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Q15139

- KPCD1_HUMAN

UniProt

Q15139 - KPCD1_HUMAN

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Protein

Serine/threonine-protein kinase D1

Gene

PRKD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. Phosphorylates the epidermal growth factor receptor (EGFR) on dual threonine residues, which leads to the suppression of epidermal growth factor (EGF)-induced MAPK8/JNK1 activation and subsequent JUN phosphorylation. Phosphorylates RIN1, inducing RIN1 binding to 14-3-3 proteins YWHAB, YWHAE and YWHAZ and increased competition with RAF1 for binding to GTP-bound form of Ras proteins (NRAS, HRAS and KRAS). Acts downstream of the heterotrimeric G-protein beta/gamma-subunit complex to maintain the structural integrity of the Golgi membranes, and is required for protein transport along the secretory pathway. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane. May act by activating the lipid kinase phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the local synthesis of phosphorylated inositol lipids, which induces a sequential production of DAG, phosphatidic acid (PA) and lyso-PA (LPA) that are necessary for membrane fission and generation of specific transport carriers to the cell surface. Under oxidative stress, is phosphorylated at Tyr-463 via SRC-ABL1 and contributes to cell survival by activating IKK complex and subsequent nuclear translocation and activation of NFKB1. Involved in cell migration by regulating integrin alpha-5/beta-3 recycling and promoting its recruitment in newly forming focal adhesion. In osteoblast differentiation, mediates the bone morphogenic protein 2 (BMP2)-induced nuclear export of HDAC7, which results in the inhibition of HDAC7 transcriptional repression of RUNX2. In neurons, plays an important role in neuronal polarity by regulating the biogenesis of TGN-derived dendritic vesicles, and is involved in the maintenance of dendritic arborization and Golgi structure in hippocampal cells. May potentiate mitogenesis induced by the neuropeptide bombesin or vasopressin 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. Plays an important role in the proliferative response induced by low calcium in keratinocytes, through sustained activation of MAPK1/3 (ERK1/2) pathway. Downstream of novel PKC signaling, plays a role in cardiac hypertrophy by phosphorylating HDAC5, which in turn triggers XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A transcriptional activation and induction of downstream target genes that promote myocyte hypertrophy and pathological cardiac remodeling. Mediates cardiac troponin I (TNNI3) phosphorylation at the PKA sites, which results in reduced myofilament calcium sensitivity, and accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway is also involved in angiogenesis by mediating VEGFA-induced specific subset of gene expression, cell migration, and tube formation. In response to VEGFA, is necessary and required for HDAC7 phosphorylation which induces HDAC7 nuclear export and endothelial cell proliferation and migration. During apoptosis induced by cytarabine and other genotoxic agents, PRKD1 is cleaved by caspase-3 at Asp-378, resulting in activation of its kinase function and increased sensitivity of cells to the cytotoxic effects of genotoxic agents. In epithelial cells, is required for transducing flagellin-stimulated inflammatory responses by binding and phosphorylating TLR5, which contributes to MAPK14/p38 activation and production of inflammatory cytokines. May play a role in inflammatory response by mediating activation of NF-kappa-B. May be involved in pain transmission by directly modulating TRPV1 receptor.10 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domain 1 binds DAG with high affinity and appears to play the dominant role in mediating translocation to the cell membrane and trans-Golgi network. Phorbol-ester/DAG-type domain 2 binds phorbol ester with higher affinity. Autophosphorylation of Ser-742 and phosphorylation of Ser-738 by PKC relieves auto-inhibition by the PH domain. Phosphorylation on Tyr-463 by the SRC-ABL1 pathway in response to oxidative stress, is also required for activation. Activated by DAPK1 under oxidative stress.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei612 – 6121ATP
Active sitei706 – 7061Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri146 – 19651Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri270 – 32051Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi589 – 5979ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. metal ion binding Source: UniProtKB-KW
  4. protein kinase C activity Source: UniProtKB-EC
  5. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. apoptotic process Source: UniProtKB-KW
  3. cell proliferation Source: ProtInc
  4. cellular response to oxidative stress Source: UniProtKB
  5. cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
  6. Golgi organization Source: UniProtKB
  7. Golgi vesicle transport Source: UniProtKB
  8. inflammatory response Source: UniProtKB-KW
  9. innate immune response Source: UniProtKB-KW
  10. integrin-mediated signaling pathway Source: BHF-UCL
  11. intracellular signal transduction Source: BHF-UCL
  12. negative regulation of cell death Source: UniProtKB
  13. negative regulation of endocytosis Source: BHF-UCL
  14. peptidyl-serine phosphorylation Source: BHF-UCL
  15. positive regulation of angiogenesis Source: UniProtKB
  16. positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
  17. positive regulation of CREB transcription factor activity Source: BHF-UCL
  18. positive regulation of endothelial cell chemotaxis Source: BHF-UCL
  19. positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  20. positive regulation of endothelial cell migration Source: UniProtKB
  21. positive regulation of endothelial cell proliferation Source: BHF-UCL
  22. positive regulation of histone deacetylase activity Source: BHF-UCL
  23. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  24. positive regulation of neuron projection development Source: UniProtKB
  25. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  26. positive regulation of osteoblast differentiation Source: UniProtKB
  27. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  28. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  29. protein autophosphorylation Source: BHF-UCL
  30. regulation of integrin-mediated signaling pathway Source: BHF-UCL
  31. regulation of keratinocyte proliferation Source: UniProtKB
  32. signal transduction Source: ProtInc
  33. small molecule metabolic process Source: Reactome
  34. sphingolipid biosynthetic process Source: Reactome
  35. sphingolipid metabolic process Source: Reactome
  36. vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Angiogenesis, Apoptosis, Differentiation, Immunity, Inflammatory response, Innate immunity, Neurogenesis

