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Reviewed, UniProtKB/Swiss-Prot P70182 (PI51A_MOUSE)

Last modified July 7, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 apparatusGolgi 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

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 546546Phosphatidylinositol-4-phosphate 5-kinase type-1 alpha
PRO_0000185457

Regions

Domain66 – 434369PIPK

Amino acid modifications

Modified residue4431Phosphoserine By similarity
Cross-link88Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence238 – 431194Missing in isoform 2.
VSP_016009

Experimental info

Sequence conflict281S → AS in AAH03763. Ref.3
Sequence conflict1201N → S in AAH03763. Ref.3
Sequence conflict2581E → D in BAA13031. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 25, 2005. Version 2.
Checksum: 6E895F22A75B7140

FASTA54660,485
        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 

« Hide

Isoform 2.

Checksum: 6090D9F312A32B99
Show »

FASTA35238,027

References

« Hide '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. expand/collapse author list , 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

D86177 mRNA. Translation: BAA13031.1.
AK158062 mRNA. Translation: BAE34344.1.
BC003763 mRNA. Translation: AAH03763.1.
BC031774 mRNA. Translation: AAH31774.1.
IPIIPI00331736.
IPI00475262.
RefSeqNP_032873.2.
UniGeneMm.296409

3D structure databases

HSSPHSSP built from PDB template 1BO1 based on UniProtKB P78356.
ModBaseSearch...

PTM databases

PhosphoSiteP70182.

Proteomic databases

PRIDEP70182.

Genome annotation databases

EnsemblENSMUSG00000028126. Mus musculus. [Contig view]
GeneID18720.
KEGGmmu:18720.

Organism-specific databases

MGIMGI:107929. Pip5k1a.

Phylogenomic databases

HOVERGENP70182.

Enzyme and pathway databases

BRENDA2.7.1.68. 244.

Gene expression databases

ArrayExpressP70182.
BgeeP70182.
GermOnlineENSMUSG00000028126. Mus musculus.

Family and domain databases

InterProIPR002498. PInositol-4-P-5-kinase_core.
IPR016034. PInositol-4P-5-kinase_core_sub.
[Graphical view]
PANTHERPTHR23086. PIP5K. 1 hit.
PfamPF01504. PIP5K. 1 hit.
[Graphical view]
SMARTSM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEPS51455. PIPK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio294821.
SOURCESearch...

Entry information

Entry namePI51A_MOUSE
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents