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

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 (EC 2.7.4.21) (EC 2.7.4.24) (Diphosphoinositol pentakisphosphate kinase 2) (Histidine acid phosphatase domain-containing protein 1) (InsP6 and PP-IP5 kinase 2) (VIP1 homolog 2) (hsVIP2)

 VIP2_HUMAN              Reviewed;        1243 AA.
O43314; A1NI53; A6NGS8; Q8TB50;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
15-JAN-2008, sequence version 3.
25-OCT-2017, entry version 133.
RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2;
EC=2.7.4.21 {ECO:0000269|PubMed:21222653};
EC=2.7.4.24 {ECO:0000269|PubMed:21222653};
AltName: Full=Diphosphoinositol pentakisphosphate kinase 2;
AltName: Full=Histidine acid phosphatase domain-containing protein 1;
AltName: Full=InsP6 and PP-IP5 kinase 2;
AltName: Full=VIP1 homolog 2;
Short=hsVIP2;
Name=PPIP5K2; Synonyms=HISPPD1, KIAA0433, VIP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9455477; DOI=10.1093/dnares/4.5.307;
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VIII.
78 new cDNA clones from brain which code for large proteins in
vitro.";
DNA Res. 4:307-313(1997).
[2]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
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).
[6]
FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBCELLULAR LOCATION.
PubMed=17690096; DOI=10.1074/jbc.M704656200;
Fridy P.C., Otto J.C., Dollins D.E., York J.D.;
"Cloning and characterization of two human VIP1-like inositol
hexakisphosphate and diphosphoinositol pentakisphosphate kinases.";
J. Biol. Chem. 282:30754-30762(2007).
[7]
FUNCTION, AND ENZYME ACTIVITY.
PubMed=17702752; DOI=10.1074/jbc.M704655200;
Choi J.H., Williams J., Cho J., Falck J.R., Shears S.B.;
"Purification, sequencing, and molecular identification of a mammalian
PP-InsP5 kinase that is activated when cells are exposed to
hyperosmotic stress.";
J. Biol. Chem. 282:30763-30775(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1006; SER-1016 AND
SER-1172, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[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]
CATALYTIC ACTIVITY, AND POLYPHOSPHOINOSITIDE-BINDING DOMAIN.
PubMed=21222653; DOI=10.1042/BJ20101437;
Gokhale N.A., Zaremba A., Shears S.B.;
"Receptor-dependent compartmentalization of PPIP5K1, a kinase with a
cryptic polyphosphoinositide binding domain.";
Biochem. J. 434:415-426(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-223; SER-1006;
SER-1016; SER-1074; SER-1091; SER-1165; SER-1172; SER-1180; SER-1220
AND SER-1221, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-1006 AND
SER-1091, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14] {ECO:0000244|PDB:3T54, ECO:0000244|PDB:3T7A, ECO:0000244|PDB:3T99, ECO:0000244|PDB:3T9A, ECO:0000244|PDB:3T9B, ECO:0000244|PDB:3T9C, ECO:0000244|PDB:3T9D, ECO:0000244|PDB:3T9E, ECO:0000244|PDB:3T9F}
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 41-366 IN COMPLEXES WITH
ATP; SUBSTRATE AND TRANSITION STATE ANALOG, AND MUTAGENESIS OF
ARG-213; LYS-248 AND ARG-262.
PubMed=22119861; DOI=10.1038/nchembio.733;
Wang H., Falck J.R., Hall T.M., Shears S.B.;
"Structural basis for an inositol pyrophosphate kinase surmounting
phosphate crowding.";
Nat. Chem. Biol. 8:111-116(2012).
-!- FUNCTION: Bifunctional inositol kinase that acts in concert with
the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the
diphosphate group-containing inositol pyrophosphates
diphosphoinositol pentakisphosphate, PP-InsP5, and bis-
diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and
(PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a
variety of cellular processes, including apoptosis, vesicle
trafficking, cytoskeletal dynamics, exocytosis, insulin signaling
and neutrophil activation. Phosphorylates inositol
hexakisphosphate (InsP6) at positions 1 or 3 to produce PP-InsP5
which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4.
Alternatively, phosphorylates at position 1 or 3 PP-InsP5,
produced by IP6Ks from InsP6, to produce (PP)2-InsP4.
{ECO:0000269|PubMed:17690096, ECO:0000269|PubMed:17702752}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate.
{ECO:0000269|PubMed:21222653}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-
pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate)
2,3,4,6-tetrakisphosphate. {ECO:0000269|PubMed:21222653}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-
pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate)
2,3,4,6-tetrakisphosphate. {ECO:0000269|PubMed:21222653}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.
{ECO:0000269|PubMed:21222653}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.13 uM for InsP6 {ECO:0000269|PubMed:17690096};
KM=0.19 uM for InsP7 {ECO:0000269|PubMed:17690096};
Vmax=0.39 nmol/min/mg enzyme with InsP6 as substrate
{ECO:0000269|PubMed:17690096};
Vmax=1.38 nmol/min/mg enzyme with InsP7 as substrate
{ECO:0000269|PubMed:17690096};
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:17690096}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O43314-1; Sequence=Displayed;
Name=2;
IsoId=O43314-2; Sequence=VSP_030636;
Note=No experimental confirmation available.;
-!- DOMAIN: The C-terminal acid phosphatase-like domain binds
PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the
phosphatase domain of histidine acid phosphatases, it has no
phosphatase activity. {ECO:0000305|PubMed:21222653}.
-!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA24863.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=EAW49076.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB007893; BAA24863.2; ALT_INIT; mRNA.
EMBL; AC011362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471086; EAW49076.1; ALT_SEQ; Genomic_DNA.
EMBL; BC024591; AAH24591.1; -; mRNA.
CCDS; CCDS34207.1; -. [O43314-2]
CCDS; CCDS64212.1; -. [O43314-1]
RefSeq; NP_001263206.1; NM_001276277.2. [O43314-1]
RefSeq; NP_001268400.1; NM_001281471.2.
RefSeq; NP_056031.2; NM_015216.4. [O43314-2]
UniGene; Hs.212046; -.
PDB; 3T54; X-ray; 1.90 A; A=37-366.
PDB; 3T7A; X-ray; 1.70 A; A=41-366.
PDB; 3T99; X-ray; 2.10 A; A=37-366.
PDB; 3T9A; X-ray; 1.80 A; A=41-366.
PDB; 3T9B; X-ray; 1.85 A; A=41-366.
PDB; 3T9C; X-ray; 1.90 A; A=41-366.
PDB; 3T9D; X-ray; 1.85 A; A=41-366.
PDB; 3T9E; X-ray; 1.90 A; A=41-366.
PDB; 3T9F; X-ray; 2.00 A; A=41-366.
PDB; 4HN2; X-ray; 1.90 A; A=41-366.
PDB; 4NZM; X-ray; 2.00 A; A=41-366.
PDB; 4NZN; X-ray; 1.75 A; A=41-366.
PDB; 4NZO; X-ray; 1.90 A; A=41-366.
PDB; 4Q4C; X-ray; 1.90 A; A=41-366.
PDB; 4Q4D; X-ray; 1.85 A; A=41-366.
PDB; 5BYA; X-ray; 1.90 A; A=41-366.
PDB; 5BYB; X-ray; 2.30 A; A=41-366.
PDB; 5DGH; X-ray; 2.10 A; A=41-366.
PDB; 5DGI; X-ray; 1.85 A; A=41-366.
PDBsum; 3T54; -.
PDBsum; 3T7A; -.
PDBsum; 3T99; -.
PDBsum; 3T9A; -.
PDBsum; 3T9B; -.
PDBsum; 3T9C; -.
PDBsum; 3T9D; -.
PDBsum; 3T9E; -.
PDBsum; 3T9F; -.
PDBsum; 4HN2; -.
PDBsum; 4NZM; -.
PDBsum; 4NZN; -.
PDBsum; 4NZO; -.
PDBsum; 4Q4C; -.
PDBsum; 4Q4D; -.
PDBsum; 5BYA; -.
PDBsum; 5BYB; -.
PDBsum; 5DGH; -.
PDBsum; 5DGI; -.
ProteinModelPortal; O43314; -.
SMR; O43314; -.
BioGrid; 116864; 23.
IntAct; O43314; 5.
STRING; 9606.ENSP00000313070; -.
iPTMnet; O43314; -.
PhosphoSitePlus; O43314; -.
EPD; O43314; -.
MaxQB; O43314; -.
PaxDb; O43314; -.
PeptideAtlas; O43314; -.
PRIDE; O43314; -.
Ensembl; ENST00000321521; ENSP00000313070; ENSG00000145725. [O43314-2]
Ensembl; ENST00000358359; ENSP00000351126; ENSG00000145725. [O43314-1]
Ensembl; ENST00000414217; ENSP00000416016; ENSG00000145725. [O43314-2]
GeneID; 23262; -.
KEGG; hsa:23262; -.
UCSC; uc003kod.6; human. [O43314-1]
CTD; 23262; -.
DisGeNET; 23262; -.
EuPathDB; HostDB:ENSG00000145725.19; -.
GeneCards; PPIP5K2; -.
H-InvDB; HIX0005068; -.
H-InvDB; HIX0029534; -.
HGNC; HGNC:29035; PPIP5K2.
HPA; HPA037895; -.
HPA; HPA038442; -.
MIM; 611648; gene.
neXtProt; NX_O43314; -.
OpenTargets; ENSG00000145725; -.
PharmGKB; PA165660454; -.
eggNOG; KOG1057; Eukaryota.
eggNOG; ENOG410XNSN; LUCA.
GeneTree; ENSGT00390000009048; -.
HOGENOM; HOG000177917; -.
HOVERGEN; HBG108657; -.
InParanoid; O43314; -.
KO; K13024; -.
PhylomeDB; O43314; -.
TreeFam; TF313594; -.
BRENDA; 2.7.4.21; 2681.
BRENDA; 2.7.4.24; 2681.
Reactome; R-HSA-1855167; Synthesis of pyrophosphates in the cytosol.
SABIO-RK; O43314; -.
ChiTaRS; PPIP5K2; human.
GenomeRNAi; 23262; -.
PRO; PR:O43314; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000145725; -.
CleanEx; HS_HISPPD1; -.
ExpressionAtlas; O43314; baseline and differential.
Genevisible; O43314; HS.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IDA:MGI.
GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IBA:GO_Central.
GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; ISS:UniProtKB.
GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IDA:MGI.
GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; ISS:UniProtKB.
GO; GO:0006020; P:inositol metabolic process; ISS:UniProtKB.
GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
CDD; cd07061; HP_HAP_like; 1.
Gene3D; 3.40.50.1240; -; 1.
InterPro; IPR033379; Acid_Pase_AS.
InterPro; IPR000560; His_Pase_clade-2.
InterPro; IPR029033; His_PPase_superfam.
Pfam; PF00328; His_Phos_2; 1.
SUPFAM; SSF53254; SSF53254; 3.
PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome; Transferase.
CHAIN 1 1243 Inositol hexakisphosphate and
diphosphoinositol-pentakisphosphate
kinase 2.
/FTId=PRO_0000315692.
NP_BIND 237 240 ATP. {ECO:0000244|PDB:3T54,
ECO:0000244|PDB:3T7A,
ECO:0000244|PDB:3T99,
ECO:0000244|PDB:3T9A,
ECO:0000244|PDB:3T9B,
ECO:0000244|PDB:3T9C,
ECO:0000244|PDB:3T9D,
ECO:0000244|PDB:3T9E,
ECO:0000244|PDB:3T9F,
ECO:0000269|PubMed:22119861}.
NP_BIND 246 248 ATP. {ECO:0000244|PDB:3T54,
ECO:0000244|PDB:3T9A,
ECO:0000244|PDB:3T9B,
ECO:0000244|PDB:3T9C,
ECO:0000244|PDB:3T9D,
ECO:0000269|PubMed:22119861}.
NP_BIND 321 323 ATP. {ECO:0000244|PDB:3T54,
ECO:0000269|PubMed:22119861}.
REGION 53 54 Substrate binding. {ECO:0000244|PDB:3T9C,
ECO:0000244|PDB:3T9D,
ECO:0000244|PDB:3T9E,
ECO:0000244|PDB:3T9F,
ECO:0000269|PubMed:22119861}.
REGION 213 214 Substrate binding. {ECO:0000244|PDB:3T9C,
ECO:0000244|PDB:3T9D,
ECO:0000244|PDB:3T9E,
ECO:0000244|PDB:3T9F,
ECO:0000269|PubMed:22119861}.
REGION 326 329 Substrate binding. {ECO:0000244|PDB:3T9D,
ECO:0000244|PDB:3T9E,
ECO:0000269|PubMed:22119861}.
REGION 371 442 Polyphosphoinositide-binding domain.
{ECO:0000269|PubMed:21222653}.
BINDING 134 134 ATP. {ECO:0000244|PDB:3T54,
ECO:0000244|PDB:3T7A,
ECO:0000244|PDB:3T99,
ECO:0000244|PDB:3T9A,
ECO:0000244|PDB:3T9B,
ECO:0000244|PDB:3T9C,
ECO:0000244|PDB:3T9D,
ECO:0000244|PDB:3T9E,
ECO:0000244|PDB:3T9F,
ECO:0000269|PubMed:22119861}.
BINDING 187 187 ATP. {ECO:0000244|PDB:3T54,
ECO:0000244|PDB:3T7A,
ECO:0000244|PDB:3T99,
ECO:0000244|PDB:3T9A,
ECO:0000244|PDB:3T9B,
ECO:0000244|PDB:3T9C,
ECO:0000244|PDB:3T9D,
ECO:0000244|PDB:3T9E,
ECO:0000244|PDB:3T9F,
ECO:0000269|PubMed:22119861}.
BINDING 194 194 ATP. {ECO:0000244|PDB:3T54,
ECO:0000244|PDB:3T7A,
ECO:0000244|PDB:3T99,
ECO:0000244|PDB:3T9A,
ECO:0000244|PDB:3T9B,
ECO:0000244|PDB:3T9C,
ECO:0000244|PDB:3T9D,
ECO:0000244|PDB:3T9E,
ECO:0000244|PDB:3T9F,
ECO:0000269|PubMed:22119861}.
BINDING 213 213 ATP. {ECO:0000244|PDB:3T9A,
ECO:0000244|PDB:3T9B,
ECO:0000244|PDB:3T9C,
ECO:0000244|PDB:3T9D,
ECO:0000269|PubMed:22119861}.
BINDING 248 248 Substrate. {ECO:0000244|PDB:3T9C,
ECO:0000244|PDB:3T9D,
ECO:0000244|PDB:3T9E,
ECO:0000244|PDB:3T9F,
ECO:0000269|PubMed:22119861}.
BINDING 262 262 Substrate. {ECO:0000244|PDB:3T9C,
ECO:0000244|PDB:3T9E,
ECO:0000244|PDB:3T9F,
ECO:0000269|PubMed:22119861}.
BINDING 264 264 ATP. {ECO:0000244|PDB:3T54,
ECO:0000244|PDB:3T7A,
ECO:0000269|PubMed:22119861}.
BINDING 309 309 ATP. {ECO:0000244|PDB:3T54,
ECO:0000244|PDB:3T7A,
ECO:0000244|PDB:3T99,
ECO:0000244|PDB:3T9B,
ECO:0000244|PDB:3T9C,
ECO:0000244|PDB:3T9D,
ECO:0000244|PDB:3T9E,
ECO:0000244|PDB:3T9F,
ECO:0000269|PubMed:22119861}.
MOD_RES 38 38 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 223 223 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1006 1006 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1016 1016 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1074 1074 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1091 1091 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1165 1165 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1172 1172 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1180 1180 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1220 1220 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1221 1221 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1097 1117 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_030636.
VARIANT 944 944 A -> G (in dbSNP:rs17155115).
/FTId=VAR_038276.
VARIANT 985 985 E -> K (in dbSNP:rs12519525).
/FTId=VAR_038277.
VARIANT 1003 1003 R -> K (in dbSNP:rs12520040).
/FTId=VAR_038278.
VARIANT 1206 1206 P -> Q (in dbSNP:rs17155138).
/FTId=VAR_038279.
VARIANT 1232 1232 T -> M (in dbSNP:rs17155147).
/FTId=VAR_038280.
MUTAGEN 213 213 R->A,K: Reduces enzyme activity by about
99%. {ECO:0000269|PubMed:22119861}.
MUTAGEN 248 248 K->A: Loss of enzyme activity.
{ECO:0000269|PubMed:22119861}.
MUTAGEN 262 262 R->A: Reduces enzyme activity by about
99%. {ECO:0000269|PubMed:22119861}.
STRAND 44 50 {ECO:0000244|PDB:3T7A}.
HELIX 52 55 {ECO:0000244|PDB:3T7A}.
HELIX 58 67 {ECO:0000244|PDB:3T7A}.
STRAND 73 77 {ECO:0000244|PDB:3T7A}.
HELIX 80 85 {ECO:0000244|PDB:3T7A}.
HELIX 88 90 {ECO:0000244|PDB:3T7A}.
STRAND 95 99 {ECO:0000244|PDB:3T7A}.
HELIX 107 117 {ECO:0000244|PDB:3T7A}.
STRAND 120 123 {ECO:0000244|PDB:3T7A}.
HELIX 127 131 {ECO:0000244|PDB:3T7A}.
HELIX 134 143 {ECO:0000244|PDB:3T7A}.
STRAND 151 154 {ECO:0000244|PDB:3T7A}.
STRAND 158 160 {ECO:0000244|PDB:4NZN}.
HELIX 161 163 {ECO:0000244|PDB:3T7A}.
STRAND 164 168 {ECO:0000244|PDB:3T7A}.
STRAND 170 175 {ECO:0000244|PDB:3T7A}.
STRAND 178 190 {ECO:0000244|PDB:3T7A}.
STRAND 197 199 {ECO:0000244|PDB:3T7A}.
HELIX 202 204 {ECO:0000244|PDB:3T7A}.
STRAND 208 215 {ECO:0000244|PDB:3T7A}.
STRAND 218 224 {ECO:0000244|PDB:3T7A}.
STRAND 230 232 {ECO:0000244|PDB:3T7A}.
STRAND 234 238 {ECO:0000244|PDB:3T7A}.
STRAND 243 253 {ECO:0000244|PDB:3T7A}.
STRAND 257 263 {ECO:0000244|PDB:3T7A}.
STRAND 265 267 {ECO:0000244|PDB:3T9A}.
STRAND 275 279 {ECO:0000244|PDB:3T9A}.
HELIX 288 300 {ECO:0000244|PDB:3T7A}.
STRAND 303 313 {ECO:0000244|PDB:3T7A}.
STRAND 316 325 {ECO:0000244|PDB:3T7A}.
HELIX 332 354 {ECO:0000244|PDB:3T7A}.
SEQUENCE 1243 AA; 140407 MW; A8831DDDAB9B2E6E CRC64;
MSEAPRFFVG PEDTEINPGN YRHFFHHADE DDEEEDDSPP ERQIVVGICS MAKKSKSKPM
KEILERISLF KYITVVVFEE EVILNEPVEN WPLCDCLISF HSKGFPLDKA VAYAKLRNPF
VINDLNMQYL IQDRREVYSI LQAEGILLPR YAILNRDPNN PKECNLIEGE DHVEVNGEVF
QKPFVEKPVS AEDHNVYIYY PTSAGGGSQR LFRKIGSRSS VYSPESNVRK TGSYIYEEFM
PTDGTDVKVY TVGPDYAHAE ARKSPALDGK VERDSEGKEV RYPVILNARE KLIAWKVCLA
FKQTVCGFDL LRANGQSYVC DVNGFSFVKN SMKYYDDCAK ILGNIVMREL APQFHIPWSI
PLEAEDIPIV PTTSGTMMEL RCVIAVIRHG DRTPKQKMKM EVRHQKFFDL FEKCDGYKSG
KLKLKKPKQL QEVLDIARQL LMELGQNNDS EIEENKPKLE QLKTVLEMYG HFSGINRKVQ
LTYLPHGCPK TSSEEEDSRR EEPSLLLVLK WGGELTPAGR VQAEELGRAF RCMYPGGQGD
YAGFPGCGLL RLHSTYRHDL KIYASDEGRV QMTAAAFAKG LLALEGELTP ILVQMVKSAN
MNGLLDSDSD SLSSCQQRVK ARLHEILQKD RDFTAEDYEK LTPSGSISLI KSMHLIKNPV
KTCDKVYSLI QSLTSQIRHR MEDPKSSDIQ LYHSETLELM LRRWSKLEKD FKTKNGRYDI
SKIPDIYDCI KYDVQHNGSL KLENTMELYR LSKALADIVI PQEYGITKAE KLEIAKGYCT
PLVRKIRSDL QRTQDDDTVN KLHPVYSRGV LSPERHVRTR LYFTSESHVH SLLSILRYGA
LCNESKDEQW KRAMDYLNVV NELNYMTQIV IMLYEDPNKD LSSEERFHVE LHFSPGAKGC
EEDKNLPSGY GYRPASRENE GRRPFKIDND DEPHTSKRDE VDRAVILFKP MVSEPIHIHR
KSPLPRSRKT ATNDEESPLS VSSPEGTGTW LHYTSGVGTG RRRRRSGEQI TSSPVSPKSL
AFTSSIFGSW QQVVSENANY LRTPRTLVEQ KQNPTVGSHC AGLFSTSVLG GSSSAPNLQD
YARTHRKKLT SSGCIDDATR GSAVKRFSIS FARHPTNGFE LYSMVPSICP LETLHNALSL
KQVDEFLASI ASPSSDVPRK TAEISSTALR SSPIMRKKVS LNTYTPAKIL PTPPATLKST
KASSKPATSG PSSAVVPNTS SRKKNITSKT ETHEHKKNTG KKK


Related products :

Catalog number Product name Quantity
EIAAB45793 Diphosphoinositol pentakisphosphate kinase 2,HISPPD1,Histidine acid phosphatase domain-containing protein 1,Homo sapiens,hsVIP2,Human,Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate
EIAAB45790 Diphosphoinositol pentakisphosphate kinase 1,Hisppd2a,Histidine acid phosphatase domain-containing protein 2A,Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1,InsP6 and PP-IP
EIAAB45789 Diphosphoinositol pentakisphosphate kinase 1,Hisppd2a,Histidine acid phosphatase domain-containing protein 2A,Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1,InsP6 and PP-IP
EIAAB45792 Diphosphoinositol pentakisphosphate kinase 2,Hisppd1,Histidine acid phosphatase domain-containing protein 1,Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2,InsP6 and PP-IP5
EIAAB45788 Bos taurus,Bovine,Diphosphoinositol pentakisphosphate kinase 1,HISPPD2A,Histidine acid phosphatase domain-containing protein 2A,Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
EIAAB45791 Diphosphoinositol pentakisphosphate kinase 1,HISPPD2A,Histidine acid phosphatase domain-containing protein 2A,Homo sapiens,hsVIP1,Human,Inositol hexakisphosphate and diphosphoinositol-pentakisphosphat
CSB-EL010373HU Human Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2(HISPPD1) ELISA kit 96T
CSB-EL010374HU Human Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1(HISPPD2A) ELISA kit 96T
CSB-EL010373HU Human Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2(HISPPD1) ELISA kit SpeciesHuman 96T
CSB-EL010374HU Human Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1(HISPPD2A) ELISA kit SpeciesHuman 96T
VIP1_MOUSE ELISA Kit FOR Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1; organism: Mouse; gene name: Ppip5k1 96T
VIP2_MOUSE ELISA Kit FOR Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2; organism: Mouse; gene name: Ppip5k2 96T
PPL PPIP5K2 Gene diphosphoinositol pentakisphosphate kinase 2
E12626h Human Diphosphoinositol Pentakisphosphate Kinase 2 96T
E12625h Human Diphosphoinositol Pentakisphosphate Kinase 1 96T
PPKB PPIP5K1 Gene diphosphoinositol pentakisphosphate kinase 1
E15053h Rat ELISA Kit FOR Inositol-pentakisphosphate 2-kinase 96T
IQCA1 IPPK Gene inositol 1,3,4,5,6-pentakisphosphate 2-kinase
CSB-EL011783RA Rat Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit 96T
201-20-2827 IPPK{inositol 1,3,4,5,6-pentakisphosphate 2-kinase}rabbit.pAb 0.2ml
CSB-EL011783HU Human Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit 96T
CSB-EL011783MO Mouse Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit 96T
CSB-EL011783RA Rat Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit SpeciesRat 96T
CSB-EL011783HU Human Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit SpeciesHuman 96T
CSB-EL011783MO Mouse Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit SpeciesMouse 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