Q5REW0 (VIP2_PONAB) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 41.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 EC=2.7.4.21 EC=2.7.4.24 Alternative name(s): Diphosphoinositol pentakisphosphate kinase 2 Histidine acid phosphatase domain-containing protein 1 InsP6 and PP-IP5 kinase 2 VIP1 homolog 2 | ||||
| Gene names |
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| Organism | Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome] | ||||
| Taxonomic identifier | 9601 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo |
Protein attributes
| Sequence length | 1244 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation. Phosphorylates inositol hexakisphosphate (InsP6) at positions 1 or 3 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates at position 1 or 3 PP-InsP5, produced by IP6Ks from InsP6, to produce (PP)2-InsP4 By similarity. |
| Catalytic activity | ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate. ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol diphosphate tetrakisphosphate (isomeric configuration unknown). ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate (isomeric configuration unknown). |
| Subcellular location | |
| Domain | The polyphosphoinositide-binding domain mediates binding of PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the phosphatase domain of histidine acid phosphatases, it has no phosphatase activity By similarity. |
| Sequence similarities | Belongs to the histidine acid phosphatase family. VIP1 subfamily. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1244 | 1244 | Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 | PRO_0000315694 | |||||
Regions | |||||||||
| Nucleotide binding | 237 – 240 | 4 | ATP By similarity | ||||||
| Nucleotide binding | 246 – 248 | 3 | ATP By similarity | ||||||
| Nucleotide binding | 321 – 323 | 3 | ATP By similarity | ||||||
| Region | 53 – 54 | 2 | Substrate binding By similarity | ||||||
| Region | 213 – 214 | 2 | Substrate binding By similarity | ||||||
| Region | 326 – 329 | 4 | Substrate binding By similarity | ||||||
| Region | 371 – 442 | 72 | Polyphosphoinositide-binding domain By similarity | ||||||
Sites | |||||||||
| Binding site | 134 | 1 | ATP By similarity | ||||||
| Binding site | 187 | 1 | ATP By similarity | ||||||
| Binding site | 194 | 1 | ATP By similarity | ||||||
| Binding site | 213 | 1 | ATP By similarity | ||||||
| Binding site | 248 | 1 | Substrate By similarity | ||||||
| Binding site | 262 | 1 | Substrate By similarity | ||||||
| Binding site | 264 | 1 | ATP By similarity | ||||||
| Binding site | 309 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 38 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 217 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 220 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1007 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1017 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1173 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1181 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR857406 mRNA. Translation: CAH89697.1. |
| UniGene | Pab.19436. |
3D structure databases | |
| ProteinModelPortal | Q5REW0. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG108657. |
Family and domain databases | |
| InterPro | IPR000560. His_Pase_superF_clade-2. [Graphical view] |
| Pfam | PF00328. His_Phos_2. 1 hit. [Graphical view] |
| PROSITE | PS00616. HIS_ACID_PHOSPHAT_1. 1 hit. PS00778. HIS_ACID_PHOSPHAT_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | VIP2_PONAB | ||||||||
| Accession | Primary (citable) accession number: Q5REW0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |