H7C398 · H7C398_HUMAN
- ProteinInositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1
- GenePPIP5K1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids259 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
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 position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Activated when cells are exposed to hyperosmotic stress.
Catalytic activity
- 1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ADPThis reaction proceeds in the forward direction.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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 |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionH7C398
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 37 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 142 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 161 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 162 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 175 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 185 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 204 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 235 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 113-259 | Disordered | ||||
Sequence: GVEEEGSAPAGCGFRPASSENEEMKTNQGSMENLCPGKASDEPDRALQTSPQPPEGPGLPRRSPLIRNRKAGSMEVLSETSSSRPGGYRLFSSSRPPTEMKQSGLGSQCTGLFSTTVLGGSSSAPNLQDYARSHGKKLPPASLKHRD | ||||||
Compositional bias | 132-146 | Polar residues | ||||
Sequence: ENEEMKTNQGSMENL | ||||||
Compositional bias | 186-241 | Polar residues | ||||
Sequence: MEVLSETSSSRPGGYRLFSSSRPPTEMKQSGLGSQCTGLFSTTVLGGSSSAPNLQD |
Sequence similarities
Belongs to the histidine acid phosphatase family. VIP1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Length259
- Mass (Da)28,626
- Last updated2012-04-18 v1
- Checksum940FADE0796742AC
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q6PFW1 | VIP1_HUMAN | PPIP5K1 | 1433 | ||
C9J5E6 | C9J5E6_HUMAN | PPIP5K1 | 114 | ||
C9J490 | C9J490_HUMAN | PPIP5K1 | 71 | ||
A0A2R8YGT1 | A0A2R8YGT1_HUMAN | PPIP5K1 | 499 | ||
C9JZX6 | C9JZX6_HUMAN | PPIP5K1 | 133 | ||
F8W9A8 | F8W9A8_HUMAN | PPIP5K1 | 1409 | ||
H0Y3Y5 | H0Y3Y5_HUMAN | PPIP5K1 | 196 | ||
A0A9L9PYJ9 | A0A9L9PYJ9_HUMAN | PPIP5K1 | 1458 | ||
H7C436 | H7C436_HUMAN | PPIP5K1 | 118 | ||
B7WPL9 | B7WPL9_HUMAN | PPIP5K1 | 1429 | ||
A0A8J8ZH50 | A0A8J8ZH50_HUMAN | PPIP5K1 | 1490 |
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: X | ||||||
Compositional bias | 132-146 | Polar residues | ||||
Sequence: ENEEMKTNQGSMENL | ||||||
Compositional bias | 186-241 | Polar residues | ||||
Sequence: MEVLSETSSSRPGGYRLFSSSRPPTEMKQSGLGSQCTGLFSTTVLGGSSSAPNLQD | ||||||
Non-terminal residue | 259 | |||||
Sequence: D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC011330 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC019011 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |