Reviewed, UniProtKB/Swiss-Prot P78356 (PI42B_HUMAN)

Names and origin

Protein names

Recommended name:
    Phosphatidylinositol-5-phosphate 4-kinase type-2 beta
    EC=2.7.1.149
Alternative name(s):
    Phosphatidylinositol-5-phosphate 4-kinase type II beta
    1-phosphatidylinositol-5-phosphate 4-kinase 2-beta
    PtdIns(5)P-4-kinase isoform 2-beta
      Short name=PIP4KII-beta
    Diphosphoinositide kinase 2-beta

Gene names

Name:	PIP4K2B
Synonyms:	PIP5K2B

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Ref.6
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein By similarity. Cell membrane; Peripheral membrane protein By similarity. Note: Associated with the plasma membrane and the endoplasmic reticulum By similarity.
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	Phosphorylated on serine residues By similarity.
Sequence similarities	Contains 1 PI5K domain.

Ontologies

Keywords
Cellular component	Cell membrane Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell surface receptor linked signal transduction Ref.1 Traceable author statement. Source: ProtInc phosphatidylinositol metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum membrane 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 Ref.1 Inferred from direct assay. 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 Ref.1 Traceable author statement. 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

119 – 415

297

PI5K

Amino acid modifications

Modified residue

98

1

Phosphotyrosine Ref.4

Modified residue

322

1

Phosphothreonine Ref.5

Modified residue

326

1

Phosphoserine Ref.5

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

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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. 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: 9038203] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Lung.
[4]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-98, MASS SPECTROMETRY.
[5]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-322 AND SER-326, MASS SPECTROMETRY.
[6]	"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: 9753329] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 34-416, HOMODIMERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U85245 mRNA. Translation: AAB48596.1.
BT019614 mRNA. Translation: AAV38420.1.
BC027459 mRNA. Translation: AAH27459.1.

IPI

IPI00216470.
IPI00235352.

RefSeq

NP_003550.1.

UniGene

Hs.260603

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

IntAct

P78356. 2 interactions.

PTM databases

PhosphoSite

P78356.

Proteomic databases

PRIDE

P78356.

Genome annotation databases

Ensembl

ENSG00000141720. Homo sapiens. [Contig view]

GeneID

8396.

KEGG

hsa:8396.

Organism-specific databases

GeneCards

GC17M034175.

H-InvDB

HIX0013764.

HGNC

HGNC:8998. PIP4K2B.

MIM

603261. gene.

PharmGKB

PA33331.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P78356.

HOVERGEN

P78356.

OMA

P78356. ECENDGM.

Enzyme and pathway databases

BRENDA

2.7.1.149. 247.

Gene expression databases

ArrayExpress

P78356.

Bgee

P78356.

CleanEx

HS_PIP4K2B.

GermOnline

ENSG00000141720. Homo sapiens.

Family and domain databases

InterPro

IPR002498. PInositol-4-P-5-kinase_core.
IPR016034. PInositol-4P-5-kinase_core_sub.
[Graphical view]

PANTHER

PTHR23086. PIP5K. 1 hit.

Pfam

PF01504. PIP5K. 1 hit.
[Graphical view]

SMART

SM00330. PIPKc. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

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:	June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)