SKIP

For other uses, see Skip (disambiguation).

INPP5K
Identifiers
Aliases	INPP5K , PPS, SKIP, inositol polyphosphate-5-phosphatase K, MDCCAID
External IDs	OMIM: 607875; MGI: 1194899; HomoloGene: 75059; GeneCards: INPP5K; OMA:INPP5K - orthologs
Gene location (Human) Chr. Chromosome 17 (human) [1] Band 17p13.3 Start 1,494,577 bp [1] End 1,516,742 bp [1]
Gene location (Mouse) Chr. Chromosome 11 (mouse) [2] Band 11 B5|11 45.92 cM Start 75,521,814 bp [2] End 75,539,697 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in retinal pigment epithelium right lung right lobe of thyroid gland left lobe of thyroid gland apex of heart granulocyte skin of leg upper lobe of left lung gastric mucosa skin of abdomen Top expressed in retinal pigment epithelium spermatocyte spermatid granulocyte parotid gland thymus olfactory epithelium right lung right lung lobe neural layer of retina More reference expression data BioGPS More reference expression data
Gene ontology Molecular function inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity inositol-1,4,5-trisphosphate 5-phosphatase activity inositol bisphosphate phosphatase activity inositol-polyphosphate 5-phosphatase activity phosphatidylinositol phosphate 5-phosphatase activity phosphatidylinositol trisphosphate phosphatase activity protein binding lipid phosphatase activity inositol trisphosphate phosphatase activity hydrolase activity vasopressin receptor activity phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Cellular component cytoplasm cytosol membrane ruffle plasma membrane ruffle membrane trans-Golgi network endoplasmic reticulum perinuclear region of cytoplasm neuron projection nucleus Biological process negative regulation of protein phosphorylation G protein-coupled receptor signaling pathway negative regulation of protein kinase B signaling positive regulation of urine volume negative regulation of dephosphorylation negative regulation of protein kinase activity glucose homeostasis cellular response to tumor necrosis factor negative regulation of peptidyl-threonine phosphorylation in utero embryonic development negative regulation of glycogen biosynthetic process positive regulation of renal water transport cellular response to epidermal growth factor stimulus positive regulation of transcription, DNA-templated response to insulin negative regulation of insulin receptor signaling pathway negative regulation of protein targeting to membrane cellular response to hormone stimulus negative regulation of glucose transmembrane transport negative regulation of glycogen (starch) synthase activity phosphatidylinositol dephosphorylation negative regulation of MAP kinase activity negative regulation of calcium ion transport negative regulation of peptidyl-serine phosphorylation cellular response to insulin stimulus phosphatidylinositol biosynthetic process regulation of glycogen biosynthetic process negative regulation of stress fiber assembly negative regulation of transcription, DNA-templated ruffle assembly inositol phosphate dephosphorylation actin cytoskeleton organization cellular response to cAMP dephosphorylation negative regulation of single stranded viral RNA replication via double stranded DNA intermediate protein localization to plasma membrane negative regulation by host of viral transcription neuromuscular junction development, skeletal muscle fiber Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 51763 19062 Ensembl ENSG00000132376 ENSMUSG00000006127 UniProt Q9BT40 Q8C5L6 RefSeq (mRNA) NM_001135642 NM_016532 NM_130766 NM_008916 RefSeq (protein) NP_001129114 NP_057616 NP_570122 NP_032942 Location (UCSC) Chr 17: 1.49 – 1.52 Mb Chr 11: 75.52 – 75.54 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

SKIP is an acronym for Skeletal muscle and kidney enriched inositol phosphatase, which is a human gene. ^[5]

Function

This gene encodes a protein with 5-phosphatase activity toward polyphosphate inositol. The protein localizes to the cytosol in regions lacking actin stress fibers. It is thought that this protein may negatively regulate the actin cytoskeleton. Alternative splicing of this gene results in two transcript variants encoding different isoforms. ^[5] Overexpression of SKIP in mice affects osmoregulation in kidney collecting ducts. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000132376 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000006127 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: SKIP skeletal muscle and kidney enriched inositol phosphatase".
6. Pernot E, Terryn S, Cheong SC, Markadieu N, Janas S, Blockmans M, Jacoby M, Pouillon V, Gayral S, Rossier BC, Beauwens R, Erneux C, Devuyst O, Schurmans S (Dec 2011). "The inositol Inpp5k 5-phosphatase affects osmoregulation through the vasopressin-aquaporin 2 pathway in the collecting system" (PDF). Pflügers Archiv. 462 (6): 871–83. doi:10.1007/s00424-011-1028-0. PMID   21938401. S2CID   27923688.

Further reading

• Drayer AL, Pesesse X, De Smedt F, Communi D, Moreau C, Erneux C (Nov 1996). "The family of inositol and phosphatidylinositol polyphosphate 5-phosphatases". Biochemical Society Transactions. 24 (4): 1001–5. doi:10.1042/bst0241001. PMID   8968500.
• Mitchell CA, Brown S, Campbell JK, Munday AD, Speed CJ (Nov 1996). "Regulation of second messengers by the inositol polyphosphate 5-phosphatases". Biochemical Society Transactions. 24 (4): 994–1000. doi:10.1042/bst0240994. PMID   8968499.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC   1847948 . PMID   17353931.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• Chen J, Xu J, Zhao W, Hu G, Cheng H, Kang Y, Xie Y, Lu Y (Nov 2005). "Characterization of human LNX, a novel ligand of Numb protein X that is downregulated in human gliomas". The International Journal of Biochemistry & Cell Biology. 37 (11): 2273–83. doi:10.1016/j.biocel.2005.02.028. PMID   16002321.
• Cardoso C, Leventer RJ, Ward HL, Toyo-Oka K, Chung J, Gross A, Martin CL, Allanson J, Pilz DT, Olney AH, Mutchinick OM, Hirotsune S, Wynshaw-Boris A, Dobyns WB, Ledbetter DH (Apr 2003). "Refinement of a 400-kb critical region allows genotypic differentiation between isolated lissencephaly, Miller-Dieker syndrome, and other phenotypes secondary to deletions of 17p13.3". American Journal of Human Genetics. 72 (4): 918–30. doi:10.1086/374320. PMC   1180354 . PMID   12621583.
• Ijuin T, Takenawa T (Feb 2003). "SKIP negatively regulates insulin-induced GLUT4 translocation and membrane ruffle formation". Molecular and Cellular Biology. 23 (4): 1209–20. doi:10.1128/MCB.23.4.1209-1220.2003. PMC   141139 . PMID   12556481.
• Gurung R, Tan A, Ooms LM, McGrath MJ, Huysmans RD, Munday AD, Prescott M, Whisstock JC, Mitchell CA (Mar 2003). "Identification of a novel domain in two mammalian inositol-polyphosphate 5-phosphatases that mediates membrane ruffle localization. The inositol 5-phosphatase skip localizes to the endoplasmic reticulum and translocates to membrane ruffles following epidermal growth factor stimulation". The Journal of Biological Chemistry. 278 (13): 11376–85. doi: 10.1074/jbc.M209991200 . PMID   12536145.
• Ijuin T, Mochizuki Y, Fukami K, Funaki M, Asano T, Takenawa T (Apr 2000). "Identification and characterization of a novel inositol polyphosphate 5-phosphatase". The Journal of Biological Chemistry. 275 (15): 10870–5. doi: 10.1074/jbc.275.15.10870 . PMID   10753883.