Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Dual specificity tyrosine-phosphorylation-regulated kinase 1B (EC 2.7.12.1) (Minibrain-related kinase) (Mirk protein kinase)

 DYR1B_HUMAN             Reviewed;         629 AA.
Q9Y463; O75258; O75788; O75789;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
22-NOV-2017, entry version 176.
RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase 1B;
EC=2.7.12.1;
AltName: Full=Minibrain-related kinase;
AltName: Full=Mirk protein kinase;
Name=DYRK1B; Synonyms=MIRK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Testis;
PubMed=9918863; DOI=10.1006/bbrc.1998.9967;
Leder S., Weber Y., Altafaj X., Estivill X., Joost H.-G., Becker W.;
"Cloning and characterization of DYRK1B, a novel member of the DYRK
family of protein kinases.";
Biochem. Biophys. Res. Commun. 254:474-479(1999).
[2]
NUCLEOTIDE SEQUENCE (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
PHOSPHORYLATION AT TYR-271 AND TYR-273, AND MUTAGENESIS OF LYS-140;
TYR-271 AND TYR-273.
TISSUE=Colon carcinoma;
PubMed=10910078;
Lee K., Deng X., Friedman E.;
"Mirk protein kinase is a mitogen-activated protein kinase substrate
that mediates survival of colon cancer cells.";
Cancer Res. 60:3631-3637(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
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).
[5]
FUNCTION, AND INTERACTION WITH DCOHM; MAP2K3 AND TCF1.
TISSUE=Muscle;
PubMed=11980910; DOI=10.1074/jbc.M203257200;
Lim S., Jin K., Friedman E.;
"Mirk protein kinase is activated by MKK3 and functions as a
transcriptional activator of HNF1alpha.";
J. Biol. Chem. 277:25040-25046(2002).
[6]
FUNCTION, DIMERIZATION, INTERACTION WITH RANBP9, AND IDENTIFICATION IN
A COMPLEX WITH RAN; RANBP9 AND COPS5.
PubMed=14500717; DOI=10.1074/jbc.M307556200;
Zou Y., Lim S., Lee K., Deng X., Friedman E.;
"Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial
cell migration and is negatively regulated by the Met adaptor Ran-
binding protein M.";
J. Biol. Chem. 278:49573-49581(2003).
[7]
INTERACTION WITH DCAF7.
PubMed=14593110; DOI=10.1074/jbc.M301769200;
Skurat A.V., Dietrich A.D.;
"Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family
protein kinases.";
J. Biol. Chem. 279:2490-2498(2004).
[8]
CATALYTIC ACTIVITY.
PubMed=22998443; DOI=10.1021/jm301034u;
Tahtouh T., Elkins J.M., Filippakopoulos P., Soundararajan M.,
Burgy G., Durieu E., Cochet C., Schmid R.S., Lo D.C., Delhommel F.,
Oberholzer A.E., Pearl L.H., Carreaux F., Bazureau J.P., Knapp S.,
Meijer L.;
"Selectivity, cocrystal structures, and neuroprotective properties of
leucettines, a family of protein kinase inhibitors derived from the
marine sponge alkaloid leucettamine B.";
J. Med. Chem. 55:9312-9330(2012).
[9]
FUNCTION, VARIANTS AOMS3 PRO-90 AND CYS-102, AND CHARACTERIZATION OF
VARIANTS AOMS3 PRO-90 AND CYS-102.
PubMed=24827035; DOI=10.1056/NEJMoa1301824;
Keramati A.R., Fathzadeh M., Go G.W., Singh R., Choi M., Faramarzi S.,
Mane S., Kasaei M., Sarajzadeh-Fard K., Hwa J., Kidd K.K.,
Babaee Bigi M.A., Malekzadeh R., Hosseinian A., Babaei M.,
Lifton R.P., Mani A.;
"A form of the metabolic syndrome associated with mutations in
DYRK1B.";
N. Engl. J. Med. 370:1909-1919(2014).
[10]
VARIANTS [LARGE SCALE ANALYSIS] PRO-28; HIS-102; GLY-234 AND ARG-275.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Dual-specificity kinase which possesses both
serine/threonine and tyrosine kinase activities. Enhances the
transcriptional activity of TCF1/HNF1A and FOXO1. Inhibits
epithelial cell migration. Mediates colon carcinoma cell survival
in mitogen-poor environments. Inhibits the SHH and WNT1 pathways,
thereby enhancing adipogenesis. In addition, promotes expression
of the gluconeogenic enzyme glucose-6-phosphatase (G6PC).
{ECO:0000269|PubMed:10910078, ECO:0000269|PubMed:11980910,
ECO:0000269|PubMed:14500717, ECO:0000269|PubMed:24827035}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:22998443}.
-!- ENZYME REGULATION: Inhibited by RANBP9.
-!- SUBUNIT: Dimer. Interacts with DCOHM, MAP2K3/MKK3, RANBP9 and
TCF1/HNF1A. Part of a complex consisting of RANBP9, RAN, DYRK1B
and COPS5. Interacts with DCAF7. {ECO:0000269|PubMed:11980910,
ECO:0000269|PubMed:14500717, ECO:0000269|PubMed:14593110}.
-!- INTERACTION:
P61962:DCAF7; NbExp=3; IntAct=EBI-634187, EBI-359808;
P20823:HNF1A; NbExp=4; IntAct=EBI-634187, EBI-636034;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-634187, EBI-741037;
P46734:MAP2K3; NbExp=2; IntAct=EBI-634187, EBI-602462;
Q9H0N5:PCBD2; NbExp=2; IntAct=EBI-634187, EBI-634289;
Q96S59:RANBP9; NbExp=4; IntAct=EBI-634187, EBI-636085;
P06400:RB1; NbExp=3; IntAct=EBI-634187, EBI-491274;
P28749:RBL1; NbExp=3; IntAct=EBI-634187, EBI-971402;
Q12815:TROAP; NbExp=5; IntAct=EBI-634187, EBI-2349743;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9Y463-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y463-2; Sequence=VSP_004925;
Name=3;
IsoId=Q9Y463-3; Sequence=VSP_004926;
-!- TISSUE SPECIFICITY: Highest expression in skeletal muscle, testis,
heart and brain with little expression in colon or lung. Expressed
in a variety of tumor cell lines. {ECO:0000269|PubMed:10910078}.
-!- PTM: Autophosphorylated on tyrosine residues. Phosphorylated by
MAP kinase. Tyrosine phosphorylation may be required for
dimerization. {ECO:0000269|PubMed:10910078}.
-!- DISEASE: Abdominal obesity-metabolic syndrome 3 (AOMS3)
[MIM:615812]: A form of abdominal obesity-metabolic syndrome, a
disorder characterized by abdominal obesity, high triglycerides,
low levels of high density lipoprotein cholesterol, high blood
pressure, and elevated fasting glucose levels. AOMS3 is
characterized by early-onset coronary artery disease, central
obesity, hypertension, and diabetes.
{ECO:0000269|PubMed:24827035}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MNB/DYRK subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC28914.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/DYRK1BID43235ch19q13.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y17999; CAA76991.1; -; mRNA.
EMBL; Y17999; CAA76990.1; -; mRNA.
EMBL; Y17999; CAA76989.1; -; mRNA.
EMBL; AF205861; AAF15893.1; -; mRNA.
EMBL; AC005393; AAC28914.1; ALT_SEQ; Genomic_DNA.
EMBL; BC018751; AAH18751.1; -; mRNA.
EMBL; BC025291; AAH25291.1; -; mRNA.
CCDS; CCDS12543.1; -. [Q9Y463-1]
CCDS; CCDS12544.1; -. [Q9Y463-3]
CCDS; CCDS46075.1; -. [Q9Y463-2]
PIR; JG0195; JG0195.
