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Q9BZL6 (KPCD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase D2

EC=2.7.11.13
Alternative name(s):
nPKC-D2
Gene names
Name:PRKD2
Synonyms:PKD2
ORF Names:HSPC187
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length878 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. In response to oxidative stress, is phosphorylated at Tyr-438 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B. In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77. Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation. During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens. In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF-kappa-B-dependent pathway. During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane. Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis. In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN. Downstream of PRKCA, plays important roles in angiotensin-2-induced monocyte adhesion to endothelial cells. Plays a regulatory role in angiogenesis and tumor growth by phosphorylating a downstream mediator CIB1 isoform 2 resulting in vascular endothelial growth factor A (VEGFA) secretion. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.17 Ref.18 Ref.24

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domains bind DAG, mediating translocation to membranes. Autophosphorylation of Ser-710 and phosphorylation of Ser-706 by PKC relieves auto-inhibition by the PH domain. Ref.5 Ref.10

Subunit structure

Interacts (via C-terminus) with LCK. Interacts (via N-terminal AP-rich region) with CIB1 isoform 2 Ref.17 Ref.24

Subcellular location

Cytoplasm. Cell membrane By similarity. Nucleus. Golgi apparatustrans-Golgi network. Note: Translocation to the cell membrane is required for kinase activation By similarity. Accumulates in the nucleus upon CK1-mediated phosphorylation after activation of G-protein-coupled receptors. Nuclear accumulation is regulated by blocking nuclear export of active PRKD2 rather than by increasing import. Ref.10 Ref.13

Tissue specificity

Widely expressed.

Post-translational modification

Phosphorylation of Ser-876 correlates with the activation status of the kinase. Ser-706 is probably phosphorylated by PKC. Phosphorylation at Ser-244 by CSNK1D and CSNK1E promotes nuclear localization and substrate targeting. Phosphorylation at Ser-244, Ser-706 and Ser-710 is required for nuclear localization. Phosphorylated at Tyr-438 by ABL1 in response to oxidative stress. Ref.1 Ref.5 Ref.6 Ref.10

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PKD subfamily.

Contains 1 PH domain.

Contains 2 phorbol-ester/DAG-type zinc fingers.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAF36107.1 differs from that shown. Reason: Frameshift at positions 604, 606, 738, 744, 755, 758, 833 and 854.

Ontologies

Keywords
   Biological processAdaptive immunity
Angiogenesis
Cell adhesion
Immunity
   Cellular componentCell membrane
Cytoplasm
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
Zinc-finger
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell receptor signaling pathway

Inferred from direct assay Ref.8. Source: BHF-UCL

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell death

Inferred from mutant phenotype Ref.8. Source: BHF-UCL

cellular response to vascular endothelial growth factor stimulus

Inferred from mutant phenotype PubMed 18059339PubMed 18440775. Source: BHF-UCL

endothelial tube morphogenesis

Traceable author statement PubMed 21488147. Source: BHF-UCL

intracellular signal transduction

Inferred from mutant phenotype PubMed 18059339PubMed 18440775. Source: BHF-UCL

peptidyl-serine phosphorylation

Inferred from direct assay PubMed 18440775. Source: BHF-UCL

positive regulation of CREB transcription factor activity

Inferred from genetic interaction PubMed 20497126. Source: BHF-UCL

positive regulation of DNA biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype Ref.6Ref.9. Source: UniProtKB

positive regulation of T cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of angiogenesis

Inferred from mutant phenotype Ref.18. Source: UniProtKB

positive regulation of blood vessel endothelial cell migration

Inferred from mutant phenotype PubMed 18440775. Source: BHF-UCL

positive regulation of cell adhesion

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of endothelial cell chemotaxis

Inferred from mutant phenotype PubMed 18440775. Source: BHF-UCL

positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 18440775. Source: BHF-UCL

positive regulation of endothelial cell migration

Inferred from mutant phenotype Ref.18. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from mutant phenotype Ref.18. Source: UniProtKB

positive regulation of fibroblast growth factor receptor signaling pathway

Inferred from mutant phenotype Ref.18. Source: UniProtKB

positive regulation of histone deacetylase activity

Inferred from genetic interaction PubMed 20497126. Source: BHF-UCL

positive regulation of interleukin-2 production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-8 production

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of intracellular signal transduction

Inferred from mutant phenotype PubMed 18440775. Source: BHF-UCL

positive regulation of peptidyl-serine phosphorylation

Inferred from genetic interaction PubMed 20497126. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype Ref.17. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.8. Source: BHF-UCL

positive regulation of vascular endothelial growth factor receptor signaling pathway

