PI5L1_HUMAN
ID PI5L1_HUMAN Reviewed; 394 AA.
AC Q5T9C9; Q8IVS3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase-like protein 1;
DE Short=PI(4)P 5-kinase-like protein 1;
DE Short=PtdIns(4)P-5-kinase-like protein 1;
DE EC=2.7.1.68;
GN Name=PIP5KL1;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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).
CC -!- FUNCTION: May act as a scaffold to localize and regulate type I PI(4)P
CC 5-kinases to specific compartments within the cell, where they generate
CC PI(4,5)P2 for actin nucleation, signaling and scaffold protein
CC recruitment and conversion to PI(3,4,5)P3. {ECO:0000250}.
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 -!- SUBUNIT: Heterodimerizes with other type I phosphatidylinositol 4-
CC phosphate 5-kinase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=Localized to large
CC cytoplasmic vesicular structures. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5T9C9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T9C9-2; Sequence=VSP_024904;
CC -!- CAUTION: It is unsure if the enzyme has intrinsic kinase activity.
CC {ECO:0000305}.
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DR EMBL; AL157935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042184; AAH42184.1; -; mRNA.
DR CCDS; CCDS48030.1; -. [Q5T9C9-1]
DR CCDS; CCDS6885.1; -. [Q5T9C9-2]
DR RefSeq; NP_001128691.1; NM_001135219.1. [Q5T9C9-1]
DR RefSeq; NP_775763.1; NM_173492.1. [Q5T9C9-2]
DR AlphaFoldDB; Q5T9C9; -.
DR SMR; Q5T9C9; -.
DR BioGRID; 126513; 5.
DR IntAct; Q5T9C9; 1.
DR STRING; 9606.ENSP00000373399; -.
DR iPTMnet; Q5T9C9; -.
DR PhosphoSitePlus; Q5T9C9; -.
DR BioMuta; PIP5KL1; -.
DR DMDM; 146325056; -.
DR MassIVE; Q5T9C9; -.
DR PaxDb; Q5T9C9; -.
DR PeptideAtlas; Q5T9C9; -.
DR PRIDE; Q5T9C9; -.
DR ProteomicsDB; 64791; -. [Q5T9C9-1]
DR ProteomicsDB; 64792; -. [Q5T9C9-2]
DR Antibodypedia; 30919; 145 antibodies from 27 providers.
DR DNASU; 138429; -.
DR Ensembl; ENST00000300432.3; ENSP00000300432.3; ENSG00000167103.12. [Q5T9C9-2]
DR Ensembl; ENST00000388747.9; ENSP00000373399.4; ENSG00000167103.12. [Q5T9C9-1]
DR GeneID; 138429; -.
DR KEGG; hsa:138429; -.
DR MANE-Select; ENST00000388747.9; ENSP00000373399.4; NM_001135219.2; NP_001128691.1.
DR UCSC; uc004bsu.3; human. [Q5T9C9-1]
DR CTD; 138429; -.
DR DisGeNET; 138429; -.
DR GeneCards; PIP5KL1; -.
DR HGNC; HGNC:28711; PIP5KL1.
DR HPA; ENSG00000167103; Low tissue specificity.
DR MIM; 612865; gene.
DR neXtProt; NX_Q5T9C9; -.
DR OpenTargets; ENSG00000167103; -.
DR PharmGKB; PA134926015; -.
DR VEuPathDB; HostDB:ENSG00000167103; -.
DR eggNOG; KOG0229; Eukaryota.
DR GeneTree; ENSGT00940000158633; -.
DR HOGENOM; CLU_043959_0_0_1; -.
DR InParanoid; Q5T9C9; -.
DR OMA; PRHELHG; -.
DR OrthoDB; 1562683at2759; -.
DR PhylomeDB; Q5T9C9; -.
DR TreeFam; TF354315; -.
DR PathwayCommons; Q5T9C9; -.
DR SignaLink; Q5T9C9; -.
DR BioGRID-ORCS; 138429; 13 hits in 1072 CRISPR screens.
DR ChiTaRS; PIP5KL1; human.
DR GenomeRNAi; 138429; -.
DR Pharos; Q5T9C9; Tbio.
DR PRO; PR:Q5T9C9; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5T9C9; protein.
DR Bgee; ENSG00000167103; Expressed in lower esophagus mucosa and 102 other tissues.
DR Genevisible; Q5T9C9; HS.
DR GO; GO:0042995; C:cell projection; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:ARUK-UCL.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IDA:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:ARUK-UCL.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Lipid metabolism;
KW Membrane; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..394
FT /note="Phosphatidylinositol 4-phosphate 5-kinase-like
FT protein 1"
FT /id="PRO_0000285758"
FT DOMAIN 36..393
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT VAR_SEQ 1..203
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024904"
SQ SEQUENCE 394 AA; 44572 MW; 34D41BC034B574FD CRC64;
MAAPSPGPRE VLAPSPEAGC RAVTSSRRGL LWRLRDKQSR LGLFEISPGH ELHGMTCMMQ
AGLWAATQVS MDHPPTGPPS RDDFSEVLTQ VHEGFELGTL AGPAFAWLRR SLGLAEEDYQ
AALGPGGPYL QFLSTSKSKA SFFLSHDQRF FLKTQGRREV QALLAHLPRY VQHLQRHPHS
LLARLLGVHS LRVDRGKKTY FIVMQSVFYP AGRISERYDI KGCEVSRWVD PAPEGSPLVL
VLKDLNFQGK TINLGPQRSW FLRQMELDTT FLRELNVLDY SLLIAFQRLH EDERGPGSSL
IFRTARSVQG AQSPEESRAQ NRRLLPDAPN ALHILDGPEQ RYFLGVVDLA TVYGLRKRLE
HLWKTLRYPG RTFSTVSPAR YARRLCQWVE AHTE
