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Protein

Protein kinase C alpha type

Gene

PRKCA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription.15 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Ca2+By similarityNote: Binds 3 Ca2+ ions per subunit. The ions are bound to the C2 domain.By similarity

Enzyme regulationi

Classical (or conventional) PKCs (PRKCA, PRKCB and PRKCG) are activated by calcium and diacylglycerol (DAG) in the presence of phosphatidylserine. Three specific sites; Thr-497 (activation loop of the kinase domain), Thr-638 (turn motif) and Ser-657 (hydrophobic region), need to be phosphorylated for its full activation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi186 – 1861Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi187 – 1871Calcium 1By similarity
Metal bindingi187 – 1871Calcium 2By similarity
Metal bindingi193 – 1931Calcium 2By similarity
Binding sitei195 – 1951Inositol phosphate groupBy similarity
Binding sitei245 – 2451Inositol phosphate groupBy similarity
Metal bindingi246 – 2461Calcium 1By similarity
Metal bindingi246 – 2461Calcium 2By similarity
Metal bindingi247 – 2471Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi248 – 2481Calcium 1By similarity
Metal bindingi248 – 2481Calcium 2By similarity
Metal bindingi248 – 2481Calcium 3By similarity
Metal bindingi252 – 2521Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi254 – 2541Calcium 1By similarity
Metal bindingi254 – 2541Calcium 3By similarity
Binding sitei368 – 3681ATPPROSITE-ProRule annotation
Active sitei463 – 4631Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri36 – 8651Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri101 – 15151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi345 – 3539ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • activation of adenylate cyclase activity Source: BHF-UCL
  • angiogenesis Source: UniProtKB-KW
  • apoptotic signaling pathway Source: ProtInc
  • cell adhesion Source: UniProtKB-KW
  • desmosome assembly Source: BHF-UCL
  • histone H3-T6 phosphorylation Source: UniProtKB
  • intracellular signal transduction Source: GO_Central
  • mitotic nuclear envelope disassembly Source: Reactome
  • negative regulation of adenylate cyclase activity Source: BHF-UCL
  • negative regulation of glial cell apoptotic process Source: UniProtKB
  • peptidyl-serine phosphorylation Source: GO_Central
  • platelet activation Source: Reactome
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of blood vessel endothelial cell migration Source: DFLAT
  • positive regulation of cardiac muscle hypertrophy Source: UniProtKB
  • positive regulation of cell adhesion Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of dense core granule biogenesis Source: UniProtKB
  • positive regulation of endothelial cell migration Source: UniProtKB
  • positive regulation of endothelial cell proliferation Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  • positive regulation of macrophage differentiation Source: UniProtKB
  • positive regulation of mitotic cell cycle Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of insulin secretion Source: Reactome
  • regulation of mRNA stability Source: Reactome
  • regulation of platelet aggregation Source: UniProtKB
  • response to interleukin-1 Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Angiogenesis, Apoptosis, Cell adhesion

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
ReactomeiR-HSA-111933. Calmodulin induced events.
R-HSA-114516. Disinhibition of SNARE formation.
R-HSA-1433557. Signaling by SCF-KIT.
R-HSA-1433559. Regulation of KIT signaling.
R-HSA-2179392. EGFR Transactivation by Gastrin.
R-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-HSA-3000170. Syndecan interactions.
R-HSA-399997. Acetylcholine regulates insulin secretion.
R-HSA-4086398. Ca2+ pathway.
R-HSA-416993. Trafficking of GluR2-containing AMPA receptors.
R-HSA-418597. G alpha (z) signalling events.
R-HSA-4419969. Depolymerisation of the Nuclear Lamina.
R-HSA-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-HSA-5099900. WNT5A-dependent internalization of FZD4.
R-HSA-5218921. VEGFR2 mediated cell proliferation.
R-HSA-76005. Response to elevated platelet cytosolic Ca2+.
SignaLinkiP17252.
SIGNORiP17252.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C alpha type (EC:2.7.11.13)
Short name:
PKC-A
Short name:
PKC-alpha
Gene namesi
Name:PRKCA
Synonyms:PKCA, PRKACA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:9393. PRKCA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: BHF-UCL
  • extracellular exosome Source: UniProtKB
  • mitochondrial membrane Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
  • nucleoplasm Source: Reactome
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA33759.

Chemistry

ChEMBLiCHEMBL2096620.
DrugBankiDB05013. Ingenol Mebutate.
DB00144. Phosphatidylserine.
DB00675. Tamoxifen.
DB00163. Vitamin E.
GuidetoPHARMACOLOGYi1482.

Polymorphism and mutation databases

BioMutaiPRKCA.
DMDMi317373571.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 672671Protein kinase C alpha typePRO_0000055679Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei10 – 101PhosphoserineCombined sources
Modified residuei226 – 2261PhosphoserineCombined sources
Modified residuei319 – 3191PhosphoserineBy similarity
Modified residuei497 – 4971Phosphothreonine; by PDPK1Curated
Modified residuei628 – 6281N6-acetyllysineCombined sources
Modified residuei631 – 6311Phosphothreonine; by autocatalysisSequence analysis
Modified residuei638 – 6381Phosphothreonine; by autocatalysisCombined sources
Modified residuei651 – 6511PhosphoserineCombined sources
Modified residuei657 – 6571PhosphoserineCombined sources
Modified residuei658 – 6581Phosphotyrosine; by SYKBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP17252.
MaxQBiP17252.
PaxDbiP17252.
PeptideAtlasiP17252.
PRIDEiP17252.

PTM databases

iPTMnetiP17252.
PhosphoSiteiP17252.
SwissPalmiP17252.

Miscellaneous databases

PMAP-CutDBP17252.

Expressioni

Gene expression databases

BgeeiENSG00000154229.
CleanExiHS_PRKACA.
HS_PRKCA.
ExpressionAtlasiP17252. baseline and differential.
GenevisibleiP17252. HS.

Organism-specific databases

HPAiCAB003844.
CAB016290.
HPA006563.
HPA006564.

Interactioni

Subunit structurei

Recruited in a circadian manner into a nuclear complex which also includes BMAL1 and RACK1 (By similarity). Interacts with ADAP1/CENTA1, CSPG4 and PRKCABP. Binds to SDPR in the presence of phosphatidylserine. Interacts with PICK1 (via PDZ domain). Interacts with TRIM41.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EGFRP005332EBI-1383528,EBI-297353
HDAC6Q9UBN72EBI-1383528,EBI-301697
inaDQ240082EBI-1383528,EBI-195326From a different organism.
SDC4P314312EBI-1383528,EBI-3913237
UBCP0CG482EBI-1383528,EBI-3390054

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi111564. 150 interactions.
DIPiDIP-531N.
IntActiP17252. 33 interactions.
MINTiMINT-140812.
STRINGi9606.ENSP00000408695.

Chemistry

BindingDBiP17252.

