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UniProtKB/Swiss-Prot entry P70182


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PI51A_MOUSE
Primary accession number P70182
Secondary accession numbers Q8K0D3 Q99L80
Integrated into Swiss-Prot on October 25, 2005
Sequence was last modified on October 25, 2005 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 54)
Name and origin of the protein
Protein name Phosphatidylinositol-4-phosphate 5-kinase type-1 alpha
Synonyms EC 2.7.1.68
Phosphatidylinositol-4-phosphate 5-kinase type I alpha
PtdIns(4)P-5-kinase alpha
PIP5KIalpha
Phosphatidylinositol-4-phosphate 5-kinase type I beta
PI4P5KIbeta
68 kDa type I phosphatidylinositol-4-phosphate 5-kinase
Gene name
Name: Pip5k1a
Synonyms: Pip5k1b
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, AND TISSUE SPECIFICITY.
TISSUE=Insulinoma;
DOI=10.1074/jbc.271.39.23611; PubMed=8798574 [NCBI, ExPASy, EBI, Israel, Japan]
Ishihara H., Shibasaki Y., Kizuki N., Katagiri H., Yazaki Y., Asano T., Oka Y.;
"Cloning of cDNAs encoding two isoforms of 68-kDa type I phosphatidylinositol 4-phosphate 5-kinase.";
J. Biol. Chem. 271:23611-23614(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
TISSUE=Inner ear;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Eye, and Mammary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1074/jbc.273.15.8741; PubMed=9535851 [NCBI, ExPASy, EBI, Israel, Japan]
Ishihara H., Shibasaki Y., Kizuki N., Wada T., Yazaki Y., Asano T., Oka Y.;
"Type I phosphatidylinositol-4-phosphate 5-kinases. Cloning of the third isoform and deletion/substitution analysis of members of this novel lipid kinase family.";
J. Biol. Chem. 273:8741-8748(1998).
[5]
FUNCTION, AND INTERACTION WITH RAC1.
DOI=10.1016/S0960-9822(00)00315-8; PubMed=10679324 [NCBI, ExPASy, EBI, Israel, Japan]
Tolias K.F., Hartwig J.H., Ishihara H., Shibasaki Y., Cantley L.C., Carpenter C.L.;
"Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac-dependent actin assembly.";
Curr. Biol. 10:153-156(2000).
[6]
INTERACTION WITH PLD1 AND PLD2, AND SUBCELLULAR LOCATION.
DOI=10.1093/emboj/19.20.5440; PubMed=11032811 [NCBI, ExPASy, EBI, Israel, Japan]
Divecha N., Roefs M., Halstead J.R., D'Andrea S., Fernandez-Borga M., Oomen L., Saqib K.M., Wakelam M.J.O., D'Santos C.;
"Interaction of the type Ialpha PIPkinase with phospholipase D: a role for the local generation of phosphatidylinositol 4, 5-bisphosphate in the regulation of PLD2 activity.";
EMBO J. 19:5440-5449(2000).
[7]
INTERACTION WITH ARF1, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.C901019199; PubMed=10747863 [NCBI, ExPASy, EBI, Israel, Japan]
Jones D.H., Morris J.B., Morgan C.P., Kondo H., Irvine R.F., Cockcroft S.;
"Type I phosphatidylinositol 4-phosphate 5-kinase directly interacts with ADP-ribosylation factor 1 and is responsible for phosphatidylinositol 4,5-bisphosphate synthesis in the Golgi compartment.";
J. Biol. Chem. 275:13962-13966(2000).
[8]
INTERACTION WITH JUB.
DOI=10.1128/MCB.25.10.3956-3966.2005; PubMed=15870270 [NCBI, ExPASy, EBI, Israel, Japan]
Kisseleva M., Feng Y., Ward M., Song C., Anderson R.A., Longmore G.D.;
"The LIM protein Ajuba regulates phosphatidylinositol 4,5-bisphosphate levels in migrating cells through an interaction with and activation of PIPKI alpha.";
Mol. Cell. Biol. 25:3956-3966(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D86177; BAA13031.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK158062; BAE34344.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003763; AAH03763.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031774; AAH31774.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_032873.2; -.
UniGene Mm.296409
3D structure databases
HSSP P78356; 1BO1. [HSSP ENTRY / PDB]
ModBase P70182.
PTM databases
PhosphoSite P70182; -.
Organism-specific databases
MGI MGI:107929; Pip5k1a.
Gene expression databases
ArrayExpress P70182; -.
GermOnline ENSMUSG00000028126; Mus musculus.
Ontologies
GO
GO:0005794; Cellular component: Golgi apparatus (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0016308; Molecular function: 1-phosphatidylinositol-4-phosphate 5-kinase activity (inferred from direct assay from MGI).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0046488; Biological process: phosphatidylinositol metabolic process (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR002498; PIP5K_core.
IPR016034; PIP5K_core_sub.
Graphical view of domain structure.
PANTHER PTHR23086; PIP5K; 1.
Pfam PF01504; PIP5K; 1.
Pfam graphical view of domain structure.
SMART SM00330; PIPKc; 1.
SMART graphical view of domain structure.
ProtoNet P70182.
Genome annotation databases
Ensembl ENSMUSG00000028126; Mus musculus. [Contig view]
GeneID 18720; -.
KEGG mmu:18720; -.
Phylogenomic databases
HOVERGEN P70182; -.
Other
NextBio 294821; -.
SOURCE Pip5k1a; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cell membrane; Golgi apparatus; Kinase; Membrane; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   546  546     Phosphatidylinositol-4-phosphate 5-kinase type-1 alpha. PRO_0000185457
DOMAIN   148   434  287     PI5K. 
VAR_SEQ   238   431        Missing (in isoform 2). VSP_016009
CONFLICT   28    28        S -> AS (in Ref. 3; AAH03763). 
CONFLICT   120   120        N -> S (in Ref. 3; AAH03763). 
CONFLICT   258   258        E -> D (in Ref. 1; BAA13031). 
Sequence information
Length: 546 AA [This is the length of the unprocessed precursor] Molecular weight: 60485 Da [This is the MW of the unprocessed precursor] CRC64: 6E895F22A75B7140 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASASSGPAA AGFSSLDAGA PAGTAAASGI KRATVSEGPS ASVMPVKKIG HRSVDSSGET 

        70         80         90        100        110        120 
TYKKTTSSAL KGAIQLGITH TVGSLSTKPE RDVLMQDFYV VESIFFPSEG SNLTPAHHYN 

       130        140        150        160        170        180 
DFRFKTYAPV AFRYFRELFG IRPDDYLYSL CSEPLIELSN SGASGSLFYV SSDDEFIIKT 

       190        200        210        220        230        240 
VQHKEAEFLQ KLLPGYYMNL NQNPRTLLPK FYGLYCVQAG GKNIRIVVMN NLLPRSVKMH 

       250        260        270        280        290        300 
MKYDLKGSTY KRRASQKERE KTLPTFKDLD FLQDIPDGLF LDADMYSALC KTLQRDCLVL 

       310        320        330        340        350        360 
QSFKIMDYSL LMSIHNMDHA QREPTSNDTQ YSADTRRPAP QKALYSTAME SIQGEARRGG 

       370        380        390        400        410        420 
TVETEDHMGG IPARNNKGER LLLYIGIIDI LQSYRFVKKL EHSWKALVHD GDTVSVHRPG 

       430        440        450        460        470        480 
FYAERFQRFM CNTVFKKIPL KPSPTKKFRS GPSFSRRSGP SGNSCTSQLM ASGEHRAQVT 

       490        500        510        520        530        540 
TKAEVEPDVH LGRPDVLPQT PPLEEISEGS PVPGPSFSPV VGQPLQILNL SSTLEKLDVA 


ESEFTH 

P70182 in FASTA format

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