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Q9WTQ1

- KPCD1_RAT

UniProt

Q9WTQ1 - KPCD1_RAT

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Protein
Serine/threonine-protein kinase D1
Gene
Prkd1, Pkcm, Pkd, Prkcm
Organism
Rattus norvegicus (Rat)
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.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei618 – 6181ATP By similarity
Active sitei712 – 7121Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri144 – 19451Phorbol-ester/DAG-type 1
Add
BLAST
Zinc fingeri276 – 32651Phorbol-ester/DAG-type 2
Add
BLAST
Nucleotide bindingi595 – 6039ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

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

ReactomeiREACT_196736. 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: Chromosome 6

Organism-specific databases

RGDi620964. Prkd1.

Subcellular locationi

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

GO - Cellular componenti

  1. cell cortex Source: Ensembl
  2. cell-cell junction Source: Ensembl
  3. cytosol Source: UniProtKB
  4. nucleus Source: Ensembl
  5. plasma membrane Source: UniProtKB
  6. trans-Golgi network Source: UniProtKB
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 D1
PRO_0000333881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 931Phosphotyrosine By similarity
Modified residuei203 – 2031Phosphoserine By similarity
Modified residuei206 – 2061Phosphoserine By similarity
Modified residuei351 – 3511Phosphoserine By similarity
Modified residuei403 – 4031Phosphoserine; by MAPK13 By similarity
Modified residuei407 – 4071Phosphoserine; by MAPK13 By similarity
Modified residuei438 – 4381Phosphotyrosine By similarity
Modified residuei454 – 4541Phosphoserine By similarity
Modified residuei469 – 4691Phosphotyrosine; by ABL By similarity
Modified residuei508 – 5081Phosphotyrosine By similarity
Modified residuei744 – 7441Phosphoserine; by PKC/PRKCD By similarity
Modified residuei748 – 7481Phosphoserine; by autocatalysis and PKC/PRKCD By 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.1 Publication

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.

Protein-protein interaction databases

IntActiQ9WTQ1. 1 interaction.
STRINGi10116.ENSRNOP00000005596.

Structurei

3D structure databases

ProteinModelPortaliQ9WTQ1.
SMRiQ9WTQ1. Positions 425-552.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini428 – 547120PH
Add
BLAST
Domaini589 – 845257Protein kinase
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi16 – 2611Poly-Ala
Add
BLAST
Compositional biasi198 – 2014Poly-Arg

Sequence similaritiesi

Contains 1 PH domain.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00750000117523.
HOGENOMiHOG000015135.
HOVERGENiHBG003564.
InParanoidiQ9WTQ1.
KOiK06070.
OMAiMAECQND.
OrthoDBiEOG75B84N.
PhylomeDBiQ9WTQ1.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015727. Protein_Kinase_C_mu-related.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
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

MSAPPLLRPP SPLLPAAAAV AAAAAALVPG SGPAPFPAPG AAPAGGISFH    50
LQIGLSREPV LLLQDSSGDY SLAHVREMAC SIVDQKFPEC GFYGLYDKIL 100
LFRHDPASEN ILQLVKIASD IQEGDLIEVV LSASATFEDF QIRPHALFVH 150
SYRAPAFCDH CGEMLWGLVR QGLKCEGCGL NYHKRCAFKI PNNCSGVRRR 200
RLSNVSLTGL GTVRTASAEF STSAPDEPLL SPVSPGFEQK SPSESFIGRE 250
KRSNSQSYVG RPIQLDKLLM SKVKVPHTFV IHSYTRPTVC QFCKKLLKGL 300
FRQGLQCKDC RFNCHKRCAP KVPNNCLGEV TINGELLSPG AESDVVMEEG 350
SDDNDSERNS GLMDDMDEAM VQDTEMALAE GQSDGAEMQD PDADQEDSNR 400
TISPSTSNNI PLMRVVQSVK HTKRRSSTVM KEGWMVHYTS KDTLRKRHYW 450
RLDSKSITLF QNDTGSRYYK EIPLSEILCL EPAKPSALIP TGANPHCFEI 500
TTANVVYYVG ENVVNPSSPP PNNSVPPSGI GTDVARMWEV AIQHALMPVI 550
PKGSSVGSGT NSHKDISVSI SVSNSQIQEN VDISTVYQIF PDEVLGSGQF 600
GIVYGGKHRK TGRDVAIKII DKLRFPTKQE SQLRNEVAIL QNLHHPGVVN 650
LECMFETPER VFVVMEKLHG DMLEMILSSE KGRLPEHITK FLITQILVAL 700
RHLHFKNIVH CDLKPENVLL ASADPFPQVK LCDFGFARII GEKSFRRSVV 750
GTPAYLAPEV LRNKGYNRSL DMWSVGVIIY VSLSGTFPFN EDEDIHDQIQ 800
NAAFMYPPNP WKEISHEAID LINNLLQVKM RKRYSVDKTL SHPWLQDYQT 850
WLDLRELECR IGERYITHES DDSRWEQYAG EQGLQYPAHL INLSASHGDS 900
PEAEEREMKA LSERVSIL 918
Length:918
Mass (Da):102,043
Last modified:May 20, 2008 - v2
Checksum:i93E46AF6C0242B86
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti718 – 7181V → G in BAA78373. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
RefSeqi NP_001263644.1. NM_001276715.1.
UniGenei Rn.144619.
Rn.234516.

3D structure databases

ProteinModelPortali Q9WTQ1.
SMRi Q9WTQ1. Positions 425-552.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9WTQ1. 1 interaction.
STRINGi 10116.ENSRNOP00000005596.

PTM databases

PhosphoSitei Q9WTQ1.

Proteomic databases

PaxDbi Q9WTQ1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000068077 ; ENSRNOP00000063159 ; ENSRNOG00000004165 .
GeneIDi 85421.
KEGGi rno:85421.
UCSCi RGD:620964. rat.

Organism-specific databases

CTDi 5587.
RGDi 620964. Prkd1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00750000117523.
HOGENOMi HOG000015135.
HOVERGENi HBG003564.
InParanoidi Q9WTQ1.
KOi K06070.
OMAi MAECQND.
OrthoDBi EOG75B84N.
PhylomeDBi Q9WTQ1.

Enzyme and pathway databases

Reactomei REACT_196736. Sphingolipid de novo biosynthesis.

Miscellaneous databases

NextBioi 617508.

Gene expression databases

Genevestigatori Q9WTQ1.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015727. Protein_Kinase_C_mu-related.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
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. "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: September 3, 2014
This is version 88 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