A0A5P1FAS3 · A0A5P1FAS3_ASPOF
- ProteinInositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1461 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Bifunctional inositol kinase that acts in concert with the IP6K kinases 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, may regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, and exocytosis. Phosphorylates inositol hexakisphosphate (InsP6).
Catalytic activity
- 1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ADP
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | diphosphoinositol-pentakisphosphate kinase activity | |
Molecular Function | inositol heptakisphosphate kinase activity | |
Molecular Function | inositol hexakisphosphate 1-kinase activity | |
Molecular Function | inositol hexakisphosphate 3-kinase activity | |
Molecular Function | inositol hexakisphosphate 5-kinase activity | |
Molecular Function | inositol-1,3,4,5,6-pentakisphosphate kinase activity | |
Biological Process | inositol metabolic process | |
Biological Process | inositol phosphate biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Asparagales > Asparagaceae > Asparagoideae > Asparagus
Accessions
- Primary accessionA0A5P1FAS3
Proteomes
Genome annotation databases
Subcellular Location
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 302-415 | Disordered | ||||
Sequence: SYKEDEQGESQAVESSGDQSSPPNESENVDETQIPSGDSLTVQQEQERVETDMERSQRDPDHKEQQQYIPRRGYQNQRGGRGGGGGARRGYPNGRVGRGGRGGGSGRYQNGQNQ | ||||||
Compositional bias | 313-345 | Polar residues | ||||
Sequence: AVESSGDQSSPPNESENVDETQIPSGDSLTVQQ | ||||||
Compositional bias | 346-369 | Basic and acidic residues | ||||
Sequence: EQERVETDMERSQRDPDHKEQQQY | ||||||
Domain | 442-523 | VIP1 N-terminal | ||||
Sequence: RHKVFSAPMGQILDRLQAFGEFEVIFFGDKVILEEPVENWPICDCLIAFHSTGYPLKKAEMYAALRKPFLVNELEPQYLLHD | ||||||
Region | 1229-1271 | Disordered | ||||
Sequence: KKEEGDTPRHQNKSEDRRSSSTSERSLEQDDDEDKETKYRLDP |
Sequence similarities
Belongs to the histidine acid phosphatase family. VIP1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,461
- Mass (Da)165,610
- Last updated2020-02-26 v1
- Checksum582F740C8AB856BC
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 313-345 | Polar residues | ||||
Sequence: AVESSGDQSSPPNESENVDETQIPSGDSLTVQQ | ||||||
Compositional bias | 346-369 | Basic and acidic residues | ||||
Sequence: EQERVETDMERSQRDPDHKEQQQY |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM007383 EMBL· GenBank· DDBJ | ONK75272.1 EMBL· GenBank· DDBJ | Genomic DNA |