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
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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.
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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.
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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:
- X-ray crystallography (95 K; pH: 5.6; Lithium acetate 100 mM; MPD 5 %; PEG 1000 20 %; Sodium citrate 100 mM)
| References:
- 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:
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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:
- X-ray crystallography (95 K; pH: 5.6; Lithium acetate 100 mM; MPD 5 %; PEG 1000 20 %; Sodium citrate 100 mM)
| References:
- 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.
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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:
- X-ray crystallography (lithium acetate 100 mM; MPD 5 %; PEG 1000 20 %; sodium citrate (pH 5.6) 100 mM)
| References:
- 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:
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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:
- X-ray crystallography (lithium acetate 100 mM; MPD 5 %; PEG 1000 20 %; sodium citrate (pH 5.6) 100 mM)
| References:
- 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:
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References |
- 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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