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P17252

- KPCA_HUMAN

UniProt

P17252 - KPCA_HUMAN

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
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 4 (11 Jan 2011)
      Previous versions | rss
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    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

    Binds 3 calcium ions per subunit. The ions are bound to the C2 domain By similarity.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 binding Source: UniProtKB
    6. protein kinase activity Source: UniProtKB
    7. protein kinase C activity Source: BHF-UCL
    8. 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

    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_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. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. dendrite Source: Ensembl
    4. endoplasmic reticulum Source: BHF-UCL
    5. extracellular vesicular exosome Source: UniProt
    6. mitochondrial membrane Source: UniProtKB-SubCell
    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

    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

    ArrayExpressiP17252.
    BgeeiP17252.
    CleanExiHS_PRKACA.
    HS_PRKCA.
    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
    HDAC6Q9UBN72EBI-1383528,EBI-301697
    inaDQ240082EBI-1383528,EBI-195326From a different organism.
    SDC4P314312EBI-1383528,EBI-3913237
    UBCP0CG482EBI-1383528,EBI-3390054

    Protein-protein interaction databases

    BioGridi111564. 104 interactions.
    DIPiDIP-531N.
    IntActiP17252. 26 interactions.
    MINTiMINT-140812.
    STRINGi9606.ENSP00000284384.

    Structurei

    Secondary structure

    1
    672
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni98 – 1003
    Beta strandi105 – 1073
    Beta strandi116 – 1183
    Beta strandi125 – 1273
    Beta strandi129 – 1313
    Beta strandi133 – 1353
    Beta strandi138 – 1403
    Turni141 – 1466
    Beta strandi161 – 1699
    Beta strandi172 – 18211
    Beta strandi194 – 2029
    Beta strandi222 – 2309
    Helixi233 – 2375
    Beta strandi239 – 2468
    Beta strandi249 – 2513
    Beta strandi254 – 2629
    Helixi263 – 2686
    Beta strandi271 – 2766
    Helixi282 – 2843
    Helixi336 – 3383
    Beta strandi339 – 34810
    Beta strandi351 – 3588
    Beta strandi364 – 3718
    Helixi372 – 3776
    Helixi381 – 39212
    Beta strandi403 – 4086
    Beta strandi410 – 4189
    Beta strandi422 – 4243
    Helixi425 – 4328
    Helixi437 – 45620
    Helixi466 – 4683
    Beta strandi469 – 4713
    Beta strandi477 – 4793
    Helixi502 – 5043
    Helixi507 – 5104
    Helixi518 – 53316
    Helixi543 – 55210
    Helixi563 – 57210
    Turni577 – 5793
    Helixi587 – 5926
    Helixi595 – 5973
    Helixi602 – 6054
    Turni606 – 6083
    Helixi642 – 6465
    Helixi650 – 6534

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR014375. Protein_kinase_C_a/b/g.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    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

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    MADVFPGNDS TASQDVANRF ARKGALRQKN VHEVKDHKFI ARFFKQPTFC    50
    SHCTDFIWGF GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPDTDDPRS 100
    KHKFKIHTYG SPTFCDHCGS LLYGLIHQGM KCDTCDMNVH KQCVINVPSL 150
    CGMDHTEKRG RIYLKAEVAD EKLHVTVRDA KNLIPMDPNG LSDPYVKLKL 200
    IPDPKNESKQ KTKTIRSTLN PQWNESFTFK LKPSDKDRRL SVEIWDWDRT 250
    TRNDFMGSLS FGVSELMKMP ASGWYKLLNQ EEGEYYNVPI PEGDEEGNME 300
    LRQKFEKAKL GPAGNKVISP SEDRKQPSNN LDRVKLTDFN FLMVLGKGSF 350
    GKVMLADRKG TEELYAIKIL KKDVVIQDDD VECTMVEKRV LALLDKPPFL 400
    TQLHSCFQTV DRLYFVMEYV NGGDLMYHIQ QVGKFKEPQA VFYAAEISIG 450
    LFFLHKRGII YRDLKLDNVM LDSEGHIKIA DFGMCKEHMM DGVTTRTFCG 500
    TPDYIAPEII AYQPYGKSVD WWAYGVLLYE MLAGQPPFDG EDEDELFQSI 550
    MEHNVSYPKS LSKEAVSVCK GLMTKHPAKR LGCGPEGERD VREHAFFRRI 600
    DWEKLENREI QPPFKPKVCG KGAENFDKFF TRGQPVLTPP DQLVIANIDQ 650
    SDFEGFSYVN PQFVHPILQS AV 672
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 104 interactions.
    DIPi DIP-531N.
    IntActi P17252. 26 interactions.
    MINTi MINT-140812.
    STRINGi 9606.ENSP00000284384.

    Chemistry

    BindingDBi P17252.
    ChEMBLi CHEMBL2096620.
    DrugBanki DB00144. Phosphatidylserine.
    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.
    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_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

    ArrayExpressi P17252.
    Bgeei P17252.
    CleanExi HS_PRKACA.
    HS_PRKCA.
    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.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR014375. Protein_kinase_C_a/b/g.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    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

    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: October 1, 2014
    This is version 173 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