VIP1 BASIC INFORMATION
| Standard Name | VIP1 1 |
|---|---|
| Systematic Name | YLR410W |
| Feature Type | ORF, Verified |
| Description | Inositol hexakisphosphate (IP6) and inositol heptakisphosphate (IP7) kinase; generation of IP7 by Vip1p is important for phosphate signaling; likely involved in cortical actin cytoskeleton function, by analogy with S. pombe ortholog asp1 (1, 2, 3 and see Summary Paragraph)
|
| GO Annotations | All VIP1 GO evidence and references |
|---|---|
| View Computational GO annotations for VIP1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| High-throughput |
| Pathways |
|---|
| Mutant Phenotype | All VIP1 Phenotype details and references |
|---|---|
| Classical genetics | |
| null | |
| Large-scale survey | |
| null |
|
| overexpression |
| Interactions | VIP1 All interactions details and references |
|---|---|
| 90 total interaction(s) for 82 unique genes/features. | |
| Physical Interactions |
|
| Genetic Interactions |
|
| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000004402 |
|---|
ADDITIONAL INFORMATION for VIP1
SUMMARY PARAGRAPH for VIP1
VIP1 encodes one of two yeast inositol pyrophosphate synthases (also known as inositol hexakisphophate kinases; IP6Ks); the other is encoded by KCS1. The inositol pyrophosphates (PP-IPs) produced by Kcs1p and/or Vip1p serve as high-energy signaling molecules involved in such diverse processes as vacuolar biogenesis, the stress response, DNA repair, cell wall synthesis, telomere maintenance, and phosphate homeostasis (see 4, 5, 6, and references therein).
Both enzymes catalyze the addition of beta-phosphate to the fully phosphorylated six-carbon ring of inositol hexakisphosphate (IP6). However, these enzymes produce different isomers of diphosphoinositol pentakisphosphate (IP7). Kcs1p phosphorylates IP6 at the C5 position forming 5PP-IP5, and Vip1p phosphorylates IP6 at the C4 or C6 position forming 4PP-IP5 or 6PP-IP5, respectively (the exact phosphorylation position has not yet been determined). The different IP7 isomers are biologically relevant: the Kcs1p product cannot substitute for the Vip1p product during phosphate homeostasis (2). Kcs1p and Vip1p also work in concert to produce bis-diphosphoinositol tetrakisphosphate ([PP]2-IP4; IP8). Kcs1p phosphorylates the Vip1p IP7 product 4/6PP-IP5, and Vip1p phosphorylates the Kcs1p IP7 product 5PP-IP5 (3).
Inositol pyrophosphate synthases are highly conserved and found across eukaryotes. In humans, three Kcs1p-like enzymes (IHPK1/IP6K1, IP6K2/IP6K2, IP6K3/IP6K3) (7, 8) and two Vip1p-like enzymes (HISPPD2a/PPIP5K1/VIP1 and PPIP5K2/VIP2) (9, 10) have been identified.
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for VIP1]
| 1) | Feoktistova A, et al. (1999) Identification and characterization of Schizosaccharomyces pombe asp1(+), a gene that interacts with mutations in the Arp2/3 complex and actin. Genetics 152(3):895-908 |
| 2) | Lee YS, et al. (2007) Regulation of a cyclin-CDK-CDK inhibitor complex by inositol pyrophosphates. Science 316(5821):109-12 |
| 3) | Mulugu S, et al. (2007) A conserved family of enzymes that phosphorylate inositol hexakisphosphate. Science 316(5821):106-9 |
| 4) | Bennett M, et al. (2006) Inositol pyrophosphates: metabolism and signaling. Cell Mol Life Sci 63(5):552-64 |
| 5) | Onnebo SM and Saiardi A (2007) Inositol pyrophosphates get the vip1 treatment. Cell 129(4):647-9 |
| 6) | Bhandari R, et al. (2007) Inositol pyrophosphate pyrotechnics. Cell Metab 5(5):321-3 |
| 7) | Saiardi A, et al. (1999) Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases. Curr Biol 9(22):1323-6 |
| 8) | Saiardi A, et al. (2001) Identification and characterization of a novel inositol hexakisphosphate kinase. J Biol Chem 276(42):39179-85 |
| 9) | Fridy PC, et al. (2007) Cloning and Characterization of Two Human VIP1-like Inositol Hexakisphosphate and Diphosphoinositol Pentakisphosphate Kinases. J Biol Chem 282(42):30754-62 |
| 10) | Choi JH, et al. (2007) Purification, sequencing, and molecular identification of a mammalian PP-InsP5 kinase that is activated when cells are exposed to hyperosmotic stress. J Biol Chem 282(42):30763-75 |





