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P78356 (PI42B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
PtdIns(5)P-4-kinase isoform 2-beta
Gene names
Name:PIP4K2B
Synonyms:PIP5K2B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.1 Ref.8 Ref.11

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein By similarity. Cell membrane; Peripheral membrane protein By similarity. Nucleus. Cytoplasm. Note: Associated with the plasma membrane and the endoplasmic reticulum By similarity. Ref.8

Tissue specificity

Highly expressed in brain, heart, pancreas, skeletal muscle and kidney. Detected at lower levels in placenta, lung and liver. Ref.1

Post-translational modification

Ubiquitinated by the SPOP/CUL3 complex. Ubiquitination is stimulated by PtdIns5P levels. Ref.8

Sequence similarities

Contains 1 PIPK domain.

Biophysicochemical properties

Kinetic parameters:

KM=30 µM for phosphatidylinositol-5- phosphate Ref.8

Vmax=0.2 pmol/min/µg enzyme

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Endoplasmic reticulum
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell surface receptor signaling pathway

Traceable author statement Ref.1. Source: ProtInc

intracellular signal transduction

Traceable author statement Ref.1. Source: GOC

phosphatidylinositol biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylinositol phosphorylation

Inferred from direct assay Ref.1. Source: GOC

phospholipid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

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-4-phosphate 5-kinase activity

Inferred from direct assay Ref.1. Source: MGI

1-phosphatidylinositol-5-phosphate 4-kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

receptor signaling protein activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P78356-1)

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: P78356-2)

The sequence of this isoform differs from the canonical sequence as follows:
     270-281: FLAQLKIMDYSL → EILVLSPGRRIA
     282-416: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 416415Phosphatidylinositol 5-phosphate 4-kinase type-2 beta
PRO_0000185470

Regions

Domain38 – 415378PIPK

Amino acid modifications

Modified residue21N-acetylserine Ref.10
Modified residue1501N6-acetyllysine Ref.7
Modified residue3261Phosphoserine Ref.4 Ref.6

Natural variations

Alternative sequence270 – 28112FLAQL…MDYSL → EILVLSPGRRIA in isoform 2.
VSP_010384
Alternative sequence282 – 416135Missing in isoform 2.
VSP_010385

Experimental info

Sequence conflict2501L → P in AAV38420. Ref.2

Secondary structure

....................................................... 416
Helix Strand Turn

Details...

Sequences

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

Last modified May 1, 1997. Version 1.
Checksum: 2288CD2883EACEBE

FASTA41647,378
        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 HVGEESKKNF LEKLKRDVEF LAQLKIMDYS LLVGIHDVDR AEQEEMEVEE 

       310        320        330        340        350        360 
RAEDEECEND GVGGNLLCSY GTPPDSPGNL LSFPRFFGPG EFDPSVDVYA MKSHESSPKK 

       370        380        390        400        410 
EVYFMAIIDI LTPYDTKKKA AHAAKTVKHG AGAEISTVNP EQYSKRFNEF MSNILT 

« Hide

Isoform 2 [UniParc].

Checksum: D83D7A24BC4B8DA6
Show »

FASTA28132,317

References

« Hide 'large scale' references
[1]"A novel interaction between the juxtamembrane region of the p55 tumor necrosis factor receptor and phosphatidylinositol-4-phosphate 5-kinase."
Castellino A.M., Parker G.J., Boronenkov I.V., Anderson R.A., Chao M.V.
J. Biol. Chem. 272:5861-5870(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH TNFRSF1A, TISSUE SPECIFICITY.
Tissue: Fetal brain.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Lung.
[4]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"PIP4Kbeta interacts with and modulates nuclear localization of the high-activity PtdIns5P-4-kinase isoform PIP4Kalpha."
Bultsma Y., Keune W.-J., Divecha N.
Biochem. J. 430:223-235(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH PIP4K2A, SUBCELLULAR LOCATION, UBIQUITINATION, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation."
Rao V.D., Misra S., Boronenkov I.V., Anderson R.A., Hurley J.H.
Cell 94:829-839(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 34-416, HOMODIMERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U85245 mRNA. Translation: AAB48596.1.
BT019614 mRNA. Translation: AAV38420.1.
BC027459 mRNA. Translation: AAH27459.1.
RefSeqNP_003550.1. NM_003559.4.
UniGeneHs.260603.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BO1X-ray3.00A/B1-416[»]
DisProtDP00054.
ProteinModelPortalP78356.
SMRP78356. Positions 34-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113985. 7 interactions.
IntActP78356. 4 interactions.
MINTMINT-2864974.
STRING9606.ENSP00000269554.

Chemistry

BindingDBP78356.
ChEMBLCHEMBL5667.
GuidetoPHARMACOLOGY2162.

PTM databases

PhosphoSiteP78356.

Polymorphism databases

DMDM47605991.

Proteomic databases

PaxDbP78356.
PRIDEP78356.

Protocols and materials databases

DNASU8396.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000269554; ENSP00000269554; ENSG00000141720. [P78356-1]
GeneID8396.
KEGGhsa:8396.
UCSCuc002hqs.3. human. [P78356-1]
uc021twj.1. human. [P78356-2]

Organism-specific databases

CTD8396.
GeneCardsGC17M036921.
HGNCHGNC:8998. PIP4K2B.
HPAHPA047875.
MIM603261. gene.
neXtProtNX_P78356.
PharmGKBPA162399640.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5253.
HOGENOMHOG000007832.
HOVERGENHBG000072.
InParanoidP78356.
KOK00920.
OMACENDGMG.
OrthoDBEOG708VZZ.
PhylomeDBP78356.
TreeFamTF354315.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP78356.

Gene expression databases

ArrayExpressP78356.
BgeeP78356.
CleanExHS_PIP4K2B.
GenevestigatorP78356.

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

ChiTaRSPIP4K2B. human.
EvolutionaryTraceP78356.
GeneWikiPIP4K2B.
GenomeRNAi8396.
NextBio31424.
PROP78356.
SOURCESearch...

Entry information

Entry namePI42B_HUMAN
AccessionPrimary (citable) accession number: P78356
Secondary accession number(s): Q5U0E8, Q8TBP2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM