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Inositol-tetrakisphosphate 1-kinase (EC 2.7.1.134) (Inositol 1,3,4-trisphosphate 5/6-kinase) (Inositol-triphosphate 5/6-kinase) (Ins(1,3,4)P(3) 5/6-kinase) (EC 2.7.1.159)

 ITPK1_HUMAN             Reviewed;         414 AA.
Q13572; Q9BTL6; Q9H2E7;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 2.
28-MAR-2018, entry version 150.
RecName: Full=Inositol-tetrakisphosphate 1-kinase;
EC=2.7.1.134;
AltName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase;
Short=Inositol-triphosphate 5/6-kinase;
Short=Ins(1,3,4)P(3) 5/6-kinase;
EC=2.7.1.159;
Name=ITPK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, COFACTOR, AND
TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=8662638; DOI=10.1074/jbc.271.20.11904;
Wilson M.P., Majerus P.W.;
"Isolation of inositol 1,3,4-trisphosphate 5/6-kinase, cDNA cloning
and expression of the recombinant enzyme.";
J. Biol. Chem. 271:11904-11910(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11042108; DOI=10.1042/bj3510551;
Yang X., Shears S.B.;
"Multitasking in signal transduction by a promiscuous human
Ins(3,4,5,6)P(4) 1-kinase/Ins(1,3,4)P(3) 5/6-kinase.";
Biochem. J. 351:551-555(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Eye, and Muscle;
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).
[4]
PUTATIVE FUNCTION AS PROTEIN KINASE.
PubMed=11533064; DOI=10.1074/jbc.M106605200;
Wilson M.P., Sun Y., Cao L., Majerus P.W.;
"Inositol 1,3,4-trisphosphate 5/6-kinase is a protein kinase that
phosphorylates the transcription factors c-Jun and ATF-2.";
J. Biol. Chem. 276:40998-41004(2001).
[5]
FUNCTION.
PubMed=11909533; DOI=10.1016/S0960-9822(02)00713-3;
Ho M.W.Y., Yang X., Carew M.A., Zhang T., Hua L., Kwon Y.-U.,
Chung S.-K., Adelt S., Vogel G., Riley A.M., Potter B.V.L.,
Shears S.B.;
"Regulation of Ins(3,4,5,6)P(4) signaling by a reversible
kinase/phosphatase.";
Curr. Biol. 12:477-482(2002).
[6]
INTERACTION WITH GPS1.
PubMed=12324474; DOI=10.1074/jbc.M208709200;
Sun Y., Wilson M.P., Majerus P.W.;
"Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9
signalosome by binding to CSN1.";
J. Biol. Chem. 277:45759-45764(2002).
[7]
FUNCTION.
PubMed=12925536; DOI=10.1074/jbc.M300674200;
Sun Y., Mochizuki Y., Majerus P.W.;
"Inositol 1,3,4-trisphosphate 5/6-kinase inhibits tumor necrosis
factor-induced apoptosis.";
J. Biol. Chem. 278:43645-43653(2003).
[8]
MUTAGENESIS OF ARG-106; LYS-157; GLY-163; ASP-281; ASP-295 AND
ASN-297.
PubMed=15762844; DOI=10.1042/BJ20050297;
Qian X., Mitchell J., Wei S.J., Williams J., Petrovich R.M.,
Shears S.B.;
"The Ins(1,3,4)P3 5/6-kinase/Ins(3,4,5,6)P4 1-kinase is not a protein
kinase.";
Biochem. J. 389:389-395(2005).
[9]
MUTAGENESIS OF LYS-18; HIS-58; LYS-59; ARG-106; HIS-162; GLY-163;
HIS-167; GLN-188; HIS-193; LYS-199; ARG-212; SER-214; LEU-215; ASN-297
AND GLY-301.
PubMed=15837423; DOI=10.1016/j.molcel.2005.03.016;
Miller G.J., Wilson M.P., Majerus P.W., Hurley J.H.;
"Specificity determinants in inositol polyphosphate synthesis: crystal
structure of inositol 1,3,4-trisphosphate 5/6-kinase.";
Mol. Cell 18:201-212(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[12]
ACETYLATION AT LYS-340; LYS-383 AND LYS-410.
PubMed=22308441; DOI=10.1073/pnas.1119740109;
Zhang C., Majerus P.W., Wilson M.P.;
"Regulation of inositol 1,3,4-trisphosphate 5/6-kinase (ITPK1) by
reversible lysine acetylation.";
Proc. Natl. Acad. Sci. U.S.A. 109:2290-2295(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-335 IN COMPLEXES WITH
MANGANESE; ATP ANALOG AND ADP, FUNCTION, AND SUBUNIT.
PubMed=17616525; DOI=10.1074/jbc.M703121200;
Chamberlain P.P., Qian X., Stiles A.R., Cho J., Jones D.H.,
Lesley S.A., Grabau E.A., Shears S.B., Spraggon G.;
"Integration of inositol phosphate signaling pathways via human
ITPK1.";
J. Biol. Chem. 282:28117-28125(2007).
[15]
X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 1-327.
Structural genomics consortium (SGC);
"Structure of human inositol 1,3,4-trisphosphate 5/6-kinase.";
Submitted (FEB-2007) to the PDB data bank.
-!- FUNCTION: Kinase that can phosphorylate various inositol
polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3.
Phosphorylates Ins(3,4,5,6)P4 at position 1 to form
Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory
importance, since Ins(3,4,5,6)P4 is an inhibitor of plasma
membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5
is not. Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form
Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate
(InsP6) pathway. Also acts as an inositol polyphosphate
phosphatase that dephosphorylate Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4
to Ins(1,3,4)P3, and Ins(1,3,4,5,6)P5 to Ins(3,4,5,6)P4. May also
act as an isomerase that interconverts the inositol
tetrakisphosphate isomers Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 in the
presence of ADP and magnesium. Probably acts as the rate-limiting
enzyme of the InsP6 pathway. Modifies TNF-alpha-induced apoptosis
by interfering with the activation of TNFRSF1A-associated death
domain. {ECO:0000269|PubMed:11909533, ECO:0000269|PubMed:12925536,
ECO:0000269|PubMed:17616525}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 3,4,5,6-
tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-
pentakisphosphate.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1,3,4-trisphosphate =
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1,3,4-trisphosphate =
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:8662638};
Note=Binds 2 magnesium ions per subunit.
{ECO:0000269|PubMed:8662638};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.3 uM for Ins(1,3,4)P3 {ECO:0000269|PubMed:11042108};
KM=0.1 uM for Ins(3,4,5,6)P4 {ECO:0000269|PubMed:11042108};
Vmax=320 pmol/min/ug enzyme with Ins(1,3,4)P3 as substrate
{ECO:0000269|PubMed:11042108};
Vmax=780 pmol/min/ug enzyme enzyme with Ins(3,4,5,6)P4 as
substrate {ECO:0000269|PubMed:11042108};
-!- SUBUNIT: Monomer. Interacts with GPS1/COPS1.
{ECO:0000269|PubMed:12324474, ECO:0000269|PubMed:17616525}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13572-1; Sequence=Displayed;
Name=2;
IsoId=Q13572-2; Sequence=VSP_016478, VSP_016479;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in brain > heart > skeletal muscle =
kidney = pancreas = liver = placenta > lung. In brain, it is
expressed in cerebellum, cerebral cortex, medulla, spinal cord,
occipital lobe, frontal lobe, temporal lobe and putamen.
{ECO:0000269|PubMed:8662638}.
-!- PTM: Acetylation by EP300 and CREBBP destabilizes ITPK1, and down-
regulates enzymatic activity. Deacetylated by SIRT1.
{ECO:0000269|PubMed:22308441}.
-!- SIMILARITY: Belongs to the ITPK1 family. {ECO:0000305}.
-!- CAUTION: PubMed:11533064 detected some protein kinase activity and
ability to phosphorylate transcription factors c-jun/JUN and ATF2.
However, PubMed:15762844 showed that it does not have protein
kinase activity. {ECO:0000305}.
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EMBL; U51336; AAC50483.1; -; mRNA.
EMBL; AF279372; AAG44835.1; -; mRNA.
EMBL; BC003622; AAH03622.1; -; mRNA.
EMBL; BC007428; AAH07428.1; -; mRNA.
EMBL; BC018192; AAH18192.1; -; mRNA.
CCDS; CCDS45157.1; -. [Q13572-2]
CCDS; CCDS9907.1; -. [Q13572-1]
RefSeq; NP_001136065.1; NM_001142593.2. [Q13572-1]
RefSeq; NP_001136066.1; NM_001142594.2. [Q13572-2]
RefSeq; NP_055031.2; NM_014216.5. [Q13572-1]
UniGene; Hs.308122; -.
PDB; 2ODT; X-ray; 2.01 A; X=1-327.
PDB; 2Q7D; X-ray; 1.60 A; A/B=1-335.
PDB; 2QB5; X-ray; 1.80 A; A/B=1-335.
PDBsum; 2ODT; -.
PDBsum; 2Q7D; -.
PDBsum; 2QB5; -.
ProteinModelPortal; Q13572; -.
SMR; Q13572; -.
BioGrid; 109910; 14.
DIP; DIP-60016N; -.
IntAct; Q13572; 5.
MINT; Q13572; -.
STRING; 9606.ENSP00000267615; -.
BindingDB; Q13572; -.
ChEMBL; CHEMBL1938220; -.
iPTMnet; Q13572; -.
PhosphoSitePlus; Q13572; -.
BioMuta; ITPK1; -.
DMDM; 83288249; -.
EPD; Q13572; -.
MaxQB; Q13572; -.
PaxDb; Q13572; -.
PeptideAtlas; Q13572; -.
PRIDE; Q13572; -.
DNASU; 3705; -.
Ensembl; ENST00000267615; ENSP00000267615; ENSG00000100605. [Q13572-1]
Ensembl; ENST00000354313; ENSP00000346272; ENSG00000100605. [Q13572-2]
Ensembl; ENST00000556603; ENSP00000451091; ENSG00000100605. [Q13572-1]
Ensembl; ENST00000614271; ENSP00000483767; ENSG00000274958. [Q13572-1]
Ensembl; ENST00000617836; ENSP00000480918; ENSG00000274958. [Q13572-2]
Ensembl; ENST00000626153; ENSP00000486991; ENSG00000274958. [Q13572-1]
GeneID; 3705; -.
KEGG; hsa:3705; -.
UCSC; uc001ybe.2; human. [Q13572-1]
CTD; 3705; -.
DisGeNET; 3705; -.
EuPathDB; HostDB:ENSG00000100605.16; -.
GeneCards; ITPK1; -.
H-InvDB; HIX0037938; -.
HGNC; HGNC:6177; ITPK1.
HPA; HPA055230; -.
MIM; 601838; gene.
neXtProt; NX_Q13572; -.
OpenTargets; ENSG00000100605; -.
PharmGKB; PA29974; -.
eggNOG; ENOG410IHA6; Eukaryota.
eggNOG; ENOG4110KIK; LUCA.
GeneTree; ENSGT00390000001278; -.
HOVERGEN; HBG079462; -.
InParanoid; Q13572; -.
KO; K00913; -.
OMA; MQDERIC; -.
OrthoDB; EOG091G08J8; -.
PhylomeDB; Q13572; -.
TreeFam; TF329288; -.
BioCyc; MetaCyc:HS02123-MONOMER; -.
BRENDA; 2.7.1.134; 2681.
BRENDA; 2.7.1.159; 2681.
Reactome; R-HSA-1855167; Synthesis of pyrophosphates in the cytosol.
Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SABIO-RK; Q13572; -.
ChiTaRS; ITPK1; human.
EvolutionaryTrace; Q13572; -.
GeneWiki; ITPK1; -.
GenomeRNAi; 3705; -.
PRO; PR:Q13572; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100605; -.
ExpressionAtlas; Q13572; baseline and differential.
Genevisible; Q13572; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003824; F:catalytic activity; TAS:ProtInc.
GO; GO:0047325; F:inositol tetrakisphosphate 1-kinase activity; EXP:Reactome.
GO; GO:0052825; F:inositol-1,3,4,5,6-pentakisphosphate 1-phosphatase activity; TAS:Reactome.
GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; TAS:Reactome.
GO; GO:0052831; F:inositol-1,3,4,6-tetrakisphosphate 1-phosphatase activity; TAS:Reactome.
GO; GO:0052830; F:inositol-1,3,4,6-tetrakisphosphate 6-phosphatase activity; TAS:Reactome.
GO; GO:0052726; F:inositol-1,3,4-trisphosphate 5-kinase activity; EXP:Reactome.
GO; GO:0052725; F:inositol-1,3,4-trisphosphate 6-kinase activity; EXP:Reactome.
GO; GO:0052835; F:inositol-3,4,6-trisphosphate 1-kinase activity; TAS:Reactome.
GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
GO; GO:0032957; P:inositol trisphosphate metabolic process; IEA:InterPro.
GO; GO:0021915; P:neural tube development; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR008656; Inositol_tetrakis-P_1-kinase.
PANTHER; PTHR14217; PTHR14217; 1.
Pfam; PF05770; Ins134_P3_kin; 1.
PROSITE; PS50975; ATP_GRASP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Hydrolase; Isomerase; Kinase; Magnesium;
Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
Transferase.
CHAIN 1 414 Inositol-tetrakisphosphate 1-kinase.
/FTId=PRO_0000220833.
DOMAIN 117 325 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
NP_BIND 188 199 ATP.
METAL 281 281 Magnesium 1.
METAL 295 295 Magnesium 1.
METAL 295 295 Magnesium 2.
METAL 297 297 Magnesium 2.
BINDING 18 18 1D-myo-inositol 1,3,4-trisphosphate.
{ECO:0000250}.
BINDING 106 106 ATP.
BINDING 157 157 ATP.
BINDING 167 167 1D-myo-inositol 1,3,4-trisphosphate.
{ECO:0000250}.
BINDING 199 199 1D-myo-inositol 1,3,4-trisphosphate.
{ECO:0000250}.
BINDING 214 214 ATP.
BINDING 232 232 ATP.
BINDING 236 236 ATP.
BINDING 297 297 1D-myo-inositol 1,3,4-trisphosphate.
{ECO:0000250}.
MOD_RES 340 340 N6-acetyllysine; by EP300 and CREBBP.
{ECO:0000269|PubMed:22308441}.
MOD_RES 383 383 N6-acetyllysine; by EP300 and CREBBP.
{ECO:0000269|PubMed:22308441}.
MOD_RES 396 396 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 410 410 N6-acetyllysine; by EP300 and CREBBP.
{ECO:0000269|PubMed:22308441}.
VAR_SEQ 302 314 YEGVSEFFTDLLN -> DCQVCFIEGWKTD (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_016478.
VAR_SEQ 315 414 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_016479.
MUTAGEN 18 18 K->A: Loss of kinase activity.
{ECO:0000269|PubMed:15837423}.
MUTAGEN 58 58 H->A: No effect.
{ECO:0000269|PubMed:15837423}.
MUTAGEN 59 59 K->A: Loss of kinase activity.
{ECO:0000269|PubMed:15837423}.
MUTAGEN 106 106 R->A: Loss of kinase activity.
{ECO:0000269|PubMed:15762844,
ECO:0000269|PubMed:15837423}.
MUTAGEN 157 157 K->A: Loss of kinase activity.
{ECO:0000269|PubMed:15762844}.
MUTAGEN 162 162 H->Q: Loss of kinase activity.
{ECO:0000269|PubMed:15837423}.
MUTAGEN 163 163 G->A,P: Loss of kinase activity.
{ECO:0000269|PubMed:15762844,
ECO:0000269|PubMed:15837423}.
MUTAGEN 163 163 G->A: No effect.
{ECO:0000269|PubMed:15762844,
ECO:0000269|PubMed:15837423}.
MUTAGEN 167 167 H->A,Q: Loss of kinase activity.
{ECO:0000269|PubMed:15837423}.
MUTAGEN 188 188 Q->A: No effect.
{ECO:0000269|PubMed:15837423}.
MUTAGEN 193 193 H->A: Loss of kinase activity.
{ECO:0000269|PubMed:15837423}.
MUTAGEN 199 199 K->A: Loss of kinase activity.
{ECO:0000269|PubMed:15837423}.
MUTAGEN 212 212 R->A: Loss of kinase activity.
{ECO:0000269|PubMed:15837423}.
MUTAGEN 214 214 S->A: Loss of kinase activity.
{ECO:0000269|PubMed:15837423}.
MUTAGEN 215 215 L->A: No effect.
{ECO:0000269|PubMed:15837423}.
MUTAGEN 281 281 D->A: Loss of kinase activity.
{ECO:0000269|PubMed:15762844}.
MUTAGEN 295 295 D->A: Loss of kinase activity.
{ECO:0000269|PubMed:15762844}.
MUTAGEN 297 297 N->A,L: Loss of kinase activity.
{ECO:0000269|PubMed:15762844,
ECO:0000269|PubMed:15837423}.
MUTAGEN 297 297 N->D: Induces a strong reduction in
kinase activity.
{ECO:0000269|PubMed:15762844,
ECO:0000269|PubMed:15837423}.
MUTAGEN 301 301 G->A: Loss of kinase activity.
{ECO:0000269|PubMed:15837423}.
CONFLICT 356 356 S -> N (in Ref. 1; AAC50483).
{ECO:0000305}.
HELIX 1 5 {ECO:0000244|PDB:2Q7D}.
STRAND 9 13 {ECO:0000244|PDB:2Q7D}.
HELIX 16 22 {ECO:0000244|PDB:2Q7D}.
HELIX 24 32 {ECO:0000244|PDB:2Q7D}.
TURN 33 35 {ECO:0000244|PDB:2Q7D}.
STRAND 37 40 {ECO:0000244|PDB:2Q7D}.
HELIX 48 50 {ECO:0000244|PDB:2Q7D}.
STRAND 54 58 {ECO:0000244|PDB:2Q7D}.
HELIX 61 68 {ECO:0000244|PDB:2Q7D}.
HELIX 72 87 {ECO:0000244|PDB:2Q7D}.
STRAND 91 95 {ECO:0000244|PDB:2Q7D}.
HELIX 97 102 {ECO:0000244|PDB:2Q7D}.
HELIX 106 120 {ECO:0000244|PDB:2Q7D}.
STRAND 130 133 {ECO:0000244|PDB:2Q7D}.
HELIX 138 140 {ECO:0000244|PDB:2ODT}.
HELIX 141 147 {ECO:0000244|PDB:2Q7D}.
STRAND 152 157 {ECO:0000244|PDB:2Q7D}.
TURN 164 167 {ECO:0000244|PDB:2QB5}.
STRAND 168 172 {ECO:0000244|PDB:2Q7D}.
HELIX 175 177 {ECO:0000244|PDB:2Q7D}.
STRAND 185 189 {ECO:0000244|PDB:2Q7D}.
STRAND 196 203 {ECO:0000244|PDB:2Q7D}.
STRAND 206 213 {ECO:0000244|PDB:2Q7D}.
STRAND 228 231 {ECO:0000244|PDB:2Q7D}.
HELIX 232 234 {ECO:0000244|PDB:2Q7D}.
HELIX 243 245 {ECO:0000244|PDB:2Q7D}.
HELIX 259 273 {ECO:0000244|PDB:2Q7D}.
STRAND 277 284 {ECO:0000244|PDB:2Q7D}.
TURN 286 288 {ECO:0000244|PDB:2Q7D}.
STRAND 291 299 {ECO:0000244|PDB:2Q7D}.
HELIX 308 324 {ECO:0000244|PDB:2Q7D}.
SEQUENCE 414 AA; 45621 MW; E89E2EE11971278E CRC64;
MQTFLKGKRV GYWLSEKKIK KLNFQAFAEL CRKRGMEVVQ LNLSRPIEEQ GPLDVIIHKL
TDVILEADQN DSQSLELVHR FQEYIDAHPE TIVLDPLPAI RTLLDRSKSY ELIRKIEAYM
EDDRICSPPF MELTSLCGDD TMRLLEKNGL TFPFICKTRV AHGTNSHEMA IVFNQEGLNA
IQPPCVVQNF INHNAVLYKV FVVGESYTVV QRPSLKNFSA GTSDRESIFF NSHNVSKPES
SSVLTELDKI EGVFERPSDE VIRELSRALR QALGVSLFGI DIIINNQTGQ HAVIDINAFP
GYEGVSEFFT DLLNHIATVL QGQSTAMAAT GDVALLRHSK LLAEPAGGLV GERTCSASPG
CCGSMMGQDA PWKAEADAGG TAKLPHQRLG CNAGVSPSFQ QHCVASLATK ASSQ


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Catalog number Product name Quantity
pka-040 Recombinant Human Inositol-Tetrakisphosphate 1-Kinase 5
pka-040 Recombinant Human Inositol-Tetrakisphosphate 1-Kinase 1mg
RPK-040 Recombinant Human Inositol-Tetrakisphosphate 1-Kinase 5
pka-040 Recombinant Human Inositol-Tetrakisphosphate 1-Kinase 20
ITPK1_MOUSE Mouse ELISA Kit FOR Inositol-tetrakisphosphate 1-kinase 96T
CSB-EL011908CH Chicken Inositol-tetrakisphosphate 1-kinase(ITPK1) ELISA kit 96T
CSB-EL011908MO Mouse Inositol-tetrakisphosphate 1-kinase(ITPK1) ELISA kit 96T
pka-040 Recombinant Human Inositol-Tetrakisphosphate 1-Kinase PROTEIN KINASES 1mg
CSB-EL011908BO Bovine Inositol-tetrakisphosphate 1-kinase(ITPK1) ELISA kit 96T
pka-040 Recombinant Human Inositol-Tetrakisphosphate 1-Kinase PROTEIN KINASES 5
CSB-EL011908HU Human Inositol-tetrakisphosphate 1-kinase(ITPK1) ELISA kit 96T
pka-040 Recombinant Human Inositol-Tetrakisphosphate 1-Kinase PROTEIN KINASES 20
26-957 ITPK1 is the kinase that can phosphorylate various inositol polyphosphate such as Ins (3,4,5,6)P4 or Ins (1,3,4)P3. It may also act as an isomerase that interconverts the inositol tetraphosphate isome 0.05 mg
CSB-EL011908CH Chicken Inositol-tetrakisphosphate 1-kinase(ITPK1) ELISA kit SpeciesChicken 96T
CSB-EL011908HU Human Inositol-tetrakisphosphate 1-kinase(ITPK1) ELISA kit SpeciesHuman 96T
CSB-EL011908BO Bovine Inositol-tetrakisphosphate 1-kinase(ITPK1) ELISA kit SpeciesBovine 96T
CSB-EL011908MO Mouse Inositol-tetrakisphosphate 1-kinase(ITPK1) ELISA kit SpeciesMouse 96T
ITPK1_MOUSE ELISA Kit FOR Inositol-tetrakisphosphate 1-kinase; organism: Mouse; gene name: Itpk1 96T
CSB-EL011909RA Rat Inositol-trisphosphate 3-kinase A(ITPKA) ELISA kit 96T
E15032m Mouse ELISA Kit FOR Inositol-trisphosphate 3-kinase A 96T
201-20-2867 ITPKC{inositol 1,4,5-trisphosphate 3-kinase C}rabbit.pAb 0.2ml
201-20-2866 ITPKB{inositol 1,4,5-trisphosphate 3-kinase B}rabbit.pAb 0.2ml
CSB-EL011911RA Rat Inositol-trisphosphate 3-kinase C(ITPKC) ELISA kit 96T
ITPR2 ITPKC Gene inositol 1,4,5-trisphosphate 3-kinase C
ITPR1 ITPKB Gene inositol 1,4,5-trisphosphate 3-kinase B


 

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