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Protein

Protein kinase C iota type

Gene

PRKCI

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.By similarity1 Publication

Kineticsi

  1. KM=13.5 µM for ATP (for recombinant purified PRKCI)1 Publication
  1. Vmax=7.4 pmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei283 – 2831ATPPROSITE-ProRule annotation
Active sitei378 – 3781Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri140 – 19051Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi260 – 2689ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • phospholipid binding Source: UniProtKB
  • protein kinase activity Source: UniProtKB
  • protein kinase C activity Source: BHF-UCL
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • actin filament organization Source: Ensembl
  • bicellular tight junction assembly Source: Reactome
  • cell-cell junction organization Source: UniProtKB
  • cell migration Source: Ensembl
  • cellular response to insulin stimulus Source: BHF-UCL
  • cytoskeleton organization Source: UniProtKB
  • establishment of apical/basal cell polarity Source: Ensembl
  • establishment or maintenance of epithelial cell apical/basal polarity Source: UniProtKB
  • eye photoreceptor cell development Source: Ensembl
  • Golgi vesicle budding Source: Ensembl
  • intracellular signal transduction Source: GO_Central
  • membrane organization Source: UniProtKB
  • negative regulation of apoptotic process Source: Reactome
  • negative regulation of glial cell apoptotic process Source: UniProtKB
  • negative regulation of neuron apoptotic process Source: UniProtKB
  • peptidyl-serine phosphorylation Source: GO_Central
  • positive regulation of endothelial cell apoptotic process Source: UniProtKB
  • positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
  • positive regulation of glial cell proliferation Source: UniProtKB
  • positive regulation of glucose import Source: BHF-UCL
  • positive regulation of neuron projection development Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • protein targeting to membrane Source: UniProtKB
  • response to interleukin-1 Source: Ensembl
  • secretion Source: UniProtKB
  • 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.
ReactomeiR-HSA-209543. p75NTR recruits signalling complexes.
R-HSA-420029. Tight junction interactions.
SignaLinkiP41743.
SIGNORiP41743.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:9404. PRKCI.

Subcellular locationi

  • Cytoplasm 3 Publications
  • Membrane 1 Publication
  • Endosome 1 Publication
  • Nucleus 2 Publications

  • 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.2 Publications

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • bicellular tight junction Source: Ensembl
  • cell leading edge Source: Ensembl
  • cytoplasm Source: HPA
  • cytosol Source: UniProtKB
  • endosome Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • Golgi membrane Source: Ensembl
  • intercellular bridge Source: HPA
  • microtubule cytoskeleton Source: HPA
  • nucleus Source: UniProtKB
  • plasma membrane Source: Reactome
  • protein complex Source: Ensembl
  • Schmidt-Lanterman incisure Source: Ensembl
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.

Chemistry

ChEMBLiCHEMBL2093867.
DrugBankiDB00675. Tamoxifen.
GuidetoPHARMACOLOGYi1490.

Polymorphism and mutation databases

BioMutaiPRKCI.
DMDMi239938658.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 596595Protein kinase C iota typePRO_0000055710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylprolineCombined sources
Modified residuei3 – 31PhosphothreonineCombined sources
Modified residuei7 – 71PhosphoserineCombined sources
Modified residuei8 – 81PhosphoserineCombined sources
Modified residuei9 – 91PhosphothreonineCombined sources
Modified residuei265 – 2651Phosphotyrosine; by SRC2 Publications
Modified residuei280 – 2801Phosphotyrosine; by SRC1 Publication
Modified residuei334 – 3341Phosphotyrosine; by SRC1 Publication
Modified residuei412 – 4121Phosphothreonine; by PDPK11 Publication
Modified residuei564 – 5641PhosphothreonineCombined sources1 Publication

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.By similarity4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP41743.
MaxQBiP41743.
PaxDbiP41743.
PeptideAtlasiP41743.
PRIDEiP41743.

PTM databases

iPTMnetiP41743.
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

BgeeiENSG00000163558.
CleanExiHS_PRKCI.
GenevisibleiP41743. HS.

Organism-specific databases

HPAiHPA026574.
HPA038635.

Interactioni

Subunit structurei

Forms a complex with SQSTM1 and MP2K5 (By similarity). Interacts directly with SQSTM1 (Probable). 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). Interacts with VAMP2 (PubMed:17313651). Interacts with WDFY2 (via WD repeats 1-3) (PubMed:16792529).By similarityCurated17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC42P609535EBI-286199,EBI-81752
ELF3P785452EBI-286199,EBI-1057285
MARK4Q96L342EBI-286199,EBI-302319
PARD3Q8TEW03EBI-286199,EBI-81968
PARD6AQ9NPB612EBI-286199,EBI-81876
PARD6BQ9BYG511EBI-286199,EBI-295391
PARD6GQ9BYG45EBI-286199,EBI-295417
PNMA1Q8ND902EBI-286199,EBI-302345
PRKCZQ055134EBI-286199,EBI-295351
RAC1P630003EBI-286199,EBI-413628
SOX2P484312EBI-286199,EBI-6124081
SQSTM1Q135015EBI-286199,EBI-307104
YWHAHQ049173EBI-286199,EBI-306940

Protein-protein interaction databases

BioGridi111570. 81 interactions.
DIPiDIP-31311N.
IntActiP41743. 51 interactions.
MINTiMINT-5004219.
STRINGi9606.ENSP00000295797.

Chemistry

BindingDBiP41743.

Structurei

Secondary structure

1
596
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 327Combined sources
Beta strandi35 – 417Combined sources
Helixi47 – 5711Combined sources
Beta strandi67 – 715Combined sources
Beta strandi73 – 753Combined sources
Beta strandi77 – 793Combined sources
Helixi83 – 9513Combined sources
Beta strandi101 – 1066Combined sources
Helixi251 – 2533Combined sources
Beta strandi254 – 2629Combined sources
Beta strandi264 – 27310Combined sources
Turni274 – 2774Combined sources
Beta strandi278 – 2869Combined sources
Helixi287 – 2893Combined sources
Helixi293 – 30816Combined sources
Turni309 – 3113Combined sources
Beta strandi318 – 3236Combined sources
Beta strandi325 – 3328Combined sources
Helixi340 – 3478Combined sources
Helixi352 – 37120Combined sources
Helixi381 – 3833Combined sources
Beta strandi384 – 3863Combined sources
Beta strandi388 – 3903Combined sources
Beta strandi392 – 3943Combined sources
Helixi397 – 3993Combined sources
Helixi417 – 4193Combined sources
Helixi422 – 4254Combined sources
Helixi433 – 44816Combined sources
Turni452 – 4576Combined sources
Helixi467 – 47610Combined sources
Helixi487 – 49610Combined sources
Turni501 – 5033Combined sources
Turni505 – 5073Combined sources
Turni509 – 5113Combined sources
Helixi512 – 5176Combined sources
Helixi520 – 5223Combined sources
Helixi527 – 5315Combined sources
Turni545 – 5473Combined sources
Helixi549 – 5513Combined sources
Helixi554 – 5574Combined sources
Helixi568 – 5714Combined sources
Helixi576 – 5794Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41743.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 10884PB1PROSITE-ProRule annotationAdd
BLAST
Domaini254 – 522269Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini523 – 59472AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 253252Regulatory domainAdd
BLAST
Regioni2 – 2827Required for interaction with RAB2Add
BLAST
Regioni72 – 9120Interaction with PARD6AAdd
BLAST

Motif

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

Domaini

The PB1 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 AGC-kinase C-terminal domain.Curated
Contains 1 PB1 domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri140 – 19051Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0695. Eukaryota.
ENOG410ZMG2. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP41743.
KOiK06069.
OMAiKLVTVEC.
OrthoDBiEOG091G03Q9.
PhylomeDBiP41743.
TreeFamiTF102004.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR000270. PB1_dom.
IPR002219. PE/DAG-bd.
IPR012233. PKC.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
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.
PS51745. PB1. 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

        10         20         30         40         50
MPTQRDSSTM SHTVAGGGSG DHSHQVRVKA YYRGDIMITH FEPSISFEGL
60 70 80 90 100
CNEVRDMCSF DNEQLFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE
110 120 130 140 150
LLIHVFPCVP ERPGMPCPGE DKSIYRRGAR RWRKLYCANG HTFQAKRFNR
160 170 180 190 200
RAHCAICTDR IWGLGRQGYK CINCKLLVHK KCHKLVTIEC GRHSLPQEPV
210 220 230 240 250
MPMDQSSMHS DHAQTVIPYN PSSHESLDQV GEEKEAMNTR ESGKASSSLG
260 270 280 290 300
LQDFDLLRVI GRGSYAKVLL VRLKKTDRIY AMKVVKKELV NDDEDIDWVQ
310 320 330 340 350
TEKHVFEQAS NHPFLVGLHS CFQTESRLFF VIEYVNGGDL MFHMQRQRKL
360 370 380 390 400
PEEHARFYSA EISLALNYLH ERGIIYRDLK LDNVLLDSEG HIKLTDYGMC
410 420 430 440 450
KEGLRPGDTT STFCGTPNYI APEILRGEDY GFSVDWWALG VLMFEMMAGR
460 470 480 490 500
SPFDIVGSSD NPDQNTEDYL FQVILEKQIR IPRSLSVKAA SVLKSFLNKD
510 520 530 540 550
PKERLGCHPQ TGFADIQGHP FFRNVDWDMM EQKQVVPPFK PNISGEFGLD
560 570 580 590
NFDSQFTNEP VQLTPDDDDI VRKIDQSEFE GFEYINPLLM SAEECV
Length:596
Mass (Da):68,262
Last modified:June 16, 2009 - v2
Checksum:i1E3F8C1D4BFC734F
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti485 – 4851L → M in AAH22016 (PubMed:15489334).Curated
Sequence conflicti508 – 5081H → L in AAH22016 (PubMed:15489334).Curated
Sequence conflicti560 – 5601P → R in AAH22016 (PubMed:15489334).Curated

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
Corresponds to variant rs56154494 [ dbSNP | Ensembl ].
VAR_042323

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111570. 81 interactions.
DIPiDIP-31311N.
IntActiP41743. 51 interactions.
MINTiMINT-5004219.
STRINGi9606.ENSP00000295797.

Chemistry

BindingDBiP41743.
ChEMBLiCHEMBL2093867.
DrugBankiDB00675. Tamoxifen.
GuidetoPHARMACOLOGYi1490.

PTM databases

iPTMnetiP41743.
PhosphoSiteiP41743.

Polymorphism and mutation databases

BioMutaiPRKCI.
DMDMi239938658.

Proteomic databases

EPDiP41743.
MaxQBiP41743.
PaxDbiP41743.
PeptideAtlasiP41743.
PRIDEiP41743.

Protocols and materials databases

DNASUi5584.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295797; ENSP00000295797; ENSG00000163558.
GeneIDi5584.
KEGGihsa:5584.
UCSCiuc003fgs.3. human.

Organism-specific databases

CTDi5584.
GeneCardsiPRKCI.
HGNCiHGNC:9404. PRKCI.
HPAiHPA026574.
HPA038635.
MIMi600539. gene.
neXtProtiNX_P41743.
PharmGKBiPA33768.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0695. Eukaryota.
ENOG410ZMG2. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP41743.
KOiK06069.
OMAiKLVTVEC.
OrthoDBiEOG091G03Q9.
PhylomeDBiP41743.
TreeFamiTF102004.

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
ReactomeiR-HSA-209543. p75NTR recruits signalling complexes.
R-HSA-420029. Tight junction interactions.
SignaLinkiP41743.
SIGNORiP41743.

Miscellaneous databases

ChiTaRSiPRKCI. human.
EvolutionaryTraceiP41743.
GeneWikiiPRKCI.
GenomeRNAii5584.
PROiP41743.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163558.
CleanExiHS_PRKCI.
GenevisibleiP41743. HS.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR000270. PB1_dom.
IPR002219. PE/DAG-bd.
IPR012233. PKC.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
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.
PS51745. PB1. 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]
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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 7, 2016
This is version 186 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.