Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O88377 (PI42B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. 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 beta

EC=2.7.1.149
Alternative name(s):
1-phosphatidylinositol 5-phosphate 4-kinase 2-beta
Diphosphoinositide kinase 2-beta
Phosphatidylinositol 5-phosphate 4-kinase type II beta
Short name=PI(5)P 4-kinase type II beta
Short name=PIP4KII-beta
Phosphatidylinositol-phosphate kinase IIgamma
Short name=PIPKIIgamma
PtdIns(5)P-4-kinase isoform 2-beta
Gene names
Name:Pip4k2b
Synonyms:Pip5k2b
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. Ref.1

Catalytic activity

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

Subunit structure

Homodimer. Binds TNFRSF1A. Interacts with PIP4K2A. Interaction with PIP4K2A suppresses ubiquitination by the SPOP/ CUL3 complex By similarity.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein By similarity. Cell membrane; Peripheral membrane protein By similarity. Nucleus By similarity. Cytoplasm By similarity. Note: Associated with the plasma membrane and the endoplasmic reticulum By similarity. Ref.1

Post-translational modification

Phosphorylated on serine residues. Ubiquitinated by the SPOP/CUL3 complex. Ubiquitination is stimulated by PtdIns5P levels By similarity. Ref.1

Sequence similarities

Contains 1 PIPK domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 416415Phosphatidylinositol 5-phosphate 4-kinase type-2 beta
PRO_0000185472

Regions

Domain38 – 415378PIPK
Compositional bias303 – 3086Poly-Glu

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue1501N6-acetyllysine By similarity
Modified residue3261Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
O88377 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 9481AC50CBB6C196

FASTA41647,264
        10         20         30         40         50         60 
MSSNCTSTTA VAVAPLSASK TKTKKKHFVC QKVKLFRASE PILSVLMWGV NHTINELSNV 

        70         80         90        100        110        120 
PVPVMLMPDD FKAYSKIKVD NHLFNKENLP SRFKFKEYCP MVFRNLRERF GIDDQDYQNS 

       130        140        150        160        170        180 
VTRSAPINSD SQGRCGTRFL TTYDRRFVIK TVSSEDVAEM HNILKKYHQF IVECHGNTLL 

       190        200        210        220        230        240 
PQFLGMYRLT VDGVETYMVV TRNVFSHRLT VHRKYDLKGS TVAREASDKE KAKDLPTFKD 

       250        260        270        280        290        300 
NDFLNEGQKL RVGEESKKNF LEKLKRDVEF LAQLKIMDYS LLVGIHDVDR AEQEETEVED 

       310        320        330        340        350        360 
RAEEEECEND GVGGGLLCSY GTPPDSPGNL LSFPRFFGPG EFDPSVDVYA MKSHESAPKK 

       370        380        390        400        410 
EVYFMAIIDI LTPYDAKKKA AHAAKTVKHG AGAEISTVNP EQYSKRFNEF MSNILT 

« Hide

References

[1]"A novel phosphatidylinositol-5-phosphate 4-kinase (phosphatidylinositol-phosphate kinase IIgamma) is phosphorylated in the endoplasmic reticulum in response to mitogenic signals."
Itoh T., Ijuin T., Takenawa T.
J. Biol. Chem. 273:20292-20299(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF033355 mRNA. Translation: AAC40203.1.
RefSeqNP_446002.1. NM_053550.1.
UniGeneRn.30025.

3D structure databases

ProteinModelPortalO88377.
SMRO88377. Positions 34-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO88377. 1 interaction.
STRING10116.ENSRNOP00000017989.

Proteomic databases

PaxDbO88377.
PRIDEO88377.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000017989; ENSRNOP00000017989; ENSRNOG00000013030.
GeneID89812.
KEGGrno:89812.

Organism-specific databases

CTD8396.
RGD621710. Pip4k2b.

Phylogenomic databases

eggNOGCOG5253.
GeneTreeENSGT00690000102069.
HOGENOMHOG000007832.
HOVERGENHBG000072.
InParanoidO88377.
KOK00920.
OMACENDGMG.
OrthoDBEOG708VZZ.
PhylomeDBO88377.
TreeFamTF354315.

Gene expression databases

GenevestigatorO88377.

Family and domain databases

Gene3D3.30.800.10. 1 hit.
3.30.810.10. 2 hits.
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

NextBio617686.
PROO88377.

Entry information

Entry namePI42B_RAT
AccessionPrimary (citable) accession number: O88377
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: November 1, 1998
Last modified: April 16, 2014
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

SIMILARITY comments

Index of protein domains and families