CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007504
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein kinase C iota type 
Protein Synonyms/Alias
 Atypical protein kinase C-lambda/iota; PRKC-lambda/iota; aPKC-lambda/iota; nPKC-iota 
Gene Name
 PRKCI 
Gene Synonyms/Alias
 DXS1179E 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
380GIIYRDLKLDNVLLDubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional 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 (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. 
Sequence Annotation
 DOMAIN 25 108 OPR.
 DOMAIN 254 522 Protein kinase.
 DOMAIN 523 594 AGC-kinase C-terminal.
 ZN_FING 140 190 Phorbol-ester/DAG-type.
 NP_BIND 260 268 ATP (By similarity).
 REGION 2 253 Regulatory domain.
 REGION 2 28 Required for interaction with RAB2.
 REGION 72 91 Interaction with PARD6A.
 MOTIF 125 134 Pseudosubstrate (By similarity).
 ACT_SITE 378 378 Proton acceptor (By similarity).
 BINDING 283 283 ATP (By similarity).
 MOD_RES 2 2 N-acetylproline.
 MOD_RES 3 3 Phosphothreonine.
 MOD_RES 7 7 Phosphoserine.
 MOD_RES 8 8 Phosphoserine.
 MOD_RES 9 9 Phosphothreonine.
 MOD_RES 265 265 Phosphotyrosine; by SRC.
 MOD_RES 280 280 Phosphotyrosine; by SRC.
 MOD_RES 334 334 Phosphotyrosine; by SRC.
 MOD_RES 412 412 Phosphothreonine; by PDPK1 (Probable).
 MOD_RES 564 564 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm; Endosome; Kinase; Membrane; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome; Serine/threonine-protein kinase; Transferase; Tumor suppressor; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 596 AA 
Protein Sequence
MPTQRDSSTM SHTVAGGGSG DHSHQVRVKA YYRGDIMITH FEPSISFEGL CNEVRDMCSF 60
DNEQLFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE LLIHVFPCVP ERPGMPCPGE 120
DKSIYRRGAR RWRKLYCANG HTFQAKRFNR RAHCAICTDR IWGLGRQGYK CINCKLLVHK 180
KCHKLVTIEC GRHSLPQEPV MPMDQSSMHS DHAQTVIPYN PSSHESLDQV GEEKEAMNTR 240
ESGKASSSLG LQDFDLLRVI GRGSYAKVLL VRLKKTDRIY AMKVVKKELV NDDEDIDWVQ 300
TEKHVFEQAS NHPFLVGLHS CFQTESRLFF VIEYVNGGDL MFHMQRQRKL PEEHARFYSA 360
EISLALNYLH ERGIIYRDLK LDNVLLDSEG HIKLTDYGMC KEGLRPGDTT STFCGTPNYI 420
APEILRGEDY GFSVDWWALG VLMFEMMAGR SPFDIVGSSD NPDQNTEDYL FQVILEKQIR 480
IPRSLSVKAA SVLKSFLNKD PKERLGCHPQ TGFADIQGHP FFRNVDWDMM EQKQVVPPFK 540
PNISGEFGLD NFDSQFTNEP VQLTPDDDDI VRKIDQSEFE GFEYINPLLM SAEECV 596 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IEA:Compara.
 GO:0031252; C:cell leading edge; IEA:Compara.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0000133; C:polarisome; TAS:UniProtKB.
 GO:0043220; C:Schmidt-Lanterman incisure; IEA:Compara.
 GO:0005524; F:ATP binding; TAS:UniProtKB.
 GO:0005543; F:phospholipid binding; IDA:UniProtKB.
 GO:0004697; F:protein kinase C activity; ISS:BHF-UCL.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007015; P:actin filament organization; IEA:Compara.
 GO:0016477; P:cell migration; IEA:Compara.
 GO:0016044; P:cellular membrane organization; NAS:UniProtKB.
 GO:0032869; P:cellular response to insulin stimulus; ISS:BHF-UCL.
 GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
 GO:0035089; P:establishment of apical/basal cell polarity; IEA:Compara.
 GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; TAS:UniProtKB.
 GO:0042462; P:eye photoreceptor cell development; IEA:Compara.
 GO:0048194; P:Golgi vesicle budding; IEA:Compara.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0034351; P:negative regulation of glial cell apoptotic process; IMP:UniProtKB.
 GO:0043524; P:negative regulation of neuron apoptotic process; IDA:UniProtKB.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:2000353; P:positive regulation of endothelial cell apoptotic process; IMP:UniProtKB.
 GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; ISS:BHF-UCL.
 GO:0060252; P:positive regulation of glial cell proliferation; IMP:UniProtKB.
 GO:0046326; P:positive regulation of glucose import; ISS:BHF-UCL.
 GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
 GO:0006612; P:protein targeting to membrane; NAS:UniProtKB.
 GO:0070555; P:response to interleukin-1; IEA:Compara.
 GO:0046903; P:secretion; NAS:UniProtKB.
 GO:0070830; P:tight junction assembly; TAS:Reactome.
 GO:0016192; P:vesicle-mediated transport; TAS:UniProtKB. 
Interpro
 IPR000961; AGC-kinase_C.
 IPR020454; DAG/PE-bd.
 IPR011009; Kinase-like_dom.
 IPR000270; OPR_PB1.
 IPR012233; PKC_zeta.
 IPR017892; Pkinase_C.
 IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00130; C1_1
 PF00564; PB1
 PF00069; Pkinase
 PF00433; Pkinase_C 
SMART
 SM00109; C1
 SM00666; PB1
 SM00133; S_TK_X
 SM00220; S_TKc 
PROSITE
 PS51285; AGC_KINASE_CTER
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST
 PS00479; ZF_DAG_PE_1
 PS50081; ZF_DAG_PE_2 
PRINTS
 PR00008; DAGPEDOMAIN.