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.
SignaLinkiQ15139.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase D1 (EC:2.7.11.13)
Alternative name(s):
Protein kinase C mu type
Protein kinase D
nPKC-D1
nPKC-mu
Gene namesi
Name:PRKD1
Synonyms:PKD, PKD1, PRKCM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:9407. PRKD1.

Subcellular locationi

Cytoplasm 1 Publication. Cell membrane 1 Publication. Golgi apparatustrans-Golgi network By similarity
Note: Translocation to the cell membrane is required for kinase activation.

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. cell cortex Source: Ensembl
  3. cytoplasm Source: HPA
  4. cytosol Source: UniProtKB
  5. integral component of plasma membrane Source: ProtInc
  6. nucleus Source: Ensembl
  7. plasma membrane Source: HPA
  8. trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi157 – 1571P → G: Increase in ability to bind phorbol ester, loss of ability to bind DAG. 1 Publication
Mutagenesisi281 – 2811P → G: No effect on ability to bind phorbol ester, slight increase in ability to bind DAG. 1 Publication
Mutagenesisi432 – 4321Y → E: Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. 1 Publication
Mutagenesisi432 – 4321Y → F: Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. Unaltered kinase activity. Decreased kinase activity; when associated with F-463 and F-502. 1 Publication
Mutagenesisi463 – 4631Y → E: Constitutive activation and constitutive phosphorylation of S-738 and S-742. 1 Publication
Mutagenesisi463 – 4631Y → F: Decreased phosphorylation level when coexpressed with either SRC or ABL in HeLa cells. Decreased kinase activity. 1 Publication
Mutagenesisi502 – 5021Y → E: Loss of activation. 1 Publication
Mutagenesisi502 – 5021Y → F: Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. Unaltered kinase activity. Decreased kinase activity; when associated with F-432 and F-502. 1 Publication
Mutagenesisi612 – 6121K → W: Loss of kinase activity. 1 Publication

Organism-specific databases

PharmGKBiPA33771.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 912912Serine/threonine-protein kinase D1PRO_0000055714Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei95 – 951Phosphotyrosine1 Publication
Modified residuei205 – 2051Phosphoserine2 Publications
Modified residuei208 – 2081Phosphoserine1 Publication
Modified residuei345 – 3451Phosphoserine1 Publication
Modified residuei397 – 3971Phosphoserine; by MAPK131 Publication
Modified residuei401 – 4011Phosphoserine; by MAPK131 Publication
Modified residuei432 – 4321Phosphotyrosine1 Publication
Modified residuei448 – 4481Phosphoserine1 Publication
Modified residuei463 – 4631Phosphotyrosine; by ABL2 Publications
Modified residuei473 – 4731Phosphoserine1 Publication
Modified residuei502 – 5021Phosphotyrosine1 Publication
Modified residuei738 – 7381Phosphoserine; by PKC/PRKCD1 Publication
Modified residuei742 – 7421Phosphoserine; by autocatalysis and PKC/PRKCD1 Publication
Modified residuei910 – 9101Phosphoserine; by autocatalysis1 Publication

Post-translational modificationi

Phosphorylated at Ser-397 and Ser-401 by MAPK13 during regulation of insulin secretion in pancreatic beta cells. Phosphorylated by DAPK1. Phosphorylated by ABL at Tyr-463, which primes the kinase in response to oxidative stress, and promotes a second step activating phosphorylation at Ser-738/Ser-742 by PKRD.7 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15139.
PaxDbiQ15139.
PRIDEiQ15139.

PTM databases

PhosphoSiteiQ15139.

Expressioni

Gene expression databases

BgeeiQ15139.
CleanExiHS_PKD1.
HS_PRKD1.
ExpressionAtlasiQ15139. baseline and differential.
GenevestigatoriQ15139.

Organism-specific databases

HPAiCAB018367.
HPA029834.

Interactioni

Subunit structurei

Interacts (via N-terminus) with ADAP1/CENTA1. Interacts with MAPK13 and SRC. Interacts with DAPK1 in an oxidative stress-regulated manner.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1181072,EBI-1181072
C1QBPQ070219EBI-1181072,EBI-347528
CDH1P128307EBI-1181072,EBI-727477
HSP90AB1P082382EBI-1181072,EBI-352572
MAPK13O152646EBI-1181072,EBI-2116951
MT2AP027957EBI-1181072,EBI-996616

Protein-protein interaction databases

BioGridi111573. 26 interactions.
DIPiDIP-38481N.
IntActiQ15139. 6 interactions.
MINTiMINT-88491.
STRINGi9606.ENSP00000333568.

Structurei

3D structure databases

ProteinModelPortaliQ15139.
SMRiQ15139. Positions 147-196, 271-320, 420-541, 550-841.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini422 – 541120PHPROSITE-ProRule annotationAdd
BLAST
Domaini583 – 839257Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi17 – 2610Poly-Ala
Compositional biasi200 – 2034Poly-Arg

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 fingeri146 – 19651Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri270 – 32051Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120480.
HOVERGENiHBG003564.
InParanoidiQ15139.
KOiK06070.
OrthoDBiEOG75B84N.
PhylomeDBiQ15139.
TreeFamiTF314320.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015727. Protein_Kinase_C_mu-related.
IPR002290. Ser/Thr_dual-sp_kinase.
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]

Sequencei

Sequence statusi: Complete.

Q15139-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAPPVLRPP SPLLPVAAAA AAAAAALVPG SGPGPAPFLA PVAAPVGGIS
60 70 80 90 100
FHLQIGLSRE PVLLLQDSSG DYSLAHVREM ACSIVDQKFP ECGFYGMYDK
110 120 130 140 150
ILLFRHDPTS ENILQLVKAA SDIQEGDLIE VVLSASATFE DFQIRPHALF
160 170 180 190 200
VHSYRAPAFC DHCGEMLWGL VRQGLKCEGC GLNYHKRCAF KIPNNCSGVR
210 220 230 240 250
RRRLSNVSLT GVSTIRTSSA ELSTSAPDEP LLQKSPSESF IGREKRSNSQ
260 270 280 290 300
SYIGRPIHLD KILMSKVKVP HTFVIHSYTR PTVCQYCKKL LKGLFRQGLQ
310 320 330 340 350
CKDCRFNCHK RCAPKVPNNC LGEVTINGDL LSPGAESDVV MEEGSDDNDS
360 370 380 390 400
ERNSGLMDDM EEAMVQDAEM AMAECQNDSG EMQDPDPDHE DANRTISPST
410 420 430 440 450
SNNIPLMRVV QSVKHTKRKS STVMKEGWMV HYTSKDTLRK RHYWRLDSKC
460 470 480 490 500
ITLFQNDTGS RYYKEIPLSE ILSLEPVKTS ALIPNGANPH CFEITTANVV
510 520 530 540 550
YYVGENVVNP SSPSPNNSVL TSGVGADVAR MWEIAIQHAL MPVIPKGSSV
560 570 580 590 600
GTGTNLHRDI SVSISVSNCQ IQENVDISTV YQIFPDEVLG SGQFGIVYGG
610 620 630 640 650
KHRKTGRDVA IKIIDKLRFP TKQESQLRNE VAILQNLHHP GVVNLECMFE
660 670 680 690 700
TPERVFVVME KLHGDMLEMI LSSEKGRLPE HITKFLITQI LVALRHLHFK
710 720 730 740 750
NIVHCDLKPE NVLLASADPF PQVKLCDFGF ARIIGEKSFR RSVVGTPAYL
760 770 780 790 800
APEVLRNKGY NRSLDMWSVG VIIYVSLSGT FPFNEDEDIH DQIQNAAFMY
810 820 830 840 850
PPNPWKEISH EAIDLINNLL QVKMRKRYSV DKTLSHPWLQ DYQTWLDLRE
860 870 880 890 900
LECKIGERYI THESDDLRWE KYAGEQGLQY PTHLINPSAS HSDTPETEET
910
EMKALGERVS IL
Length:912
Mass (Da):101,704
Last modified:October 14, 2008 - v2
Checksum:i0BC9414C335D2DBB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351A → R in CAA53384. (PubMed:8119958)Curated
Sequence conflicti877 – 8771G → R in CAA53384. (PubMed:8119958)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti152 – 1521H → Y in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035468
Natural varianti225 – 2251S → P.1 Publication
VAR_042324
Natural varianti478 – 4781K → Q.1 Publication
Corresponds to variant rs55852813 [ dbSNP | Ensembl ].
VAR_042325
Natural varianti585 – 5851P → S in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_042326
Natural varianti677 – 6771R → M in a lung bronchoalveolar carcinoma sample; somatic mutation. 1 Publication
VAR_042327
Natural varianti679 – 6791P → L.1 Publication
Corresponds to variant rs34588699 [ dbSNP | Ensembl ].
VAR_042328
Natural varianti825 – 8251R → K.
Corresponds to variant rs11161065 [ dbSNP | Ensembl ].
VAR_046988
Natural varianti857 – 8571E → K in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035469
Natural varianti891 – 8911H → R.1 Publication
Corresponds to variant rs45582934 [ dbSNP | Ensembl ].
VAR_042329

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75756 mRNA. Translation: CAA53384.1.
AK314170 mRNA. Translation: BAG36853.1.
AL135858 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65971.1.
CCDSiCCDS9637.1.
PIRiA53215.
RefSeqiNP_002733.2. NM_002742.2.
UniGeneiHs.508999.

Genome annotation databases

EnsembliENST00000331968; ENSP00000333568; ENSG00000184304.
ENST00000616995; ENSP00000482645; ENSG00000184304.
GeneIDi5587.
KEGGihsa:5587.
UCSCiuc001wqh.3. human.

Polymorphism databases

DMDMi209572639.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75756 mRNA. Translation: CAA53384.1 .
AK314170 mRNA. Translation: BAG36853.1 .
AL135858 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65971.1 .
CCDSi CCDS9637.1.
PIRi A53215.
RefSeqi NP_002733.2. NM_002742.2.
UniGenei Hs.508999.

3D structure databases

ProteinModelPortali Q15139.
SMRi Q15139. Positions 147-196, 271-320, 420-541, 550-841.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111573. 26 interactions.
DIPi DIP-38481N.
IntActi Q15139. 6 interactions.
MINTi MINT-88491.
STRINGi 9606.ENSP00000333568.

Chemistry

BindingDBi Q15139.
ChEMBLi CHEMBL2093867.
GuidetoPHARMACOLOGYi 1489.

PTM databases

PhosphoSitei Q15139.

Polymorphism databases

DMDMi 209572639.

Proteomic databases

MaxQBi Q15139.
PaxDbi Q15139.
PRIDEi Q15139.

Protocols and materials databases

DNASUi 5587.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331968 ; ENSP00000333568 ; ENSG00000184304 .
ENST00000616995 ; ENSP00000482645 ; ENSG00000184304 .
GeneIDi 5587.
KEGGi hsa:5587.
UCSCi uc001wqh.3. human.

Organism-specific databases

CTDi 5587.
GeneCardsi GC14M030045.
H-InvDB HIX0037727.
HGNCi HGNC:9407. PRKD1.
HPAi CAB018367.
HPA029834.
MIMi 605435. gene.
neXtProti NX_Q15139.
PharmGKBi PA33771.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120480.
HOVERGENi HBG003564.
InParanoidi Q15139.
KOi K06070.
OrthoDBi EOG75B84N.
PhylomeDBi Q15139.
TreeFami TF314320.

Enzyme and pathway databases

BRENDAi 2.7.11.13. 2681.
Reactomei REACT_115810. Sphingolipid de novo biosynthesis.
SignaLinki Q15139.

Miscellaneous databases

ChiTaRSi PRKD1. human.
GeneWikii Protein_kinase_D1.
GenomeRNAii 5587.
NextBioi 21670.
PROi Q15139.
SOURCEi Search...

Gene expression databases

Bgeei Q15139.
CleanExi HS_PKD1.
HS_PRKD1.
ExpressionAtlasi Q15139. baseline and differential.
Genevestigatori Q15139.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015727. Protein_Kinase_C_mu-related.
IPR002290. Ser/Thr_dual-sp_kinase.
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

« Hide 'large scale' publications
  1. "PKCmu is a novel, atypical member of the protein kinase C family."
    Johannes F.-J., Prestle J., Eis S., Oberhagemann P., Pfizenmaier K.
    J. Biol. Chem. 269:6140-6148(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor."
    Bagowski C.P., Stein-Gerlach M., Choidas A., Ullrich A.
    EMBO J. 18:5567-5576(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EGFR PHOSPHORYLATION.
  6. "Proteolytic cleavage and activation of protein kinase C [micro] by caspase-3 in the apoptotic response of cells to 1-beta -D-arabinofuranosylcytosine and other genotoxic agents."
    Endo K., Oki E., Biedermann V., Kojima H., Yoshida K., Johannes F.J., Kufe D., Datta R.
    J. Biol. Chem. 275:18476-18481(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS.
  7. "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.
  8. "Protein kinase D mediates a stress-induced NF-kappaB activation and survival pathway."
    Storz P., Toker A.
    EMBO J. 22:109-120(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL SURVIVAL.
  9. "Tyrosine phosphorylation of protein kinase D in the pleckstrin homology domain leads to activation."
    Storz P., Doppler H., Johannes F.J., Toker A.
    J. Biol. Chem. 278:17969-17976(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT TYR-432; TYR-463 AND TYR-502, MUTAGENESIS OF TYR-432; TYR-463; TYR-502 AND LYS-612.
  10. "Interaction between protein kinase Cmu and the vanilloid receptor type 1."
    Wang Y., Kedei N., Wang M., Wang Q.J., Huppler A.R., Toth A., Tran R., Blumberg P.M.
    J. Biol. Chem. 279:53674-53682(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TRPV1.
  11. "Protein kinase Cdelta selectively regulates protein kinase D-dependent activation of NF-kappaB in oxidative stress signaling."
    Storz P., Doppler H., Toker A.
    Mol. Cell. Biol. 24:2614-2626(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-463; SER-738 AND SER-742.
  12. "DAP kinase regulates JNK signaling by binding and activating protein kinase D under oxidative stress."
    Eisenberg-Lerner A., Kimchi A.
    Cell Death Differ. 14:1908-1915(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY DAPK1, INTERACTION WITH DAPK1, PHOSPHORYLATION AT SER-910, ENZYME REGULATION.
  13. "A novel tyrosine phosphorylation site in protein kinase D contributes to oxidative stress-mediated activation."
    Doppler H., Storz P.
    J. Biol. Chem. 282:31873-31881(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-95.
  14. "Protein kinase D interaction with TLR5 is required for inflammatory signaling in response to bacterial flagellin."
    Ivison S.M., Graham N.R., Bernales C.Q., Kifayet A., Ng N., Shobab L.A., Steiner T.S.
    J. Immunol. 178:5735-5743(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INNATE IMMUNITY.
  15. "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, PHORBOL-ESTER BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF PRO-157 AND PRO-281.
  16. "Protein kinase D-dependent phosphorylation and nuclear export of histone deacetylase 5 mediates vascular endothelial growth factor-induced gene expression and angiogenesis."
    Ha C.H., Wang W., Jhun B.S., Wong C., Hausser A., Pfizenmaier K., McKinsey T.A., Olson E.N., Jin Z.G.
    J. Biol. Chem. 283:14590-14599(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC5, FUNCTION IN ANGIOGENESIS.
  17. "Control of endothelial cell proliferation and migration by VEGF signaling to histone deacetylase 7."
    Wang S., Li X., Parra M., Verdin E., Bassel-Duby R., Olson E.N.
    Proc. Natl. Acad. Sci. U.S.A. 105:7738-7743(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC7.
  18. "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].
  19. Cited for: PHOSPHORYLATION AT SER-397 AND SER-401, INTERACTION WITH MAPK13, FUNCTION.
  20. "Protein kinase D controls the integrity of Golgi apparatus and the maintenance of dendritic arborization in hippocampal neurons."
    Czoendoer K., Ellwanger K., Fuchs Y.F., Lutz S., Gulyas M., Mansuy I.M., Hausser A., Pfizenmaier K., Schlett K.
    Mol. Biol. Cell 20:2108-2120(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANGIOGENESIS.
  21. Cited for: REVIEW ON FUNCTION IN TRAFFICKING.
  22. Cited for: REVIEW ON FUNCTION.
  23. "Protein kinase d in the cardiovascular system: emerging roles in health and disease."
    Avkiran M., Rowland A.J., Cuello F., Haworth R.S.
    Circ. Res. 102:157-163(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-345; SER-448 AND SER-473, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Protein kinase D1, a new molecular player in VEGF signaling and angiogenesis."
    Ha C.H., Jin Z.G.
    Mol. Cells 28:1-5(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN ANGIOGENESIS.
  26. "Protein kinase D signaling: multiple biological functions in health and disease."
    Rozengurt E.
    Physiology (Bethesda) 26:23-33(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  27. "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-205 AND SER-208, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. Cited for: VARIANTS [LARGE SCALE ANALYSIS] TYR-152 AND LYS-857.
  29. "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] PRO-225; GLN-478; SER-585; MET-677; LEU-679 AND ARG-891.

Entry informationi

Entry nameiKPCD1_HUMAN
AccessioniPrimary (citable) accession number: Q15139
Secondary accession number(s): A6NL64, B2RAF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 14, 2008
Last modified: November 26, 2014
This is version 152 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3