Reviewed, UniProtKB/Swiss-Prot P70182 (PI51A_MOUSE)

Names and origin

Protein names

Recommended name:
    Phosphatidylinositol-4-phosphate 5-kinase type-1 alpha
    EC=2.7.1.68
Alternative name(s):
    Phosphatidylinositol-4-phosphate 5-kinase type I alpha
      Short name=PtdIns(4)P-5-kinase alpha
      Short name=PIP5KIalpha
    Phosphatidylinositol-4-phosphate 5-kinase type I beta
      Short name=PI4P5KIbeta
    68 kDa type I phosphatidylinositol-4-phosphate 5-kinase

Gene names

Name:	Pip5k1a
Synonyms:	Pip5k1b

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	546 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Participates in the biosynthesis of phosphatidylinositol-4,5-bisphosphate. Mediates RAC1-dependent reorganization of actin filaments. Contributes to the activation of PLD2. Ref.1 Ref.5
Catalytic activity	ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
Enzyme regulation	Activated by phosphatidic acid. Ref.1 Ref.4
Subunit structure	Interacts with ARF1, RAC1, PLD1, PLD2 and JUB. Ref.5 Ref.6 Ref.7 Ref.8
Subcellular location	Cell membrane. Golgi apparatus › Golgi stack. Note: Detected on RAC1-induced plasma membrane ruffles, and on membrane ruffles induced by platelet-derived growth factor By similarity.
Tissue specificity	Highly expressed in skeletal muscle, testis, brain and lung. Ref.1
Sequence similarities	Contains 1 PIPK domain.
Biophysicochemical properties	Kinetic parameters: KM=26 µM for PtdIns4P KM=33 µM for ATP

Ontologies

Keywords
Cellular component	Cell membrane Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	phosphatidylinositol metabolic process Ref.1 Inferred from direct assay. Source: MGI
Cellular component	Golgi stack Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	1-phosphatidylinositol-4-phosphate 5-kinase activity Ref.1 Inferred from direct assay. Source: MGI ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P70182-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P70182-2)

The sequence of this isoform differs from the canonical sequence as follows:
     238-431: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 546	546	Phosphatidylinositol-4-phosphate 5-kinase type-1 alpha		PRO_0000185457
Regions
	Domain	66 – 434	369	PIPK
Amino acid modifications
	Modified residue	443	1	Phosphoserine By similarity
	Cross-link	88		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Natural variations
	Alternative sequence	238 – 431	194	Missing in isoform 2.		VSP_016009
Experimental info
	Sequence conflict	28	1	S → AS in AAH03763. Ref.3
	Sequence conflict	120	1	N → S in AAH03763. Ref.3
	Sequence conflict	258	1	E → D in BAA13031. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 25, 2005. Version 2. Checksum: 6E895F22A75B7140	FASTA	546	60,485
	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
	Isoform 2. Checksum: 6090D9F312A32B99	FASTA	352	38,027
	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 NLLPRSVNTV 250 260 270 280 290 300 FKKIPLKPSP TKKFRSGPSF SRRSGPSGNS CTSQLMASGE HRAQVTTKAE VEPDVHLGRP 310 320 330 340 350 DVLPQTPPLE EISEGSPVPG PSFSPVVGQP LQILNLSSTL EKLDVAESEF TH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of cDNAs encoding two isoforms of 68-kDa type I phosphatidylinositol 4-phosphate 5-kinase." Ishihara H., Shibasaki Y., Kizuki N., Katagiri H., Yazaki Y., Asano T., Oka Y. J. Biol. Chem. 271:23611-23614(1996) [PubMed: 8798574] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY. Tissue: Insulinoma.
[2]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Inner ear.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Eye and Mammary gland.
[4]	"Type I phosphatidylinositol-4-phosphate 5-kinases. Cloning of the third isoform and deletion/substitution analysis of members of this novel lipid kinase family." Ishihara H., Shibasaki Y., Kizuki N., Wada T., Yazaki Y., Asano T., Oka Y. J. Biol. Chem. 273:8741-8748(1998) [PubMed: 9535851] [Abstract] Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[5]	"Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac-dependent actin assembly." Tolias K.F., Hartwig J.H., Ishihara H., Shibasaki Y., Cantley L.C., Carpenter C.L. Curr. Biol. 10:153-156(2000) [PubMed: 10679324] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAC1.
[6]	"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." 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. EMBO J. 19:5440-5449(2000) [PubMed: 11032811] [Abstract] Cited for: INTERACTION WITH PLD1 AND PLD2, SUBCELLULAR LOCATION.
[7]	"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." Jones D.H., Morris J.B., Morgan C.P., Kondo H., Irvine R.F., Cockcroft S. J. Biol. Chem. 275:13962-13966(2000) [PubMed: 10747863] [Abstract] Cited for: INTERACTION WITH ARF1, SUBCELLULAR LOCATION.
[8]	"The LIM protein Ajuba regulates phosphatidylinositol 4,5-bisphosphate levels in migrating cells through an interaction with and activation of PIPKI alpha." Kisseleva M., Feng Y., Ward M., Song C., Anderson R.A., Longmore G.D. Mol. Cell. Biol. 25:3956-3966(2005) [PubMed: 15870270] [Abstract] Cited for: INTERACTION WITH JUB.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D86177 mRNA. Translation: BAA13031.1. AK158062 mRNA. Translation: BAE34344.1. BC003763 mRNA. Translation: AAH03763.1. BC031774 mRNA. Translation: AAH31774.1.
IPI	IPI00331736. IPI00475262.
RefSeq	NP_032873.2.
UniGene	Mm.296409
3D structure databases
HSSP	HSSP built from PDB template 1BO1 based on UniProtKB P78356.
ModBase	Search...
PTM databases
PhosphoSite	P70182.
Proteomic databases
PRIDE	P70182.
Genome annotation databases
Ensembl	ENSMUSG00000028126. Mus musculus. [Contig view]
GeneID	18720.
KEGG	mmu:18720.
Organism-specific databases
MGI	MGI:107929. Pip5k1a.
Phylogenomic databases
HOVERGEN	P70182.
Enzyme and pathway databases
BRENDA	2.7.1.68. 244.
Gene expression databases
ArrayExpress	P70182.
Bgee	P70182.
GermOnline	ENSMUSG00000028126. Mus musculus.
Family and domain databases
InterPro	IPR002498. PInositol-4-P-5-kinase_core. IPR016034. PInositol-4P-5-kinase_core_sub. [Graphical view]
PANTHER	PTHR23086. PIP5K. 1 hit.
Pfam	PF01504. PIP5K. 1 hit. [Graphical view]
SMART	SM00330. PIPKc. 1 hit. [Graphical view]
PROSITE	PS51455. PIPK. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	294821.
SOURCE	Search...

Entry information

Entry name

PI51A_MOUSE

Accession

Primary (citable) accession number: P70182
Secondary accession number(s): Q8K0D3, Q99L80

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	October 25, 2005
Last modified:	July 7, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)