PI51B_HUMAN
ID PI51B_HUMAN Reviewed; 540 AA.
AC O14986; A8K9L9; B4DIG7; P78518; P78519; Q5T5K6; Q5T5K8; Q5T5K9; Q5VZ00;
AC Q7KYT5; Q8NHQ5; Q92749;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase type-1 beta {ECO:0000305|PubMed:8955136};
DE Short=PIP5K1-beta {ECO:0000303|PubMed:8955136};
DE Short=PtdIns(4)P-5-kinase 1 beta {ECO:0000305|PubMed:8955136};
DE EC=2.7.1.68 {ECO:0000250|UniProtKB:P70181};
DE AltName: Full=Phosphatidylinositol 4-phosphate 5-kinase type I beta {ECO:0000305|PubMed:8955136};
DE Short=PIP5KIbeta {ECO:0000303|PubMed:8955136};
DE AltName: Full=Protein STM-7 {ECO:0000303|PubMed:8841185};
DE AltName: Full=Type I phosphatidylinositol 4-phosphate 5-kinase beta {ECO:0000305|PubMed:8955136};
GN Name=PIP5K1B {ECO:0000312|HGNC:HGNC:8995};
GN Synonyms=STM7 {ECO:0000303|PubMed:8841185};
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8841185; DOI=10.1038/ng1096-157;
RA Carvajal J.J., Pook M.A., dos Santos M., Doudney K., Hillermann R.,
RA Minogue S., Williamson R., Hsuan J.J., Chamberlain S.;
RT "The Friedreich's ataxia gene encodes a novel phosphatidylinositol-4-
RT phosphate 5-kinase.";
RL Nat. Genet. 14:157-162(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-415, AND ALTERNATIVE
RP SPLICING.
RX PubMed=9177790; DOI=10.1006/geno.1997.4726;
RA Pook M.A., Carvajal J.J., Doudney K., Hillermann R., Chamberlain S.;
RT "Exon-intron structure of a 2.7-kb transcript of the STM7 gene with
RT phosphatidylinositol-4-phosphate 5-kinase activity.";
RL Genomics 42:170-172(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 340-540 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=8955136; DOI=10.1074/jbc.271.51.32937;
RA Loijens J.C., Anderson R.A.;
RT "Type I phosphatidylinositol-4-phosphate 5-kinases are distinct members of
RT this novel lipid kinase family.";
RL J. Biol. Chem. 271:32937-32943(1996).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-
CC phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-
CC bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that
CC regulates several cellular processes such as signal transduction,
CC vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and
CC cell motility (By similarity). PtdIns(4,5)P2 can directly act as a
CC second messenger or can be utilized as a precursor to generate other
CC second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol
CC (DAG) or phosphatidylinositol-3,4,5-trisphosphate
CC (PtdIns(3,4,5)P3/PIP3) (By similarity). Mediates RAC1-dependent
CC reorganization of actin filaments. Contributes to the activation of
CC phospholipase PLD2. Together with PIP5K1A, is required, after
CC stimulation by G-protein coupled receptors, for the synthesis of IP3
CC that will induce stable platelet adhesion (By similarity).
CC {ECO:0000250|UniProtKB:P70181, ECO:0000250|UniProtKB:Q99755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14426;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-
CC 3-phospho-1D-myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol
CC 4,5-bisphosphate + ADP + H(+); Xref=Rhea:RHEA:40363,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77136,
CC ChEBI:CHEBI:77137, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40364;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-
CC myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-
CC sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40367, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:77139, ChEBI:CHEBI:77140, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40368;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-
CC myo-inositol + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phospho-1D-myo-inositol 5-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40379, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:77163, ChEBI:CHEBI:77164, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40380;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phospho-1D-myo-inositol + ATP = 1-octadecanoyl-2-(9Z,12Z)-
CC octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate +
CC ADP + H(+); Xref=Rhea:RHEA:40383, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77158, ChEBI:CHEBI:77159,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P70181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40384;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phospho-(1D-myo-inositol) + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate +
CC ADP + H(+); Xref=Rhea:RHEA:40375, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77160, ChEBI:CHEBI:133606,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P70181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40376;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-
CC inositol + ATP = 1,2-di(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-
CC 1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40387,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77165,
CC ChEBI:CHEBI:77167, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40388;
CC Evidence={ECO:0000250|UniProtKB:P70181};
CC -!- SUBUNIT: Interacts with RAC1, AJUBA, PLD1, PLD2 and ARF1.
CC {ECO:0000250|UniProtKB:P70181}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P70181}. Cell membrane
CC {ECO:0000250|UniProtKB:P70181}. Endomembrane system. Note=Associated
CC with membranes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O14986-1; Sequence=Displayed;
CC Name=2; Synonyms=Isoform 1;
CC IsoId=O14986-2; Sequence=VSP_016010, VSP_016011;
CC Name=3;
CC IsoId=O14986-3; Sequence=VSP_054771;
CC -!- TISSUE SPECIFICITY: Detected in heart, pancreas, brain, kidney,
CC skeletal muscle and lung. {ECO:0000269|PubMed:8955136}.
CC -!- CAUTION: There is confusion in the literature with phosphatidylinositol
CC 4-phosphate 5-kinase type I nomenclature due to the fact that
CC frequently mouse PIP5K1B is named Phosphatidylinositol 4-phosphate 5-
CC kinase type I alpha. {ECO:0000305}.
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DR EMBL; X92493; CAA63224.1; -; mRNA.
DR EMBL; U52387; AAC51327.1; -; Genomic_DNA.
DR EMBL; U52376; AAC51327.1; JOINED; Genomic_DNA.
DR EMBL; U52377; AAC51327.1; JOINED; Genomic_DNA.
DR EMBL; U52378; AAC51327.1; JOINED; Genomic_DNA.
DR EMBL; U52379; AAC51327.1; JOINED; Genomic_DNA.
DR EMBL; U52380; AAC51327.1; JOINED; Genomic_DNA.
DR EMBL; U52381; AAC51327.1; JOINED; Genomic_DNA.
DR EMBL; U52382; AAC51327.1; JOINED; Genomic_DNA.
DR EMBL; U52383; AAC51327.1; JOINED; Genomic_DNA.
DR EMBL; U52384; AAC51327.1; JOINED; Genomic_DNA.
DR EMBL; U52385; AAC51327.1; JOINED; Genomic_DNA.
DR EMBL; U52386; AAC51327.1; JOINED; Genomic_DNA.
DR EMBL; AK292734; BAF85423.1; -; mRNA.
DR EMBL; AK295587; BAG58479.1; -; mRNA.
DR EMBL; AL162730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62465.1; -; Genomic_DNA.
DR EMBL; BC030587; AAH30587.1; -; mRNA.
DR EMBL; U78580; AAC50915.1; -; mRNA.
DR CCDS; CCDS65063.1; -. [O14986-3]
DR CCDS; CCDS6624.1; -. [O14986-1]
DR RefSeq; NP_001265182.1; NM_001278253.1. [O14986-3]
DR RefSeq; NP_003549.1; NM_003558.3. [O14986-1]
DR RefSeq; XP_005252318.1; XM_005252261.3.
DR RefSeq; XP_005252319.1; XM_005252262.4. [O14986-1]
DR RefSeq; XP_006717363.1; XM_006717300.2.
DR RefSeq; XP_006717364.1; XM_006717301.1.
DR RefSeq; XP_011517384.1; XM_011519082.2. [O14986-1]
DR RefSeq; XP_011517385.1; XM_011519083.2. [O14986-1]
DR RefSeq; XP_011517386.1; XM_011519084.2. [O14986-1]
DR RefSeq; XP_016870677.1; XM_017015188.1. [O14986-1]
DR RefSeq; XP_016870678.1; XM_017015189.1. [O14986-1]
DR RefSeq; XP_016870679.1; XM_017015190.1.
DR RefSeq; XP_016870680.1; XM_017015191.1.
DR AlphaFoldDB; O14986; -.
DR SMR; O14986; -.
DR BioGRID; 113984; 10.
DR CORUM; O14986; -.
DR STRING; 9606.ENSP00000265382; -.
DR ChEMBL; CHEMBL4802064; -.
DR iPTMnet; O14986; -.
DR PhosphoSitePlus; O14986; -.
DR SwissPalm; O14986; -.
DR BioMuta; PIP5K1B; -.
DR EPD; O14986; -.
DR jPOST; O14986; -.
DR MassIVE; O14986; -.
DR MaxQB; O14986; -.
DR PaxDb; O14986; -.
DR PeptideAtlas; O14986; -.
DR PRIDE; O14986; -.
DR ProteomicsDB; 4304; -.
DR ProteomicsDB; 48360; -. [O14986-1]
DR ProteomicsDB; 48361; -. [O14986-2]
DR Antibodypedia; 2767; 157 antibodies from 28 providers.
DR DNASU; 8395; -.
DR Ensembl; ENST00000265382.8; ENSP00000265382.2; ENSG00000107242.20. [O14986-1]
DR Ensembl; ENST00000478500.3; ENSP00000435778.1; ENSG00000107242.20. [O14986-2]
DR Ensembl; ENST00000541509.5; ENSP00000438082.1; ENSG00000107242.20. [O14986-3]
DR GeneID; 8395; -.
DR KEGG; hsa:8395; -.
DR MANE-Select; ENST00000265382.8; ENSP00000265382.2; NM_003558.4; NP_003549.1.
DR UCSC; uc004agu.5; human. [O14986-1]
DR CTD; 8395; -.
DR DisGeNET; 8395; -.
DR GeneCards; PIP5K1B; -.
DR HGNC; HGNC:8995; PIP5K1B.
DR HPA; ENSG00000107242; Tissue enhanced (choroid).
DR MIM; 602745; gene.
DR neXtProt; NX_O14986; -.
DR OpenTargets; ENSG00000107242; -.
DR PharmGKB; PA33328; -.
DR VEuPathDB; HostDB:ENSG00000107242; -.
DR eggNOG; KOG0229; Eukaryota.
DR GeneTree; ENSGT00940000156639; -.
DR HOGENOM; CLU_004312_5_1_1; -.
DR InParanoid; O14986; -.
DR OMA; NSNMKER; -.
DR OrthoDB; 1562683at2759; -.
DR PhylomeDB; O14986; -.
DR TreeFam; TF319618; -.
DR BioCyc; MetaCyc:HS02982-MON; -.
DR BRENDA; 2.7.1.68; 2681.
DR PathwayCommons; O14986; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-HSA-201688; WNT mediated activation of DVL.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR SABIO-RK; O14986; -.
DR SignaLink; O14986; -.
DR SIGNOR; O14986; -.
DR BioGRID-ORCS; 8395; 9 hits in 1075 CRISPR screens.
DR ChiTaRS; PIP5K1B; human.
DR GeneWiki; PIP5K1B; -.
DR GenomeRNAi; 8395; -.
DR Pharos; O14986; Tbio.
DR PRO; PR:O14986; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O14986; protein.
DR Bgee; ENSG00000107242; Expressed in choroid plexus epithelium and 166 other tissues.
DR ExpressionAtlas; O14986; baseline and differential.
DR Genevisible; O14986; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001931; C:uropod; IDA:UniProtKB.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; TAS:Reactome.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; ISS:UniProtKB.
DR GO; GO:0052810; F:1-phosphatidylinositol-5-kinase activity; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052812; F:phosphatidylinositol-3,4-bisphosphate 5-kinase activity; TAS:Reactome.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
DR Gene3D; 3.30.800.10; -; 1.
DR InterPro; IPR023610; PInositol-4-P-5-kinase.
DR InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR PANTHER; PTHR23086; PTHR23086; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00330; PIPKc; 1.
DR PROSITE; PS51455; PIPK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; Kinase;
KW Lipid metabolism; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..540
FT /note="Phosphatidylinositol 4-phosphate 5-kinase type-1
FT beta"
FT /id="PRO_0000185458"
FT DOMAIN 25..395
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70181"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70181"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70181"
FT VAR_SEQ 24
FT /note="T -> TQVKNQILSRLPKIPCTFIQAWTNTEMITLLACYYFRSVST (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016010"
FT VAR_SEQ 501..540
FT /note="SKGLPSSSTFTLEEGTIYLTAEPNTLEVQDDNASVLDVYL -> RFKMATSE
FT H (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016011"
FT VAR_SEQ 503..540
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054771"
FT VARIANT 415
FT /note="A -> T (in dbSNP:rs55897616)"
FT /evidence="ECO:0000269|PubMed:9177790"
FT /id="VAR_023712"
FT CONFLICT 346
FT /note="M -> T (in Ref. 6; AAH30587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 61036 MW; 7A683794A39A20B6 CRC64;
MSSAAENGEA APGKQNEEKT YKKTASSAIK GAIQLGIGYT VGNLTSKPER DVLMQDFYVV
ESVFLPSEGS NLTPAHHYPD FRFKTYAPLA FRYFRELFGI KPDDYLYSIC SEPLIELSNP
GASGSLFFVT SDDEFIIKTV QHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCMQSGG
INIRIVVMNN VLPRSMRMHF TYDLKGSTYK RRASRKEREK SNPTFKDLDF LQDMHEGLYF
DTETYNALMK TLQRDCRVLE SFKIMDYSLL LGIHFLDHSL KEKEEETPQN VPDAKRTGMQ
KVLYSTAMES IQGPGKSGDG IITENPDTMG GIPAKSHRGE KLLLFMGIID ILQSYRLMKK
LEHSWKALVY DGDTVSVHRP SFYADRFLKF MNSRVFKKIQ ALKASPSKKR CNSIAALKAT
SQEIVSSISQ EWKDEKRDLL TEGQSFSSLD EEALGSRHRP DLVPSTPSLF EAASLATTIS
SSSLYVNEHY PHDRPTLYSN SKGLPSSSTF TLEEGTIYLT AEPNTLEVQD DNASVLDVYL
