ID   VIP1_HUMAN              Reviewed;        1433 AA.
AC   Q6PFW1; O15082; Q5HYF8; Q7Z3A7; Q86TE7; Q86UV3; Q86UV4; Q86XW8; Q8IZN0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JUL-2024, entry version 164.
DE   RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1 {ECO:0000305};
DE            EC=2.7.4.24 {ECO:0000269|PubMed:17690096, ECO:0000269|PubMed:17702752, ECO:0000269|PubMed:18981179};
DE   AltName: Full=Diphosphoinositol pentakisphosphate kinase 1;
DE   AltName: Full=Histidine acid phosphatase domain-containing protein 2A;
DE   AltName: Full=IP6 kinase;
DE   AltName: Full=Inositol pyrophosphate synthase 1;
DE   AltName: Full=InsP6 and PP-IP5 kinase 1;
DE   AltName: Full=VIP1 homolog;
DE            Short=hsVIP1;
GN   Name=PPIP5K1 {ECO:0000312|HGNC:HGNC:29023};
GN   Synonyms=HISPPD2A, IP6K, IPS1, KIAA0377, VIP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5).
RC   TISSUE=Bone marrow, Testis, and Trachea;
RX   PubMed=12825070; DOI=10.1038/sj.ejhg.5200991;
RA   Avidan N., Tamary H., Dgany O., Cattan D., Pariente A., Thulliez M.,
RA   Borot N., Moati L., Barthelme A., Shalmon L., Krasnov T., Ben-Asher E.,
RA   Olender T., Khen M., Yaniv I., Zaizov R., Shalev H., Delaunay J.,
RA   Fellous M., Lancet D., Beckmann J.S.;
RT   "CATSPER2, a human autosomal nonsyndromic male infertility gene.";
RL   Eur. J. Hum. Genet. 11:497-502(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC   TISSUE=Brain;
RX   PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA   Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VII. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 4:141-150(1997).
RN   [3]
RP   SEQUENCE REVISION.
RA   Ohara O., Nagase T., Kikuno R., Nomura N.;
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   TISSUE=Endometrial adenocarcinoma;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
RC   TISSUE=Eye, and Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17690096; DOI=10.1074/jbc.m704656200;
RA   Fridy P.C., Otto J.C., Dollins D.E., York J.D.;
RT   "Cloning and characterization of two human VIP1-like inositol
RT   hexakisphosphate and diphosphoinositol pentakisphosphate kinases.";
RL   J. Biol. Chem. 282:30754-30762(2007).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=17702752; DOI=10.1074/jbc.m704655200;
RA   Choi J.H., Williams J., Cho J., Falck J.R., Shears S.B.;
RT   "Purification, sequencing, and molecular identification of a mammalian PP-
RT   InsP5 kinase that is activated when cells are exposed to hyperosmotic
RT   stress.";
RL   J. Biol. Chem. 282:30763-30775(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1152, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18981179; DOI=10.1074/jbc.m805686200;
RA   Lin H., Fridy P.C., Ribeiro A.A., Choi J.H., Barma D.K., Vogel G.,
RA   Falck J.R., Shears S.B., York J.D., Mayr G.W.;
RT   "Structural analysis and detection of biological inositol pyrophosphates
RT   reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases
RT   are 1/3-kinases.";
RL   J. Biol. Chem. 284:1863-1872(2009).
RN   [13]
RP   BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP   POLYPHOSPHOINOSITIDE-BINDING DOMAIN, AND MUTAGENESIS OF ARG-399 AND
RP   ARG-417.
RX   PubMed=21222653; DOI=10.1042/bj20101437;
RA   Gokhale N.A., Zaremba A., Shears S.B.;
RT   "Receptor-dependent compartmentalization of PPIP5K1, a kinase with a
RT   cryptic polyphosphoinositide binding domain.";
RL   Biochem. J. 434:415-426(2011).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-944; SER-987; SER-1037;
RP   SER-1073 AND SER-1152, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-944, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC       IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate
CC       group-containing inositol pyrophosphates diphosphoinositol
CC       pentakisphosphate, PP-InsP5, and bis-diphosphoinositol
CC       tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also
CC       respectively called InsP7 and InsP8, regulate a variety of cellular
CC       processes, including apoptosis, vesicle trafficking, cytoskeletal
CC       dynamics, exocytosis, insulin signaling and neutrophil activation.
CC       Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to
CC       produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce
CC       (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1,
CC       produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Activated when
CC       cells are exposed to hyperosmotic stress. {ECO:0000269|PubMed:17690096,
CC       ECO:0000269|PubMed:17702752}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-
CC         inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946,
CC         ChEBI:CHEBI:456216; EC=2.7.4.24;
CC         Evidence={ECO:0000269|PubMed:17690096, ECO:0000269|PubMed:17702752,
CC         ECO:0000269|PubMed:18981179, ECO:0000269|PubMed:21222653};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460;
CC         Evidence={ECO:0000269|PubMed:18981179, ECO:0000305|PubMed:17690096,
CC         ECO:0000305|PubMed:17702752, ECO:0000305|PubMed:21222653};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
CC         + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate
CC         + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216;
CC         EC=2.7.4.24; Evidence={ECO:0000269|PubMed:17690096,
CC         ECO:0000269|PubMed:17702752, ECO:0000269|PubMed:18981179,
CC         ECO:0000269|PubMed:21222653};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277;
CC         Evidence={ECO:0000269|PubMed:18981179, ECO:0000305|PubMed:17690096,
CC         ECO:0000305|PubMed:17702752, ECO:0000305|PubMed:21222653};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.12 uM for InsP6 {ECO:0000269|PubMed:17690096,
CC         ECO:0000269|PubMed:17702752, ECO:0000269|PubMed:21222653};
CC         KM=0.10 uM for InsP7 {ECO:0000269|PubMed:17690096,
CC         ECO:0000269|PubMed:17702752, ECO:0000269|PubMed:21222653};
CC         Vmax=0.03 nmol/min/mg enzyme with InsP6 as substrate
CC         {ECO:0000269|PubMed:17690096, ECO:0000269|PubMed:17702752,
CC         ECO:0000269|PubMed:21222653};
CC         Vmax=0.13 nmol/min/mg enzyme with InsP7 as substrate
CC         {ECO:0000269|PubMed:17690096, ECO:0000269|PubMed:17702752,
CC         ECO:0000269|PubMed:21222653};
CC         Note=The catalytic efficiency is 80 folds higher for 5-PP-InsP5
CC         (InsP7) compared to InsP6.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17690096,
CC       ECO:0000269|PubMed:17702752, ECO:0000269|PubMed:21222653}. Cell
CC       membrane {ECO:0000269|PubMed:21222653}. Note=Relocalizes to the plasma
CC       membrane upon activation of the PtdIns 3-kinase pathway.
CC       {ECO:0000269|PubMed:21222653}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1;
CC         IsoId=Q6PFW1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PFW1-2; Sequence=VSP_030618, VSP_030622;
CC       Name=3;
CC         IsoId=Q6PFW1-3; Sequence=VSP_030618, VSP_030621;
CC       Name=4;
CC         IsoId=Q6PFW1-4; Sequence=VSP_030615, VSP_030618, VSP_030621;
CC       Name=5;
CC         IsoId=Q6PFW1-5; Sequence=VSP_030616, VSP_030619, VSP_030623;
CC       Name=6;
CC         IsoId=Q6PFW1-6; Sequence=VSP_030617;
CC       Name=7;
CC         IsoId=Q6PFW1-7; Sequence=VSP_030618, VSP_030620, VSP_030624;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with a higher expression in
CC       skeletal muscle, heart and brain. {ECO:0000269|PubMed:17690096}.
CC   -!- DOMAIN: The C-terminal acid phosphatase-like domain binds
CC       PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the phosphatase
CC       domain of histidine acid phosphatases, it has no phosphatase activity.
CC       {ECO:0000269|PubMed:21222653}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA20831.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF502586; AAP30842.1; -; mRNA.
DR   EMBL; AF502587; AAP30843.1; -; mRNA.
DR   EMBL; AF502588; AAP30844.1; -; mRNA.
DR   EMBL; AF502589; AAP30845.1; -; mRNA.
DR   EMBL; AF543190; AAN40768.1; -; mRNA.
DR   EMBL; AB002375; BAA20831.2; ALT_INIT; mRNA.
DR   EMBL; BX538022; CAD97968.1; -; mRNA.
DR   EMBL; BX647814; CAI46011.1; -; mRNA.
DR   EMBL; BC050263; AAH50263.1; -; mRNA.
DR   EMBL; BC057395; AAH57395.1; -; mRNA.
DR   CCDS; CCDS32215.1; -. [Q6PFW1-3]
DR   CCDS; CCDS45252.1; -. [Q6PFW1-1]
DR   CCDS; CCDS53937.1; -. [Q6PFW1-7]
DR   RefSeq; NP_001124330.1; NM_001130858.2. [Q6PFW1-1]
DR   RefSeq; NP_001124331.1; NM_001130859.2. [Q6PFW1-3]
DR   RefSeq; NP_001177143.1; NM_001190214.1. [Q6PFW1-7]
DR   RefSeq; NP_055474.3; NM_014659.5. [Q6PFW1-3]
DR   RefSeq; XP_005254861.1; XM_005254804.1. [Q6PFW1-3]
DR   RefSeq; XP_016878237.1; XM_017022748.1.
DR   RefSeq; XP_016878238.1; XM_017022749.1.
DR   RefSeq; XP_016878239.1; XM_017022750.1.
DR   RefSeq; XP_016878240.1; XM_017022751.1.
DR   RefSeq; XP_016878248.1; XM_017022759.1.
DR   AlphaFoldDB; Q6PFW1; -.
DR   SMR; Q6PFW1; -.
DR   BioGRID; 115031; 69.
DR   IntAct; Q6PFW1; 1.
DR   STRING; 9606.ENSP00000400887; -.
DR   ChEMBL; CHEMBL5046; -.
DR   DEPOD; PPIP5K1; -.
DR   GlyGen; Q6PFW1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6PFW1; -.
DR   PhosphoSitePlus; Q6PFW1; -.
DR   BioMuta; PPIP5K1; -.
DR   DMDM; 74758334; -.
DR   jPOST; Q6PFW1; -.
DR   MassIVE; Q6PFW1; -.
DR   PaxDb; 9606-ENSP00000400887; -.
DR   PeptideAtlas; Q6PFW1; -.
DR   ProteomicsDB; 67105; -. [Q6PFW1-1]
DR   ProteomicsDB; 67106; -. [Q6PFW1-2]
DR   ProteomicsDB; 67107; -. [Q6PFW1-3]
DR   ProteomicsDB; 67108; -. [Q6PFW1-4]
DR   ProteomicsDB; 67109; -. [Q6PFW1-5]
DR   ProteomicsDB; 67110; -. [Q6PFW1-6]
DR   ProteomicsDB; 67111; -. [Q6PFW1-7]
DR   Pumba; Q6PFW1; -.
DR   Antibodypedia; 35179; 58 antibodies from 15 providers.
DR   DNASU; 9677; -.
DR   Ensembl; ENST00000334933.8; ENSP00000334779.4; ENSG00000168781.24. [Q6PFW1-3]
DR   Ensembl; ENST00000360135.8; ENSP00000353253.4; ENSG00000168781.24. [Q6PFW1-7]
DR   Ensembl; ENST00000360301.8; ENSP00000353446.4; ENSG00000168781.24. [Q6PFW1-3]
DR   Ensembl; ENST00000396923.7; ENSP00000380129.2; ENSG00000168781.24. [Q6PFW1-1]
DR   GeneID; 9677; -.
DR   KEGG; hsa:9677; -.
DR   UCSC; uc001zrw.3; human. [Q6PFW1-1]
DR   AGR; HGNC:29023; -.
DR   CTD; 9677; -.
DR   DisGeNET; 9677; -.
DR   GeneCards; PPIP5K1; -.
DR   HGNC; HGNC:29023; PPIP5K1.
DR   HPA; ENSG00000168781; Tissue enhanced (brain).
DR   MIM; 610979; gene.
DR   neXtProt; NX_Q6PFW1; -.
DR   OpenTargets; ENSG00000168781; -.
DR   PharmGKB; PA165479401; -.
DR   VEuPathDB; HostDB:ENSG00000168781; -.
DR   eggNOG; KOG1057; Eukaryota.
DR   GeneTree; ENSGT00390000009048; -.
DR   HOGENOM; CLU_000914_0_0_1; -.
DR   InParanoid; Q6PFW1; -.
DR   OMA; AWPRCDA; -.
DR   OrthoDB; 5476261at2759; -.
DR   PhylomeDB; Q6PFW1; -.
DR   TreeFam; TF313594; -.
DR   BioCyc; MetaCyc:HS09822-MONOMER; -.
DR   BRENDA; 2.7.4.21; 2681.
DR   BRENDA; 2.7.4.24; 2681.
DR   BRENDA; 3.6.1.B18; 2681.
DR   PathwayCommons; Q6PFW1; -.
DR   Reactome; R-HSA-1855167; Synthesis of pyrophosphates in the cytosol.
DR   SABIO-RK; Q6PFW1; -.
DR   SignaLink; Q6PFW1; -.
DR   BioGRID-ORCS; 9677; 9 hits in 1151 CRISPR screens.
DR   ChiTaRS; PPIP5K1; human.
DR   GenomeRNAi; 9677; -.
DR   Pharos; Q6PFW1; Tbio.
DR   PRO; PR:Q6PFW1; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q6PFW1; Protein.
DR   Bgee; ENSG00000168781; Expressed in right hemisphere of cerebellum and 190 other cell types or tissues.
DR   ExpressionAtlas; Q6PFW1; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IDA:UniProtKB.
DR   GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IBA:GO_Central.
DR   GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IDA:UniProtKB.
DR   GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IDA:MGI.
DR   GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IDA:UniProtKB.
DR   GO; GO:0006020; P:inositol metabolic process; IDA:UniProtKB.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.11950; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR037446; His_Pase_VIP1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR040557; VIP1_N.
DR   PANTHER; PTHR12750; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1.
DR   PANTHER; PTHR12750:SF11; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE 1; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   Pfam; PF18086; PPIP5K2_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; Kinase;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..1433
FT                   /note="Inositol hexakisphosphate and diphosphoinositol-
FT                   pentakisphosphate kinase 1"
FT                   /id="PRO_0000315688"
FT   REGION          382..453
FT                   /note="Polyphosphoinositide-binding domain"
FT                   /evidence="ECO:0000269|PubMed:21222653"
FT   REGION          915..1020
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1134..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1235..1257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..948
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        988..1020
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         64..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         224..225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         248..251
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         257..259
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         275
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         332..334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         337..340
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   MOD_RES         944
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         987
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1037
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1073
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1145
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A2ARP1"
FT   MOD_RES         1152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         653
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_030615"
FT   VAR_SEQ         810..821
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:12825070"
FT                   /id="VSP_030616"
FT   VAR_SEQ         818..1433
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_030617"
FT   VAR_SEQ         818..821
FT                   /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT                   isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:12825070,
FT                   ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:9205841"
FT                   /id="VSP_030618"
FT   VAR_SEQ         865..957
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:12825070"
FT                   /id="VSP_030619"
FT   VAR_SEQ         1020..1082
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:9205841"
FT                   /id="VSP_030620"
FT   VAR_SEQ         1062..1082
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12825070,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_030621"
FT   VAR_SEQ         1082
FT                   /note="N -> NG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12825070"
FT                   /id="VSP_030622"
FT   VAR_SEQ         1107..1240
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:12825070"
FT                   /id="VSP_030623"
FT   VAR_SEQ         1167
FT                   /note="Y -> LETRFCHVGQAGLELLTSSDLPASASQSAGITGVSHRTQPD (in
FT                   isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:9205841"
FT                   /id="VSP_030624"
FT   MUTAGEN         399
FT                   /note="R->A: Decreases 8-fold the affinity for
FT                   PtdIns(3,4,5)P3."
FT                   /evidence="ECO:0000269|PubMed:21222653"
FT   MUTAGEN         417
FT                   /note="R->A: Decreases 16-fold the affinity for
FT                   PtdIns(3,4,5)P3."
FT                   /evidence="ECO:0000269|PubMed:21222653"
FT   CONFLICT        44
FT                   /note="D -> G (in Ref. 4; CAD97968)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        304
FT                   /note="V -> M (in Ref. 4; CAD97968)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        374
FT                   /note="E -> V (in Ref. 4; CAD97968)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        423
FT                   /note="E -> Q (in Ref. 1; AAP30843/AAP30845/AAN40768)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        473
FT                   /note="L -> P (in Ref. 4; CAD97968)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        483
FT                   /note="F -> S (in Ref. 1; AAP30845/AAN40768)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        490
FT                   /note="V -> E (in Ref. 4; CAD97968)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        548
FT                   /note="G -> V (in Ref. 4; CAD97968)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        738
FT                   /note="I -> L (in Ref. 1; AAP30845/AAN40768)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        788
FT                   /note="V -> A (in Ref. 1; AAP30845/AAN40768)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        936
FT                   /note="E -> G (in Ref. 4; CAI46011)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        985
FT                   /note="A -> V (in Ref. 1; AAP30845/AAN40768)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1020
FT                   /note="G -> A (in Ref. 1; AAP30843)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1041
FT                   /note="L -> P (in Ref. 1; AAP30845/AAN40768)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1066
FT                   /note="V -> L (in Ref. 1; AAP30842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1126
FT                   /note="A -> T (in Ref. 4; CAI46011)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1134
FT                   /note="M -> V (in Ref. 4; CAI46011)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1198
FT                   /note="P -> R (in Ref. 4; CAI46011)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1293
FT                   /note="H -> M (in Ref. 1; AAP30845/AAN40768)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1294
FT                   /note="D -> T (in Ref. 1; AAP30845/AAN40768)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1433 AA;  159521 MW;  BA0DEFB2A71B1467 CRC64;
     MWSLTASEGE STTAHFFLGA GDEGLGTRGI GMRPEESDSE LLEDEEDEVP PEPQIIVGIC
     AMTKKSKSKP MTQILERLCR FDYLTVVILG EDVILNEPVE NWPSCHCLIS FHSKGFPLDK
     AVAYSKLRNP FLINDLAMQY YIQDRREVYR ILQEEGIDLP RYAVLNRDPA RPEECNLIEG
     EDQVEVNGAV FPKPFVEKPV SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESSVR
     KTGSYIYEEF MPTDGTDVKV YTVGPDYAHA EARKSPALDG KVERDSEGKE IRYPVMLTAM
     EKLVARKVCV AFKQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA KILGNTIMRE
     LAPQFQIPWS IPTEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK MEVKHPRFFA
     LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL LLAELEKEPG GEIEEKTGKL EQLKSVLEMY
     GHFSGINRKV QLTYYPHGVK ASNEGQDPQR ETLAPSLLLV LKWGGELTPA GRVQAEELGR
     AFRCMYPGGQ GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL
     TPILVQMVKS ANMNGLLDSD GDSLSSCQHR VKARLHHILQ QDAPFGPEDY DQLAPTRSTS
     LLNSMTIIQN PVKVCDQVFA LIENLTHQIR ERMQDPRSVD LQLYHSETLE LMLQRWSKLE
     RDFRQKSGRY DISKIPDIYD CVKYDVQHNG SLGLQGTAEL LRLSKALADV VIPQEYGISR
     EEKLEIAVGF CLPLLRKILL DLQRTHEDES VNKLHPLCYL RYSRGVLSPG RHVRTRLYFT
     SESHVHSLLS VFRYGGLLDE TQDAQWQRAL DYLSAISELN YMTQIVIMLY EDNTQDPLSE
     ERFHVELHFS PGVKGVEEEG SAPAGCGFRP ASSENEEMKT NQGSMENLCP GKASDEPDRA
     LQTSPQPPEG PGLPRRSPLI RNRKAGSMEV LSETSSSRPG GYRLFSSSRP PTEMKQSGLG
     SQCTGLFSTT VLGGSSSAPN LQDYARSHGK KLPPASLKHR DELLFVPAVK RFSVSFAKHP
     TNGFEGCSMV PTIYPLETLH NALSLRQVSE FLSRVCQRHT DAQAQASAAL FDSMHSSQAS
     DNPFSPPRTL HSPPLQLQQR SEKPPWYSSG PSSTVSSAGP SSPTTVDGNS QFGFSDQPSL
     NSHVAEEHQG LGLLQETPGS GAQELSIEGE QELFEPNQSP QVPPMETSQP YEEVSQPCQE
     VPDISQPCQD ISEALSQPCQ KVPDISQQCQ ENHDNGNHTC QEVPHISQPC QKSSQLCQKV
     SEEVCQLCLE NSEEVSQPCQ GVSVEVGKLV HKFHVGVGSL VQETLVEVGS PAEEIPEEVI
     QPYQEFSVEV GRLAQETSAI NLLSQGIPEI DKPSQEFPEE IDLQAQEVPE EIN
//