Structurei

Secondary structure

1
672
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni98 – 1003Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi138 – 1403Combined sources
Turni141 – 1466Combined sources
Beta strandi161 – 1699Combined sources
Beta strandi172 – 18211Combined sources
Beta strandi194 – 2029Combined sources
Beta strandi222 – 2309Combined sources
Helixi233 – 2375Combined sources
Beta strandi239 – 2468Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi254 – 2629Combined sources
Helixi263 – 2686Combined sources
Beta strandi271 – 2766Combined sources
Helixi282 – 2843Combined sources
Helixi336 – 3383Combined sources
Beta strandi339 – 35012Combined sources
Beta strandi352 – 36110Combined sources
Beta strandi364 – 3718Combined sources
Helixi372 – 3776Combined sources
Helixi381 – 39212Combined sources
Beta strandi403 – 4086Combined sources
Beta strandi410 – 4178Combined sources
Beta strandi422 – 4243Combined sources
Helixi425 – 4328Combined sources
Helixi437 – 45620Combined sources
Helixi466 – 4683Combined sources
Beta strandi469 – 4713Combined sources
Beta strandi477 – 4793Combined sources
Helixi502 – 5043Combined sources
Helixi507 – 5104Combined sources
Helixi518 – 53316Combined sources
Helixi543 – 55210Combined sources
Helixi563 – 57210Combined sources
Helixi577 – 5793Combined sources
Helixi587 – 5937Combined sources
Helixi595 – 5973Combined sources
Helixi602 – 6065Combined sources
Helixi642 – 6465Combined sources
Helixi650 – 6534Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ELINMR-A93-169[»]
3IW4X-ray2.80A/B/C320-672[»]
4DNLX-ray1.90A155-293[»]
4RA4X-ray2.63A318-672[»]
ProteinModelPortaliP17252.
SMRiP17252. Positions 37-670.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17252.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini172 – 26089C2PROSITE-ProRule annotationAdd
BLAST
Domaini339 – 597259Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini598 – 66871AGC-kinase C-terminalAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri36 – 8651Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri101 – 15151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP17252.
KOiK02677.
OMAiQSKKDMI.
OrthoDBiEOG091G0QRS.
PhylomeDBiP17252.
TreeFamiTF351133.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000550. PKC_alpha. 1 hit.
PRINTSiPR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. 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. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P17252-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADVFPGNDS TASQDVANRF ARKGALRQKN VHEVKDHKFI ARFFKQPTFC
60 70 80 90 100
SHCTDFIWGF GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPDTDDPRS
110 120 130 140 150
KHKFKIHTYG SPTFCDHCGS LLYGLIHQGM KCDTCDMNVH KQCVINVPSL
160 170 180 190 200
CGMDHTEKRG RIYLKAEVAD EKLHVTVRDA KNLIPMDPNG LSDPYVKLKL
210 220 230 240 250
IPDPKNESKQ KTKTIRSTLN PQWNESFTFK LKPSDKDRRL SVEIWDWDRT
260 270 280 290 300
TRNDFMGSLS FGVSELMKMP ASGWYKLLNQ EEGEYYNVPI PEGDEEGNME
310 320 330 340 350
LRQKFEKAKL GPAGNKVISP SEDRKQPSNN LDRVKLTDFN FLMVLGKGSF
360 370 380 390 400
GKVMLADRKG TEELYAIKIL KKDVVIQDDD VECTMVEKRV LALLDKPPFL
410 420 430 440 450
TQLHSCFQTV DRLYFVMEYV NGGDLMYHIQ QVGKFKEPQA VFYAAEISIG
460 470 480 490 500
LFFLHKRGII YRDLKLDNVM LDSEGHIKIA DFGMCKEHMM DGVTTRTFCG
510 520 530 540 550
TPDYIAPEII AYQPYGKSVD WWAYGVLLYE MLAGQPPFDG EDEDELFQSI
560 570 580 590 600
MEHNVSYPKS LSKEAVSVCK GLMTKHPAKR LGCGPEGERD VREHAFFRRI
610 620 630 640 650
DWEKLENREI QPPFKPKVCG KGAENFDKFF TRGQPVLTPP DQLVIANIDQ
660 670
SDFEGFSYVN PQFVHPILQS AV
Length:672
Mass (Da):76,750
Last modified:January 11, 2011 - v4
Checksum:i9EB157789A062349
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501C → S in AAA60098 (PubMed:1714454).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti98 – 981P → S in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042301
Natural varianti467 – 4671D → N in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_042302
Natural varianti489 – 4891M → V.1 Publication
Corresponds to variant rs34406842 [ dbSNP | Ensembl ].
VAR_042303
Natural varianti568 – 5681V → I.4 Publications
Corresponds to variant rs6504459 [ dbSNP | Ensembl ].
VAR_050558

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52479 mRNA. Translation: CAA36718.1.
AB451258 mRNA. Translation: BAG70072.1.
AB451383 mRNA. Translation: BAG70197.1.
AC005918 Genomic DNA. No translation available.
AC005988 Genomic DNA. No translation available.
AC006263 Genomic DNA. No translation available.
AC006947 Genomic DNA. No translation available.
AC009452 Genomic DNA. No translation available.
AC060796 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89014.1.
BC109273 mRNA. Translation: AAI09274.1.
BC109274 mRNA. Translation: AAI09275.1.
M22199 mRNA. Translation: AAA60098.1.
AF395829 Genomic DNA. Translation: AAK84184.1.
CCDSiCCDS11664.1.
PIRiS09496. KIHUCA.
RefSeqiNP_002728.1. NM_002737.2.
UniGeneiHs.531704.
Hs.708867.

Genome annotation databases

EnsembliENST00000413366; ENSP00000408695; ENSG00000154229.
GeneIDi5578.
KEGGihsa:5578.
UCSCiuc002jfp.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52479 mRNA. Translation: CAA36718.1.
AB451258 mRNA. Translation: BAG70072.1.
AB451383 mRNA. Translation: BAG70197.1.
AC005918 Genomic DNA. No translation available.
AC005988 Genomic DNA. No translation available.
AC006263 Genomic DNA. No translation available.
AC006947 Genomic DNA. No translation available.
AC009452 Genomic DNA. No translation available.
AC060796 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89014.1.
BC109273 mRNA. Translation: AAI09274.1.
BC109274 mRNA. Translation: AAI09275.1.
M22199 mRNA. Translation: AAA60098.1.
AF395829 Genomic DNA. Translation: AAK84184.1.
CCDSiCCDS11664.1.
PIRiS09496. KIHUCA.
RefSeqiNP_002728.1. NM_002737.2.
UniGeneiHs.531704.
Hs.708867.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ELINMR-A93-169[»]
3IW4X-ray2.80A/B/C320-672[»]
4DNLX-ray1.90A155-293[»]
4RA4X-ray2.63A318-672[»]
ProteinModelPortaliP17252.
SMRiP17252. Positions 37-670.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111564. 150 interactions.
DIPiDIP-531N.
IntActiP17252. 33 interactions.
MINTiMINT-140812.
STRINGi9606.ENSP00000408695.

Chemistry

BindingDBiP17252.
ChEMBLiCHEMBL2096620.
DrugBankiDB05013. Ingenol Mebutate.
DB00144. Phosphatidylserine.
DB00675. Tamoxifen.
DB00163. Vitamin E.
GuidetoPHARMACOLOGYi1482.

PTM databases

iPTMnetiP17252.
PhosphoSiteiP17252.
SwissPalmiP17252.

Polymorphism and mutation databases

BioMutaiPRKCA.
DMDMi317373571.

Proteomic databases

EPDiP17252.
MaxQBiP17252.
PaxDbiP17252.
PeptideAtlasiP17252.
PRIDEiP17252.

Protocols and materials databases

DNASUi5578.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000413366; ENSP00000408695; ENSG00000154229.
GeneIDi5578.
KEGGihsa:5578.
UCSCiuc002jfp.2. human.

Organism-specific databases

CTDi5578.
GeneCardsiPRKCA.
HGNCiHGNC:9393. PRKCA.
HPAiCAB003844.
CAB016290.
HPA006563.
HPA006564.
MIMi176960. gene.
neXtProtiNX_P17252.
PharmGKBiPA33759.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP17252.
KOiK02677.
OMAiQSKKDMI.
OrthoDBiEOG091G0QRS.
PhylomeDBiP17252.
TreeFamiTF351133.

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
ReactomeiR-HSA-111933. Calmodulin induced events.
R-HSA-114516. Disinhibition of SNARE formation.
R-HSA-1433557. Signaling by SCF-KIT.
R-HSA-1433559. Regulation of KIT signaling.
R-HSA-2179392. EGFR Transactivation by Gastrin.
R-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-HSA-3000170. Syndecan interactions.
R-HSA-399997. Acetylcholine regulates insulin secretion.
R-HSA-4086398. Ca2+ pathway.
R-HSA-416993. Trafficking of GluR2-containing AMPA receptors.
R-HSA-418597. G alpha (z) signalling events.
R-HSA-4419969. Depolymerisation of the Nuclear Lamina.
R-HSA-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-HSA-5099900. WNT5A-dependent internalization of FZD4.
R-HSA-5218921. VEGFR2 mediated cell proliferation.
R-HSA-76005. Response to elevated platelet cytosolic Ca2+.
SignaLinkiP17252.
SIGNORiP17252.

Miscellaneous databases

ChiTaRSiPRKCA. human.
EvolutionaryTraceiP17252.
GeneWikiiPKC_alpha.
GenomeRNAii5578.
PMAP-CutDBP17252.
PROiP17252.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000154229.
CleanExiHS_PRKACA.
HS_PRKCA.
ExpressionAtlasiP17252. baseline and differential.
GenevisibleiP17252. HS.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000550. PKC_alpha. 1 hit.
PRINTSiPR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. 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. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKPCA_HUMAN
AccessioniPrimary (citable) accession number: P17252
Secondary accession number(s): B5BU22
, Q15137, Q32M72, Q96RE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 11, 2011
Last modified: September 7, 2016
This is version 195 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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.