link-
246PhosphoserineSGKASSSLG
CCCEEEEEE
24.76Phosphositeplus
Link-
247PhosphoserineGKASSSLGL
CCEEEEEEE
34.15Phosphositeplus
Link-
265Phosphotyrosine (SRC)GRGSYAKVL
EEEECCCCC
17.17HPRD
Link-
265Phosphotyrosine (SRC)GRGSYAKVL
EEEECCCCC
17.17PhosphoELM
Link-
265Phosphotyrosine; by SRC.GRGSYAKVL
EEEECCCCC
17.17UniProtKB
Link-
280Phosphotyrosine (SRC)TDRIYAMKV
EEHHHCCCH
11.09HPRD
Link-
280Phosphotyrosine (SRC)TDRIYAMKV
EEHHHCCCH
11.09PhosphoELM
Link-
280Phosphotyrosine; by SRC.TDRIYAMKV
EEHHHCCCH
11.09UniProtKB
Link-
334Phosphotyrosine (SRC)FVIEYVNGG
HHHHHHHHC
6.52HPRD
Link-
334Phosphotyrosine (SRC)FVIEYVNGG
HHHHHHHHC
6.52PhosphoELM
Link-
334Phosphotyrosine; by SRC.FVIEYVNGG
HHHHHHHHC
6.52UniProtKB
Link-
380Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YRDLKLDNV
EECCCCCEE
59.07Phosphositeplus
Link-
409PhosphothreonineRPGDTTSTF
CCCHHHCCH
28.67HPRD
Link-
409PhosphothreonineRPGDTTSTF
CCCHHHCCH
28.67PhosphoELM
Link-
409PhosphothreonineRPGDTTSTF
CCCHHHCCH
28.67Phosphositeplus
Link-
410PhosphothreoninePGDTTSTFC
CCHHHCCHH
30.43HPRD
Link-
410PhosphothreoninePGDTTSTFC
CCHHHCCHH
30.43PhosphoELM
Link-
410PhosphothreoninePGDTTSTFC
CCHHHCCHH
30.43Phosphositeplus
Link-
411PhosphoserineGDTTSTFCG
CHHHCCHHH
22.91HPRD
Link-
411PhosphoserineGDTTSTFCG
CHHHCCHHH
22.91PhosphoELM
Link-
412PhosphothreonineDTTSTFCGT
HHHCCHHHH
22.35HPRD
Link-
412PhosphothreonineDTTSTFCGT
HHHCCHHHH
22.35PhosphoELM
Link-
412PhosphothreonineDTTSTFCGT
HHHCCHHHH
22.35Phosphositeplus
Link-
416PhosphothreonineTFCGTPNYI
CHHHHCCCC
15.00HPRD
Link-
416PhosphothreonineTFCGTPNYI
CHHHHCCCC
15.00Phosphositeplus
Link-
430PhosphotyrosineRGEDYGFSV
HHHHHHHHH
18.77Phosphositeplus
Link-
459PhosphoserineIVGSSDNPD
HHHHHHHHH
35.16HPRD
Link-
459PhosphoserineIVGSSDNPD
HHHHHHHHH
35.16Phosphositeplus
Link-
564PhosphothreoninePVQLTPDDD
HHHHHHHHH
13.95HPRD
Link-
564PhosphothreoninePVQLTPDDD
HHHHHHHHH
13.95Phosphositeplus
Link-
564Phosphothreonine.PVQLTPDDD
HHHHHHHHH
13.95UniProtKB
Link-
591PhosphoserinePLLMSAEEC
C
32.28HPRD
Link-
591PhosphoserinePLLMSAEEC
C
32.28Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PAR6A_HUMANphysical interactionMINT-4085663MINT17057644
PAR6A_HUMANphysical interaction
direct interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical inter
EBI-752629
EBI-1041315
EBI-28
intact16189514
15590654
11257119
11257119
11257119
11260256
14676191
14676191
PAR6G_HUMANphysical interactionEBI-295426
intact11260256
PAR6B_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
EBI-295401
EBI-295530
EBI-295
intact11260256
11260256
11260256
11260256
14676191
14676191
1433F_HUMANphysical interaction
physical interaction
EBI-306968
EBI-307271
intact14676191
14676191
1433Z_HUMANphysical interactionEBI-354745
intact14676191
PARD3_HUMANphysical interaction
physical interaction
EBI-354833
EBI-307257
intact14676191
14676191
PNMA1_HUMANphysical interactionEBI-349771
intact14676191
1433F_HUMANin vivoHPRD:02105HPRD14676191
CDC42_HUMANin vivoHPRD:02105HPRD10934474
14676191
G3P_HUMANin vitro
in vivo
HPRD:02105HPRD11724794
IRAK1_HUMANin vitro
in vivo
HPRD:02105HPRD14684752
IKKA_HUMANin vitroHPRD:02105HPRD10848576
RAB2A_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:02105HPRD14570876
ANXA1_HUMANin vitroHPRD:02105HPRD2457390
PAR6A_HUMANENSP00000295797STRING
L2GL1_HUMANENSP00000295797STRING
PAR6G_HUMANENSP00000295797STRING
PDPK1_HUMANENSP00000295797STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00675Tamoxifen
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Nerve growth factor stimulates multisite tyrosine phosphorylation andactivation of the atypical protein kinase C's via a src kinasepathway.";
Wooten M.W., Vandenplas M.L., Seibenhener M.L., Geetha T.,Diaz-Meco M.T.;
Mol. Cell. Biol. 21:8414-8427(2001).
Cited for: PHOSPHORYLATION AT TYR-265; TYR-280 AND TYR-334, AND MUTAGENESIS OFTYR-265; TYR-280 AND TYR-334.
"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: INTERACTION WITH KPNB1, SUBCELLULAR LOCATION, PHOSPHORYLATION ATTYR-265, AND MUTAGENESIS OF TYR-265.
"Crystal structure of the catalytic domain of human atypical proteinkinase C-iota reveals interaction mode of phosphorylation site in turnmotif.";
Messerschmidt A., Macieira S., Velarde M., Baedeker M., Benda C.,Jestel A., Brandstetter H., Neuefeind T., Blaesse M.;
J. Mol. Biol. 352:918-931(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 233-596, IDENTIFICATION BYMASS SPECTROMETRY, AND PHOSPHORYLATION AT THR-412 AND THR-564.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures