ID   IP6K2_MOUSE             Reviewed;         448 AA.
AC   Q80V72; E9QMT6;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 143.
DE   RecName: Full=Inositol hexakisphosphate kinase 2;
DE            Short=InsP6 kinase 2;
DE            EC=2.7.4.- {ECO:0000250|UniProtKB:Q9UHH9};
DE   AltName: Full=P(i)-uptake stimulator;
DE            Short=PiUS;
GN   Name=Ip6k2; Synonyms=Ihpk2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=10574768; DOI=10.1016/s0960-9822(00)80055-x;
RA   Saiardi A., Erdjument-Bromage H., Snowman A.M., Tempst P., Snyder S.H.;
RT   "Synthesis of diphosphoinositol pentakisphosphate by a newly identified
RT   family of higher inositol polyphosphate kinases.";
RL   Curr. Biol. 9:1323-1326(1999).
CC   -!- FUNCTION: Converts inositol hexakisphosphate (InsP6) to
CC       diphosphoinositol pentakisphosphate (InsP7/PP-InsP5) (By similarity).
CC       May play a role in the regulation of Na(+)-dependent phosphate
CC       cotransport, possibly via its role in diphosphoinositol
CC       pentakisphosphate (InsP7/PP-InsP5) biosynthesis (By similarity).
CC       {ECO:0000250|UniProtKB:Q95221, ECO:0000250|UniProtKB:Q9UHH9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-
CC         inositol 1,2,3,4,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:12793,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:58628,
CC         ChEBI:CHEBI:456216;
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism.
CC       {ECO:0000250|UniProtKB:Q9UHH9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UHH9}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and lung, and at slightly
CC       lower levels in liver, kidney and testis.
CC       {ECO:0000269|PubMed:10574768}.
CC   -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC       {ECO:0000305}.
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DR   EMBL; AC168054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC173341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC039922; AAH39922.1; -; mRNA.
DR   CCDS; CCDS23537.1; -.
DR   RefSeq; NP_083910.2; NM_029634.2.
DR   RefSeq; XP_006511913.1; XM_006511850.2.
DR   RefSeq; XP_006511914.1; XM_006511851.3.
DR   AlphaFoldDB; Q80V72; -.
DR   SMR; Q80V72; -.
DR   BioGRID; 218156; 2.
DR   STRING; 10090.ENSMUSP00000082091; -.
DR   ChEMBL; CHEMBL4523367; -.
DR   iPTMnet; Q80V72; -.
DR   PhosphoSitePlus; Q80V72; -.
DR   PaxDb; 10090-ENSMUSP00000082091; -.
DR   PeptideAtlas; Q80V72; -.
DR   ProteomicsDB; 266998; -.
DR   Antibodypedia; 1556; 252 antibodies from 31 providers.
DR   DNASU; 76500; -.
DR   Ensembl; ENSMUST00000085018.6; ENSMUSP00000082091.5; ENSMUSG00000032599.13.
DR   GeneID; 76500; -.
DR   KEGG; mmu:76500; -.
DR   UCSC; uc009rqw.1; mouse.
DR   AGR; MGI:1923750; -.
DR   CTD; 51447; -.
DR   MGI; MGI:1923750; Ip6k2.
DR   VEuPathDB; HostDB:ENSMUSG00000032599; -.
DR   eggNOG; KOG1620; Eukaryota.
DR   GeneTree; ENSGT00940000156310; -.
DR   InParanoid; Q80V72; -.
DR   OMA; SDCEPKN; -.
DR   OrthoDB; 20436at2759; -.
DR   PhylomeDB; Q80V72; -.
DR   TreeFam; TF314066; -.
DR   BRENDA; 2.7.4.21; 3474.
DR   Reactome; R-MMU-1855191; Synthesis of IPs in the nucleus.
DR   UniPathway; UPA00949; -.
DR   BioGRID-ORCS; 76500; 0 hits in 80 CRISPR screens.
DR   ChiTaRS; Ip6k2; mouse.
DR   PRO; PR:Q80V72; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q80V72; Protein.
DR   Bgee; ENSMUSG00000032599; Expressed in layer of retina and 104 other cell types or tissues.
DR   ExpressionAtlas; Q80V72; baseline and differential.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0097243; F:flavonoid binding; ISS:UniProtKB.
DR   GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; ISS:UniProtKB.
DR   GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IMP:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:1905396; P:cellular response to flavonoid; ISS:UniProtKB.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; IMP:MGI.
DR   GO; GO:0043647; P:inositol phosphate metabolic process; ISS:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR   GO; GO:0006817; P:phosphate ion transport; ISO:MGI.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISO:MGI.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:MGI.
DR   GO; GO:0050821; P:protein stabilization; IMP:MGI.
DR   Gene3D; 3.30.470.160; Inositol polyphosphate kinase; 1.
DR   InterPro; IPR005522; IPK.
DR   InterPro; IPR038286; IPK_sf.
DR   PANTHER; PTHR12400:SF47; INOSITOL HEXAKISPHOSPHATE KINASE 2; 1.
DR   PANTHER; PTHR12400; INOSITOL POLYPHOSPHATE KINASE; 1.
DR   Pfam; PF03770; IPK; 1.
DR   SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR   Genevisible; Q80V72; MM.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Lipid metabolism; Nucleotide-binding; Nucleus;
KW   Phospholipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..448
FT                   /note="Inositol hexakisphosphate kinase 2"
FT                   /id="PRO_0000066878"
FT   BINDING         229..231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT   BINDING         238..246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT   BINDING         244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT   BINDING         258..265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT   BINDING         405
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT   BINDING         408
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT   CONFLICT        292
FT                   /note="M -> I (in Ref. 2; AAH39922)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   448 AA;  51644 MW;  A1B483785C5DAE25 CRC64;
     MSPAFRTMDV EPRTKGILLE PFVHQVGGHS CVLRFNETTL CKPLVPREHQ FYETLPAEMR
     RFTPQYKAVL IFVRCADEFG ASGNIETKEQ GVVSVRFEED EDRNLCLIAY PLKGDHGTVD
     IVDNSDCEPK SKLLRWTNKK HHALETEKNP KDWVRQHRKE EKMKSHKLEE EFEWLKKSEV
     LYYSVEKKGN VSSQLKHYNP WSMKCHQQQL QRMKENAKHR NQYKFILLEN LTSRYEVPCV
     LDLKMGTRQH GDDASEEKAA NQIRKCQQST SAVIGVRVCG MQVYQAGTGQ LMFMNKYHGR
     KLSVQGFKEA LFQFFHNGRY LRRELLGPVL KKLTELKAVL ERQESYRFYS SSLLVIYDGK
     EWPEVTLDSD AEDLEDLSEE SADESAGAYA YKPIGASSVD VRMIDFAHTT CRLYGEDSVV
     HEGQDAGYIF GLQSLIDIVT EISEESGE
//