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P41743

- KPCI_HUMAN

UniProt

P41743 - KPCI_HUMAN

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Protein
Protein kinase C iota type
Gene
PRKCI, DXS1179E
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.14 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Atypical PKCs (PRKCI and PRKCZ) exhibit an elevated basal enzymatic activity (that may be due to the interaction with SMG1 or SQSTM1) and are not regulated by diacylglycerol, phosphatidylserine, phorbol esters or calcium ions. Two specific sites, Thr-412 (activation loop of the kinase domain) and Thr-564 (turn motif), need to be phosphorylated for its full activation By similarity. Might also be a target for novel lipid activators that are elevated during nutrient-stimulated insulin secretion.1 Publication

Kineticsi

  1. KM=13.5 µM for ATP (for recombinant purified PRKCI)1 Publication

Vmax=7.4 pmol/min/mg enzyme

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei283 – 2831ATP By similarity
Active sitei378 – 3781Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri140 – 19051Phorbol-ester/DAG-type
Add
BLAST
Nucleotide bindingi260 – 2689ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. phospholipid binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. protein kinase C activity Source: BHF-UCL
  5. protein kinase activity Source: UniProtKB
  6. protein serine/threonine kinase activity Source: UniProtKB
  7. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. Golgi vesicle budding Source: Ensembl
  2. actin filament organization Source: Ensembl
  3. cell junction assembly Source: Reactome
  4. cell migration Source: Ensembl
  5. cell-cell junction organization Source: UniProtKB
  6. cellular response to insulin stimulus Source: BHF-UCL
  7. cytoskeleton organization Source: UniProtKB
  8. establishment of apical/basal cell polarity Source: Ensembl
  9. establishment or maintenance of epithelial cell apical/basal polarity Source: UniProtKB
  10. eye photoreceptor cell development Source: Ensembl
  11. intracellular signal transduction Source: InterPro
  12. membrane organization Source: UniProtKB
  13. negative regulation of apoptotic process Source: Reactome
  14. negative regulation of glial cell apoptotic process Source: UniProtKB
  15. negative regulation of neuron apoptotic process Source: UniProtKB
  16. neurotrophin TRK receptor signaling pathway Source: Reactome
  17. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  18. positive regulation of endothelial cell apoptotic process Source: UniProtKB
  19. positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
  20. positive regulation of glial cell proliferation Source: UniProtKB
  21. positive regulation of glucose import Source: BHF-UCL
  22. positive regulation of neuron projection development Source: UniProtKB
  23. protein phosphorylation Source: UniProtKB
  24. protein targeting to membrane Source: UniProtKB
  25. response to interleukin-1 Source: Ensembl
  26. secretion Source: UniProtKB
  27. tight junction assembly Source: Reactome
  28. vesicle-mediated transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
ReactomeiREACT_13415. p75NTR recruits signalling complexes.
REACT_19373. Tight junction interactions.
SignaLinkiP41743.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C iota type (EC:2.7.11.13)
Alternative name(s):
Atypical protein kinase C-lambda/iota
Short name:
PRKC-lambda/iota
Short name:
aPKC-lambda/iota
nPKC-iota
Gene namesi
Name:PRKCI
Synonyms:DXS1179E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:9404. PRKCI.

Subcellular locationi

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. Transported to vesicular tubular clusters (VTCs) through interaction with RAB2A.4 Publications

GO - Cellular componenti

  1. Golgi membrane Source: GOC
  2. Schmidt-Lanterman incisure Source: Ensembl
  3. apical plasma membrane Source: Ensembl
  4. cell leading edge Source: Ensembl
  5. cytoplasm Source: HPA
  6. cytosol Source: UniProtKB
  7. endosome Source: UniProtKB-SubCell
  8. extracellular vesicular exosome Source: UniProt
  9. intercellular bridge Source: HPA
  10. microtubule cytoskeleton Source: HPA
  11. nucleus Source: UniProtKB
  12. plasma membrane Source: Reactome
  13. polarisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi29 – 291K → A: No effect on interaction with SQSTM1. 1 Publication
Mutagenesisi72 – 721D → A: Loss of interaction with ECT2, PARD6A and with SQSTM1. 3 Publications
Mutagenesisi85 – 851E → A: Slight decrease of interaction with PARD6A. Loss of interaction with PARD6A; when associated with A-91. 1 Publication
Mutagenesisi91 – 911R → A: Slight decrease of interaction with PARD6A. Loss of interaction with PARD6A; when associated with A-85. 1 Publication
Mutagenesisi265 – 2651Y → F: No effect on the SRC-mediated phosphorylation state. No effect on SRC-induced enzyme activity. Little effect on TRAF6-mediated activation of NF-kappa-B. Decreased binding to KPNB1/importin-beta. 2 Publications
Mutagenesisi274 – 2741K → R: No effect on activity. 1 Publication
Mutagenesisi274 – 2741K → W: Abolishes activity. 1 Publication
Mutagenesisi280 – 2801Y → F: No effect on the SRC-mediated phosphorylation state. No effect on SRC-induced enzyme activity. No effect on TRAF6-mediated activation of NF-kappa-B. 1 Publication
Mutagenesisi334 – 3341Y → F: No effect on the SRC-mediated phosphorylation state. Significant reduction of SRC-induced enzyme activity. Greatly reduced TRAF6-mediated activation of NF-kappa-B. Reduces NGF-dependent cell survival. 1 Publication

Keywords - Diseasei

Proto-oncogene, Tumor suppressor

Organism-specific databases

PharmGKBiPA33768.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 596595Protein kinase C iota type
PRO_0000055710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylproline1 Publication
Modified residuei3 – 31Phosphothreonine1 Publication
Modified residuei7 – 71Phosphoserine1 Publication
Modified residuei8 – 81Phosphoserine1 Publication
Modified residuei9 – 91Phosphothreonine1 Publication
Modified residuei265 – 2651Phosphotyrosine; by SRC2 Publications
Modified residuei280 – 2801Phosphotyrosine; by SRC1 Publication
Modified residuei334 – 3341Phosphotyrosine; by SRC1 Publication
Modified residuei412 – 4121Phosphothreonine; by PDPK1 Inferred
Modified residuei564 – 5641Phosphothreonine2 Publications

Post-translational modificationi

Phosphorylation at Thr-412 in the activation loop is not mandatory for activation By similarity. Upon neuronal growth factor (NGF) stimulation, phosphorylated by SRC at Tyr-265, Tyr-280 and Tyr-334. Phosphorylation at Tyr-265 facilitates binding to KPNB1/importin-beta regulating entry of PRKCI into the nucleus. Phosphorylation on Tyr-334 is important for NF-kappa-B stimulation.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP41743.
PaxDbiP41743.
PRIDEiP41743.

PTM databases

PhosphoSiteiP41743.

Expressioni

Tissue specificityi

Predominantly expressed in lung and brain, but also expressed at lower levels in many tissues including pancreatic islets. Highly expressed in non-small cell lung cancers.3 Publications

Gene expression databases

BgeeiP41743.
CleanExiHS_PRKCI.
GenevestigatoriP41743.

Organism-specific databases

HPAiHPA026574.
HPA038635.

Interactioni

Subunit structurei

Forms a complex with SQSTM1 and MP2K5 By similarity. Interacts directly with SQSTM1 Inferred. Interacts with IKBKB. Interacts with PARD6A, PARD6B and PARD6G. Part of a quaternary complex containing aPKC, PARD3, a PARD6 protein (PARD6A, PARD6B or PARD6G) and a GTPase protein (CDC42 or RAC1). Part of a complex with LLGL1 and PARD6B. Interacts with ADAP1/CENTA1. Interaction with SMG1, through the ZN-finger domain, activates the kinase activity. Interacts with CDK7. Forms a complex with RAB2A and GAPDH involved in recruitment onto the membrane of vesicular tubular clusters (VTCs). Interacts with ECT2 ('Thr-359' phosphorylated form).14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC42P609535EBI-286199,EBI-81752
MARK4Q96L342EBI-286199,EBI-302319
PARD3Q8TEW03EBI-286199,EBI-81968
PARD6AQ9NPB611EBI-286199,EBI-81876
PARD6BQ9BYG59EBI-286199,EBI-295391
PARD6GQ9BYG45EBI-286199,EBI-295417
PNMA1Q8ND902EBI-286199,EBI-302345
PRKCZQ055132EBI-286199,EBI-295351
RAC1P630003EBI-286199,EBI-413628
SOX2P484312EBI-286199,EBI-6124081
SQSTM1Q135015EBI-286199,EBI-307104
YWHAHQ049173EBI-286199,EBI-306940

Protein-protein interaction databases

BioGridi111570. 59 interactions.
DIPiDIP-31311N.
IntActiP41743. 39 interactions.
MINTiMINT-5004219.
STRINGi9606.ENSP00000295797.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 327
Beta strandi35 – 417
Helixi47 – 5711
Beta strandi67 – 715
Beta strandi73 – 753
Beta strandi77 – 793
Helixi83 – 9513
Beta strandi101 – 1066
Helixi251 – 2533
Beta strandi254 – 2629
Beta strandi264 – 27310
Turni274 – 2774
Beta strandi278 – 2869
Helixi287 – 2893
Helixi293 – 30816
Turni309 – 3113
Beta strandi318 – 3236
Beta strandi325 – 3328
Helixi340 – 3478
Helixi352 – 37120
Helixi381 – 3833
Beta strandi384 – 3863
Beta strandi388 – 3903
Beta strandi392 – 3943
Helixi397 – 3993
Helixi417 – 4193
Helixi422 – 4254
Helixi433 – 44816
Turni452 – 4576
Helixi467 – 47610
Helixi487 – 49610
Turni501 – 5033
Turni505 – 5073
Turni509 – 5113
Helixi512 – 5176
Helixi520 – 5223
Helixi527 – 5315
Turni545 – 5473
Helixi549 – 5513
Helixi554 – 5574
Helixi568 – 5714
Helixi576 – 5794

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VD2NMR-A25-108[»]
1WMHX-ray1.50A25-108[»]
1ZRZX-ray3.00A233-596[»]
3A8WX-ray2.10A/B249-588[»]
3A8XX-ray2.00A/B249-588[»]
3ZH8X-ray2.74A/B/C248-594[»]
ProteinModelPortaliP41743.
SMRiP41743. Positions 25-192, 201-588.

Miscellaneous databases

EvolutionaryTraceiP41743.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 10884OPR
Add
BLAST
Domaini254 – 522269Protein kinase
Add
BLAST
Domaini523 – 59472AGC-kinase C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 253252Regulatory domain
Add
BLAST
Regioni2 – 2827Required for interaction with RAB2
Add
BLAST
Regioni72 – 9120Interaction with PARD6A
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi125 – 13410Pseudosubstrate By similarity

Domaini

The OPR domain mediates interaction with SQSTM1 By similarity.
The C1 zinc finger does not bind diacylglycerol (DAG).
The pseudosubstrate motif resembles the sequence around sites phosphorylated on target proteins, except the presence of a non-phosphorylatable residue in place of Ser, it modulates activity by competing with substrates By similarity.

Sequence similaritiesi

Contains 1 OPR domain.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP41743.
KOiK06069.
OMAiFEPSISY.
OrthoDBiEOG7HF1J3.
PhylomeDBiP41743.
TreeFamiTF102004.

Family and domain databases

InterProiIPR000961. 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_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24357:SF60. PTHR24357:SF60. 1 hit.
PfamiPF00130. C1_1. 1 hit.
PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000554. PKC_zeta. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00666. PB1. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P41743-1 [UniParc]FASTAAdd to Basket

« Hide

MPTQRDSSTM SHTVAGGGSG DHSHQVRVKA YYRGDIMITH FEPSISFEGL    50
CNEVRDMCSF DNEQLFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE 100
LLIHVFPCVP ERPGMPCPGE DKSIYRRGAR RWRKLYCANG HTFQAKRFNR 150
RAHCAICTDR IWGLGRQGYK CINCKLLVHK KCHKLVTIEC GRHSLPQEPV 200
MPMDQSSMHS DHAQTVIPYN PSSHESLDQV GEEKEAMNTR ESGKASSSLG 250
LQDFDLLRVI GRGSYAKVLL VRLKKTDRIY AMKVVKKELV NDDEDIDWVQ 300
TEKHVFEQAS NHPFLVGLHS CFQTESRLFF VIEYVNGGDL MFHMQRQRKL 350
PEEHARFYSA EISLALNYLH ERGIIYRDLK LDNVLLDSEG HIKLTDYGMC 400
KEGLRPGDTT STFCGTPNYI APEILRGEDY GFSVDWWALG VLMFEMMAGR 450
SPFDIVGSSD NPDQNTEDYL FQVILEKQIR IPRSLSVKAA SVLKSFLNKD 500
PKERLGCHPQ TGFADIQGHP FFRNVDWDMM EQKQVVPPFK PNISGEFGLD 550
NFDSQFTNEP VQLTPDDDDI VRKIDQSEFE GFEYINPLLM SAEECV 596
Length:596
Mass (Da):68,262
Last modified:June 16, 2009 - v2
Checksum:i1E3F8C1D4BFC734F
GO

Sequence cautioni

The sequence AAA60171.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAB17011.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH22016.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti118 – 1181P → L in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_042322
Natural varianti130 – 1301R → C.1 Publication
VAR_042323

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti485 – 4851L → M in AAH22016. 1 Publication
Sequence conflicti508 – 5081H → L in AAH22016. 1 Publication
Sequence conflicti560 – 5601P → R in AAH22016. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L18964 mRNA. Translation: AAA60171.1. Different initiation.
L33881 mRNA. Translation: AAB17011.1. Different initiation.
CH471052 Genomic DNA. Translation: EAW78513.1.
CH471052 Genomic DNA. Translation: EAW78515.1.
BC022016 mRNA. Translation: AAH22016.3. Different initiation.
CCDSiCCDS3212.2.
PIRiA49509.
RefSeqiNP_002731.4. NM_002740.5.
UniGeneiHs.478199.

Genome annotation databases

EnsembliENST00000295797; ENSP00000295797; ENSG00000163558.
GeneIDi5584.
KEGGihsa:5584.
UCSCiuc003fgs.2. human.

Polymorphism databases

DMDMi239938658.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L18964 mRNA. Translation: AAA60171.1 . Different initiation.
L33881 mRNA. Translation: AAB17011.1 . Different initiation.
CH471052 Genomic DNA. Translation: EAW78513.1 .
CH471052 Genomic DNA. Translation: EAW78515.1 .
BC022016 mRNA. Translation: AAH22016.3 . Different initiation.
CCDSi CCDS3212.2.
PIRi A49509.
RefSeqi NP_002731.4. NM_002740.5.
UniGenei Hs.478199.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1VD2 NMR - A 25-108 [» ]
1WMH X-ray 1.50 A 25-108 [» ]
1ZRZ X-ray 3.00 A 233-596 [» ]
3A8W X-ray 2.10 A/B 249-588 [» ]
3A8X X-ray 2.00 A/B 249-588 [» ]
3ZH8 X-ray 2.74 A/B/C 248-594 [» ]
ProteinModelPortali P41743.
SMRi P41743. Positions 25-192, 201-588.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111570. 59 interactions.
DIPi DIP-31311N.
IntActi P41743. 39 interactions.
MINTi MINT-5004219.
STRINGi 9606.ENSP00000295797.

Chemistry

BindingDBi P41743.
ChEMBLi CHEMBL2093867.
GuidetoPHARMACOLOGYi 1490.

PTM databases

PhosphoSitei P41743.

Polymorphism databases

DMDMi 239938658.

Proteomic databases

MaxQBi P41743.
PaxDbi P41743.
PRIDEi P41743.

Protocols and materials databases

DNASUi 5584.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295797 ; ENSP00000295797 ; ENSG00000163558 .
GeneIDi 5584.
KEGGi hsa:5584.
UCSCi uc003fgs.2. human.

Organism-specific databases

CTDi 5584.
GeneCardsi GC03P169940.
HGNCi HGNC:9404. PRKCI.
HPAi HPA026574.
HPA038635.
MIMi 600539. gene.
neXtProti NX_P41743.
PharmGKBi PA33768.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233033.
HOVERGENi HBG108317.
InParanoidi P41743.
KOi K06069.
OMAi FEPSISY.
OrthoDBi EOG7HF1J3.
PhylomeDBi P41743.
TreeFami TF102004.

Enzyme and pathway databases

BRENDAi 2.7.11.13. 2681.
Reactomei REACT_13415. p75NTR recruits signalling complexes.
REACT_19373. Tight junction interactions.
SignaLinki P41743.

Miscellaneous databases

ChiTaRSi PRKCI. human.
EvolutionaryTracei P41743.
GeneWikii PRKCI.
GenomeRNAii 5584.
NextBioi 21656.
PROi P41743.
SOURCEi Search...

Gene expression databases

Bgeei P41743.
CleanExi HS_PRKCI.
Genevestigatori P41743.

Family and domain databases

InterProi 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_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR24357:SF60. PTHR24357:SF60. 1 hit.
Pfami PF00130. C1_1. 1 hit.
PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000554. PKC_zeta. 1 hit.
PRINTSi PR00008. DAGPEDOMAIN.
SMARTi SM00109. C1. 1 hit.
SM00666. PB1. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of PKC iota, an atypical isoform of protein kinase C derived from insulin-secreting cells."
    Selbie L.A., Schmitz-Peiffer C., Sheng Y., Biden T.J.
    J. Biol. Chem. 268:24296-24302(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Kidney.
  2. "Human protein kinase C iota gene (PRKCI) is closely linked to the BTK gene in Xq21.3."
    Mazzarella R., Ciccodicola A., Esposito T., Arcucci A., Migliaccio C., Jones C., Schlessinger D., D'Urso M., D'Esposito M.
    Genomics 26:629-631(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Teratocarcinoma.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  5. "Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo."
    Diaz-Meco M.T., Municio M.M., Sanchez P., Lozano J., Moscat J.
    Mol. Cell. Biol. 16:105-114(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMG1, ENZYME REGULATION.
  6. "Atypical protein kinase C iota protects human leukemia cells against drug-induced apoptosis."
    Murray N.R., Fields A.P.
    J. Biol. Chem. 272:27521-27524(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL SURVIVAL.
  7. "Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62."
    Sanchez P., De Carcer G., Sandoval I.V., Moscat J., Diaz-Meco M.T.
    Mol. Cell. Biol. 18:3069-3080(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION.
  8. "Overexpression of atypical PKC in PC12 cells enhances NGF-responsiveness and survival through an NF-kappaB dependent pathway."
    Wooten M.W., Seibenhener M.L., Zhou G., Vandenplas M.L., Tan T.H.
    Cell Death Differ. 6:753-764(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL SURVIVAL.
  9. "The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation."
    Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.
    EMBO J. 18:3044-3053(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SQSTM1 AND IKBKB, FUNCTION.
  10. "Unique structural and functional properties of the ATP-binding domain of atypical protein kinase C-iota."
    Spitaler M., Villunger A., Grunicke H., Uberall F.
    J. Biol. Chem. 275:33289-33296(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-274.
  11. "Protein kinase C iota protects neural cells against apoptosis induced by amyloid beta-peptide."
    Xie J., Guo Q., Zhu H., Wooten M.W., Mattson M.P.
    Brain Res. Mol. Brain Res. 82:107-113(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL SURVIVAL.
  12. "Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C."
    Noda Y., Takeya R., Ohno S., Naito S., Ito T., Sumimoto H.
    Genes Cells 6:107-119(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARD6A; PARD6B AND PARD6G, SUBUNIT OF A COMPLEX CONTAINING PARD6B AND CDC42/RAC1.
  13. "Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures."
    Suzuki A., Yamanaka T., Hirose T., Manabe N., Mizuno K., Shimizu M., Akimoto K., Izumi Y., Ohnishi T., Ohno S.
    J. Cell Biol. 152:1183-1196(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARD3 AND PARD6B IN THE TERNARY AKPC/PAR3/PAR6 COMPLEX.
  14. "Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway."
    Tisdale E.J.
    J. Biol. Chem. 277:3334-3341(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GAPDH.
  15. "Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase C's via a src kinase pathway."
    Wooten M.W., Vandenplas M.L., Seibenhener M.L., Geetha T., Diaz-Meco M.T.
    Mol. Cell. Biol. 21:8414-8427(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-265; TYR-280 AND TYR-334, MUTAGENESIS OF TYR-265; TYR-280 AND TYR-334.
  16. "Phosphorylation of tyrosine 256 facilitates nuclear import of atypical protein kinase C."
    White W.O., Seibenhener M.L., Wooten M.W.
    J. Cell. Biochem. 85:42-53(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KPNB1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-265, MUTAGENESIS OF TYR-265.
  17. "Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C."
    Zemlickova E., Dubois T., Kerai P., Clokie S., Cronshaw A.D., Wakefield R.I.D., Johannes F.-J., Aitken A.
    Biochem. Biophys. Res. Commun. 307:459-465(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADAP1.
  18. "Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of PAR-3 to regulate epithelial cell polarity."
    Yamanaka T., Horikoshi Y., Sugiyama Y., Ishiyama C., Suzuki A., Hirose T., Iwamatsu A., Shinohara A., Ohno S.
    Curr. Biol. 13:734-743(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARD6B/PAR-6 AND LLGL1.
  19. "Atypical protein kinase C plays a critical role in protein transport from pre-Golgi intermediates."
    Tisdale E.J., Wang J., Silver R.B., Artalejo C.R.
    J. Biol. Chem. 278:38015-38021(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Rab2 interacts directly with atypical protein kinase C (aPKC) iota/lambda and inhibits aPKCiota/lambda-dependent glyceraldehyde-3-phosphate dehydrogenase phosphorylation."
    Tisdale E.J.
    J. Biol. Chem. 278:52524-52530(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB2A.
  21. "Regulation of interleukin receptor-associated kinase (IRAK) phosphorylation and signaling by iota protein kinase C."
    Mamidipudi V., Lin C., Seibenhener M.L., Wooten M.W.
    J. Biol. Chem. 279:4161-4165(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF IRAK1.
  22. "Atypical protein kinase Ciota plays a critical role in human lung cancer cell growth and tumorigenicity."
    Regala R.P., Weems C., Jamieson L., Copland J.A., Thompson E.A., Fields A.P.
    J. Biol. Chem. 280:31109-31115(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  23. "Cyclin-dependent kinase activating kinase/Cdk7 co-localizes with PKC-iota in human glioma cells."
    Bicaku E., Patel R., Acevedo-Duncan M.
    Tissue Cell 37:53-58(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDK7, SUBCELLULAR LOCATION.
  24. "Src-dependent protein kinase C iota/lambda (aPKCiota/lambda) tyrosine phosphorylation is required for aPKCiota/lambda association with Rab2 and glyceraldehyde-3-phosphate dehydrogenase on pre-Golgi intermediates."
    Tisdale E.J., Artalejo C.R.
    J. Biol. Chem. 281:8436-8442(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB2A AND GADPH, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  25. "Atypical protein kinase C (iota) activates ezrin in the apical domain of intestinal epithelial cells."
    Wald F.A., Oriolo A.S., Mashukova A., Fregien N.L., Langshaw A.H., Salas P.J.
    J. Cell Sci. 121:644-654(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF EZR.
  26. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. "Protein kinase C iota mediates lipid-induced apoptosis of human coronary artery endothelial cells."
    Staiger K., Schatz U., Staiger H., Weyrich P., Haas C., Guirguis A., Machicao F., Haering H.U., Kellerer M.
    Microvasc. Res. 78:40-44(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS.
  30. "Ect2 links the PKCiota-Par6alpha complex to Rac1 activation and cellular transformation."
    Justilien V., Fields A.P.
    Oncogene 28:3597-3607(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ECT2 AND PARD6A, MUTAGENESIS OF ASP-72.
  31. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  32. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT PRO-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-7; SER-8 AND THR-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "PKC-? promotes glioblastoma cell survival by phosphorylating and inhibiting BAD through a phosphatidylinositol 3-kinase pathway."
    Desai S., Pillai P., Win-Piazza H., Acevedo-Duncan M.
    Biochim. Biophys. Acta 1813:1190-1197(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BAD.
  35. "Oncogenic activity of Ect2 is regulated through protein kinase C iota-mediated phosphorylation."
    Justilien V., Jameison L., Der C.J., Rossman K.L., Fields A.P.
    J. Biol. Chem. 286:8149-8157(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ECT2.
  36. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-564, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "Solution structure of atypical protein kinase C PB1 domain and its mode of interaction with ZIP/p62 and MEK5."
    Hirano Y., Yoshinaga S., Ogura K., Yokochi M., Noda Y., Sumimoto H., Inagaki F.
    J. Biol. Chem. 279:31883-31890(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 25-108, INTERACTION WITH SQSTM1 AND MAP2K5, MUTAGENESIS OF LYS-29 AND ASP-72.
  38. "Structure of a cell polarity regulator, a complex between atypical PKC and Par6 PB1 domains."
    Hirano Y., Yoshinaga S., Takeya R., Suzuki N.N., Horiuchi M., Kohjima M., Sumimoto H., Inagaki F.
    J. Biol. Chem. 280:9653-9661(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 25-108 IN COMPLEX WITH PARD6A, MUTAGENESIS OF ASP-72; GLU-85 AND ARG-91.
  39. "Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif."
    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) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 233-596, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT THR-412 AND THR-564.
  40. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-118 AND CYS-130.

Entry informationi

Entry nameiKPCI_HUMAN
AccessioniPrimary (citable) accession number: P41743
Secondary accession number(s): D3DNQ4, Q8WW06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 16, 2009
Last modified: September 3, 2014
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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