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Serine/threonine-protein kinase D2 (EC 2.7.11.13) (nPKC-D2)

 KPCD2_MOUSE             Reviewed;         875 AA.
Q8BZ03; Q3TCE5; Q3TDF0; Q3U4V4;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
12-SEP-2018, entry version 149.
RecName: Full=Serine/threonine-protein kinase D2;
EC=2.7.11.13 {ECO:0000269|PubMed:20819079};
AltName: Full=nPKC-D2;
Name=Prkd2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, and Vagina;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION IN CELL PROLIFERATION.
PubMed=17226786; DOI=10.1002/jcp.20984;
Sinnett-Smith J., Zhukova E., Rey O., Rozengurt E.;
"Protein kinase D2 potentiates MEK/ERK/RSK signaling, c-Fos
accumulation and DNA synthesis induced by bombesin in Swiss 3T3
cells.";
J. Cell. Physiol. 211:781-790(2007).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[5]
FUNCTION IN T-CELLS, CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-707;
SER-711 AND SER-873, AND MUTAGENESIS OF SER-707 AND SER-711.
PubMed=20819079; DOI=10.1042/BJ20101188;
Matthews S.A., Navarro M.N., Sinclair L.V., Emslie E.,
Feijoo-Carnero C., Cantrell D.A.;
"Unique functions for protein kinase D1 and protein kinase D2 in
mammalian cells.";
Biochem. J. 432:153-163(2010).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-200; SER-206;
SER-211; SER-212; SER-214 AND SER-711, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: 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 (PubMed:17226786, PubMed:20819079). 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 (PubMed:17226786). In
response to oxidative stress, is phosphorylated at Tyr-438 and
Tyr-718 by ABL1, which leads to the activation of PRKD2 without
increasing its catalytic activity, and mediates activation of NF-
kappa-B (By similarity). 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 (By similarity). 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
(PubMed:20819079). 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 (By similarity). 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 (By similarity). 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 (By similarity). 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 (By similarity). In secretory pathway, is required
for the release of chromogranin-A (CHGA)-containing secretory
granules from the TGN (By similarity). Downstream of PRKCA, plays
important roles in angiotensin-2-induced monocyte adhesion to
endothelial cells (By similarity). {ECO:0000250|UniProtKB:Q9BZL6,
ECO:0000269|PubMed:17226786, ECO:0000269|PubMed:20819079}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:20819079}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9BZL6};
-!- ACTIVITY REGULATION: 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.
Catalytic activity is further increased by phosphorylation at Tyr-
718 in response to oxidative stress.
{ECO:0000250|UniProtKB:Q9BZL6}.
-!- SUBUNIT: Interacts (via C-terminus) with LCK. Interacts (via N-
terminus and zing-finger domain 1 and 2) with PRKCD in response to
oxidative stress; the interaction is independent of PRKD2 tyrosine
phosphorylation. {ECO:0000250|UniProtKB:Q9BZL6}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BZL6}.
Cell membrane {ECO:0000250|UniProtKB:Q15139}. Golgi apparatus,
trans-Golgi network {ECO:0000250|UniProtKB:Q9BZL6}.
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.
{ECO:0000250|UniProtKB:Q9BZL6}.
-!- PTM: 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.
Phosphorylated at Tyr-718 by ABL1 specifically in response to
oxidative stress; requires prior phosphorylation at Ser-707 or/and
Ser-711. {ECO:0000250|UniProtKB:Q9BZL6}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. PKD subfamily. {ECO:0000305}.
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EMBL; AK037030; BAC29677.1; -; mRNA.
EMBL; AK154029; BAE32326.1; -; mRNA.
EMBL; AK170236; BAE41652.1; -; mRNA.
EMBL; AK170761; BAE42012.1; -; mRNA.
EMBL; BC095949; AAH95949.1; -; mRNA.
EMBL; BC096444; AAH96444.1; -; mRNA.
CCDS; CCDS20855.1; -.
RefSeq; NP_001239387.1; NM_001252458.1.
RefSeq; NP_849231.1; NM_178900.4.
UniGene; Mm.1881; -.
UniGene; Mm.488710; -.
ProteinModelPortal; Q8BZ03; -.
SMR; Q8BZ03; -.
BioGrid; 221683; 1.
IntAct; Q8BZ03; 1.
MINT; Q8BZ03; -.
STRING; 10090.ENSMUSP00000083273; -.
iPTMnet; Q8BZ03; -.
PhosphoSitePlus; Q8BZ03; -.
EPD; Q8BZ03; -.
MaxQB; Q8BZ03; -.
PaxDb; Q8BZ03; -.
PeptideAtlas; Q8BZ03; -.
PRIDE; Q8BZ03; -.
Ensembl; ENSMUST00000086104; ENSMUSP00000083273; ENSMUSG00000041187.
Ensembl; ENSMUST00000168093; ENSMUSP00000131192; ENSMUSG00000041187.
GeneID; 101540; -.
KEGG; mmu:101540; -.
UCSC; uc009fig.2; mouse.
CTD; 25865; -.
MGI; MGI:2141917; Prkd2.
eggNOG; KOG4236; Eukaryota.
eggNOG; ENOG410XQZ3; LUCA.
GeneTree; ENSGT00910000144054; -.
HOGENOM; HOG000015135; -.
HOVERGEN; HBG003564; -.
InParanoid; Q8BZ03; -.
KO; K06070; -.
OMA; CIILFQN; -.
OrthoDB; EOG091G02RG; -.
PhylomeDB; Q8BZ03; -.
TreeFam; TF314320; -.
Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
PRO; PR:Q8BZ03; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000041187; Expressed in 229 organ(s), highest expression level in spleen.
CleanEx; MM_PRKD2; -.
Genevisible; Q8BZ03; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; ISO:MGI.
GO; GO:0004697; F:protein kinase C activity; IEA:UniProtKB-EC.
GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0008219; P:cell death; ISO:MGI.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISO:MGI.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IDA:UniProtKB.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; ISO:MGI.
GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; ISO:MGI.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:1901727; P:positive regulation of histone deacetylase activity; ISO:MGI.
GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:UniProtKB.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
GO; GO:1902533; P:positive regulation of intracellular signal transduction; ISO:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
GO; GO:0089700; P:protein kinase D signaling; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0050852; P:T cell receptor signaling pathway; ISO:MGI.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; ISO:MGI.
CDD; cd00029; C1; 2.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR015727; Protein_Kinase_C_mu-related.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR22968; PTHR22968; 1.
Pfam; PF00130; C1_1; 2.
Pfam; PF00069; Pkinase; 1.
PIRSF; PIRSF000552; PKC_mu_nu_D2; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 2.
SMART; SM00233; PH; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 2.
PROSITE; PS50081; ZF_DAG_PE_2; 2.
1: Evidence at protein level;
Adaptive immunity; Angiogenesis; ATP-binding; Cell adhesion;
Cell membrane; Complete proteome; Cytoplasm; Golgi apparatus;
Immunity; Kinase; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
CHAIN 1 875 Serine/threonine-protein kinase D2.
/FTId=PRO_0000260436.
DOMAIN 398 510 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 552 808 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 138 188 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 265 315 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 558 566 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 725 727 Important for ABL1-mediated Tyr-718
phosphorylation.
{ECO:0000250|UniProtKB:Q9BZL6}.
ACT_SITE 675 675 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 581 581 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000250|UniProtKB:O94806}.
MOD_RES 87 87 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q15139}.
MOD_RES 197 197 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 198 198 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BZL6}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BZL6}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 212 212 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 244 244 Phosphoserine; by CSNK1D and CSNK1E.
{ECO:0000250|UniProtKB:Q9BZL6}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BZL6}.
MOD_RES 408 408 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q15139}.
MOD_RES 439 439 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:Q9BZL6}.
MOD_RES 519 519 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BZL6}.
MOD_RES 707 707 Phosphoserine; by PKC.
{ECO:0000269|PubMed:20819079}.
MOD_RES 711 711 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:20819079}.
MOD_RES 718 718 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:Q9BZL6}.
MOD_RES 873 873 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:20819079}.
MUTAGEN 707 707 S->A: Strong decrease in catalytic
activity; when associated with A-711.
{ECO:0000269|PubMed:20819079}.
MUTAGEN 711 711 S->A: Strong decrease in catalytic
activity; when associated with A-707.
{ECO:0000269|PubMed:20819079}.
CONFLICT 213 213 E -> G (in Ref. 1; BAE42012).
{ECO:0000305}.
CONFLICT 220 220 E -> G (in Ref. 1; BAE41652).
{ECO:0000305}.
CONFLICT 310 310 R -> H (in Ref. 1; BAE32326/BAE41652).
{ECO:0000305}.
CONFLICT 630 630 K -> N (in Ref. 1; BAE42012).
{ECO:0000305}.
SEQUENCE 875 AA; 96542 MW; C7173546FA1E6DB1 CRC64;
MAAAPSHPAG LPGSPGPGSP PPPGGLDLQS PPPLLPQIPA PGSGVSFHIQ IGLTREFVLL
PAASELAHVK QLACSIVDQK FPECGFYGLY DKILLFKHDP TSANLLQLVR SAADIQEGDL
VEVVLSASAT FEDFQIRPHA LTVHSYRAPA FCDHCGEMLF GLVRQGLKCD GCGLNYHKRC
AFSIPNNCSG ARKRRLSSTS LASGHSVRLG SSESLPCTAE ELSRSTTDLL PRRPPSSSSS
SSSSSFYTGR PIELDKMLMS KVKVPHTFLI HSYTRPTVCQ ACKKLLKGLF RQGLQCKDCK
FNCHKRCATR VPNDCLGEAL INGDVPMEEA ADYSEADKSS ISDELEDSGV IPGSHSESAL
HASEEEEGEG HKAQSSLGYI PLMRVVQSVR HTTRKSSTTL REGWVVHYSN KDTLRKRHYW
RLDCKCITLF QNNTTNRYYK EIPLSEILAV EPAQNFSLVP PGTNPHCFEI ITANVTYFVG
ETPGGAPGGP SGQGTEAVRG WETAIRQALM PVILQDAPSA PGHTPHRQAS LSISVSNSQI
QENVDIATVY QIFPDEVLGS GQFGVVYGGK HRKTGRDVAV KVIDKLRFPT KQESQLRNEV
AILQSLRHPG IVNLECMFET PEKVFVVMEK LHGDMLEMIL SSEKGRLPER LTKFLITQIL
VALRHLHFKN IVHCDLKPEN VLLASADPFP QVKLCDFGFA RIIGEKSFRR SVVGTPAYLA
PEVLLNQGYN RSLDMWSVGV IMYVSLSGTF PFNEDEDIND QIQNAAFMYP ASPWSHISSG
AIDLINNLLQ VKMRKRYSVD KSLSHPWLQE YQTWLDLREL EGKMGERYIT HESDDARWDQ
FVAERHGTPA EGDLGGACLP QDHEMQGLAE RISIL


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EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
18-785-210370 PKD_PKC-mu (Phospho-Ser738) - EC 2.7.11.13; nPKC-D1; Protein kinase D; Protein kinase C mu type; nPKC-mu Polyclonal 0.05 mg
18-785-210371 PKD_PKC-mu (Phospho-Ser910) - EC 2.7.11.13; nPKC-D1; Protein kinase D; Protein kinase C mu type; nPKC-mu Polyclonal 0.1 mg
18-785-210370 PKD_PKC-mu (Phospho-Ser738) - EC 2.7.11.13; nPKC-D1; Protein kinase D; Protein kinase C mu type; nPKC-mu Polyclonal 0.1 mg
18-785-210371 PKD_PKC-mu (Phospho-Ser910) - EC 2.7.11.13; nPKC-D1; Protein kinase D; Protein kinase C mu type; nPKC-mu Polyclonal 0.05 mg
18-785-210372 PKD_PKC-mu (Ab-738) - EC 2.7.11.13; nPKC-D1; Protein kinase D; Protein kinase C mu type; nPKC-mu Polyclonal 0.1 mg
18-785-210372 PKD_PKC-mu (Ab-738) - EC 2.7.11.13; nPKC-D1; Protein kinase D; Protein kinase C mu type; nPKC-mu Polyclonal 0.05 mg
18-785-210373 PKD_PKC-mu (Ab-910) - EC 2.7.11.13; nPKC-D1; Protein kinase D; Protein kinase C mu type; nPKC-mu Polyclonal 0.05 mg
18-785-210373 PKD_PKC-mu (Ab-910) - EC 2.7.11.13; nPKC-D1; Protein kinase D; Protein kinase C mu type; nPKC-mu Polyclonal 0.1 mg
GWB-5BE1E2 Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Mouse anti-Human Monoclonal
GWB-CEE83D Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Rabbit anti-Human Polyclonal
31-031 Cdk7 is the catalytic subunit of the CDK-activating kinase (CAK) complex, a serine-threonine kinase. CAK activates the cyclin-associated kinases CDC2_CDK1, CDK2, CDK4 and CDK6 by threonine phosphoryla 0.1 mg
10-782-55105 Serine_threonine-protein kinase D1 - EC 2.7.11.13; nPKC-D1; Protein kinase D; Protein kinase C mu type; nPKC-mu N_A 0.005 mg
10-782-55105 Serine_threonine-protein kinase D1 - EC 2.7.11.13; nPKC-D1; Protein kinase D; Protein kinase C mu type; nPKC-mu N_A 0.001 mg
10-782-55105 Serine_threonine-protein kinase D1 - EC 2.7.11.13; nPKC-D1; Protein kinase D; Protein kinase C mu type; nPKC-mu N_A 0.02 mg
10-782-55105 Serine_threonine-protein kinase D1 - EC 2.7.11.13; nPKC-D1; Protein kinase D; Protein kinase C mu type; nPKC-mu N_A 0.01 mg
MKNK1_RAT Rat ELISA Kit FOR MAP kinase-interacting serine per threonine-protein kinase 1 96T
MKNK1_MOUSE ELISA Kit FOR MAP kinase-interacting serine per threonine-protein kinase 1; organism: Mouse; gene name: Mknk1 96T
MKNK2_MOUSE ELISA Kit FOR MAP kinase-interacting serine per threonine-protein kinase 2; organism: Mouse; gene name: Mknk2 96T
3987 Serine-threonine protein kinase 11 0.5 mg
3987 Serine-threonine protein kinase 11 0.1 mg
E0570Ra Rat serine per threonine protein kinase,STK ELISA Kit 48T
SL0771Ra Rat serine threonine protein kinase,STK ELISA Kit 96T
YHB0970Ra Rat serine-threonine protein kinase,STK ELISA Kit 48T


 

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