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O94806

- KPCD3_HUMAN

UniProt

O94806 - KPCD3_HUMAN

Protein

Serine/threonine-protein kinase D3

Gene

PRKD3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domains 1 and 2 bind both DAG and phorbol ester with high affinity and mediate translocation to the cell membrane. Autophosphorylation of Ser-735 and phosphorylation of Ser-731 by PKC relieves auto-inhibition by the PH domain.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei605 – 6051ATPPROSITE-ProRule annotation
    Active sitei699 – 6991Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri154 – 20451Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri271 – 32151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi582 – 5909ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. protein kinase C activity Source: ProtInc

    GO - Biological processi

    1. intracellular signal transduction Source: InterPro
    2. protein kinase C-activating G-protein coupled receptor signaling pathway Source: ProtInc
    3. protein phosphorylation Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.7.11.13. 2681.
    SignaLinkiO94806.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase D3 (EC:2.7.11.13)
    Alternative name(s):
    Protein kinase C nu type
    Protein kinase EPK2
    nPKC-nu
    Gene namesi
    Name:PRKD3
    Synonyms:EPK2, PRKCN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:9408. PRKD3.

    Subcellular locationi

    Cytoplasm 1 Publication. Membrane 1 Publication
    Note: Translocation to the cell membrane is required for kinase activation.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. membrane Source: UniProtKB-SubCell
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi156 – 1561T → A: Slight loss in ability to bind DAG and phorbol-ester; when associated with F-158. 1 Publication
    Mutagenesisi158 – 1581Y → F: Slight loss in ability to bind DAG and phorbol-ester; when associated with A-156. 1 Publication
    Mutagenesisi165 – 1651P → G: No effect on ability to bind phorbol ester, loss of ability to bind DAG, reduced DAG-induced membrane translocation. 1 Publication
    Mutagenesisi166 – 1661T → A: Slight loss in ability to bind DAG and phorbol-ester. 1 Publication
    Mutagenesisi170 – 1701Y → F: Slight loss in ability to bind DAG and phorbol-ester. 1 Publication
    Mutagenesisi282 – 2821P → G: No effect on ability to bind phorbol ester, increase in ability to bind DAG. 1 Publication
    Mutagenesisi284 – 2841I → V: Slight increase in ability to bind DAG, no effect on phorbol-ester binding.
    Mutagenesisi293 – 2931K → W: Increased ability to bind DAG, no effect on phorbol-ester binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA33772.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 890890Serine/threonine-protein kinase D3PRO_0000055717Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei6 – 61Phosphoserine1 Publication
    Modified residuei27 – 271Phosphoserine4 Publications
    Modified residuei37 – 371Phosphoserine1 Publication
    Modified residuei41 – 411Phosphoserine4 Publications
    Modified residuei44 – 441Phosphoserine2 Publications
    Modified residuei213 – 2131Phosphoserine2 Publications
    Modified residuei216 – 2161Phosphoserine2 Publications
    Modified residuei364 – 3641Phosphoserine4 Publications
    Modified residuei535 – 5351Phosphothreonine2 Publications
    Modified residuei731 – 7311Phosphoserine; by PKC
    Modified residuei735 – 7351Phosphoserine; by autocatalysis

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO94806.
    PaxDbiO94806.
    PRIDEiO94806.

    PTM databases

    PhosphoSiteiO94806.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiO94806.
    BgeeiO94806.
    CleanExiHS_PRKD3.
    GenevestigatoriO94806.

    Organism-specific databases

    HPAiHPA029529.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    VAMP2P630277EBI-1255366,EBI-520113

    Protein-protein interaction databases

    BioGridi117199. 8 interactions.
    IntActiO94806. 10 interactions.
    MINTiMINT-5003932.
    STRINGi9606.ENSP00000234179.

    Structurei

    Secondary structure

    1
    890
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi417 – 42913
    Beta strandi434 – 44310
    Beta strandi445 – 4495
    Turni462 – 4643
    Beta strandi477 – 4793
    Beta strandi485 – 4895
    Beta strandi494 – 4974
    Turni508 – 5147
    Helixi517 – 53216

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D9ZNMR-A417-532[»]
    ProteinModelPortaliO94806.
    SMRiO94806. Positions 155-204, 241-321, 414-532, 537-859.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO94806.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini416 – 532117PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini576 – 832257Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PH 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 fingeri154 – 20451Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri271 – 32151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000015135.
    HOVERGENiHBG003564.
    InParanoidiO94806.
    KOiK06070.
    OMAiFRHDLNS.
    OrthoDBiEOG75B84N.
    PhylomeDBiO94806.
    TreeFamiTF314320.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR015727. Protein_Kinase_C_mu-related.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR22968. PTHR22968. 1 hit.
    PfamiPF00130. C1_1. 2 hits.
    PF00169. PH. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000552. PKC_mu_nu_D2. 1 hit.
    PRINTSiPR00008. DAGPEDOMAIN.
    SMARTiSM00109. C1. 2 hits.
    SM00233. PH. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50003. PH_DOMAIN. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O94806-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSANNSPPSA QKSVLPTAIP AVLPAASPCS SPKTGLSARL SNGSFSAPSL    50
    TNSRGSVHTV SFLLQIGLTR ESVTIEAQEL SLSAVKDLVC SIVYQKFPEC 100
    GFFGMYDKIL LFRHDMNSEN ILQLITSADE IHEGDLVEVV LSALATVEDF 150
    QIRPHTLYVH SYKAPTFCDY CGEMLWGLVR QGLKCEGCGL NYHKRCAFKI 200
    PNNCSGVRKR RLSNVSLPGP GLSVPRPLQP EYVALPSEES HVHQEPSKRI 250
    PSWSGRPIWM EKMVMCRVKV PHTFAVHSYT RPTICQYCKR LLKGLFRQGM 300
    QCKDCKFNCH KRCASKVPRD CLGEVTFNGE PSSLGTDTDI PMDIDNNDIN 350
    SDSSRGLDDT EEPSPPEDKM FFLDPSDLDV ERDEEAVKTI SPSTSNNIPL 400
    MRVVQSIKHT KRKSSTMVKE GWMVHYTSRD NLRKRHYWRL DSKCLTLFQN 450
    ESGSKYYKEI PLSEILRISS PRDFTNISQG SNPHCFEIIT DTMVYFVGEN 500
    NGDSSHNPVL AATGVGLDVA QSWEKAIRQA LMPVTPQASV CTSPGQGKDH 550
    KDLSTSISVS NCQIQENVDI STVYQIFADE VLGSGQFGIV YGGKHRKTGR 600
    DVAIKVIDKM RFPTKQESQL RNEVAILQNL HHPGIVNLEC MFETPERVFV 650
    VMEKLHGDML EMILSSEKSR LPERITKFMV TQILVALRNL HFKNIVHCDL 700
    KPENVLLASA EPFPQVKLCD FGFARIIGEK SFRRSVVGTP AYLAPEVLRS 750
    KGYNRSLDMW SVGVIIYVSL SGTFPFNEDE DINDQIQNAA FMYPPNPWRE 800
    ISGEAIDLIN NLLQVKMRKR YSVDKSLSHP WLQDYQTWLD LREFETRIGE 850
    RYITHESDDA RWEIHAYTHN LVYPKHFIMA PNPDDMEEDP 890
    Length:890
    Mass (Da):100,471
    Last modified:May 1, 1999 - v1
    Checksum:i66D5E7E7235064F5
    GO
    Isoform 2 (identifier: O94806-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         595-611: HRKTGRDVAIKVIDKMR → QLQPFAYCTHYFKNWKM
         612-890: Missing.

    Show »
    Length:611
    Mass (Da):68,123
    Checksum:i1714FAD7DA82C942
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti42 – 421N → D.
    Corresponds to variant rs11896614 [ dbSNP | Ensembl ].
    VAR_037147
    Natural varianti128 – 1281A → T.1 Publication
    Corresponds to variant rs17852819 [ dbSNP | Ensembl ].
    VAR_037148
    Natural varianti225 – 2251P → S.
    Corresponds to variant rs34280934 [ dbSNP | Ensembl ].
    VAR_050561
    Natural varianti445 – 4451L → I.
    Corresponds to variant rs55912911 [ dbSNP | Ensembl ].
    VAR_061532
    Natural varianti546 – 5461Q → R.1 Publication
    Corresponds to variant rs17856887 [ dbSNP | Ensembl ].
    VAR_037149
    Natural varianti716 – 7161V → M in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_042336

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei595 – 61117HRKTG…IDKMR → QLQPFAYCTHYFKNWKM in isoform 2. 1 PublicationVSP_029405Add
    BLAST
    Alternative sequencei612 – 890279Missing in isoform 2. 1 PublicationVSP_029406Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB015982 mRNA. Translation: BAA36514.1.
    AC007390 Genomic DNA. Translation: AAY14817.1.
    CH471053 Genomic DNA. Translation: EAX00398.1.
    CH471053 Genomic DNA. Translation: EAX00399.1.
    BC030706 mRNA. Translation: AAH30706.1.
    CCDSiCCDS1789.1. [O94806-1]
    RefSeqiNP_005804.1. NM_005813.3. [O94806-1]
    XP_005264294.1. XM_005264237.1. [O94806-1]
    UniGeneiHs.660757.
    Hs.716034.

    Genome annotation databases

    EnsembliENST00000234179; ENSP00000234179; ENSG00000115825. [O94806-1]
    ENST00000379066; ENSP00000368356; ENSG00000115825. [O94806-1]
    GeneIDi23683.
    KEGGihsa:23683.
    UCSCiuc002rqd.3. human. [O94806-1]
    uc002rqf.1. human. [O94806-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB015982 mRNA. Translation: BAA36514.1 .
    AC007390 Genomic DNA. Translation: AAY14817.1 .
    CH471053 Genomic DNA. Translation: EAX00398.1 .
    CH471053 Genomic DNA. Translation: EAX00399.1 .
    BC030706 mRNA. Translation: AAH30706.1 .
    CCDSi CCDS1789.1. [O94806-1 ]
    RefSeqi NP_005804.1. NM_005813.3. [O94806-1 ]
    XP_005264294.1. XM_005264237.1. [O94806-1 ]
    UniGenei Hs.660757.
    Hs.716034.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D9Z NMR - A 417-532 [» ]
    ProteinModelPortali O94806.
    SMRi O94806. Positions 155-204, 241-321, 414-532, 537-859.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117199. 8 interactions.
    IntActi O94806. 10 interactions.
    MINTi MINT-5003932.
    STRINGi 9606.ENSP00000234179.

    Chemistry

    BindingDBi O94806.
    ChEMBLi CHEMBL2595.
    GuidetoPHARMACOLOGYi 2174.

    PTM databases

    PhosphoSitei O94806.

    Proteomic databases

    MaxQBi O94806.
    PaxDbi O94806.
    PRIDEi O94806.

    Protocols and materials databases

    DNASUi 23683.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000234179 ; ENSP00000234179 ; ENSG00000115825 . [O94806-1 ]
    ENST00000379066 ; ENSP00000368356 ; ENSG00000115825 . [O94806-1 ]
    GeneIDi 23683.
    KEGGi hsa:23683.
    UCSCi uc002rqd.3. human. [O94806-1 ]
    uc002rqf.1. human. [O94806-2 ]

    Organism-specific databases

    CTDi 23683.
    GeneCardsi GC02M037477.
    H-InvDB HIX0030377.
    HGNCi HGNC:9408. PRKD3.
    HPAi HPA029529.
    MIMi 607077. gene.
    neXtProti NX_O94806.
    PharmGKBi PA33772.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000015135.
    HOVERGENi HBG003564.
    InParanoidi O94806.
    KOi K06070.
    OMAi FRHDLNS.
    OrthoDBi EOG75B84N.
    PhylomeDBi O94806.
    TreeFami TF314320.

    Enzyme and pathway databases

    BRENDAi 2.7.11.13. 2681.
    SignaLinki O94806.

    Miscellaneous databases

    EvolutionaryTracei O94806.
    GeneWikii PRKD3.
    GenomeRNAii 23683.
    NextBioi 46561.
    PROi O94806.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O94806.
    Bgeei O94806.
    CleanExi HS_PRKD3.
    Genevestigatori O94806.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR015727. Protein_Kinase_C_mu-related.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR22968. PTHR22968. 1 hit.
    Pfami PF00130. C1_1. 2 hits.
    PF00169. PH. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000552. PKC_mu_nu_D2. 1 hit.
    PRINTSi PR00008. DAGPEDOMAIN.
    SMARTi SM00109. C1. 2 hits.
    SM00233. PH. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50003. PH_DOMAIN. 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. "PKCnu, a new member of the protein kinase C family, composes a fourth subfamily with PKCmu."
      Hayashi A., Seki N., Hattori A., Kozuma S., Saito T.
      Biochim. Biophys. Acta 1450:99-106(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Embryo.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 2), VARIANTS THR-128 AND ARG-546.
      Tissue: Testis.
    6. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Selective binding of phorbol esters and diacylglycerol by individual C1 domains of the PKD family."
      Chen J., Deng F., Li J., Wang Q.J.
      Biochem. J. 411:333-342(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION, PHORBOL-ESTER BINDING, MUTAGENESIS OF THR-156; TYR-158; PRO-165; THR-166; TYR-170; PRO-282 AND LYS-293.
    8. "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 SER-6; SER-27; SER-37; SER-41; SER-213; SER-216; SER-364 AND THR-535, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41; SER-44 AND SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41; SER-213; SER-216; SER-364 AND THR-535, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-27; SER-41 AND SER-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Solution structure of the PH domain of protein kinase C, nu type from human."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JAN-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 414-532.
    14. "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: VARIANT [LARGE SCALE ANALYSIS] MET-716.

    Entry informationi

    Entry nameiKPCD3_HUMAN
    AccessioniPrimary (citable) accession number: O94806
    Secondary accession number(s): D6W587, Q53TR7, Q8NEL8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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