RefSeq; NP_004705.1; NM_004714.2. [Q9Y463-1]
RefSeq; NP_006474.1; NM_006483.2. [Q9Y463-2]
RefSeq; NP_006475.1; NM_006484.2. [Q9Y463-3]
RefSeq; XP_005259455.1; XM_005259398.4. [Q9Y463-1]
UniGene; Hs.130988; -.
ProteinModelPortal; Q9Y463; -.
SMR; Q9Y463; -.
BioGrid; 114596; 63.
ELM; Q9Y463; -.
IntAct; Q9Y463; 54.
MINT; MINT-2790122; -.
STRING; 9606.ENSP00000312789; -.
BindingDB; Q9Y463; -.
ChEMBL; CHEMBL5543; -.
GuidetoPHARMACOLOGY; 2010; -.
iPTMnet; Q9Y463; -.
PhosphoSitePlus; Q9Y463; -.
BioMuta; DYRK1B; -.
DMDM; 9296963; -.
EPD; Q9Y463; -.
PaxDb; Q9Y463; -.
PeptideAtlas; Q9Y463; -.
PRIDE; Q9Y463; -.
DNASU; 9149; -.
Ensembl; ENST00000323039; ENSP00000312789; ENSG00000105204. [Q9Y463-1]
Ensembl; ENST00000348817; ENSP00000221803; ENSG00000105204. [Q9Y463-3]
Ensembl; ENST00000430012; ENSP00000403182; ENSG00000105204. [Q9Y463-2]
Ensembl; ENST00000593685; ENSP00000469863; ENSG00000105204. [Q9Y463-1]
Ensembl; ENST00000597639; ENSP00000472941; ENSG00000105204. [Q9Y463-3]
Ensembl; ENST00000625388; ENSP00000486839; ENSG00000281320. [Q9Y463-3]
Ensembl; ENST00000625438; ENSP00000487313; ENSG00000281320. [Q9Y463-3]
Ensembl; ENST00000625757; ENSP00000485915; ENSG00000281320. [Q9Y463-1]
Ensembl; ENST00000627034; ENSP00000487539; ENSG00000281320. [Q9Y463-2]
Ensembl; ENST00000631090; ENSP00000486377; ENSG00000281320. [Q9Y463-1]
GeneID; 9149; -.
KEGG; hsa:9149; -.
UCSC; uc002omi.4; human. [Q9Y463-1]
CTD; 9149; -.
DisGeNET; 9149; -.
EuPathDB; HostDB:ENSG00000105204.13; -.
GeneCards; DYRK1B; -.
HGNC; HGNC:3092; DYRK1B.
HPA; HPA028522; -.
HPA; HPA028786; -.
MalaCards; DYRK1B; -.
MIM; 604556; gene.
MIM; 615812; phenotype.
neXtProt; NX_Q9Y463; -.
OpenTargets; ENSG00000105204; -.
PharmGKB; PA27549; -.
eggNOG; KOG0667; Eukaryota.
eggNOG; ENOG410XPET; LUCA.
GeneTree; ENSGT00760000119032; -.
HOGENOM; HOG000220863; -.
HOVERGEN; HBG051425; -.
InParanoid; Q9Y463; -.
KO; K08825; -.
OMA; DCEMNSP; -.
OrthoDB; EOG091G03J7; -.
PhylomeDB; Q9Y463; -.
TreeFam; TF314624; -.
BioCyc; MetaCyc:HS02690-MONOMER; -.
BRENDA; 2.7.12.1; 2681.
SignaLink; Q9Y463; -.
SIGNOR; Q9Y463; -.
ChiTaRS; DYRK1B; human.
GeneWiki; DYRK1B; -.
GenomeRNAi; 9149; -.
PRO; PR:Q9Y463; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105204; -.
CleanEx; HS_DYRK1B; -.
ExpressionAtlas; Q9Y463; baseline and differential.
Genevisible; Q9Y463; HS.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0060612; P:adipose tissue development; IMP:UniProtKB.
GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
InterPro; IPR033565; DYRK1B.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24058:SF27; PTHR24058:SF27; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome;
Diabetes mellitus; Kinase; Nucleotide-binding; Nucleus; Obesity;
Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
CHAIN 1 629 Dual specificity tyrosine-
phosphorylation-regulated kinase 1B.
/FTId=PRO_0000085934.
DOMAIN 111 431 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 117 125 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 190 193 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 480 520 Interaction with RANBP9.
{ECO:0000269|PubMed:14500717}.
MOTIF 69 86 Bipartite nuclear localization signal.
{ECO:0000255}.
COMPBIAS 558 561 Poly-Pro.
ACT_SITE 239 239 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 140 140 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 63 63 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 92 92 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 111 111 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 129 129 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 171 171 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q63470}.
MOD_RES 262 262 Phosphoserine.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 271 271 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10910078}.
MOD_RES 273 273 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10910078}.
MOD_RES 401 401 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 624 624 Phosphoserine.
{ECO:0000250|UniProtKB:Q13627}.
VAR_SEQ 366 405 Missing (in isoform 2).
{ECO:0000303|PubMed:9918863}.
/FTId=VSP_004925.
VAR_SEQ 378 405 Missing (in isoform 3).
{ECO:0000303|PubMed:9918863}.
/FTId=VSP_004926.
VARIANT 28 28 L -> P (in dbSNP:rs34587974).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040454.
VARIANT 90 90 H -> P (in AOMS3; expression of glucose-
6-phosphatase is significantly higher
than wild-type; dbSNP:rs587777380).
{ECO:0000269|PubMed:24827035}.
/FTId=VAR_071773.
VARIANT 102 102 R -> C (in AOMS3; accumulation of
intracellular lipid is significantly
greater than with wild-type protein;
cells expressing the variant are able to
transform into mature adipocytes without
requiring adipogenic medium; expression
levels of CEBPA, PPARG forms 1 and 2 and
PPARGC1A are higher and those of GLI1 and
CDKN1B are lower in cells transfected
with the mutant protein compared to wild-
type; WNT1 signaling activity is lower in
mutant cells compared to wild-type;
dbSNP:rs367643250).
{ECO:0000269|PubMed:24827035}.
/FTId=VAR_071774.
VARIANT 102 102 R -> H (in dbSNP:rs55687541).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040455.
VARIANT 234 234 S -> G (in dbSNP:rs35858874).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040456.
VARIANT 275 275 Q -> R (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040457.
MUTAGEN 140 140 K->R: Abolishes kinase activity.
{ECO:0000269|PubMed:10910078}.
MUTAGEN 271 271 Y->F: Abolishes kinase activity; when
associated with F-273.
{ECO:0000269|PubMed:10910078}.
MUTAGEN 273 273 Y->F: Abolishes kinase activity; when
associated with F-271.
{ECO:0000269|PubMed:10910078}.
SEQUENCE 629 AA; 69198 MW; D7C354AC55943A8B CRC64;
MAVPPGHGPF SGFPGPQEHT QVLPDVRLLP RRLPLAFRDA TSAPLRKLSV DLIKTYKHIN
EVYYAKKKRR AQQAPPQDSS NKKEKKVLNH GYDDDNHDYI VRSGERWLER YEIDSLIGKG
SFGQVVKAYD HQTQELVAIK IIKNKKAFLN QAQIELRLLE LMNQHDTEMK YYIVHLKRHF
MFRNHLCLVF ELLSYNLYDL LRNTHFRGVS LNLTRKLAQQ LCTALLFLAT PELSIIHCDL
KPENILLCNP KRSAIKIVDF GSSCQLGQRI YQYIQSRFYR SPEVLLGTPY DLAIDMWSLG
CILVEMHTGE PLFSGSNEVD QMNRIVEVLG IPPAAMLDQA PKARKYFERL PGGGWTLRRT
KELRKDYQGP GTRRLQEVLG VQTGGPGGRR AGEPGHSPAD YLRFQDLVLR MLEYEPAARI
SPLGALQHGF FRRTADEATN TGPAGSSAST SPAPLDTCPS SSTASSISSS GGSSGSSSDN
RTYRYSNRYC GGPGPPITDC EMNSPQVPPS QPLRPWAGGD VPHKTHQAPA SASSLPGTGA
QLPPQPRYLG RPPSPTSPPP PELMDVSLVG GPADCSPPHP APAPQHPAAS ALRTRMTGGR
PPLPPPDDPA TLGPHLGLRG VPQSTAASS


Related products :

Catalog number Product name Quantity
EIAAB12210 Dual specificity tyrosine-phosphorylation-regulated kinase 1B,DYRK1B,Homo sapiens,Human,Minibrain-related kinase,MIRK,Mirk protein kinase
EIAAB12207 Dual specificity tyrosine-phosphorylation-regulated kinase 1A,Dual specificity YAK1-related kinase,Dyrk,Dyrk1a,MNBH,Protein kinase minibrain homolog,Rat,Rattus norvegicus,RP86
EIAAB12208 Dual specificity tyrosine-phosphorylation-regulated kinase 1A,Dual specificity YAK1-related kinase,Dyrk,Dyrk1a,MNBH,Mouse,MP86,Mus musculus,Protein kinase minibrain homolog
EIAAB12205 Dual specificity tyrosine-phosphorylation-regulated kinase 1A,Dual specificity YAK1-related kinase,DYRK,DYRK1A,MNBH,Oryctolagus cuniculus,Protein kinase minibrain homolog,Rabbit,RP86
EIAAB12206 Dual specificity tyrosine-phosphorylation-regulated kinase 1A,Dual specificity YAK1-related kinase,DYRK,DYRK1A,hMNB,Homo sapiens,HP86,Human,MNB,MNBH,MNBH,Protein kinase minibrain homolog
EIAAB12215 Dual specificity tyrosine-phosphorylation-regulated kinase 3,DYRK3,Homo sapiens,Human,REDK,Regulatory erythroid kinase
EIAAB25239 C-JUN N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,JNK kinase 1,JNK-activating kinase 1,JNKK 1,Jnkk1,MAP kinase kinase 4,Map2k4,MAPK_ERK kinase 4,MAPKK 4,MEK 4
EIAAB25244 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Mkk7,
EIAAB25245 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Rat,R
6257 Dual-specificity tyrosine phosphorylation-regulated kinase 2 0.5 mg
6255 Dual-specificity tyrosine phosphorylation-regulated kinase 1A 0.5 mg
6255 Dual-specificity tyrosine phosphorylation-regulated kinase 1A 0.1 mg
6257 Dual-specificity tyrosine phosphorylation-regulated kinase 2 0.1 mg
DYSF DYRK3 Gene dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 3
CSB-EL007307RA Rat Dual specificity tyrosine-phosphorylation-regulated kinase 1A(DYRK1A) ELISA kit 96T
DYRK2_CHICK Chicken ELISA Kit FOR Dual specificity tyrosine-phosphorylation-regulated kinase 2 96T
DYRK3_MOUSE Mouse ELISA Kit FOR Dual specificity tyrosine-phosphorylation-regulated kinase 3 96T
DYRK1AIP2 DYRK1A Gene dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 1A
DYR1B_MOUSE Mouse ELISA Kit FOR Dual specificity tyrosine-phosphorylation-regulated kinase 1B 96T
DYRK3 DYRK1B Gene dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 1B
DYRK4 DYRK2 Gene dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2
DYSFIP1 DYRK4 Gene dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 4
E98193Mu ELISA Kit for Dual Specificity Tyrosine Phosphorylation Regulated Kinase 1A (DYRK1A) 96T/Kit
DYR1A_HUMAN Human ELISA Kit FOR Dual specificity tyrosine-phosphorylation-regulated kinase 1A 96T
E0871r Mouse ELISA Kit FOR Dual specificity tyrosine-phosphorylation-regulated kinase 1A 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur