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Q62101

- KPCD1_MOUSE

UniProt

Q62101 - KPCD1_MOUSE

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Protein

Serine/threonine-protein kinase D1

Gene

Prkd1

Organism
Mus musculus (Mouse)
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-469 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.7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.

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-748 and phosphorylation of Ser-744 by PKC relieves auto-inhibition by the PH domain. Phosphorylation on Tyr-469 by the SRC-ABL1 pathway in response to oxidative stress, is also required for activation. Activated by DAPK1 under oxidative stress By similarity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei618 – 6181ATPPROSITE-ProRule annotation
Active sitei712 – 7121Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri144 – 19451Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri276 – 32651Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi595 – 6039ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. apoptotic process Source: UniProtKB-KW
  3. cellular response to oxidative stress Source: UniProtKB
  4. cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
  5. Golgi organization Source: UniProtKB
  6. Golgi vesicle transport Source: UniProtKB
  7. inflammatory response Source: UniProtKB-KW
  8. innate immune response Source: UniProtKB-KW
  9. intracellular signal transduction Source: Ensembl
  10. negative regulation of cell death Source: UniProtKB
  11. peptidyl-serine phosphorylation Source: Ensembl
  12. positive regulation of angiogenesis Source: UniProtKB
  13. positive regulation of blood vessel endothelial cell migration Source: Ensembl
  14. positive regulation of CREB transcription factor activity Source: Ensembl
  15. positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: Ensembl
  16. positive regulation of endothelial cell migration Source: UniProtKB
  17. positive regulation of endothelial cell proliferation Source: Ensembl
  18. positive regulation of histone deacetylase activity Source: Ensembl
  19. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  20. positive regulation of neuron projection development Source: UniProtKB
  21. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  22. positive regulation of osteoblast differentiation Source: UniProtKB
  23. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
  24. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  25. regulation of keratinocyte proliferation Source: UniProtKB
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

BRENDAi2.7.11.1. 3474.
ReactomeiREACT_198151. Sphingolipid de novo biosynthesis.

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:Pkcm, Pkd, Prkcm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:99879. Prkd1.

Subcellular locationi

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

GO - Cellular componenti

  1. cell-cell junction Source: MGI
  2. cell cortex Source: MGI
  3. cytoplasm Source: MGI
  4. cytosol Source: UniProtKB
  5. nucleus Source: MGI
  6. plasma membrane Source: UniProtKB
  7. 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
Mutagenesisi744 – 7441S → A: Loss of basal kinase activity and phorbol ester-stimulated kinase activity; when associated with A-748. 1 Publication
Mutagenesisi744 – 7441S → D: High basal kinase activity, loss of phorbol ester-stimulated kinase activity; when associated with D-748. 1 Publication
Mutagenesisi748 – 7481S → A: Loss of basal kinase activity and phorbol ester-stimulated kinase activity; when associated with A-744. 1 Publication
Mutagenesisi748 – 7481S → D: High basal kinase activity, loss of phorbol ester-stimulated kinase activity; when associated with D-744. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 918918Serine/threonine-protein kinase D1PRO_0000055715Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 931PhosphotyrosineBy similarity
Modified residuei203 – 2031PhosphoserineBy similarity
Modified residuei206 – 2061PhosphoserineBy similarity
Modified residuei351 – 3511PhosphoserineBy similarity
Modified residuei403 – 4031Phosphoserine; by MAPK13By similarity
Modified residuei407 – 4071Phosphoserine; by MAPK13By similarity
Modified residuei438 – 4381PhosphotyrosineBy similarity
Modified residuei454 – 4541PhosphoserineBy similarity
Modified residuei469 – 4691Phosphotyrosine; by ABLBy similarity
Modified residuei508 – 5081PhosphotyrosineBy similarity
Modified residuei744 – 7441Phosphoserine; by PKC/PRKCD2 Publications
Modified residuei748 – 7481Phosphoserine; by autocatalysis and PKC/PRKCD2 Publications
Modified residuei916 – 9161Phosphoserine; by autocatalysis1 Publication

Post-translational modificationi

Phosphorylated at Ser-403 and Ser-407 by MAPK13 during regulation of insulin secretion in pancreatic beta cells. Phosphorylated by DAPK1. Phosphorylated by ABL at Tyr-469, which primes the kinase in response to oxidative stress, and promotes a second step activating phosphorylation at Ser-744/Ser-748 by PKRD By similarity.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ62101.
PaxDbiQ62101.
PRIDEiQ62101.

PTM databases

PhosphoSiteiQ62101.

Expressioni

Gene expression databases

BgeeiQ62101.
CleanExiMM_PRKD1.
GenevestigatoriQ62101.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
ITGB3P051062EBI-6903636,EBI-702847From a different organism.

Protein-protein interaction databases

IntActiQ62101. 2 interactions.
STRINGi10090.ENSMUSP00000002765.

Structurei

3D structure databases

ProteinModelPortaliQ62101.
SMRiQ62101. Positions 145-194, 277-326, 426-547, 556-847.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini428 – 547120PHPROSITE-ProRule annotationAdd
BLAST
Domaini589 – 845257Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi16 – 2611Poly-AlaAdd
BLAST
Compositional biasi198 – 2014Poly-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 fingeri144 – 19451Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri276 – 32651Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00750000117523.
HOGENOMiHOG000015135.
HOVERGENiHBG003564.
InParanoidiQ62101.
KOiK06070.
OMAiMAECQND.
OrthoDBiEOG75B84N.
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.

Q62101-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVPPLLRPP SPLLPAAAAV AAAAAALVPG SGPAPFPAPG AAPAGGISFH
60 70 80 90 100
LQIGLSREPV LLLQDSSGDY SLAHVREMAC SIVDQKFPEC GFYGLYDKIL
110 120 130 140 150
LFRHDPASDN ILQLVKIASD IQEGDLIEVV LSASATFEDF QIRPHALFVH
160 170 180 190 200
SYRAPAFCDH CGEMLWGLVR QGLKCEGCGL NYHKRCAFKI PNNCSGVRRR
210 220 230 240 250
RLSNVSLTGL GTVRTASAEF STSVPDEPLL SPVSPGFEQK SPSESFIGRE
260 270 280 290 300
KRSNSQSYIG RPIQLDKLLM SKVKVPHTFV IHSYTRPTVC QFCKKLLKGL
310 320 330 340 350
FRQGLQCKDC RFNCHKRCAP KVPNNCLGEV TINGELLSPG AESDVVMEEG
360 370 380 390 400
SDDNDSERNS GLMDDMDEAM VQDTEMALAE GQSGGAEMQD PDADQEDSNR
410 420 430 440 450
TISPSTSNNI PLMRVVQSVK HTKRRSSTVM KEGWMVHYTS KDTLRKRHYW
460 470 480 490 500
RLDSKCITLF QNDTGSRYYK EIPLSEILCL EPAKPSALTP VGATPHCFEI
510 520 530 540 550
TTANVVYYVG ENVVNPSSSP PNNSVLPSGI GPDVARMWEV AIQHALMPVI
560 570 580 590 600
PKGSSVGSGS NSHKDISVSI SVSNCQIQEN VDISTVYQIF PDEVLGSGQF
610 620 630 640 650
GIVYGGKHRK TGRDVAIKII DKLRFPTKQE SQLRNEVAIL QNLHHPGVVN
660 670 680 690 700
LECMFETPER VFVVMEKLHG DMLEMILSSE KGRLPEHITK FLITQILVAL
710 720 730 740 750
RHLHFKNIVH CDLKPENVLL ASADPFPQVK LCDFGFARII GEKSFRRSVV
760 770 780 790 800
GTPAYLAPEV LRNKGYNRSL DMWSVGVIIY VSLSGTFPFN EDEDIHDQIQ
810 820 830 840 850
NAAFMYPPNP WKEISHEAID LINNLLQVKM RKRYSVDKTL SHPWLQDYQT
860 870 880 890 900
WLDLRELECR IGERYITHES DDSRWEQYAG EQGLQYPAHL ISLSASHSDS
910
PEAEEREMKA LSERVSIL
Length:918
Mass (Da):102,037
Last modified:July 27, 2011 - v2
Checksum:iA59FEBAFCE0D0F13
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti683 – 6831R → W in CAA84283. (PubMed:8078925)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z34524 mRNA. Translation: CAA84283.1.
AC099603 Genomic DNA. No translation available.
AC154543 Genomic DNA. No translation available.
CT009740 Genomic DNA. No translation available.
CT010578 Genomic DNA. No translation available.
CCDSiCCDS49059.1.
PIRiI48719.
RefSeqiNP_032884.2. NM_008858.3.
UniGeneiMm.133719.

Genome annotation databases

EnsembliENSMUST00000002765; ENSMUSP00000002765; ENSMUSG00000002688.
GeneIDi18760.
KEGGimmu:18760.
UCSCiuc007nmj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z34524 mRNA. Translation: CAA84283.1 .
AC099603 Genomic DNA. No translation available.
AC154543 Genomic DNA. No translation available.
CT009740 Genomic DNA. No translation available.
CT010578 Genomic DNA. No translation available.
CCDSi CCDS49059.1.
PIRi I48719.
RefSeqi NP_032884.2. NM_008858.3.
UniGenei Mm.133719.

3D structure databases

ProteinModelPortali Q62101.
SMRi Q62101. Positions 145-194, 277-326, 426-547, 556-847.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q62101. 2 interactions.
STRINGi 10090.ENSMUSP00000002765.

PTM databases

PhosphoSitei Q62101.

Proteomic databases

MaxQBi Q62101.
PaxDbi Q62101.
PRIDEi Q62101.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000002765 ; ENSMUSP00000002765 ; ENSMUSG00000002688 .
GeneIDi 18760.
KEGGi mmu:18760.
UCSCi uc007nmj.1. mouse.

Organism-specific databases

CTDi 5587.
MGIi MGI:99879. Prkd1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00750000117523.
HOGENOMi HOG000015135.
HOVERGENi HBG003564.
InParanoidi Q62101.
KOi K06070.
OMAi MAECQND.
OrthoDBi EOG75B84N.
TreeFami TF314320.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 3474.
Reactomei REACT_198151. Sphingolipid de novo biosynthesis.

Miscellaneous databases

NextBioi 294945.
PROi Q62101.
SOURCEi Search...

Gene expression databases

Bgeei Q62101.
CleanExi MM_PRKD1.
Genevestigatori Q62101.

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. "Molecular cloning and characterization of protein kinase D: a target for diacylglycerol and phorbol esters with a distinctive catalytic domain."
    Valverde A.M., Sinnet-Smith J., Van Lint J., Rozengurt E.
    Proc. Natl. Acad. Sci. U.S.A. 91:8572-8576(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Lung.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Characterization of serine 916 as an in vivo autophosphorylation site for protein kinase D/protein kinase Cmu."
    Matthews S.A., Rozengurt E., Cantrell D.
    J. Biol. Chem. 274:26543-26549(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-916.
  4. "Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network."
    Liljedahl M., Maeda Y., Colanzi A., Ayala I., Van Lint J., Malhotra V.
    Cell 104:409-420(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF TRANS-GOLGI NETWORK, SUBCELLULAR LOCATION.
  5. "Activation loop Ser744 and Ser748 in protein kinase D are transphosphorylated in vivo."
    Waldron R.T., Rey O., Iglesias T., Tugal T., Cantrell D., Rozengurt E.
    J. Biol. Chem. 276:32606-32615(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-744 AND SER-748.
  6. "The RAS effector RIN1 directly competes with RAF and is regulated by 14-3-3 proteins."
    Wang Y., Waldron R.T., Dhaka A., Patel A., Riley M.M., Rozengurt E., Colicelli J.
    Mol. Cell. Biol. 22:916-926(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RIN1 PHOSPHORYLATION.
  7. "Protein kinase C phosphorylates protein kinase D activation loop Ser744 and Ser748 and releases autoinhibition by the pleckstrin homology domain."
    Waldron R.T., Rozengurt E.
    J. Biol. Chem. 278:154-163(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF SER-744 AND SER-748, PHOSPHORYLATION AT SER-744 AND SER-748.
  8. "PKD1/PKCmu promotes alphavbeta3 integrin recycling and delivery to nascent focal adhesions."
    Woods A.J., White D.P., Caswell P.T., Norman J.C.
    EMBO J. 23:2531-2543(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION.
  9. "Protein kinase D potentiates DNA synthesis induced by Gq-coupled receptors by increasing the duration of ERK signaling in swiss 3T3 cells."
    Sinnett-Smith J., Zhukova E., Hsieh N., Jiang X., Rozengurt E.
    J. Biol. Chem. 279:16883-16893(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL PROLIFERATION.
  10. "Bone morphogenic protein 2 activates protein kinase D to regulate histone deacetylase 7 localization and repression of Runx2."
    Jensen E.D., Gopalakrishnan R., Westendorf J.J.
    J. Biol. Chem. 284:2225-2234(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN OSTEOBLAST DIFFERENTIATION.
  11. "Protein kinase D is implicated in the reversible commitment to differentiation in primary cultures of mouse keratinocytes."
    Jadali A., Ghazizadeh S.
    J. Biol. Chem. 285:23387-23397(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL PROLIFERATION.

Entry informationi

Entry nameiKPCD1_MOUSE
AccessioniPrimary (citable) accession number: Q62101
Secondary accession number(s): E9QNA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3