Inferred from mutant phenotype Ref.18. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.8. Source: BHF-UCL

protein phosphorylation

Non-traceable author statement Ref.1. Source: UniProtKB

vascular endothelial growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 18059339. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.8. Source: BHF-UCL

nucleus

Inferred from direct assay Ref.8. Source: BHF-UCL

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase C activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein kinase activity

Inferred from direct assay Ref.8. Source: BHF-UCL

protein serine/threonine kinase activity

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HDAC7Q8WUI46EBI-1384325,EBI-1048378

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 878878Serine/threonine-protein kinase D2
PRO_0000055716

Regions

Domain397 – 509113PH
Domain551 – 807257Protein kinase
Zinc finger138 – 18851Phorbol-ester/DAG-type 1
Zinc finger264 – 31451Phorbol-ester/DAG-type 2
Nucleotide binding557 – 5659ATP By similarity

Sites

Active site6741Proton acceptor By similarity
Binding site5801ATP By similarity

Amino acid modifications

Modified residue2001Phosphoserine Ref.15
Modified residue2031Phosphoserine Ref.15 Ref.23
Modified residue2061Phosphoserine Ref.15 Ref.19
Modified residue2141Phosphoserine Ref.15
Modified residue2441Phosphoserine; by CSNK1D and CSNK1E Ref.10
Modified residue4381Phosphotyrosine; by ABL1 Ref.6
Modified residue5181Phosphoserine Ref.19
Modified residue7061Phosphoserine; by PKC Ref.5
Modified residue7101Phosphoserine Ref.5 Ref.14 Ref.15 Ref.19
Modified residue7171Phosphotyrosine Ref.19
Modified residue8761Phosphoserine; by autocatalysis Ref.1 Ref.5 Ref.14 Ref.19

Natural variations

Natural variant3241V → M. Ref.27
Corresponds to variant rs45455991 [ dbSNP | Ensembl ].
VAR_042330
Natural variant4961A → V. Ref.27
Corresponds to variant rs55716765 [ dbSNP | Ensembl ].
VAR_042331
Natural variant6041S → G. Ref.27
Corresponds to variant rs34325043 [ dbSNP | Ensembl ].
VAR_042332
Natural variant7731W → R. Ref.27
Corresponds to variant rs55933311 [ dbSNP | Ensembl ].
VAR_042333
Natural variant8351V → A. Ref.1 Ref.3 Ref.4
Corresponds to variant rs314665 [ dbSNP | Ensembl ].
VAR_061531
Natural variant8481G → E in a lung adenocarcinoma sample; somatic mutation. Ref.27
VAR_042334
Natural variant8701G → E in a gastric adenocarcinoma sample; somatic mutation. Ref.27
VAR_042335

Experimental info

Mutagenesis2441S → E: Constitutive kinase activity; when associated with E-706 and E-710. Ref.24
Mutagenesis2751P → G: Increase in ability to bind phorbol ester, slight increase in ability to bind DAG. Ref.12
Mutagenesis4381Y → F: Loss of phosphorylation. Ref.6
Mutagenesis6951D → A: Loss of kinase activity. Ref.24
Mutagenesis7061S → E: Constitutive kinase activity; when associated with E-710 or with E-244 and E-710. Ref.24
Mutagenesis7101S → E: Constitutive kinase activity; when associated with E-706 or with E-244 and E-706. Ref.24
Sequence conflict7901V → L in AAF36107. Ref.4

Secondary structure

...................... 878
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BZL6 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 8BAB45FB5B1718E7

FASTA87896,750
        10         20         30         40         50         60 
MATAPSYPAG LPGSPGPGSP PPPGGLELQS PPPLLPQIPA PGSGVSFHIQ IGLTREFVLL 

        70         80         90        100        110        120 
PAASELAHVK QLACSIVDQK FPECGFYGLY DKILLFKHDP TSANLLQLVR SSGDIQEGDL 

       130        140        150        160        170        180 
VEVVLSASAT FEDFQIRPHA LTVHSYRAPA FCDHCGEMLF GLVRQGLKCD GCGLNYHKRC 

       190        200        210        220        230        240 
AFSIPNNCSG ARKRRLSSTS LASGHSVRLG TSESLPCTAE ELSRSTTELL PRRPPSSSSS 

       250        260        270        280        290        300 
SSASSYTGRP IELDKMLLSK VKVPHTFLIH SYTRPTVCQA CKKLLKGLFR QGLQCKDCKF 

       310        320        330        340        350        360 
NCHKRCATRV PNDCLGEALI NGDVPMEEAT DFSEADKSAL MDESEDSGVI PGSHSENALH 

       370        380        390        400        410        420 
ASEEEEGEGG KAQSSLGYIP LMRVVQSVRH TTRKSSTTLR EGWVVHYSNK DTLRKRHYWR 

