IP6K2_MOUSE
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 03-AUG-2022, entry version 135.
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; Q80V72; -.
DR PeptideAtlas; Q80V72; -.
DR PRIDE; Q80V72; -.
DR ProteomicsDB; 266998; -.
DR Antibodypedia; 1556; 217 antibodies from 31 providers.
DR DNASU; 76500; -.
DR Ensembl; ENSMUST00000085018; ENSMUSP00000082091; ENSMUSG00000032599.
DR GeneID; 76500; -.
DR KEGG; mmu:76500; -.
DR UCSC; uc009rqw.1; mouse.
DR CTD; 51447; -.
DR MGI; MGI:1923750; Ip6k2.
DR VEuPathDB; HostDB:ENSMUSG00000032599; -.
DR eggNOG; KOG1620; Eukaryota.
DR GeneTree; ENSGT00940000156310; -.
DR InParanoid; Q80V72; -.
DR OMA; CEPKSKV; -.
DR OrthoDB; 902814at2759; -.
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 75 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 101 other tissues.
DR ExpressionAtlas; Q80V72; baseline and differential.
DR Genevisible; Q80V72; MM.
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; ISO:MGI.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:1905396; P:cellular response to flavonoid; ISS:UniProtKB.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
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 Gene3D; 3.30.470.160; -; 1.
DR InterPro; IPR005522; IPK.
DR InterPro; IPR038286; IPK_sf.
DR PANTHER; PTHR12400; PTHR12400; 1.
DR Pfam; PF03770; IPK; 1.
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
