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P17252

- KPCA_HUMAN

UniProt

P17252 - KPCA_HUMAN

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Protein

Protein kinase C alpha type

Gene

PRKCA

Organism
Homo sapiens (Human)
Status
Reviewed - 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 Ca(2+) 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

  1. ATP binding Source: UniProtKB-KW
  2. calcium-dependent protein kinase C activity Source: Ensembl
  3. enzyme binding Source: BHF-UCL
  4. histone kinase activity (H3-T6 specific) Source: UniProtKB
  5. protein kinase activity Source: UniProtKB
  6. protein kinase C activity Source: BHF-UCL
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. activation of adenylate cyclase activity Source: BHF-UCL
  2. activation of phospholipase C activity Source: Reactome
  3. angiogenesis Source: UniProtKB-KW
  4. apoptotic signaling pathway Source: ProtInc
  5. blood coagulation Source: Reactome
  6. cell adhesion Source: UniProtKB-KW
  7. cellular calcium ion homeostasis Source: Ensembl
  8. cellular response to carbohydrate stimulus Source: Ensembl
  9. chondrocyte differentiation Source: Ensembl
  10. desmosome assembly Source: BHF-UCL
  11. energy reserve metabolic process Source: Reactome
  12. epidermal growth factor receptor signaling pathway Source: Reactome
  13. extracellular matrix organization Source: Reactome
  14. fibroblast growth factor receptor signaling pathway Source: Reactome
  15. gene expression Source: Reactome
  16. histone H3-T6 phosphorylation Source: UniProtKB
  17. inactivation of MAPK activity Source: Ensembl
  18. induction of positive chemotaxis Source: Ensembl
  19. innate immune response Source: Reactome
  20. intrinsic apoptotic signaling pathway Source: Ensembl
  21. mRNA metabolic process Source: Reactome
  22. negative regulation of adenylate cyclase activity Source: BHF-UCL
  23. negative regulation of cell proliferation Source: Ensembl
  24. negative regulation of glial cell apoptotic process Source: UniProtKB
  25. negative regulation of glucose import Source: Ensembl
  26. negative regulation of insulin receptor signaling pathway Source: Ensembl
  27. neurotrophin TRK receptor signaling pathway Source: Reactome
  28. neutrophil chemotaxis Source: Ensembl
  29. peptidyl-serine autophosphorylation Source: Ensembl
  30. phototransduction, visible light Source: Reactome
  31. platelet activation Source: Reactome
  32. positive regulation of angiogenesis Source: UniProtKB
  33. positive regulation of blood vessel endothelial cell migration Source: DFLAT
  34. positive regulation of cardiac muscle hypertrophy Source: UniProtKB
  35. positive regulation of cell adhesion Source: UniProtKB
  36. positive regulation of cell migration Source: UniProtKB
  37. positive regulation of dense core granule biogenesis Source: UniProtKB
  38. positive regulation of endothelial cell migration Source: UniProtKB
  39. positive regulation of endothelial cell proliferation Source: UniProtKB
  40. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  41. positive regulation of inflammatory response Source: Ensembl
  42. positive regulation of lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  43. positive regulation of macrophage differentiation Source: UniProtKB
  44. positive regulation of mitotic cell cycle Source: UniProtKB
  45. positive regulation of protein phosphorylation Source: Ensembl
  46. protein phosphorylation Source: UniProtKB
  47. regulation of insulin secretion Source: Reactome
  48. regulation of muscle contraction Source: Ensembl
  49. regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  50. regulation of platelet aggregation Source: UniProtKB
  51. regulation of rhodopsin mediated signaling pathway Source: Reactome
  52. regulation of the force of heart contraction Source: Ensembl
  53. response to interleukin-1 Source: BHF-UCL
  54. rhodopsin mediated signaling pathway Source: Reactome
  55. RNA metabolic process Source: Reactome
  56. signal transduction Source: Reactome
  57. small molecule metabolic process Source: Reactome
  58. synaptic transmission Source: Reactome
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.
ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_111225. Regulation of KIT signaling.
REACT_1178. Disinhibition of SNARE formation.
REACT_121096. EGFR Transactivation by Gastrin.
REACT_1280. Response to elevated platelet cytosolic Ca2+.
REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_163942. Syndecan interactions.
REACT_172599. WNT5A-dependent internalization of FZD4.
REACT_172761. Ca2+ pathway.
REACT_18405. Acetylcholine regulates insulin secretion.
REACT_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_19333. G alpha (z) signalling events.
REACT_200828. Depolymerisation of the Nuclear Lamina.
REACT_228024. VEGFR2 mediated cell proliferation.
REACT_25218. HuR stabilizes mRNA.
REACT_9000. Calmodulin induced events.
SignaLinkiP17252.

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
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:9393. PRKCA.

Subcellular locationi

GO - Cellular componenti

  1. apical part of cell Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. dendrite Source: Ensembl
  5. endoplasmic reticulum Source: BHF-UCL
  6. extracellular vesicular exosome Source: UniProt
  7. mitochondrion Source: UniProt
  8. neuronal cell body Source: Ensembl
  9. nucleoplasm Source: Reactome
  10. perinuclear region of cytoplasm Source: UniProtKB
  11. photoreceptor outer segment Source: Ensembl
  12. 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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 672671Protein kinase C alpha typePRO_0000055679Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei226 – 2261Phosphoserine3 Publications
Modified residuei250 – 2501Phosphothreonine; by autocatalysis
Modified residuei497 – 4971Phosphothreonine; by PDPK1Curated
Modified residuei628 – 6281N6-acetyllysine1 Publication
Modified residuei631 – 6311Phosphothreonine; by autocatalysisSequence Analysis
Modified residuei638 – 6381Phosphothreonine; by autocatalysis2 Publications
Modified residuei651 – 6511Phosphoserine1 Publication
Modified residuei657 – 6571PhosphoserineBy similarity
Modified residuei658 – 6581Phosphotyrosine; by SYKBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP17252.
PaxDbiP17252.
PRIDEiP17252.

PTM databases

PhosphoSiteiP17252.

Miscellaneous databases

PMAP-CutDBP17252.

Expressioni

Gene expression databases

BgeeiP17252.
CleanExiHS_PRKACA.
HS_PRKCA.
ExpressionAtlasiP17252. baseline and differential.
GenevestigatoriP17252.

Organism-specific databases

HPAiCAB003844.
CAB016290.
HPA006563.
HPA006564.

Interactioni

Subunit structurei

Recruited in a circadian manner into a nuclear complex which also includes BMAL1 and GNB2L1/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

Protein-protein interaction databases

BioGridi111564. 112 interactions.
DIPiDIP-531N.
IntActiP17252. 27 interactions.
MINTiMINT-140812.
STRINGi9606.ENSP00000284384.

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 – 34810Combined sources
Beta strandi351 – 3588Combined sources
Beta strandi364 – 3718Combined sources
Helixi372 – 3776Combined sources
Helixi381 – 39212Combined sources
Beta strandi403 – 4086Combined sources
Beta strandi410 – 4189Combined 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
Turni577 – 5793Combined sources
Helixi587 – 5926Combined sources
Helixi595 – 5973Combined sources
Helixi602 – 6054Combined sources
Turni606 – 6083Combined 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[»]
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

eggNOGiCOG0515.
GeneTreeiENSGT00770000120449.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP17252.
KOiK02677.
OMAiPQFVHPL.
OrthoDBiEOG77M8QM.
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.
IPR002290. Ser/Thr_dual-sp_kinase.
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.
UCSCiuc002jfo.1. human.

Polymorphism databases

DMDMi317373571.

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 .
CCDSi CCDS11664.1.
PIRi S09496. KIHUCA.
RefSeqi NP_002728.1. NM_002737.2.
UniGenei Hs.531704.
Hs.708867.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ELI NMR - A 93-169 [» ]
3IW4 X-ray 2.80 A/B/C 320-672 [» ]
4DNL X-ray 1.90 A 155-293 [» ]
ProteinModelPortali P17252.
SMRi P17252. Positions 37-670.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111564. 112 interactions.
DIPi DIP-531N.
IntActi P17252. 27 interactions.
MINTi MINT-140812.
STRINGi 9606.ENSP00000284384.

Chemistry

BindingDBi P17252.
ChEMBLi CHEMBL2096620.
DrugBanki DB05013. Ingenol Mebutate.
DB00144. Phosphatidylserine.
DB00675. Tamoxifen.
DB00163. Vitamin E.
GuidetoPHARMACOLOGYi 1482.

PTM databases

PhosphoSitei P17252.

Polymorphism databases

DMDMi 317373571.

Proteomic databases

MaxQBi P17252.
PaxDbi P17252.
PRIDEi P17252.

Protocols and materials databases

DNASUi 5578.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000413366 ; ENSP00000408695 ; ENSG00000154229 .
GeneIDi 5578.
KEGGi hsa:5578.
UCSCi uc002jfo.1. human.

Organism-specific databases

CTDi 5578.
GeneCardsi GC17P064298.
HGNCi HGNC:9393. PRKCA.
HPAi CAB003844.
CAB016290.
HPA006563.
HPA006564.
MIMi 176960. gene.
neXtProti NX_P17252.
PharmGKBi PA33759.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120449.
HOGENOMi HOG000233022.
HOVERGENi HBG108317.
InParanoidi P17252.
KOi K02677.
OMAi PQFVHPL.
OrthoDBi EOG77M8QM.
PhylomeDBi P17252.
TreeFami TF351133.

Enzyme and pathway databases

BRENDAi 2.7.11.13. 2681.
Reactomei REACT_111040. Signaling by SCF-KIT.
REACT_111225. Regulation of KIT signaling.
REACT_1178. Disinhibition of SNARE formation.
REACT_121096. EGFR Transactivation by Gastrin.
REACT_1280. Response to elevated platelet cytosolic Ca2+.
REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_163942. Syndecan interactions.
REACT_172599. WNT5A-dependent internalization of FZD4.
REACT_172761. Ca2+ pathway.
REACT_18405. Acetylcholine regulates insulin secretion.
REACT_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_19333. G alpha (z) signalling events.
REACT_200828. Depolymerisation of the Nuclear Lamina.
REACT_228024. VEGFR2 mediated cell proliferation.
REACT_25218. HuR stabilizes mRNA.
REACT_9000. Calmodulin induced events.
SignaLinki P17252.

Miscellaneous databases

ChiTaRSi PRKCA. human.
EvolutionaryTracei P17252.
GeneWikii PKC_alpha.
GenomeRNAii 5578.
NextBioi 21628.
PMAP-CutDB P17252.
PROi P17252.
SOURCEi Search...

Gene expression databases

Bgeei P17252.
CleanExi HS_PRKACA.
HS_PRKCA.
ExpressionAtlasi P17252. baseline and differential.
Genevestigatori P17252.

Family and domain databases

Gene3Di 2.60.40.150. 1 hit.
InterProi IPR000961. 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.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000550. PKC_alpha. 1 hit.
PRINTSi PR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTi SM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-568.
    Tissue: Blood.
  2. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-568.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-568.
  5. "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], VARIANT ILE-568.
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-445.
  7. "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.
  8. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19.
    Tissue: Platelet.
  9. "A functional role for mitochondrial protein kinase Calpha in Bcl2 phosphorylation and suppression of apoptosis."
    Ruvolo P.P., Deng X., Carr B.K., May W.S.
    J. Biol. Chem. 273:25436-25442(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS, SUBCELLULAR LOCATION.
  10. "Protein kinase C-alpha modulates lipopolysaccharide-induced functions in a murine macrophage cell line."
    St-Denis A., Chano F., Tremblay P., St-Pierre Y., Descoteaux A.
    J. Biol. Chem. 273:32787-32792(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INFLAMMATORY RESPONSE.
  11. "Interleukin-1-induced nuclear factor-kappaB-IkappaBalpha autoregulatory feedback loop in hepatocytes. A role for protein kinase calpha in post-transcriptional regulation of ikappabalpha resynthesis."
    Han Y., Meng T., Murray N.R., Fields A.P., Brasier A.R.
    J. Biol. Chem. 274:939-947(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INFLAMMATORY RESPONSE.
  12. "Induction of p53-dependent, insulin-like growth factor-binding protein-3-mediated apoptosis in glioblastoma multiforme cells by a protein kinase Calpha antisense oligonucleotide."
    Shen L., Dean N.M., Glazer R.I.
    Mol. Pharmacol. 55:396-402(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS.
  13. "Involvement of p21(Waf1/Cip1) in protein kinase C alpha-induced cell cycle progression."
    Besson A., Yong V.W.
    Mol. Cell. Biol. 20:4580-4590(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL CYCLE PROGRESSION.
  14. "Inhibition of protein kinase Calpha prevents endothelial cell migration and vascular tube formation in vitro and myocardial neovascularization in vivo."
    Wang A., Nomura M., Patan S., Ware J.A.
    Circ. Res. 90:609-616(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANGIOGENESIS.
  15. "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.
  16. "Direct demonstration of involvement of protein kinase Calpha in the Ca2+-induced platelet aggregation."
    Tabuchi A., Yoshioka A., Higashi T., Shirakawa R., Nishioka H., Kita T., Horiuchi H.
    J. Biol. Chem. 278:26374-26379(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PLATELET AGGREGATION.
  17. "Identification of a functionally critical protein kinase C phosphorylation residue of cardiac troponin T."
    Sumandea M.P., Pyle W.G., Kobayashi T., de Tombe P.P., Solaro R.J.
    J. Biol. Chem. 278:35135-35144(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TNNT2/CTNT.
  18. "Signal transduction via the stem cell factor receptor/c-Kit."
    Ronnstrand L.
    Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN KIT SIGNALING.
  19. "Protein kinase Calpha phosphorylates the TRPC1 channel and regulates store-operated Ca2+ entry in endothelial cells."
    Ahmmed G.U., Mehta D., Vogel S., Holinstat M., Paria B.C., Tiruppathi C., Malik A.B.
    J. Biol. Chem. 279:20941-20949(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TRPC1.
  20. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PICK1.
  21. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CSPG4, INTERACTION WITH CSPG4.
  22. "Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor."
    Roskoski R. Jr.
    Biochem. Biophys. Res. Commun. 337:1-13(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ROLE IN KIT SIGNALING.
  23. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM41.
  25. "Protein kinase C alpha promotes angiogenic activity of human endothelial cells via induction of vascular endothelial growth factor."
    Xu H., Czerwinski P., Hortmann M., Sohn H.Y., Foerstermann U., Li H.
    Cardiovasc. Res. 78:349-355(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANGIOGENESIS.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-638 AND SER-651, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  30. "Phosphorylation of activation transcription factor-2 at serine 121 by protein kinase c controls c-Jun-mediated activation of transcription."
    Yamasaki T., Takahashi A., Pan J., Yamaguchi N., Yokoyama K.K.
    J. Biol. Chem. 284:8567-8581(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  32. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-628, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND THR-638, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  34. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "Phosphorylation of eukaryotic translation initiation factor 4G1 (eIF4G1) by protein kinase C{alpha} regulates eIF4G1 binding to Mnk1."
    Dobrikov M., Dobrikova E., Shveygert M., Gromeier M.
    Mol. Cell. Biol. 31:2947-2959(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF EIF4G1.
  36. "Protein kinase C alpha (PKC alpha): regulation and biological function."
    Nakashima S.
    J. Biochem. 132:669-675(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION, REVIEW ON ENZYME REGULATION.
  37. "Protein kinase Calpha: disease regulator and therapeutic target."
    Konopatskaya O., Poole A.W.
    Trends Pharmacol. Sci. 31:8-14(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  38. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. "Unraveling the role of KIAA1199, a novel endoplasmic reticulum protein, in cancer cell migration."
    Evensen N.A., Kuscu C., Nguyen H.L., Zarrabi K., Dufour A., Kadam P., Hu Y.J., Pulkoski-Gross A., Bahou W.F., Zucker S., Cao J.
    J. Natl. Cancer Inst. 105:1402-1416(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION, SUBCELLULAR LOCATION.
  40. "Discovery of 3-(1H-indol-3-yl)-4-[2-(4-methylpiperazin-1-yl)quinazolin-4-yl]pyrrole-2,5-dione (AEB071), a potent and selective inhibitor of protein kinase C isotypes."
    Wagner J., von Matt P., Sedrani R., Albert R., Cooke N., Ehrhardt C., Geiser M., Rummel G., Stark W., Strauss A., Cowan-Jacob S.W., Beerli C., Weckbecker G., Evenou J.P., Zenke G., Cottens S.
    J. Med. Chem. 52:6193-6196(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 320-672 IN COMPLEX WITH INHIBITOR.
  41. "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.
  42. "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] SER-98; ASN-467 AND VAL-489.

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: November 26, 2014
This is version 175 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

External Data

Dasty 3