       430        440        450        460        470        480 
LDCKCITLFQ NNTTNRYYKE IPLSEILTVE SAQNFSLVPP GTNPHCFEIV TANATYFVGE 

       490        500        510        520        530        540 
MPGGTPGGPS GQGAEAARGW ETAIRQALMP VILQDAPSAP GHAPHRQASL SISVSNSQIQ 

       550        560        570        580        590        600 
ENVDIATVYQ IFPDEVLGSG QFGVVYGGKH RKTGRDVAVK VIDKLRFPTK QESQLRNEVA 

       610        620        630        640        650        660 
ILQSLRHPGI VNLECMFETP EKVFVVMEKL HGDMLEMILS SEKGRLPERL TKFLITQILV 

       670        680        690        700        710        720 
ALRHLHFKNI VHCDLKPENV LLASADPFPQ VKLCDFGFAR IIGEKSFRRS VVGTPAYLAP 

       730        740        750        760        770        780 
EVLLNQGYNR SLDMWSVGVI MYVSLSGTFP FNEDEDINDQ IQNAAFMYPA SPWSHISAGA 

       790        800        810        820        830        840 
IDLINNLLQV KMRKRYSVDK SLSHPWLQEY QTWLDLRELE GKMGERYITH ESDDVRWEQF 

       850        860        870 
AAEHPLPGSG LPTDRDLGGA CPPQDHDMQG LAERISVL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of the human protein kinase D2. A novel member of the protein kinase d family of serine threonine kinases."
Sturany S., Van Lint J., Mueller F., Wilda M., Hameister H., Hoecker M., Brey A., Gern U., Vandenheede J., Gress T., Adler G., Seufferlein T.
J. Biol. Chem. 276:3310-3318(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-876, VARIANT ALA-835.
Tissue: Pancreas.
[2]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-878, VARIANT ALA-835.
Tissue: Uterus.
[4]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 574-878, VARIANT ALA-835.
Tissue: Umbilical cord blood.
[5]"Mechanism of activation of protein kinase D2(PKD2) by the CCK(B)/gastrin receptor."
Sturany S., Van Lint J., Gilchrist A., Vandenheede J.R., Adler G., Seufferlein T.
J. Biol. Chem. 277:29431-29436(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-706; SER-710 AND SER-876.
[6]"Protein kinase D2 mediates activation of nuclear factor kappaB by Bcr-Abl in Bcr-Abl+ human myeloid leukemia cells."
Mihailovic T., Marx M., Auer A., Van Lint J., Schmid M., Weber C., Seufferlein T.
Cancer Res. 64:8939-8944(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NF-KAPPA-B ACTIVATION, PHOSPHORYLATION AT TYR-438, MUTAGENESIS OF TYR-438.
[7]"Protein kinase D regulates basolateral membrane protein exit from trans-Golgi network."
Yeaman C., Ayala M.I., Wright J.R., Bard F., Bossard C., Ang A., Maeda Y., Seufferlein T., Mellman I., Nelson W.J., Malhotra V.
Nat. Cell Biol. 6:106-112(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRAFFICKING.
[8]"Protein kinase D2 contributes to either IL-2 promoter regulation or induction of cell death upon TCR stimulation depending on its activity in Jurkat cells."
Irie A., Harada K., Tsukamoto H., Kim J.R., Araki N., Nishimura Y.
Int. Immunol. 18:1737-1747(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ADAPTIVE IMMUNE RESPONSE.
[9]"Protein kinase D2 mediates lysophosphatidic acid-induced interleukin 8 production in nontransformed human colonic epithelial cells through NF-kappaB."
Chiu T.T., Leung W.Y., Moyer M.P., Strieter R.M., Rozengurt E.
Am. J. Physiol. 292:C767-C777(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Phosphorylation at Ser244 by CK1 determines nuclear localization and substrate targeting of PKD2."
von Blume J., Knippschild U., Dequiedt F., Giamas G., Beck A., Auer A., Van Lint J., Adler G., Seufferlein T.
EMBO J. 26:4619-4633(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC7, ENZYME REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-244.
[11]"Angiotensin II directly triggers endothelial exocytosis via protein kinase C-dependent protein kinase D2 activation."
Ge X., Low B., Liang M., Fu J.
J. Pharmacol. Sci. 105:168-176(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL ADHESION.
[12]"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: PHORBOL-ESTER BINDING, MUTAGENESIS OF PRO-275.
[13]"Protein kinase D2 regulates chromogranin A secretion in human BON neuroendocrine tumour cells."
von Wichert G., Edenfeld T., von Blume J., Krisp H., Krndija D., Schmid H., Oswald F., Lother U., Walther P., Adler G., Seufferlein T.
Cell. Signal. 20:925-934(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SECRETORY PATHWAY, SUBCELLULAR LOCATION.
[14]"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-710 AND SER-876, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-203; SER-206; SER-214 AND SER-710, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"PKD2 interacts with Lck and regulates NFAT activity in T cells."
Li Q., Sun X., Wu J., Lin Z., Luo Y.
BMB Rep. 42:35-40(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LCK.
[18]"Identification of protein kinase D2 as a pivotal regulator of endothelial cell proliferation, migration, and angiogenesis."
Hao Q., Wang L., Zhao Z.J., Tang H.
J. Biol. Chem. 284:799-806(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ANGIOGENESIS.
[19]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-518; SER-710; TYR-717 AND SER-876, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"A novel splice variant of calcium and integrin-binding protein 1 mediates protein kinase D2-stimulated tumour growth by regulating angiogenesis."
Armacki M., Joodi G., Nimmagadda S.C., de Kimpe L., Pusapati G.V., Vandoninck S., Van Lint J., Illing A., Seufferlein T.
Oncogene 0:0-0(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CIB1 ISOFORM 2, MUTAGENESIS OF SER-244; ASP-695; SER-706 AND SER-710.
[25]"Solution structure of the PH domain of protein kinase C, D2 type from human."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 395-509.
[26]"Phosphorylation-dependent interaction between antigenic peptides and MHC class I: a molecular basis for the presentation of transformed self."
Mohammed F., Cobbold M., Zarling A.L., Salim M., Barrett-Wilt G.A., Shabanowitz J., Hunt D.F., Engelhard V.H., Willcox B.E.
Nat. Immunol. 9:1236-1243(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 526-534.
[27]"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. expand/collapse author list , 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] MET-324; VAL-496; GLY-604; ARG-773; GLU-848 AND GLU-870.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF309082 mRNA. Translation: AAK01149.1.
AC008635 Genomic DNA. No translation available.
AC093503 Genomic DNA. No translation available.
AL050147 mRNA. Translation: CAB43292.1.
AF151021 mRNA. Translation: AAF36107.1. Frameshift.
PIRT08777.
RefSeqNP_001073349.1. NM_001079880.1.
NP_001073350.1. NM_001079881.1.
NP_001073351.1. NM_001079882.1.
NP_057541.2. NM_016457.4.
UniGeneHs.466987.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2COANMR-A398-509[»]
3BGMX-ray1.60C526-534[»]
ProteinModelPortalQ9BZL6.
SMRQ9BZL6. Positions 138-188, 237-357, 395-509, 537-851.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117384. 20 interactions.
IntActQ9BZL6. 27 interactions.
MINTMINT-1179710.
STRING9606.ENSP00000291281.

Chemistry

BindingDBQ9BZL6.
ChEMBLCHEMBL4900.
GuidetoPHARMACOLOGY2173.

PTM databases

PhosphoSiteQ9BZL6.

Polymorphism databases

DMDM296434570.

Proteomic databases

PaxDbQ9BZL6.
PRIDEQ9BZL6.

Protocols and materials databases

DNASU25865.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000291281; ENSP00000291281; ENSG00000105287.
ENST00000433867; ENSP00000393978; ENSG00000105287.
GeneID25865.
KEGGhsa:25865.
UCSCuc002pfh.3. human.

Organism-specific databases

CTD25865.
GeneCardsGC19M047177.
HGNCHGNC:17293. PRKD2.
HPAHPA021490.
MIM607074. gene.
neXtProtNX_Q9BZL6.
PharmGKBPA134903505.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000015135.
HOVERGENHBG003564.
InParanoidQ9BZL6.
KOK06070.
OrthoDBEOG75B84N.
PhylomeDBQ9BZL6.
TreeFamTF314320.

Enzyme and pathway databases

BRENDA2.7.11.13. 2681.
SignaLinkQ9BZL6.

Gene expression databases

ArrayExpressQ9BZL6.
BgeeQ9BZL6.
CleanExHS_PKD2.
HS_PRKD2.
GenevestigatorQ9BZL6.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
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]
PANTHERPTHR22968. PTHR22968. 1 hit.
PfamPF00130. C1_1. 2 hits.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF000552. PKC_mu_nu_D2. 1 hit.
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 2 hits.
SM00233. PH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50003. 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]
ProtoNetSearch...

Other

ChiTaRSPRKD2. human.
EvolutionaryTraceQ9BZL6.
GeneWikiPRKD2.
GenomeRNAi25865.
NextBio47239.
PROQ9BZL6.
SOURCESearch...

Entry information

Entry nameKPCD2_HUMAN
AccessionPrimary (citable) accession number: Q9BZL6
Secondary accession number(s): Q8TB08, Q9P0T6, Q9Y3X8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM