P78356 (PI42B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Protein existence	Evidence 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.10
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 component	Cell membrane Cytoplasm Endoplasmic reticulum Membrane Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell surface receptor signaling pathway Traceable author statement Ref.1. Source: ProtInc phosphatidylinositol biosynthetic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol 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_function	1-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: 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 416

416

Phosphatidylinositol 5-phosphate 4-kinase type-2 beta

PRO_0000185470

Regions

Domain

38 – 415

378

PIPK

Amino acid modifications

Modified residue

150

1

N6-acetyllysine Ref.7

Modified residue

326

1

Phosphoserine Ref.4 Ref.6

Natural variations

Alternative sequence

270 – 281

12

FLAQL…MDYSL → EILVLSPGRRIA in isoform 2.

VSP_010384

Alternative sequence

282 – 416

135

Missing in isoform 2.

VSP_010385

Experimental info

Sequence conflict

250

1

L → P in AAV38420. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

416

Helix Strand Turn

Details...

Helix

41 – 57

17

Helix

68 – 71

4

Beta strand

74 – 80

7

Beta strand

82 – 85

4

Beta strand

87 – 89

3

Beta strand

91 – 98

8

Helix

100 – 109

10

Helix

114 – 122

9

Beta strand

139 – 141

3

Beta strand

145 – 150

6

Helix

154 – 172

19

Turn

173 – 176

4

Beta strand

183 – 191

9

Beta strand

194 – 202

9

Beta strand

207 – 209

3

Beta strand

212 – 217

6

Beta strand

221 – 224

4

Helix

229 – 231

3

Beta strand

232 – 234

3

Helix

240 – 245

6

Helix

256 – 274

19

Beta strand

281 – 287

7

Helix

288 – 301

14

Turn

302 – 305

4

Turn

347 – 349

3

Beta strand

353 – 355

3

Beta strand

361 – 367

7

Beta strand

394 – 396

3

Helix

400 – 414

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 2288CD2883EACEBE	FASTA	416	47,378
	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
	Isoform 2 [UniParc]. Checksum: D83D7A24BC4B8DA6	FASTA	281	32,317
	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 NDFLNEGQKL HVGEESKKNF LEKLKRDVEE ILVLSPGRRI A

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY.
[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]	"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.

IPI

IPI00216470.
IPI00235352.

RefSeq

NP_003550.1. NM_003559.4.

UniGene

Hs.743962.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BO1	X-ray	3.00	A/B	1-416	[»]

ProteinModelPortal

P78356.

ModBase

Search...

Protein-protein interaction databases

IntAct

P78356. 2 interactions.

MINT

MINT-2864974.

STRING

9606.ENSP00000269554.

PTM databases

PhosphoSite

P78356.

Polymorphism databases

DMDM

47605991.

Proteomic databases

PaxDb

P78356.

PRIDE

P78356.

Protocols and materials databases

DNASU

8396.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000269554; ENSP00000269554; ENSG00000141720.

GeneID

8396.

KEGG

hsa:8396.

UCSC

uc002hqs.3. human.

Organism-specific databases

CTD

8396.

GeneCards

GC17M036921.

HGNC

HGNC:8998. PIP4K2B.

HPA

HPA047875.

MIM

603261. gene.

neXtProt

NX_P78356.

PharmGKB

PA162399640.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5253.

HOGENOM

HOG000007832.

HOVERGEN

HBG000072.

InParanoid

P78356.

KO

K00920.

OMA

ECENDGM.

OrthoDB

EOG4SQWX1.

PhylomeDB

P78356.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P78356.

Gene expression databases

Bgee

P78356.

CleanEx

HS_PIP4K2B.

Genevestigator

P78356.

GermOnline

ENSG00000141720. Homo sapiens.

Family and domain databases

Gene3D

3.30.800.10. 1 hit.
3.30.810.10. 2 hits.

InterPro

IPR023610. 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]

PANTHER

PTHR23086. PTHR23086. 1 hit.

Pfam

PF01504. PIP5K. 1 hit.
[Graphical view]

SMART

SM00330. PIPKc. 1 hit.
[Graphical view]

PROSITE

PS51455. PIPK. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P78356.

ChEMBL

CHEMBL5667.

ChiTaRS

PIP4K2B. human.

EvolutionaryTrace

P78356.

GenomeRNAi

8396.

NextBio

31424.

SOURCE

Search...

Entry information

Entry name

PI42B_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.