Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8BZ03

- KPCD2_MOUSE

UniProt

Q8BZ03 - KPCD2_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Serine/threonine-protein kinase D2

Gene

Prkd2

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 cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. In response to oxidative stress, is phosphorylated at Tyr-439 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B. In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77. Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation. During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens. In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF-kappa-B-dependent pathway. During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane. Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis. In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN. Downstream of PRKCA, plays important roles in angiotensin-2-induced monocyte adhesion to endothelial cells.2 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 domains bind DAG, mediating translocation to membranes. Autophosphorylation of Ser-711 and phosphorylation of Ser-707 by PKC relieves auto-inhibition by the PH domain (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei581 – 5811ATPPROSITE-ProRule annotation
Active sitei675 – 6751Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri138 – 18851Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri265 – 31551Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi558 – 5669ATPPROSITE-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. cell adhesion Source: UniProtKB-KW
  3. cell death Source: Ensembl
  4. intracellular signal transduction Source: Ensembl
  5. peptidyl-serine phosphorylation Source: Ensembl
  6. positive regulation of angiogenesis Source: UniProtKB
  7. positive regulation of blood vessel endothelial cell migration Source: Ensembl
  8. positive regulation of cell adhesion Source: UniProtKB
  9. positive regulation of CREB transcription factor activity Source: Ensembl
  10. positive regulation of DNA biosynthetic process Source: UniProtKB
  11. positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: Ensembl
  12. positive regulation of endothelial cell migration Source: UniProtKB
  13. positive regulation of endothelial cell proliferation Source: UniProtKB
  14. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  15. positive regulation of fibroblast growth factor receptor signaling pathway Source: UniProtKB
  16. positive regulation of histone deacetylase activity Source: Ensembl
  17. positive regulation of interleukin-2 production Source: UniProtKB
  18. positive regulation of interleukin-8 production Source: UniProtKB
  19. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  20. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
  21. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  22. positive regulation of T cell receptor signaling pathway Source: UniProtKB
  23. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  24. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
  25. protein autophosphorylation Source: Ensembl
  26. T cell receptor signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Adaptive immunity, Angiogenesis, Cell adhesion, Immunity

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase D2 (EC:2.7.11.13)
Alternative name(s):
nPKC-D2
Gene namesi
Name:Prkd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:2141917. Prkd2.

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. Accumulates in the nucleus upon CK1-mediated phosphorylation after activation of G-protein-coupled receptors. Nuclear accumulation is regulated by blocking nuclear export of active PRKD2 rather than by increasing import (By similarity).By similarity

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-KW
  2. nucleus Source: Ensembl
  3. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi707 – 7071S → A: Strong decrease in catalytic activity; when associated with A-711. 1 Publication
Mutagenesisi711 – 7111S → A: Strong decrease in catalytic activity; when associated with A-707. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 875875Serine/threonine-protein kinase D2PRO_0000260436Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei200 – 2001PhosphoserineBy similarity
Modified residuei203 – 2031PhosphoserineBy similarity
Modified residuei206 – 2061PhosphoserineBy similarity
Modified residuei214 – 2141PhosphoserineBy similarity
Modified residuei244 – 2441Phosphoserine; by CSNK1D and CSNK1EBy similarity
Modified residuei439 – 4391Phosphotyrosine; by ABL1By similarity
Modified residuei519 – 5191PhosphoserineBy similarity
Modified residuei707 – 7071Phosphoserine; by PKC1 Publication
Modified residuei711 – 7111Phosphoserine; by autocatalysis1 Publication
Modified residuei718 – 7181PhosphotyrosineBy similarity
Modified residuei873 – 8731Phosphoserine; by autocatalysis1 Publication

Post-translational modificationi

Phosphorylation of Ser-873 correlates with the activation status of the kinase. Ser-707 is probably phosphorylated by PKC. Phosphorylation at Ser-244 by CSNK1D and CSNK1E promotes nuclear localization and substrate targeting. Phosphorylation at Ser-244, Ser-707 and Ser-711 is required for nuclear localization. Phosphorylated at Tyr-438 by ABL1 in response to oxidative stress (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BZ03.
PaxDbiQ8BZ03.
PRIDEiQ8BZ03.

PTM databases

PhosphoSiteiQ8BZ03.

Expressioni

Gene expression databases

BgeeiQ8BZ03.
CleanExiMM_PRKD2.
GenevestigatoriQ8BZ03.

Interactioni

Subunit structurei

Interacts (via C-terminus) with LCK.By similarity

Protein-protein interaction databases

IntActiQ8BZ03. 1 interaction.
MINTiMINT-4113563.

Structurei

3D structure databases

ProteinModelPortaliQ8BZ03.
SMRiQ8BZ03. Positions 138-188, 266-358, 396-510, 518-842.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini398 – 510113PHPROSITE-ProRule annotationAdd
BLAST
Domaini552 – 808257Protein kinasePROSITE-ProRule annotationAdd
BLAST

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 fingeri138 – 18851Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri265 – 31551Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120480.
HOGENOMiHOG000015135.
HOVERGENiHBG003564.
InParanoidiQ8BZ03.
KOiK06070.
OMAiLPQDHEM.
OrthoDBiEOG75B84N.
PhylomeDBiQ8BZ03.
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.

Q8BZ03-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAAPSHPAG LPGSPGPGSP PPPGGLDLQS PPPLLPQIPA PGSGVSFHIQ
60 70 80 90 100
IGLTREFVLL PAASELAHVK QLACSIVDQK FPECGFYGLY DKILLFKHDP
110 120 130 140 150
TSANLLQLVR SAADIQEGDL VEVVLSASAT FEDFQIRPHA LTVHSYRAPA
160 170 180 190 200
FCDHCGEMLF GLVRQGLKCD GCGLNYHKRC AFSIPNNCSG ARKRRLSSTS
210 220 230 240 250
LASGHSVRLG SSESLPCTAE ELSRSTTDLL PRRPPSSSSS SSSSSFYTGR
260 270 280 290 300
PIELDKMLMS KVKVPHTFLI HSYTRPTVCQ ACKKLLKGLF RQGLQCKDCK
310 320 330 340 350
FNCHKRCATR VPNDCLGEAL INGDVPMEEA ADYSEADKSS ISDELEDSGV
360 370 380 390 400
IPGSHSESAL HASEEEEGEG HKAQSSLGYI PLMRVVQSVR HTTRKSSTTL
410 420 430 440 450
REGWVVHYSN KDTLRKRHYW RLDCKCITLF QNNTTNRYYK EIPLSEILAV
460 470 480 490 500
EPAQNFSLVP PGTNPHCFEI ITANVTYFVG ETPGGAPGGP SGQGTEAVRG
510 520 530 540 550
WETAIRQALM PVILQDAPSA PGHTPHRQAS LSISVSNSQI QENVDIATVY
560 570 580 590 600
QIFPDEVLGS GQFGVVYGGK HRKTGRDVAV KVIDKLRFPT KQESQLRNEV
610 620 630 640 650
AILQSLRHPG IVNLECMFET PEKVFVVMEK LHGDMLEMIL SSEKGRLPER
660 670 680 690 700
LTKFLITQIL VALRHLHFKN IVHCDLKPEN VLLASADPFP QVKLCDFGFA
710 720 730 740 750
RIIGEKSFRR SVVGTPAYLA PEVLLNQGYN RSLDMWSVGV IMYVSLSGTF
760 770 780 790 800
PFNEDEDIND QIQNAAFMYP ASPWSHISSG AIDLINNLLQ VKMRKRYSVD
810 820 830 840 850
KSLSHPWLQE YQTWLDLREL EGKMGERYIT HESDDARWDQ FVAERHGTPA
860 870
EGDLGGACLP QDHEMQGLAE RISIL
Length:875
Mass (Da):96,542
Last modified:March 1, 2003 - v1
Checksum:iC7173546FA1E6DB1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti213 – 2131E → G in BAE42012. (PubMed:16141072)Curated
Sequence conflicti220 – 2201E → G in BAE41652. (PubMed:16141072)Curated
Sequence conflicti310 – 3101R → H in BAE32326. (PubMed:16141072)Curated
Sequence conflicti310 – 3101R → H in BAE41652. (PubMed:16141072)Curated
Sequence conflicti630 – 6301K → N in BAE42012. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK037030 mRNA. Translation: BAC29677.1.
AK154029 mRNA. Translation: BAE32326.1.
AK170236 mRNA. Translation: BAE41652.1.
AK170761 mRNA. Translation: BAE42012.1.
BC095949 mRNA. Translation: AAH95949.1.
BC096444 mRNA. Translation: AAH96444.1.
CCDSiCCDS20855.1.
RefSeqiNP_001239387.1. NM_001252458.1.
NP_849231.1. NM_178900.4.
UniGeneiMm.1881.
Mm.488710.

Genome annotation databases

EnsembliENSMUST00000086104; ENSMUSP00000083273; ENSMUSG00000041187.
ENSMUST00000168093; ENSMUSP00000131192; ENSMUSG00000041187.
GeneIDi101540.
KEGGimmu:101540.
UCSCiuc009fig.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK037030 mRNA. Translation: BAC29677.1 .
AK154029 mRNA. Translation: BAE32326.1 .
AK170236 mRNA. Translation: BAE41652.1 .
AK170761 mRNA. Translation: BAE42012.1 .
BC095949 mRNA. Translation: AAH95949.1 .
BC096444 mRNA. Translation: AAH96444.1 .
CCDSi CCDS20855.1.
RefSeqi NP_001239387.1. NM_001252458.1.
NP_849231.1. NM_178900.4.
UniGenei Mm.1881.
Mm.488710.

3D structure databases

ProteinModelPortali Q8BZ03.
SMRi Q8BZ03. Positions 138-188, 266-358, 396-510, 518-842.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8BZ03. 1 interaction.
MINTi MINT-4113563.

PTM databases

PhosphoSitei Q8BZ03.

Proteomic databases

MaxQBi Q8BZ03.
PaxDbi Q8BZ03.
PRIDEi Q8BZ03.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000086104 ; ENSMUSP00000083273 ; ENSMUSG00000041187 .
ENSMUST00000168093 ; ENSMUSP00000131192 ; ENSMUSG00000041187 .
GeneIDi 101540.
KEGGi mmu:101540.
UCSCi uc009fig.2. mouse.

Organism-specific databases

CTDi 25865.
MGIi MGI:2141917. Prkd2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120480.
HOGENOMi HOG000015135.
HOVERGENi HBG003564.
InParanoidi Q8BZ03.
KOi K06070.
OMAi LPQDHEM.
OrthoDBi EOG75B84N.
PhylomeDBi Q8BZ03.
TreeFami TF314320.

Miscellaneous databases

NextBioi 355000.
PROi Q8BZ03.
SOURCEi Search...

Gene expression databases

Bgeei Q8BZ03.
CleanExi MM_PRKD2.
Genevestigatori Q8BZ03.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Thymus and Vagina.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon and Mammary tumor.
  3. "Protein kinase D2 potentiates MEK/ERK/RSK signaling, c-Fos accumulation and DNA synthesis induced by bombesin in Swiss 3T3 cells."
    Sinnett-Smith J., Zhukova E., Rey O., Rozengurt E.
    J. Cell. Physiol. 211:781-790(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL PROLIFERATION.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Unique functions for protein kinase D1 and protein kinase D2 in mammalian cells."
    Matthews S.A., Navarro M.N., Sinclair L.V., Emslie E., Feijoo-Carnero C., Cantrell D.A.
    Biochem. J. 432:153-163(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN T-CELLS, PHOSPHORYLATION AT SER-707; SER-711 AND SER-873, MUTAGENESIS OF SER-707 AND SER-711.

Entry informationi

Entry nameiKPCD2_MOUSE
AccessioniPrimary (citable) accession number: Q8BZ03
Secondary accession number(s): Q3TCE5, Q3TDF0, Q3U4V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 117 of the entry and version 1 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