P17252 (KPCA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein kinase C alpha type
Short name=PKC-alpha
Short name=PKC-A
EC=2.7.11.13

Gene names

Name:	PRKCA
Synonyms:	PKCA, PRKACA

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	672 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. May play a role in cell motility by phosphorylating CSPG4. Ref.9 PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Binds 3 calcium ions per subunit. The ions are bound to the C2 domain By similarity.
Subunit structure	Interacts with ADAP1/CENTA1, CSPG4 and PRKCABP. Binds to SDPR in the presence of phosphatidylserine. Interacts with PICK1 (via PDZ domain). Interacts with TRIM41. Ref.9 Ref.7 Ref.8 Ref.13
Subcellular location	Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 C2 domain. Contains 2 phorbol-ester/DAG-type zinc fingers. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	ATP-binding Calcium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	induction of apoptosis by extracellular signals Traceable author statement. Source: ProtInc response to interleukin-1 Inferred from mutant phenotype. Source: BHF-UCL
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB plasma membrane Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW histone kinase activity (H3-T6 specific) Inferred from direct assay. Source: UniProtKB protein binding Ref.7 Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRIM41	Q8WV44	1	EBI-1383528,EBI-725997

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 672

671

Protein kinase C alpha type

PRO_0000055679

Regions

Domain

172 – 260

89

C2

Domain

339 – 597

259

Protein kinase

Domain

598 – 668

71

AGC-kinase C-terminal

Zinc finger

36 – 86

51

Phorbol-ester/DAG-type 1

Zinc finger

101 – 151

51

Phorbol-ester/DAG-type 2

Nucleotide binding

345 – 353

9

ATP By similarity

Sites

Active site

463

1

Proton acceptor By similarity

Metal binding

186

1

Calcium 1; via carbonyl oxygen By similarity

Metal binding

187

1

Calcium 1 By similarity

Metal binding

187

1

Calcium 2 By similarity

Metal binding

193

1

Calcium 2 By similarity

Metal binding

246

1

Calcium 1 By similarity

Metal binding

246

1

Calcium 2 By similarity

Metal binding

247

1

Calcium 2; via carbonyl oxygen By similarity

Metal binding

248

1

Calcium 1 By similarity

Metal binding

248

1

Calcium 2 By similarity

Metal binding

248

1

Calcium 3 By similarity

Metal binding

252

1

Calcium 3; via carbonyl oxygen By similarity

Metal binding

254

1

Calcium 1 By similarity

Metal binding

254

1

Calcium 3 By similarity

Binding site

195

1

Inositol phosphate group By similarity

Binding site

245

1

Inositol phosphate group By similarity

Binding site

368

1

ATP By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.19

Modified residue

195

1

Phosphotyrosine Ref.12

Modified residue

208

1

Phosphoserine Ref.16

Modified residue

226

1

Phosphoserine Ref.16 Ref.10 Ref.14 Ref.17 Ref.20

Modified residue

319

1

Phosphoserine Ref.16 Ref.10 Ref.11 Ref.15

Modified residue

494

1

Phosphothreonine By similarity

Modified residue

495

1

Phosphothreonine By similarity

Modified residue

497

1

Phosphothreonine Ref.16 Ref.14

Modified residue

501

1

Phosphothreonine Ref.14

Modified residue

604

1

N6-acetyllysine Ref.21

Modified residue

628

1

N6-acetyllysine Ref.21

Modified residue

631

1

Phosphothreonine; by autocatalysis Potential

Modified residue

638

1

Phosphothreonine; by autocatalysis Ref.14

Modified residue

657

1

Phosphoserine By similarity

Modified residue

658

1

Phosphotyrosine Ref.14

Natural variations

Natural variant

98

1

P → S in a colorectal adenocarcinoma sample; somatic mutation. Ref.23

VAR_042301

Natural variant

467

1

D → N in a glioblastoma multiforme sample; somatic mutation. Ref.23

VAR_042302

Natural variant

489

1

M → V. [dbSNP:rs34406842] Ref.23

VAR_042303

Natural variant

568

1

I → V. [dbSNP:rs6504459] Ref.2

VAR_050558

Experimental info

Sequence conflict

50

1

C → S in AAA60098. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

672

Helix Strand Turn

Details...

Turn

98 – 100

3

Beta strand

105 – 107

3

Beta strand

116 – 118

3

Beta strand

125 – 127

3

Beta strand

129 – 131

3

Beta strand

133 – 135

3

Beta strand

138 – 140

3

Turn

141 – 146

6

Sequences

	Sequence		Length	Mass (Da)
	P17252-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 8780DD50388C12DA	FASTA	672	76,764
	10 20 30 40 50 60 MADVFPGNDS TASQDVANRF ARKGALRQKN VHEVKDHKFI ARFFKQPTFC SHCTDFIWGF 70 80 90 100 110 120 GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPDTDDPRS KHKFKIHTYG SPTFCDHCGS 130 140 150 160 170 180 LLYGLIHQGM KCDTCDMNVH KQCVINVPSL CGMDHTEKRG RIYLKAEVAD EKLHVTVRDA 190 200 210 220 230 240 KNLIPMDPNG LSDPYVKLKL IPDPKNESKQ KTKTIRSTLN PQWNESFTFK LKPSDKDRRL 250 260 270 280 290 300 SVEIWDWDRT TRNDFMGSLS FGVSELMKMP ASGWYKLLNQ EEGEYYNVPI PEGDEEGNME 310 320 330 340 350 360 LRQKFEKAKL GPAGNKVISP SEDRKQPSNN LDRVKLTDFN FLMVLGKGSF GKVMLADRKG 370 380 390 400 410 420 TEELYAIKIL KKDVVIQDDD VECTMVEKRV LALLDKPPFL TQLHSCFQTV DRLYFVMEYV 430 440 450 460 470 480 NGGDLMYHIQ QVGKFKEPQA VFYAAEISIG LFFLHKRGII YRDLKLDNVM LDSEGHIKIA 490 500 510 520 530 540 DFGMCKEHMM DGVTTRTFCG TPDYIAPEII AYQPYGKSVD WWAYGVLLYE MLAGQPPFDG 550 560 570 580 590 600 EDEDELFQSI MEHNVSYPKS LSKEAVSICK GLMTKHPAKR LGCGPEGERD VREHAFFRRI 610 620 630 640 650 660 DWEKLENREI QPPFKPKVCG KGAENFDKFF TRGQPVLTPP DQLVIANIDQ SDFEGFSYVN 670 PQFVHPILQS AV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of human protein kinase C alpha." Finkenzeller G., Marme D., Hug H. Nucleic Acids Res. 18:2183-2183(1990) [PubMed: 2336401] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Blood.
[2]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-568.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Phorbol diester-induced alterations in the expression of protein kinase C isozymes and their mRNAs. Analysis in wild-type and phorbol diester-resistant HL-60 cell clones." McSwine-Kennick R.L., McKeegan E.M., Johnson M.D., Morin M.J. J. Biol. Chem. 266:15135-15143(1991) [PubMed: 1714454] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-445.
[5]	"Homo sapiens protein kinase C alpha 5-flanking sequence." Haridasse V., Hackenbruck J., Glazer R.I. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
[6]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-19. Tissue: Platelet.
[7]	"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: 12893243] [Abstract] Cited for: INTERACTION WITH ADAP1.
[8]	"The PDZ domain of PICK1 differentially accepts protein kinase C-alpha and GluR2 as interacting ligands." Dev K.K., Nakanishi S., Henley J.M. J. Biol. Chem. 279:41393-41397(2004) [PubMed: 15247289] [Abstract] Cited for: INTERACTION WITH PICK1.
[9]	"Phosphorylation of NG2 proteoglycan by protein kinase C-alpha regulates polarized membrane distribution and cell motility." Makagiansar I.T., Williams S., Dahlin-Huppe K., Fukushi J., Mustelin T., Stallcup W.B. J. Biol. Chem. 279:55262-55270(2004) [PubMed: 15504744] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CSPG4, INTERACTION WITH CSPG4.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-319, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-195, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[13]	"Amplitude control of protein kinase C by RINCK, a novel E3 ubiquitin ligase." Chen D., Gould C., Garza R., Gao T., Hampton R.Y., Newton A.C. J. Biol. Chem. 282:33776-33787(2007) [PubMed: 17893151] [Abstract] Cited for: INTERACTION WITH TRIM41.
[14]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; THR-497; THR-501; THR-638 AND TYR-658, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, MASS SPECTROMETRY. Tissue: Platelet.
[16]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208; SER-226; SER-319 AND THR-497, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[21]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-604 AND LYS-628, MASS SPECTROMETRY.
[22]	"Solution structure of the second phorbol esters/diacylglycerol binding domain of human protein kinase C alpha type." RIKEN structural genomics initiative (RSGI) Submitted (APR-2008) to the PDB data bank Cited for: STRUCTURE BY NMR OF 88-169.
[23]	"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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-98; ASN-467 AND VAL-489.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X52479 mRNA. Translation: CAA36718.1.
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.
BC109273 mRNA. Translation: AAI09274.1.
BC109274 mRNA. Translation: AAI09275.1.
M22199 mRNA. Translation: AAA60098.1.
AF395829 Genomic DNA. Translation: AAK84184.1.

IPI

IPI00385449.

PIR

KIHUCA. S09496.

RefSeq

NP_002728.1.

UniGene

Hs.531704.
Hs.708867.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ELI	NMR	-	A	92-169	[»]
3IW4	X-ray	2.80	A/B/C	320-672	[»]

ProteinModelPortal

P17252.

SMR

P17252. Positions 37-106, 156-292.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-531N.

IntAct

P17252. 3 interactions.

MINT

MINT-140812.

STRING

P17252.

PTM databases

PhosphoSite

P17252.

Proteomic databases

PRIDE

P17252.

Genome annotation databases

Ensembl

ENST00000284384; ENSP00000284384; ENSG00000154229; Homo sapiens. [Genome view]

GeneID

5578.

KEGG

hsa:5578.

UCSC

uc002jfp.1. human.

Organism-specific databases

CTD

5578.

GeneCards

GC17P064298.

H-InvDB

HIX0014097.

HGNC

HGNC:9393. PRKCA.

HPA

CAB003844.
CAB016290.
HPA006563.
HPA006564.

MIM

176960. gene.

PharmGKB

PA33759.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05005.

HOGENOM

HBG755340.

HOVERGEN

HBG108317.

InParanoid

P17252.

PhylomeDB

P17252.

Enzyme and pathway databases

BRENDA

2.7.11.13. 247.

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
nfkappabcanonicalpathway. Canonical NF-kappaB pathway.
cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
endothelinpathway. Endothelins.
tcrraspathway. Ras signaling in the CD4+ TCR pathway.
retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
ret_pathway. Signaling events regulated by Ret tyrosine kinase.
syndecan_4_pathway. Syndecan-4-mediated signaling events.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.
txa2pathway. Thromboxane A2 receptor signaling.
vegfr1_pathway. VEGFR1 specific signals.

Reactome

REACT_11061. Signalling by NGF.
REACT_13685. Synaptic Transmission.
REACT_14797. Signaling by GPCR.
REACT_1505. Integration of energy metabolism.
REACT_15295. Opioid Signalling.
REACT_15380. Diabetes pathways.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P17252.

Bgee

P17252.

CleanEx

HS_PRKACA.
HS_PRKCA.

Genevestigator

P17252.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR020477. C2_region.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR015745. PKC.
IPR017892. Pkinase_C.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]

PANTHER

PTHR22985:SF86. PKC. 1 hit.

Pfam

PF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000550. PKC_alpha. 1 hit.

PRINTS

PR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.

SMART

SM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF49562. C2_CaLB. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS51285. 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]

ProtoNet

Search...

Other Resources

BindingDB

P17252.

DrugBank

DB00144. Phosphatidylserine.
DB00163. Vitamin E.

NextBio

21628.

PMAP-CutDB

P17252.

SOURCE

Search...

Entry information

Entry name

KPCA_HUMAN

Accession

Primary (citable) accession number: P17252
Secondary accession number(s): Q15137, Q32M72, Q96RE4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	August 10, 2010
This is version 130 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.