VIP1_HUMAN
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 03-AUG-2022, entry version 153.
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-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. [Q6PFW1-3]
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. [Q6PFW1-6]
DR AlphaFoldDB; Q6PFW1; -.
DR SMR; Q6PFW1; -.
DR BioGRID; 115031; 65.
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 EPD; Q6PFW1; -.
DR jPOST; Q6PFW1; -.
DR MassIVE; Q6PFW1; -.
DR MaxQB; Q6PFW1; -.
DR PaxDb; Q6PFW1; -.
DR PeptideAtlas; Q6PFW1; -.
DR PRIDE; 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 Antibodypedia; 35179; 52 antibodies from 14 providers.
DR DNASU; 9677; -.
DR Ensembl; ENST00000334933.8; ENSP00000334779.4; ENSG00000168781.23. [Q6PFW1-3]
DR Ensembl; ENST00000360135.8; ENSP00000353253.4; ENSG00000168781.23. [Q6PFW1-7]
DR Ensembl; ENST00000360301.8; ENSP00000353446.4; ENSG00000168781.23. [Q6PFW1-3]
DR Ensembl; ENST00000396923.7; ENSP00000380129.2; ENSG00000168781.23. [Q6PFW1-1]
DR GeneID; 9677; -.
DR KEGG; hsa:9677; -.
DR UCSC; uc001zrw.3; human. [Q6PFW1-1]
DR CTD; 9677; -.
DR DisGeNET; 9677; -.
DR GeneCards; PPIP5K1; -.
DR HGNC; HGNC:29023; PPIP5K1.
DR HPA; ENSG00000168781; Low tissue specificity.
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; IQERWCC; -.
DR OrthoDB; 93740at2759; -.
DR PhylomeDB; Q6PFW1; -.
DR TreeFam; TF313594; -.
DR BioCyc; MetaCyc:HS09822-MON; -.
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 1072 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 188 other tissues.
DR ExpressionAtlas; Q6PFW1; baseline and differential.
DR Genevisible; Q6PFW1; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0102092; F:5-diphosphoinositol pentakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 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; PTHR12750; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF18086; PPIP5K2_N; 1.
DR SUPFAM; SSF53254; SSF53254; 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
