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P70181 (PI51B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
Short name=PIP5K1-beta
Short name=PtdIns(4)P-5-kinase 1 beta
EC=2.7.1.68
Alternative name(s):
Phosphatidylinositol 4-phosphate 5-kinase type I alpha
Short name=PIP5KIalpha
Phosphatidylinositol 4-phosphate 5-kinase type I beta
Short name=PIP5KIbeta
Gene names
Name:Pip5k1b
Synonyms:Pip5k1a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
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. Together with PIP5K1A is required after stimulation of G-protein coupled receptors for stable platelet adhesion. Ref.1 Ref.6 Ref.10

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.5

Subunit structure

Interacts with RAC1, AJUBA, PLD1, PLD2 and ARF1. Ref.6 Ref.7 Ref.8 Ref.9

Subcellular location

Endomembrane system By similarity. Note: Associated with membranes By similarity. Ref.7

Tissue specificity

Highly expressed in brain and testis. Barely detectable in liver and skeletal muscle. Ref.1

Sequence similarities

Contains 1 PIPK domain.

Caution

There is confusion in the literature with phosphatidylinositol 4-phosphate 5-kinase type I nomenclature due to the fact that frequently mouse PIP5K1B is named Phosphatidylinositol 4-phosphate 5-kinase type I alpha.

Biophysicochemical properties

Kinetic parameters:

KM=34 µM for PtdIns4P Ref.5

KM=27 µM for ATP

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentendomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

uropod

Inferred from electronic annotation. Source: Compara

   Molecular_function1-phosphatidylinositol-4-phosphate 5-kinase activity

Inferred from direct assay Ref.1. Source: MGI

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Clic4Q9QYB14EBI-645167,EBI-645175

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P70181-1)

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: P70181-2)

The sequence of this isoform differs from the canonical sequence as follows:
     401-452: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 539539Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
PRO_0000185459

Regions

Domain25 – 395371PIPK

Natural variations

Alternative sequence401 – 45252Missing in isoform 2.
VSP_016012

Experimental info

Mutagenesis1381K → A: Almost complete loss of kinase activity. Ref.5
Mutagenesis2271D → A: Reduces kinase activity by 98%. Loss of actin-remodeling activity. Ref.6
Sequence conflict2911V → A in AAC05374. Ref.2
Sequence conflict4251V → L in AAC05374. Ref.2
Sequence conflict4371R → Q in AAC05374. Ref.2
Sequence conflict525 – 5284TLDL → ALET in AAC05374. Ref.2

Sequences

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

Last modified February 1, 1997. Version 1.
Checksum: A8478C9E21546AC3

FASTA53960,803
        10         20         30         40         50         60 
MSSTAENGDA VPGKQNEEKT YKKTASSAIK GAIQLGIGYT VGNLTSKPER DVLMQDFYVV 

        70         80         90        100        110        120 
ESVFLPSEGS NLTPAHHYPD FRFKTYAPLA FRYFRELFGI KPDDYLYSIC SEPLIELSNP 

       130        140        150        160        170        180 
GASGSLFFLT SDDEFIIKTV QHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCMQSGG 

       190        200        210        220        230        240 
INIRIVVMNN VLPRAMRMHL TYDLKGSTYK RRASRKEREK PNPTFKDLDF LQDMHEGLYF 

       250        260        270        280        290        300 
DTETYNALMK TLQRDCRVLE SFKIMDYSLL LGIHILDHSL KDKEEEPLQN VPDAKRPGMQ 

       310        320        330        340        350        360 
KVLYSTAMES IQGPGKSADG IIAENPDTMG GIPAKSHKGE KLLLFMGIID ILQSYRLMKK 

       370        380        390        400        410        420 
LEHSWKALVY DGDTVSVHRP SFYADRFLKF MNSRVFKKIQ ALKASPSKKR CNSIAALKAT 

       430        440        450        460        470        480 
SQEIVSSISQ EWKDEKRDLL TEGQSFSSLD EEALGSRHRP DLVPSTPSLF EAASLATTIS 

       490        500        510        520        530 
SSSLYVGEHY PHDRTTLYSN SKGLPSSSTF TLEEGTIYLT AEPNTLDLQD DASVLDVYL

« Hide

Isoform 2 [UniParc].

Checksum: 41ADCD8B56419DC8
Show »

FASTA48755,080

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
Tissue: Insulinoma.
[2]Machesky L.M.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Amnion, Heart and Retina.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Thymus.
[5]"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] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-138, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAC1, MUTAGENESIS OF ASP-227.
[7]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLD1 AND PLD2, SUBCELLULAR LOCATION.
[8]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARF1.
[9]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AJUBA.
[10]"Loss of PIP5KIbeta demonstrates that PIP5KI isoform-specific PIP2 synthesis is required for IP3 formation."
Wang Y., Chen X., Lian L., Tang T., Stalker T.J., Sasaki T., Kanaho Y., Brass L.F., Choi J.K., Hartwig J.H., Abrams C.S.
Proc. Natl. Acad. Sci. U.S.A. 105:14064-14069(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PLATELETS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D86176 mRNA. Translation: BAA13030.1.
AF048695 mRNA. Translation: AAC05374.1.
AK149354 mRNA. Translation: BAE28830.1.
AK164552 mRNA. Translation: BAE37836.1.
AK146100 mRNA. Translation: BAE26901.1.
BC034864 mRNA. Translation: AAH34864.1.
IPIIPI00117305.
IPI00170400.
RefSeqNP_032872.1. NM_008846.2.
UniGeneMm.217214.

3D structure databases

ProteinModelPortalP70181.
SMRP70181. Positions 25-288.
ModBaseSearch...

Protein-protein interaction databases

IntActP70181. 3 interactions.
STRING10090.ENSMUSP00000025800.

PTM databases

PhosphoSiteP70181.

Proteomic databases

PaxDbP70181.
PRIDEP70181.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025800; ENSMUSP00000025800; ENSMUSG00000024867.
ENSMUST00000112673; ENSMUSP00000108292; ENSMUSG00000024867.
GeneID18719.
KEGGmmu:18719.
UCSCuc008hap.1. mouse.
uc012bjs.1. mouse.

Organism-specific databases

CTD8395.
MGIMGI:107930. Pip5k1b.

Phylogenomic databases

eggNOGCOG5253.
GeneTreeENSGT00690000101870.
HOGENOMHOG000193876.
HOVERGENHBG052818.
InParanoidP70181.
KOK00889.
OMAEHYPHDR.
OrthoDBEOG41G33V.

Gene expression databases

BgeeP70181.
GenevestigatorP70181.
GermOnlineENSMUSG00000024867. Mus musculus.

Family and domain databases

InterProIPR023610. PInositol-4-P-5-kinase.
IPR002498. PInositol-4-P-5-kinase_core.
IPR016034. PInositol-4P-5-kinase_core_sub.
[Graphical view]
PANTHERPTHR23086. PTHR23086. 1 hit.
PfamPF01504. PIP5K. 1 hit.
[Graphical view]
SMARTSM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEPS51455. PIPK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio294817.
SOURCESearch...

Entry information

Entry namePI51B_MOUSE
AccessionPrimary (citable) accession number: P70181
Secondary accession number(s): O70335, Q8JZY6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: February 1, 1997
Last modified: May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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