DP00054: Phosphatidylinositol-4-phosphate 5-kinase type II betaFASTA viewXML view

General information
DisProt:DP00054
Name:Phosphatidylinositol-4-phosphate 5-kinase type II beta
Synonym(s):PI42B_HUMAN
Phosphatidylinositol-5-phosphate 4-kinase type II beta
1-phosphatidylinositol-5-phosphate 4-kinase 2-beta
PtdIns(5)P-4-kinase isoform 2-beta
PIP4KII-beta
Diphosphoinositide kinase 2-beta
Type II PIP kinase
EC=2.7.1.149
First appeared in release:Release 1.0 (08/01/2003)
UniProt:P78356
UniGene:Hs.260603
SwissProt: PI42B_HUMAN
TrEMBL:  
NCBI (GI): 47605991
Source organism:Homo sapiens (Human)
Sequence length:416
Percent disordered:23%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MSSNCTSTTA VAVAPLSASK TKTKKKHFVC QKVKLFRASE PILSVLMWGV NHTINELSNV - 60
PVPVMLMPDD FKAYSKIKVD NHLFNKENLP SRFKFKEYCP MVFRNLRERF GIDDQDYQNS - 120
VTRSAPINSD SQGRCGTRFL TTYDRRFVIK TVSSEDVAEM HNILKKYHQF IVECHGNTLL - 180
PQFLGMYRLT VDGVETYMVV TRNVFSHRLT VHRKYDLKGS TVAREASDKE KAKDLPTFKD - 240
NDFLNEGQKL HVGEESKKNF LEKLKRDVEF LAQLKIMDYS LLVGIHDVDR AEQEEMEVEE - 300
RAEDEECEND GVGGNLLCSY GTPPDSPGNL LSFPRFFGPG EFDPSVDVYA MKSHESSPKK - 360
EVYFMAIIDI LTPYDTKKKA AHAAKTVKHG AGAEISTVNP EQYSKRFNEF MSNILT



Functional narrative    

Phosphatidylinositol-4-phosphate 5-kinase type II beta (PIP5K2B) plays a key role in signal transduction and membrane trafficking by phosphorylating the inositol ring at specific positions. The phosphorylation of all PIPKs results in a phosphatidylinositol bisphosphate, however, different routes are taken by each type. The type II PIPKs phosphorylate PI3P or PI5P on 4-Hydroxyl. The characterization of an ATP- binding core groups all phosphoinositide kinases into one superfamily. PIP5K2B exists as a homodimer with a basic flat face which suggests electrostatic mechanisms for plasma membrane targeting. It is one of the smallest phosphatidylinositol kinases and is not known to heterodimerize with regulatory subunits.

Region 1: 1-33 Region 2: 130-137 Region 3: 307-341 Region 4: 373-390

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered - Extended
Name:N-Terminal
Location:1 - 33
Length:33
Region sequence:

MSSNCTSTTAVAVAPLSASKTKTKKKHFVCQKV

Modification type: Native
PDB: 1BO1:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (95 K; pH: 5.6; Lithium acetate 100 mM; MPD 5 %; PEG 1000 20 %; Sodium citrate 100 mM)

References:
  1. Rao VD, Misra S, Boronenkov IV, Anderson RA, Hurley JH. "Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation." Cell. 1998; 94(6): 829-839. PubMed: 9753329

Comments:
 



Region 2
Type:Disordered - Extended
Name:G-Loop
Location:130 - 137
Length:8
Region sequence:

DSQGRCGT

Modification type: Native
PDB: 1BO1:A
Structural/functional type: Function arises from the disordered state
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. X-ray crystallography (95 K; pH: 5.6; Lithium acetate 100 mM; MPD 5 %; PEG 1000 20 %; Sodium citrate 100 mM)

References:
  1. Rao VD, Misra S, Boronenkov IV, Anderson RA, Hurley JH. "Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation." Cell. 1998; 94(6): 829-839. PubMed: 9753329

Comments:
The G-loop aids in conformational stabilization of consecutive peptide groups in alignment with each other so that their amide NH groups can interact with the phosphates of ATP.




Region 3
Type:Disordered
Name: 
Location:307 - 341
Length:35
Region sequence:

CENDGVGGNLLCSYGTPPDSPGNLLSFPRFFGPGE

Modification type: Native
PDB: 1BO1:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (lithium acetate 100 mM; MPD 5 %; PEG 1000 20 %; sodium citrate (pH 5.6) 100 mM)

References:
  1. Rao VD, Misra S, Boronenkov IV, Anderson RA, Hurley JH. "Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation." Cell. 1998; 94(6): 829-839. PubMed: 9753329

Comments:
 



Region 4
Type:Disordered
Name: 
Location:373 - 390
Length:18
Region sequence:

PYDTKKKAAHAAKTVKHG

Modification type: Native
PDB: 1BO1:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (lithium acetate 100 mM; MPD 5 %; PEG 1000 20 %; sodium citrate (pH 5.6) 100 mM)

References:
  1. Rao VD, Misra S, Boronenkov IV, Anderson RA, Hurley JH. "Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation." Cell. 1998; 94(6): 829-839. PubMed: 9753329

Comments:
 



References

  1. Castellino AM, Parker GJ, Boronenkov IV, Anderson RA, Chao MV. "A novel interaction between the juxtamembrane region of the p55 tumor necrosis factor receptor and phosphatidylinositol-4-phosphate 5-kinase." J Biol Chem. 1997; 272(9): 5861-70. PubMed: 9038203


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