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Homeodomain-interacting protein kinase 2 (EC 2.7.11.1) (Nuclear body-associated kinase 1) (Sialophorin tail-associated nuclear serine/threonine-protein kinase)

 HIPK2_MOUSE             Reviewed;        1196 AA.
Q9QZR5; O88905; Q99P45; Q99P46; Q9D2E6; Q9D474; Q9EQL2; Q9QZR4;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 2.
25-OCT-2017, entry version 172.
RecName: Full=Homeodomain-interacting protein kinase 2;
EC=2.7.11.1;
AltName: Full=Nuclear body-associated kinase 1;
AltName: Full=Sialophorin tail-associated nuclear serine/threonine-protein kinase;
Name=Hipk2; Synonyms=Nbak1, Stank;
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
INTERACTION WITH NKX1-2 AND NKX2-5, AND MUTAGENESIS OF LYS-228.
STRAIN=BALB/cJ;
PubMed=9748262; DOI=10.1074/jbc.273.40.25875;
Kim Y.H., Choi C.Y., Lee S.-J., Conti M.A., Kim Y.;
"Homeodomain-interacting protein kinases, a novel family of co-
repressors for homeodomain transcription factors.";
J. Biol. Chem. 273:25875-25879(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH SPN, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION.
STRAIN=BALB/cJ; TISSUE=Heart;
PubMed=11078605; DOI=10.1006/cimm.2000.1716;
Wang W., Link V., Green J.M.;
"Identification and cloning of a CD43-associated serine/threonine
kinase.";
Cell. Immunol. 205:34-39(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
PubMed=11267674; DOI=10.1016/S0167-4781(00)00308-0;
Wang Y., Hofmann T.G., Runkel L., Haaf T., Schaller H., Debatin K.-M.,
Hug H.;
"Isolation and characterization of cDNAs for the protein kinase
HIPK2.";
Biochim. Biophys. Acta 1518:168-172(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
TISSUE=Heart;
PubMed=14990717; DOI=10.1128/JVI.78.6.2984-2993.2004;
Giraud S., Diaz-Latoud C., Hacot S., Textoris J., Bourette R.P.,
Diaz J.-J.;
"US11 of herpes simplex virus type 1 interacts with HIPK2 and
antagonizes HIPK2-induced cell growth arrest.";
J. Virol. 78:2984-2993(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Sather S.L., Johnson N.L., Johnson G.L.;
"Protein kinases associated with PML/CBP nuclear bodies and
filamentous threads regulate transcription and inhibit cell growth.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
STRAIN=C57BL/6J; TISSUE=Testis;
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).
[7]
SUBCELLULAR LOCATION, INTERACTION WITH UBE2I, SUMOYLATION, AND
MUTAGENESIS OF LYS-1189.
PubMed=10535925; DOI=10.1073/pnas.96.22.12350;
Kim Y.H., Choi C.Y., Kim Y.;
"Covalent modification of the homeodomain-interacting protein kinase 2
(HIPK2) by the ubiquitin-like protein SUMO-1.";
Proc. Natl. Acad. Sci. U.S.A. 96:12350-12355(1999).
[8]
INTERACTION WITH HMGA1, FUNCTION, PHOSPHORYLATION,
AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-228.
PubMed=11593421; DOI=10.1038/sj.onc.1204635;
Pierantoni G.M., Fedele M., Pentimalli F., Benvenuto G., Pero R.,
Viglietto G., Santoro M., Chiariotti L., Fusco A.;
"High mobility group I (Y) proteins bind HIPK2, a serine-threonine
kinase protein which inhibits cell growth.";
Oncogene 20:6132-6141(2001).
[9]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=11798164; DOI=10.1006/bbrc.2001.6310;
Pierantoni G.M., Bulfone A., Pentimalli F., Fedele M., Iuliano R.,
Santoro M., Chiariotti L., Ballabio A., Fusco A.;
"The homeodomain-interacting protein kinase 2 gene is expressed late
in embryogenesis and preferentially in retina, muscle, and neural
tissues.";
Biochem. Biophys. Res. Commun. 290:942-947(2002).
[10]
FUNCTION, INTERACTION WITH TP53, AUTOPHOSPHORYLATION, AND MUTAGENESIS
OF LYS-228.
PubMed=11780126; DOI=10.1038/ncb714;
D'Orazi G., Cecchinelli B., Bruno T., Manni I., Higashimoto Y.,
Saito S., Gostissa M., Coen S., Marchetti A., Del Sal G., Piaggio G.,
Fanciulli M., Appella E., Soddu S.;
"Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46
and mediates apoptosis.";
Nat. Cell Biol. 4:11-19(2002).
[11]
FUNCTION, AND INTERACTION WITH CTBP1.
PubMed=14567915; DOI=10.1016/S0092-8674(03)00802-X;
Zhang Q., Yoshimatsu Y., Hildebrand J., Frisch S.M., Goodman R.H.;
"Homeodomain interacting protein kinase 2 promotes apoptosis by
downregulating the transcriptional corepressor CtBP.";
Cell 115:177-186(2003).
[12]
INTERACTION WITH AXIN1, AND IDENTIFICATION IN A COMPLEX WITH TP53 AND
AXIN1.
PubMed=15526030; DOI=10.1038/sj.emboj.7600475;
Rui Y., Xu Z., Lin S., Li Q., Rui H., Luo W., Zhou H.-M.,
Cheung P.-Y., Wu Z., Ye Z., Li P., Han J., Lin S.-C.;
"Axin stimulates p53 functions by activation of HIPK2 kinase through
multimeric complex formation.";
EMBO J. 23:4583-4594(2004).
[13]
FUNCTION IN WNT SIGNALING, INTERACTION WITH NLK AND MYB, AND
MUTAGENESIS OF LYS-228.
PubMed=15082531; DOI=10.1101/gad.1170604;
Kanei-Ishii C., Ninomiya-Tsuji J., Tanikawa J., Nomura T.,
Ishitani T., Kishida S., Kokura K., Kurahashi T., Ichikawa-Iwata E.,
Kim Y., Matsumoto K., Ishii S.;
"Wnt-1 signal induces phosphorylation and degradation of c-Myb protein
via TAK1, HIPK2, and NLK.";
Genes Dev. 18:816-829(2004).
[14]
FUNCTION, INTERACTION WITH POU4F1; POU4F2 AND POU4F3, AND
DEVELOPMENTAL STAGE.
PubMed=15492043; DOI=10.1083/jcb.200406131;
Wiggins A.K., Wei G., Doxakis E., Wong C., Tang A.A., Zang K.,
Luo E.J., Neve R.L., Reichardt L.F., Huang E.J.;
"Interaction of Brn3a and HIPK2 mediates transcriptional repression of
sensory neuron survival.";
J. Cell Biol. 167:257-267(2004).
[15]
FUNCTION AS KINASE AND IN ANGIOGENESIS, AND INTERACTION WITH RUNX1 AND
EP300.
PubMed=16917507; DOI=10.1038/sj.emboj.7601273;
Aikawa Y., Nguyen L.A., Isono K., Takakura N., Tagata Y.,
Schmitz M.L., Koseki H., Kitabayashi I.;
"Roles of HIPK1 and HIPK2 in AML1- and p300-dependent transcription,
hematopoiesis and blood vessel formation.";
EMBO J. 25:3955-3965(2006).
[16]
INDUCTION BY ZINC DURING HYPOXIA.
PubMed=19714248; DOI=10.1371/journal.pone.0006819;
Nardinocchi L., Puca R., Sacchi A., Rechavi G., Givol D., D'Orazi G.;
"Targeting hypoxia in cancer cells by restoring homeodomain
interacting protein-kinase 2 and p53 activity and suppressing HIF-
1alpha.";
PLoS ONE 4:E6819-E6819(2009).
[17]
FUNCTION AS CTNNB1 KINASE, AND DISRUPTION PHENOTYPE.
PubMed=20307497; DOI=10.1016/j.bbrc.2010.03.099;
Kim E.-A., Kim J.E., Sung K.S., Choi D.W., Lee B.J., Choi C.Y.;
"Homeodomain-interacting protein kinase 2 (HIPK2) targets beta-catenin
for phosphorylation and proteasomal degradation.";
Biochem. Biophys. Res. Commun. 394:966-971(2010).
[18]
FUNCTION AS PDX1 KINASE.
PubMed=20637728; DOI=10.1016/j.bbrc.2010.07.035;
An R., da Silva Xavier G., Semplici F., Vakhshouri S., Hao H.X.,
Rutter J., Pagano M.A., Meggio F., Pinna L.A., Rutter G.A.;
"Pancreatic and duodenal homeobox 1 (PDX1) phosphorylation at serine-
269 is HIPK2-dependent and affects PDX1 subnuclear localization.";
Biochem. Biophys. Res. Commun. 399:155-161(2010).
[19]
FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=20231426; DOI=10.1182/blood-2009-07-235093;
Hattangadi S.M., Burke K.A., Lodish H.F.;
"Homeodomain-interacting protein kinase 2 plays an important role in
normal terminal erythroid differentiation.";
Blood 115:4853-4861(2010).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pancreas;
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).
[21]
FUNCTION IN EYE DEVELOPMENT, DEVELOPMENTAL STAGE, SUBCELLULAR
LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=20579985; DOI=10.1016/j.febslet.2010.06.020;
Inoue T., Kagawa T., Inoue-Mochita M., Isono K., Ohtsu N.,
Nobuhisa I., Fukushima M., Tanihara H., Taga T.;
"Involvement of the Hipk family in regulation of eyeball size, lens
formation and retinal morphogenesis.";
FEBS Lett. 584:3233-3238(2010).
[22]
PHOSPHORYLATION AT SER-16; SER-118; SER-135; THR-141; THR-252;
THR-273; TYR-361; SER-441; THR-482; THR-517; THR-566; SER-634;
SER-668; THR-687; SER-815; SER-827; SER-934; SER-991; SER-991;
SER-1042; SER-1153 AND SER-1186, ENZYME REGULATION, AND MUTAGENESIS OF
TYR-361.
PubMed=23485397; DOI=10.1016/j.bbamcr.2013.02.018;
Siepi F., Gatti V., Camerini S., Crescenzi M., Soddu S.;
"HIPK2 catalytic activity and subcellular localization are regulated
by activation-loop Y354 autophosphorylation.";
Biochim. Biophys. Acta 1833:1443-1453(2013).
-!- FUNCTION: Serine/threonine-protein kinase involved in
transcription regulation, p53/TP53-mediated cellular apoptosis and
regulation of the cell cycle. Acts as a corepressor of several
transcription factors, including SMAD1 and POU4F1/Brn3a and
probably NK homeodomain transcription factors. Phosphorylates
PDX1, ATF1, PML, p53/TP53, CREB1, CTBP1, CBX4, RUNX1, EP300,
CTNNB1, HMGA1 and ZBTB4. Inhibits cell growth and promotes
apoptosis through the activation of p53/TP53 both at the
transcription level and at the protein level (by phosphorylation
and indirect acetylation). The phosphorylation of p53/TP53 may be
mediated by a p53/TP53-HIPK2-AXIN1 complex. Involved in the
response to hypoxia by acting as a transcriptional co-suppressor
of HIF1A. Mediates transcriptional activation of TP73. In response
to TGFB, cooperates with DAXX to activate JNK. Negative regulator
through phosphorylation and subsequent proteasomal degradation of
CTNNB1 and the antiapoptotic factor CTBP1. In the Wnt/beta-catenin
signaling pathway acts as an intermediate kinase between
MAP3K7/TAK1 and NLK to promote the proteasomal degradation of MYB.
Phosphorylates CBX4 upon DNA damage and promotes its E3 SUMO-
protein ligase activity. Activates CREB1 and ATF1 transcription
factors by phosphorylation in response to genotoxic stress. In
response to DNA damage, stabilizes PML by phosphorylation. PML,
HIPK2 and FBXO3 may act synergically to activate p53/TP53-
dependent transactivation. Promotes angiogenesis, and is involved
in erythroid differentiation, especially during fetal liver
erythropoiesis. Phosphorylation of RUNX1 and EP300 stimulates
EP300 transcription regulation activity. Triggers ZBTB4 protein
degradation in response to DNA damage. Modulates HMGA1 DNA-binding
affinity. In response to high glucose, triggers phosphorylation-
mediated subnuclear localization shifting of PDX1. Involved in the
regulation of eye size, lens formation and retinal lamination
during late embryogenesis. {ECO:0000269|PubMed:11593421,
ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:14567915,
ECO:0000269|PubMed:15082531, ECO:0000269|PubMed:15492043,
ECO:0000269|PubMed:16917507, ECO:0000269|PubMed:20231426,
ECO:0000269|PubMed:20307497, ECO:0000269|PubMed:20579985,
ECO:0000269|PubMed:20637728}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts with CREB1, SIAH1, WSB1, CBX4, TRADD, p53/TP53,
TP73, TP63, CREBBP, DAXX, P53DINP1, SKI, SMAD1, SMAD2 and SMAD3,
but not SMAD4. Interacts with SP100; positively regulates TP53-
dependent transcription (By similarity). Interacts with ATF1, PML,
RUNX1, EP300, NKX1-2, NKX2-5, SPN/CD43, UBE2I, HMGA1, CTBP1,
AXIN1, NLK, MYB, POU4F1, POU4F2, POU4F3, UBE2I, UBL1 and ZBTB4.
Probably part of a complex consisting of p53/TP53, HIPK2 and
AXIN1. {ECO:0000250, ECO:0000269|PubMed:10535925,
ECO:0000269|PubMed:11078605, ECO:0000269|PubMed:11593421,
ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:14567915,
ECO:0000269|PubMed:15082531, ECO:0000269|PubMed:15492043,
ECO:0000269|PubMed:15526030, ECO:0000269|PubMed:16917507,
ECO:0000269|PubMed:9748262}.
-!- INTERACTION:
P51608:MECP2 (xeno); NbExp=3; IntAct=EBI-366905, EBI-1189067;
Q8CFN5:Mef2c; NbExp=5; IntAct=EBI-366905, EBI-643797;
P06876:Myb; NbExp=2; IntAct=EBI-366905, EBI-366934;
O54949:Nlk; NbExp=2; IntAct=EBI-366905, EBI-366894;
Q9Y6I7:WSB1 (xeno); NbExp=5; IntAct=EBI-366905, EBI-1171494;
-!- SUBCELLULAR LOCATION: Nucleus, PML body
{ECO:0000269|PubMed:10535925, ECO:0000269|PubMed:11078605,
ECO:0000269|PubMed:14990717, ECO:0000269|PubMed:20579985,
ECO:0000269|PubMed:9748262}. Cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus. Cytoplasm. Note=Isoform
2 seems to be both nuclear and cytoplasmic.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=Nbak1b, b;
IsoId=Q9QZR5-1; Sequence=Displayed;
Name=2; Synonyms=Nbak1a, a;
IsoId=Q9QZR5-2; Sequence=VSP_004808;
Name=3;
IsoId=Q9QZR5-3; Sequence=VSP_013135, VSP_013137;
Name=4;
IsoId=Q9QZR5-4; Sequence=VSP_013135, VSP_004808;
Name=5;
IsoId=Q9QZR5-5; Sequence=VSP_013136, VSP_013138, VSP_013139;
-!- TISSUE SPECIFICITY: Ubiquitous. Abundant in muscle, heart, small
intestine, stomach, kidney and brain; and low in testis, skin and
lung. {ECO:0000269|PubMed:11078605, ECO:0000269|PubMed:11798164,
ECO:0000269|PubMed:14990717}.
-!- DEVELOPMENTAL STAGE: At E15-E17, mainly in the developing retina,
telencephalon and myoblasts. At E12.5, detected in the developing
trigeminal and dorsal root ganglia, and in the developing spinal
cord (at protein level). Highly induced during primary fetal liver
erythropoiesis. Expressed in the inner retina during late
embryogenesis, in nucleus. Highest levels at E14.5 for isoform 2
and P12.5 for isoform 1. {ECO:0000269|PubMed:11798164,
ECO:0000269|PubMed:15492043, ECO:0000269|PubMed:20231426,
ECO:0000269|PubMed:20579985}.
-!- INDUCTION: During T-cell activation. {ECO:0000269|PubMed:11078605,
ECO:0000269|PubMed:19714248}.
-!- PTM: Sumoylated. When conjugated it is directed to nuclear
speckles. Desumoylated by SENP1. Sumoylation on Lys-32 is promoted
by the E3 SUMO-protein ligase CBX4 (By similarity). {ECO:0000250}.
-!- PTM: Autophosphorylation at Tyr-361 in the activation loop
activates the kinase and promotes nuclear localization.
{ECO:0000269|PubMed:23485397}.
-!- PTM: Ubiquitinated by FBXO3, WSB1 and SIAH1, leading to rapid
proteasome-dependent degradation. The degradation mediated by
FBXO3, but not ubiquitination, is prevented in the presence of
PML. The degradation mediated by WSB1 and SIAH1 is reversibly
reduced upon DNA damage (By similarity). {ECO:0000250}.
-!- PTM: Cleaved at Asp-923 and Asp-984 by CASP6 in a p53/TP53-
dependent manner. The cleaved form lacks the autoinhibitory C-
terminal domain (AID), resulting in a hyperactive kinase, which
potentiates p53/TP53 Ser-46 phosphorylation and subsequent
activation of the cell death machinery.
-!- DISRUPTION PHENOTYPE: Inhibited terminal erythroid cell
proliferation and terminal enucleation, as well as reduced
accumulation of hemoglobin. Impaired transcription of many genes
involved in cell proliferation and apoptosis, and of erythroid-
specific genes involved in hemoglobin biosynthesis, such as HBA
and SLC25A37/MFRN. Enhanced stability of CTNNB1; accumulation of
beta-catenin leading to the potentiation of beta-catenin-mediated
cell proliferation and tumor formation. Small eyes with deficient
lens, abnormal retinal lamination, and thickened retinas.
{ECO:0000269|PubMed:20231426, ECO:0000269|PubMed:20307497,
ECO:0000269|PubMed:20579985}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. HIPK subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC63011.1; Type=Frameshift; Positions=2; Evidence={ECO:0000305};
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EMBL; AF077659; AAC63011.1; ALT_FRAME; mRNA.
EMBL; AF273680; AAG02078.1; -; mRNA.
EMBL; AF208292; AAG41237.1; -; mRNA.
EMBL; AF333791; AAK07649.1; -; mRNA.
EMBL; AF333792; AAK07650.1; -; mRNA.
EMBL; AF170301; AAD52566.1; -; mRNA.
EMBL; AF170302; AAD52567.1; -; mRNA.
EMBL; AK016742; BAB30405.1; -; mRNA.
EMBL; AK019821; BAB31866.1; -; mRNA.
CCDS; CCDS20017.2; -. [Q9QZR5-1]
CCDS; CCDS80527.1; -. [Q9QZR5-2]
PIR; T17088; T17088.
RefSeq; NP_001129537.1; NM_001136065.2.
RefSeq; NP_001281072.1; NM_001294143.1. [Q9QZR5-2]
RefSeq; NP_001281073.1; NM_001294144.1.
RefSeq; NP_034563.2; NM_010433.2. [Q9QZR5-1]
UniGene; Mm.23790; -.
UniGene; Mm.391962; -.
UniGene; Mm.486937; -.
ProteinModelPortal; Q9QZR5; -.
BioGrid; 200307; 6.
DIP; DIP-31712N; -.
IntAct; Q9QZR5; 11.
STRING; 10090.ENSMUSP00000124133; -.
iPTMnet; Q9QZR5; -.
PhosphoSitePlus; Q9QZR5; -.
PaxDb; Q9QZR5; -.
PRIDE; Q9QZR5; -.
Ensembl; ENSMUST00000161779; ENSMUSP00000124133; ENSMUSG00000061436. [Q9QZR5-1]
Ensembl; ENSMUST00000162359; ENSMUSP00000125150; ENSMUSG00000061436. [Q9QZR5-2]
GeneID; 15258; -.
KEGG; mmu:15258; -.
UCSC; uc009bkw.3; mouse. [Q9QZR5-4]
UCSC; uc009bkx.2; mouse. [Q9QZR5-1]
UCSC; uc009blb.3; mouse. [Q9QZR5-3]
CTD; 28996; -.
MGI; MGI:1314872; Hipk2.
eggNOG; KOG0667; Eukaryota.
eggNOG; ENOG410XPET; LUCA.
GeneTree; ENSGT00760000119032; -.
HOVERGEN; HBG051908; -.
InParanoid; Q9QZR5; -.
KO; K08826; -.
OMA; PHLYTYT; -.
OrthoDB; EOG091G0UMX; -.
PhylomeDB; Q9QZR5; -.
TreeFam; TF105417; -.
BRENDA; 2.7.11.1; 3474.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
ChiTaRS; Hipk2; mouse.
PRO; PR:Q9QZR5; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000061436; -.
CleanEx; MM_HIPK2; -.
ExpressionAtlas; Q9QZR5; baseline and differential.
Genevisible; Q9QZR5; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; TAS:MGI.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IMP:BHF-UCL.
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; IDA:BHF-UCL.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:BHF-UCL.
GO; GO:0046332; F:SMAD binding; ISO:MGI.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0046790; F:virion binding; ISS:UniProtKB.
GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
GO; GO:0007628; P:adult walking behavior; IMP:MGI.
GO; GO:0009952; P:anterior/posterior pattern specification; IGI:MGI.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISO:MGI.
GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:DFLAT.
GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IMP:DFLAT.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IGI:MGI.
GO; GO:0061072; P:iris morphogenesis; IMP:DFLAT.
GO; GO:0060235; P:lens induction in camera-type eye; IMP:DFLAT.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0030182; P:neuron differentiation; IMP:DFLAT.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
GO; GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IGI:MGI.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0010842; P:retina layer formation; IMP:DFLAT.
GO; GO:0060395; P:SMAD protein signal transduction; ISO:MGI.
GO; GO:0007224; P:smoothened signaling pathway; IGI:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:MGI.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
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; Apoptosis; ATP-binding; Complete proteome;
Cytoplasm; DNA damage; Isopeptide bond; Kinase; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase; Tumor suppressor;
Ubl conjugation.
CHAIN 1 1196 Homeodomain-interacting protein kinase 2.
/FTId=PRO_0000085997.
DOMAIN 199 527 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 205 213 ATP. {ECO:0000305}.
REGION 97 230 Transcriptional corepression.
REGION 189 520 Interaction with DAXX. {ECO:0000250}.
REGION 539 844 Interaction with SKI and SMAD1.
{ECO:0000250}.
REGION 752 897 Interaction with POU4F1.
{ECO:0000269|PubMed:15492043}.
REGION 774 876 Interaction with CTBP1.
{ECO:0000269|PubMed:14567915}.
REGION 787 897 Interaction with HMGA1.
{ECO:0000269|PubMed:11593421}.
REGION 839 934 Interaction with TP53 and TP73.
{ECO:0000269|PubMed:11780126}.
REGION 873 980 Localization to nuclear speckles.
REGION 873 980 Required for localization to nuclear
speckles. {ECO:0000250}.
REGION 873 907 Interaction with UBE2I.
{ECO:0000269|PubMed:10535925}.
REGION 884 908 SUMO interaction motifs (SIM); required
for nuclear localization and kinase
activity. {ECO:0000250}.
REGION 935 1050 Interaction with AXIN1.
{ECO:0000269|PubMed:15526030}.
REGION 984 1196 Autoinhibitory domain (AID).
{ECO:0000250}.
MOTIF 802 805 Nuclear localization signal 1 (NLS1).
{ECO:0000250}.
MOTIF 832 835 Nuclear localization signal 2 (NLS2).
{ECO:0000250}.
COMPBIAS 1089 1092 Poly-Ala.
ACT_SITE 324 324 Proton acceptor. {ECO:0000305}.
BINDING 228 228 ATP. {ECO:0000305}.
SITE 923 924 Cleavage; by CASP6. {ECO:0000250}.
SITE 984 985 Cleavage; by CASP6. {ECO:0000250}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 135 135 Phosphoserine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 141 141 Phosphothreonine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 252 252 Phosphothreonine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 273 273 Phosphothreonine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 361 361 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:23485397}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 482 482 Phosphothreonine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 517 517 Phosphothreonine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 566 566 Phosphothreonine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 634 634 Phosphoserine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 668 668 Phosphoserine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 687 687 Phosphothreonine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 815 815 Phosphoserine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 827 827 Phosphoserine.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:23485397}.
MOD_RES 934 934 Phosphoserine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 991 991 Phosphoserine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 993 993 Phosphoserine.
{ECO:0000269|PubMed:11593421}.
MOD_RES 1042 1042 Phosphoserine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 1153 1153 Phosphoserine.
{ECO:0000269|PubMed:23485397}.
MOD_RES 1186 1186 Phosphoserine.
{ECO:0000269|PubMed:23485397}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q9H2X6}.
CROSSLNK 953 953 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H2X6}.
CROSSLNK 973 973 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H2X6}.
CROSSLNK 1189 1189 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
VAR_SEQ 1 480 Missing (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_013136.
VAR_SEQ 1 7 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:11267674,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_013135.
VAR_SEQ 369 1196 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_013137.
VAR_SEQ 594 620 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:11078605,
ECO:0000303|PubMed:11267674,
ECO:0000303|PubMed:14990717,
ECO:0000303|Ref.5}.
/FTId=VSP_004808.
VAR_SEQ 595 605 APTTSSATLSL -> KSQLIGLSPES (in isoform
5). {ECO:0000303|PubMed:16141072}.
/FTId=VSP_013138.
VAR_SEQ 606 1196 Missing (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_013139.
MUTAGEN 228 228 K->R: No enzymatic activity, but still
interacts with TP53 and NLK. Blocks the
ability to induce cell growth arrest.
Decreases corepressor activity.
{ECO:0000269|PubMed:11593421,
ECO:0000269|PubMed:11780126,
ECO:0000269|PubMed:15082531,
ECO:0000269|PubMed:9748262}.
MUTAGEN 361 361 Y->A: Strongly reduced nuclear
localization.
{ECO:0000269|PubMed:23485397}.
MUTAGEN 1189 1189 K->R: Inhibits localization to nuclear
speckles. {ECO:0000269|PubMed:10535925}.
CONFLICT 460 460 I -> T (in Ref. 1; AAC63011).
{ECO:0000305}.
CONFLICT 479 479 V -> G (in Ref. 1; AAC63011).
{ECO:0000305}.
CONFLICT 705 705 Missing (in Ref. 3; AAG41237 and 4;
AAK07649). {ECO:0000305}.
CONFLICT 719 719 A -> T (in Ref. 1; AAC63011).
{ECO:0000305}.
CONFLICT 1120 1120 A -> R (in Ref. 1; AAC63011).
{ECO:0000305}.
CONFLICT 1132 1132 T -> A (in Ref. 4; AAK07650).
{ECO:0000305}.
SEQUENCE 1196 AA; 130498 MW; 5C863BE377F3AAEF CRC64;
MAPVYEGMAS HVQVFSPHTL QSSAFCSVKK LKVEPSSNWD MTGYGSHSKV YSQSKNIPPS
QPASTTVSTS LPIPNPSLPY EQTIIFPGST GHIVVTSASS TSVTGQVLGG PHNLMRRSTV
SLLDTYQKCG LKRKSEEIEN TSSVQIIEEH PPMIQNNASG ATVATATTST ATSKNSGSNS
EGDYQLVQHE VLCSMTNTYE VLEFLGRGTF GQVVKCWKRG TNEIVAIKIL KNHPSYARQG
QIEVSILARL STESADDYNF VRAYECFQHK NHTCLVFEML EQNLYDFLKQ NKFSPLPLKY
IRPVLQQVAT ALMKLKSLGL IHADLKPENI MLVDPSRQPY RVKVIDFGSA SHVSKAVCST
YLQSRYYRAP EIILGLPFCE AIDMWSLGCV IAELFLGWPL YPGASEYDQI RYISQTQGLP
AEYLLSAGTK TTRFFNRDTD SPYPLWRLKT PDDHEAETGI KSKEARKYIF NCLDDMAQVN
MTTDLEGSDM LVEKADRREF IDLLKKMLTI DADKRVTPIE TLNHPFVTMT HLLDFPHSAH
VKSCFQNMEI CKRRVNMYDT VNQSKTPFIT HVAPSTSTNL TMTFNNQLTT VHNQAPTTSS
ATLSLANPEV SILNYQSALY QPSAASMAAV APRSMPLQTG TAQICARPDP FQQALIVCPP
GFQGLQASPS KHAGYSVRME NAVPIVTQAP GAQPLQIQPG LLAQQAWPGG AQQILLPPAW
QQLTGVATHT SVQHAAVIPE TMAGTQQLAD WRNTHAHGSH YNPIMQQPAL LTGHVTLPAA
QPLNVGVAHV MRQQPTSTTS SRKSKQHQSS VRNVSTCEVT SSQAISSPQR SKRVKENTPP
RCAMVHSSPA CSTSVTCGWG DVASSTTRER QRQTIVIPDT PSPTVSVITI SSDTDEEEEQ
KHAPTSTVSK QRKNVISCVT VHDSPYSDSS SNTSPYSVQQ RTGHNGTNTL DTKGGLENHC
TGNPRTIIVP PLKTQASEVL VECDSLGPAI SASHHSSSFK SKSSSTVTST SGHSSGSSSG
AIAYRQQRPG PHFQQQQPLN LSQAQQHMAA DRTGSHRRQQ AYITPTMAQA PYTFPHNSPS
HGTVHPHLAA AAHLPTQPHL YTYTAPTALG STGTVAHLVA SQGSARHTVQ HTAYPASIVH
QVPVSMGPRV LPSPTIHPSQ YPAQFAHQTY ISASPASTVY TGYPLSPAKV NQYPYI


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