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Q9R0I8 (PI42A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha

EC=2.7.1.149
Alternative name(s):
1-phosphatidylinositol 5-phosphate 4-kinase 2-alpha
Diphosphoinositide kinase 2-alpha
PIPK2 alpha
Phosphatidylinositol 5-phosphate 4-kinase type II alpha
Short name=PI(5)P 4-kinase type II alpha
Short name=PIP4KII-alpha
PtdIns(5)P-4-kinase isoform 2-alpha
Gene names
Name:Pip4k2a
Synonyms:Pip5k2a
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2. May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation. May be involved in thrombopoiesis and the terminal maturation of megakaryocytes and regulation of their size By similarity. May negatively regulate insulin-stimulated glucose uptake by lowering the levels of PtdIns5P. Ref.2

Catalytic activity

ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.

Subunit structure

Homodimer. Interacts with PIP4K2B. Interaction with PIP4K2B may modulate localization to the nucleus By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Cell membrane By similarity. Note: Localization to the nucleus is modulated by the interaction with PIP4K2B By similarity. May translocate from the cytosol to the cell membrane upon activation of tyrosine phosphorylation By similarity. May translocate from the inner to the outer segments of the rod photoreceptor cells in response to light By similarity.

Sequence similarities

Contains 1 PIPK domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function1-phosphatidylinositol-5-phosphate 4-kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
PRO_0000185468

Regions

Domain33 – 405373PIPK

Amino acid modifications

Modified residue891N6-acetyllysine By similarity
Modified residue1451N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9R0I8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: CA54529BC7FD8622

FASTA40646,210
        10         20         30         40         50         60 
MATPSNLGSS VLASKTKTKK KHFVAQKVKL FRASDPLLSV LMWGVNHSIN ELSHVQIPVM 

        70         80         90        100        110        120 
LMPDDFKAYS KIKVDNHLFN KENMPSHFKF KEYCPMVFRN LRERFGIDDQ DFQNSLTRSA 

       130        140        150        160        170        180 
PLPNDSQARS GARFHTSYDK RYVIKTITSE DVAEMHNILK KYHQYIVECH GVTLLPQFLG 

       190        200        210        220        230        240 
MYRLNVDGVE IYVIVTRNVF SHRLSVYRKY DLKGSTVARE ASDKEKAKEL PTLKDNDFIN 

       250        260        270        280        290        300 
EGQKIYIDDS NKKIFLEKLK KDVEFLAQLK LMDYSLLVGI HDVERAEQEE VECEENEGEE 

       310        320        330        340        350        360 
EGESDGAHPI GTPPDSPGNT LNSSPPLAPG EFDPNIDVYA IKCHENAPRK EVYFMAIIDI 

       370        380        390        400 
LTHYDAKKKA AHAAKTVKHG AGAEISTVNP EQYSKRFLDF IGHILT 

« Hide

References

[1]"Rattus rat phosphatidylinositol 5-phosphate 4-kinase alpha, complete cds."
Kudo M., Saito S., Kondo H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Involvement of phosphatidylinositol 5-phosphate in insulin-stimulated glucose uptake in the L6 myotube model of skeletal muscle."
Grainger D.L., Tavelis C., Ryan A.J., Hinchliffe K.A.
Pflugers Arch. 462:723-732(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN INSULIN-MEDIATED GLUCOSE UPTAKE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB032899 mRNA. Translation: BAA85160.1.
RefSeqNP_446378.1. NM_053926.2.
UniGeneRn.24177.

3D structure databases

ProteinModelPortalQ9R0I8.
SMRQ9R0I8. Positions 29-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9R0I8. 1 interaction.
STRING10116.ENSRNOP00000022375.

Proteomic databases

PaxDbQ9R0I8.
PRIDEQ9R0I8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID116723.
KEGGrno:116723.
UCSCRGD:621708. rat.

Organism-specific databases

CTD5305.
RGD621708. Pip4k2a.

Phylogenomic databases

eggNOGCOG5253.
HOVERGENHBG000072.
KOK00920.
PhylomeDBQ9R0I8.

Gene expression databases

GenevestigatorQ9R0I8.

Family and domain databases

Gene3D3.30.800.10. 1 hit.
3.30.810.10. 1 hit.
InterProIPR023610. PInositol-4-P-5-kinase.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
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

NextBio619640.

Entry information

Entry namePI42A_RAT
AccessionPrimary (citable) accession number: Q9R0I8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families