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Reviewed, UniProtKB/Swiss-Prot P70181 (PI51B_MOUSE)

Last modified November 3, 2009. Version 65. 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 · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

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

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Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Participates in the biosynthesis of phosphatidylinositol-4,5-bisphosphate. Mediates RAC1-dependent reorganization of actin filaments. Ref.1 Ref.6

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. Ref.6

Subcellular location

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

Tissue specificity

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

Sequence similarities

Contains 1 PIPK domain.

Biophysicochemical properties

Kinetic parameters:

KM=34 µM for PtdIns4P

KM=27 µM for ATP

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Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Gene Ontology (GO)
   Biological processphosphatidylinositol metabolic process Ref.1

Inferred from direct assay. Source: MGI

   Cellular componentendomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function1-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: IntAct

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

Clic1Q9Z1Q52EBI-645167,EBI-645184
Clic4Q9QYB13EBI-645167,EBI-645175

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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.

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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

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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.

Checksum: 41ADCD8B56419DC8
Show »

FASTA48755,080

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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]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: 16141072] [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: 15489334] [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: 9535851] [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: 10679324] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAC1, MUTAGENESIS OF ASP-227.
+Additional computationally mapped references.

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Cross-references

Sequence databases

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.
UniGeneMm.217214

3D structure databases

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

Protein-protein interaction databases

IntActP70181. 3 interactions.
STRINGP70181.

PTM databases

PhosphoSiteP70181.

Proteomic databases

PRIDEP70181.

Genome annotation databases

EnsemblENSMUST00000025800; ENSMUSP00000025800; ENSMUSG00000024867; Mus musculus. [Genome view]
ENSMUST00000112673; ENSMUSP00000108292; ENSMUSG00000024867; Mus musculus. [Genome view]
GeneID18719.
KEGGmmu:18719.
UCSCuc008hap.1. mouse.

Organism-specific databases

CTD18719.
MGIMGI:107930. Pip5k1b.

Phylogenomic databases

HOGENOMP70181.
HOVERGENP70181.
OMAFYGLYCM.

Enzyme and pathway databases

BRENDA2.7.1.68. 244.

Gene expression databases

ArrayExpressP70181.
BgeeP70181.
GenevestigatorP70181.
GermOnlineENSMUSG00000024867. 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

NextBio294817.
SOURCESearch...

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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: November 3, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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 · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents