Q9BZL6 (KPCD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	878 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.16 Ref.17
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. Ref.16
Subcellular location	Cytoplasm. Cell membrane By similarity. Nucleus. Golgi apparatus › trans-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 process	Adaptive immunity Angiogenesis Cell adhesion Immunity
Cellular component	Cell membrane Cytoplasm Golgi apparatus Membrane Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T 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 endothelial tube morphogenesis Traceable author statement PubMed 21488147. Source: BHF-UCL intracellular protein kinase cascade 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.17. 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 by VEGF-activated vascular endothelial growth factor receptor signaling pathway Inferred from mutant phenotype PubMed 18440775. Source: BHF-UCL positive regulation of endothelial cell proliferation Inferred from mutant phenotype Ref.17. Source: UniProtKB positive regulation of fibroblast growth factor receptor signaling pathway Inferred from mutant phenotype Ref.17. 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 peptidyl-serine phosphorylation Inferred from genetic interaction PubMed 20497126. Source: BHF-UCL 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.17. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.8. Source: BHF-UCL
Cellular_component	Golgi 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_function	ATP binding Non-traceable author statement. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipid binding Inferred from electronic annotation. Source: InterPro protein kinase C activity Inferred from electronic annotation. Source: EC protein serine/threonine kinase activity Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 878

878

Serine/threonine-protein kinase D2

PRO_0000055716

Regions

Domain

397 – 509

113

PH

Domain

551 – 807

257

Protein kinase

Zinc finger

138 – 188

51

Phorbol-ester/DAG-type 1

Zinc finger

264 – 314

51

Phorbol-ester/DAG-type 2

Nucleotide binding

557 – 565

9

ATP By similarity

Sites

Active site

674

1

Proton acceptor By similarity

Binding site

580

1

ATP By similarity

Amino acid modifications

Modified residue

200

1

Phosphoserine Ref.15

Modified residue

203

1

Phosphoserine Ref.15 Ref.22

Modified residue

206

1

Phosphoserine Ref.15 Ref.18

Modified residue

212

1

Phosphoserine By similarity

Modified residue

214

1

Phosphoserine Ref.15

Modified residue

244

1

Phosphoserine; by CSNK1D and CSNK1E Ref.10

Modified residue

438

1

Phosphotyrosine; by ABL1 Ref.6

Modified residue

518

1

Phosphoserine Ref.18

Modified residue

706

1

Phosphoserine; by PKC Ref.5

Modified residue

710

1

Phosphoserine Ref.5 Ref.14 Ref.15 Ref.18

Modified residue

717

1

Phosphotyrosine Ref.18

Modified residue

876

1

Phosphoserine; by autocatalysis Ref.1 Ref.5 Ref.14 Ref.18

Natural variations

Natural variant

324

1

V → M. Ref.25
Corresponds to variant rs45455991 [ dbSNP | Ensembl ].

VAR_042330

Natural variant

496

1

A → V. Ref.25
Corresponds to variant rs55716765 [ dbSNP | Ensembl ].

VAR_042331

Natural variant

604

1

S → G. Ref.25
Corresponds to variant rs34325043 [ dbSNP | Ensembl ].

VAR_042332

Natural variant

773

1

W → R. Ref.25
Corresponds to variant rs55933311 [ dbSNP | Ensembl ].

VAR_042333

Natural variant

835

1

V → A. Ref.1 Ref.3 Ref.4
Corresponds to variant rs314665 [ dbSNP | Ensembl ].

VAR_061531

Natural variant

848

1

G → E in a lung adenocarcinoma sample; somatic mutation. Ref.25

VAR_042334

Natural variant

870

1

G → E in a gastric adenocarcinoma sample; somatic mutation. Ref.25

VAR_042335

Experimental info

Mutagenesis

275

1

P → G: Increase in ability to bind phorbol ester, slight increase in ability to bind DAG. Ref.12

Mutagenesis

438

1

Y → F: Loss of phosphorylation. Ref.6

Sequence conflict

790

1

V → L in AAF36107. Ref.4

Secondary structure

1

.

.

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.

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.

.

.

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.

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.

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878

Helix Strand Turn

Details...

Beta strand

399 – 406

8

Beta strand

409 – 411

3

Beta strand

415 – 421

7

Beta strand

423 – 433

11

Beta strand

438 – 442

5

Turn

443 – 445

3

Beta strand

448 – 452

5

Beta strand

456 – 458

3

Beta strand

465 – 470

6

Beta strand

486 – 488

3

Helix

495 – 507

13

Sequences

	Sequence		Length	Mass (Da)
	Q9BZL6 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 8BAB45FB5B1718E7	FASTA	878	96,750
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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.
[17]	"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.
[18]	"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, MASS SPECTROMETRY.
[19]	"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.
[20]	"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.
[21]	"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].
[22]	"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, MASS SPECTROMETRY.
[23]	"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.
[24]	"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.
[25]	"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] 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.

IPI

IPI00941257.

PIR

T08777.

RefSeq

NP_001073349.1. NM_001079880.1.
NP_001073350.1. NM_001079881.1.
NP_001073351.1. NM_001079882.1.
NP_057541.2. NM_016457.4.

UniGene

Hs.466987.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2COA	NMR	-	A	398-509	[»]
3BGM	X-ray	1.60	C	526-534	[»]

ProteinModelPortal

Q9BZL6.

SMR

Q9BZL6. Positions 138-188, 237-357, 395-509, 537-846.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BZL6. 2 interactions.

MINT

MINT-1179710.

STRING

9606.ENSP00000291281.

PTM databases

PhosphoSite

Q9BZL6.

Polymorphism databases

DMDM

296434570.

Proteomic databases

PaxDb

Q9BZL6.

PRIDE

Q9BZL6.

Protocols and materials databases

DNASU

25865.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000291281; ENSP00000291281; ENSG00000105287.
ENST00000433867; ENSP00000393978; ENSG00000105287.

GeneID

25865.

KEGG

hsa:25865.

UCSC

uc002pfh.3. human.

Organism-specific databases

CTD

25865.

GeneCards

GC19M047177.

HGNC

HGNC:17293. PRKD2.

HPA

HPA021490.

MIM

607074. gene.

neXtProt

NX_Q9BZL6.

PharmGKB

PA134903505.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000015135.

HOVERGEN

HBG003564.

InParanoid

Q9BZL6.

KO

K06070.

OMA

DFSEADK.

OrthoDB

EOG4548XW.

PhylomeDB

Q9BZL6.

Enzyme and pathway databases

BRENDA

2.7.11.13. 2681.

Gene expression databases

Bgee

Q9BZL6.

CleanEx

HS_PKD2.
HS_PRKD2.

Genevestigator

Q9BZL6.

GermOnline

ENSG00000105287. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR020454. 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_cat_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]

PANTHER

PTHR22968. PTHR22968. 1 hit.

Pfam

PF00130. C1_1. 2 hits.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

PIRSF

PIRSF000552. PKC_mu_nu_D2. 1 hit.

PRINTS

PR00008. DAGPEDOMAIN.

SMART

SM00109. C1. 2 hits.
SM00233. PH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

BindingDB

Q9BZL6.

ChEMBL

CHEMBL4900.

ChiTaRS

PRKD2. human.

EvolutionaryTrace

Q9BZL6.

GenomeRNAi

25865.

NextBio

47239.

SOURCE

Search...

Entry information

Entry name

KPCD2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 137 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.