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Protein

Serine/threonine-protein kinase D1

Gene

Prkd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

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

GO - Biological processi

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

ReactomeiREACT_296412. 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi620964. Prkd1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 918918Serine/threonine-protein kinase D1PRO_0000333881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311PhosphoserineBy similarity
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/PRKCDBy similarity
Modified residuei748 – 7481Phosphoserine; by autocatalysis and PKC/PRKCDBy similarity
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

PaxDbiQ9WTQ1.

PTM databases

PhosphoSiteiQ9WTQ1.

Expressioni

Gene expression databases

GenevestigatoriQ9WTQ1.

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

Protein-protein interaction databases

BioGridi250093. 1 interaction.
IntActiQ9WTQ1. 1 interaction.
STRINGi10116.ENSRNOP00000005596.

Structurei

3D structure databases

ProteinModelPortaliQ9WTQ1.
SMRiQ9WTQ1. Positions 425-552.
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.
GeneTreeiENSGT00780000121901.
HOGENOMiHOG000015135.
HOVERGENiHBG003564.
InParanoidiQ9WTQ1.
KOiK06070.
OMAiMQDPDPD.
OrthoDBiEOG75B84N.
PhylomeDBiQ9WTQ1.

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.

Q9WTQ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAPPLLRPP SPLLPAAAAV AAAAAALVPG SGPAPFPAPG AAPAGGISFH
60 70 80 90 100
LQIGLSREPV LLLQDSSGDY SLAHVREMAC SIVDQKFPEC GFYGLYDKIL
110 120 130 140 150
LFRHDPASEN ILQLVKIASD IQEGDLIEVV LSASATFEDF QIRPHALFVH
160 170 180 190 200
SYRAPAFCDH CGEMLWGLVR QGLKCEGCGL NYHKRCAFKI PNNCSGVRRR
210 220 230 240 250
RLSNVSLTGL GTVRTASAEF STSAPDEPLL SPVSPGFEQK SPSESFIGRE
260 270 280 290 300
KRSNSQSYVG RPIQLDKLLM SKVKVPHTFV IHSYTRPTVC QFCKKLLKGL
310 320 330 340 350
FRQGLQCKDC RFNCHKRCAP KVPNNCLGEV TINGELLSPG AESDVVMEEG
360 370 380 390 400
SDDNDSERNS GLMDDMDEAM VQDTEMALAE GQSDGAEMQD PDADQEDSNR
410 420 430 440 450
TISPSTSNNI PLMRVVQSVK HTKRRSSTVM KEGWMVHYTS KDTLRKRHYW
460 470 480 490 500
RLDSKSITLF QNDTGSRYYK EIPLSEILCL EPAKPSALIP TGANPHCFEI
510 520 530 540 550
TTANVVYYVG ENVVNPSSPP PNNSVPPSGI GTDVARMWEV AIQHALMPVI
560 570 580 590 600
PKGSSVGSGT NSHKDISVSI SVSNSQIQEN 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 INLSASHGDS
910
PEAEEREMKA LSERVSIL
Length:918
Mass (Da):102,043
Last modified:May 20, 2008 - v2
Checksum:i93E46AF6C0242B86
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti718 – 7181V → G in BAA78373 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03048549 Genomic DNA. No translation available.
AABR03048623 Genomic DNA. No translation available.
AABR03048825 Genomic DNA. No translation available.
AABR03049215 Genomic DNA. No translation available.
AABR03049278 Genomic DNA. No translation available.
AABR03050321 Genomic DNA. No translation available.
AABR03052344 Genomic DNA. No translation available.
AB020616 mRNA. Translation: BAA78373.1.
RefSeqiNP_001263644.1. NM_001276715.1.
UniGeneiRn.144619.
Rn.234516.

Genome annotation databases

EnsembliENSRNOT00000068077; ENSRNOP00000063159; ENSRNOG00000004165.
GeneIDi85421.
KEGGirno:85421.
UCSCiRGD:620964. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03048549 Genomic DNA. No translation available.
AABR03048623 Genomic DNA. No translation available.
AABR03048825 Genomic DNA. No translation available.
AABR03049215 Genomic DNA. No translation available.
AABR03049278 Genomic DNA. No translation available.
AABR03050321 Genomic DNA. No translation available.
AABR03052344 Genomic DNA. No translation available.
AB020616 mRNA. Translation: BAA78373.1.
RefSeqiNP_001263644.1. NM_001276715.1.
UniGeneiRn.144619.
Rn.234516.

3D structure databases

ProteinModelPortaliQ9WTQ1.
SMRiQ9WTQ1. Positions 425-552.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250093. 1 interaction.
IntActiQ9WTQ1. 1 interaction.
STRINGi10116.ENSRNOP00000005596.

PTM databases

PhosphoSiteiQ9WTQ1.

Proteomic databases

PaxDbiQ9WTQ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000068077; ENSRNOP00000063159; ENSRNOG00000004165.
GeneIDi85421.
KEGGirno:85421.
UCSCiRGD:620964. rat.

Organism-specific databases

CTDi5587.
RGDi620964. Prkd1.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121901.
HOGENOMiHOG000015135.
HOVERGENiHBG003564.
InParanoidiQ9WTQ1.
KOiK06070.
OMAiMQDPDPD.
OrthoDBiEOG75B84N.
PhylomeDBiQ9WTQ1.

Enzyme and pathway databases

ReactomeiREACT_296412. Sphingolipid de novo biosynthesis.

Miscellaneous databases

NextBioi617508.
PROiQ9WTQ1.

Gene expression databases

GenevestigatoriQ9WTQ1.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Rat PKC mu mRNA partial cds."
    Minami H., Owada Y., Kondo H.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 718-864.
    Strain: Wistar.
    Tissue: Brain.
  3. "Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D."
    Jamora C., Yamanouye N., Van Lint J., Laudenslager J., Vandenheede J.R., Faulkner D.J., Malhotra V.
    Cell 98:59-68(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN GOLGI REGULATION.
  4. "Protein kinase D is a novel mediator of cardiac troponin I phosphorylation and regulates myofilament function."
    Haworth R.S., Cuello F., Herron T.J., Franzen G., Kentish J.C., Gautel M., Avkiran M.
    Circ. Res. 95:1091-1099(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CARDIOMYOCYTE.
  5. "Hepatocyte resistance to oxidative stress is dependent on protein kinase C-mediated down-regulation of c-Jun/AP-1."
    Wang Y., Schattenberg J.M., Rigoli R.M., Storz P., Czaja M.J.
    J. Biol. Chem. 279:31089-31097(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-744; SER-748 AND SER-916.
  6. "Protein kinases C and D mediate agonist-dependent cardiac hypertrophy through nuclear export of histone deacetylase 5."
    Vega R.B., Harrison B.C., Meadows E., Roberts C.R., Papst P.J., Olson E.N., McKinsey T.A.
    Mol. Cell. Biol. 24:8374-8385(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CARDIAC HYPERTROPHY.
  7. "Protein kinase d regulates trafficking of dendritic membrane proteins in developing neurons."
    Bisbal M., Conde C., Donoso M., Bollati F., Sesma J., Quiroga S., Diaz Anel A., Malhotra V., Marzolo M.P., Caceres A.
    J. Neurosci. 28:9297-9308(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEURONAL POLARITY.

Entry informationi

Entry nameiKPCD1_RAT
AccessioniPrimary (citable) accession number: Q9WTQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: May 27, 2015
This is version 97 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.