Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1 (P40485)

Identification
NamePhosphatidylinositol 4,5-bisphosphate-binding protein SLM1
Synonyms
  • Synthetic lethal with MSS4 protein 1
  • TORC2 effector protein SLM1
Gene NameSLM1
Enzyme ClassNot Available
Biological Properties
General FunctionInvolved in identical protein binding
Specific FunctionTogether with SLM2, effector of the TORC2- and calcineurin-signaling pathways. Phosphorylated and activated by TORC2 under favorable growth conditions. Mediates actin polarization via inhibition of calcineurin-dependent transcription. Upon nutrient limitation or environmental stress, gets dephosphorylated by calcineurin. Dephosphorylation inhibits its interaction with TORC2, thereby antagonizing TORC2 signaling and mediating calcineurin-dependent actin depolarization. Also functions in heat-induced, calcineurin-mediated uracil permease (FUR4) endocytosis
Cellular LocationCell membrane; Peripheral membrane protein; Cytoplasmic side.
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
GO ClassificationNot Available
Gene Properties
Chromosome LocationNot Available
Locus
Gene Sequence>2061 bp ATGTCGAAAAACAACACAATGACCTCTGCGGTCTCTGATATGCTGTCACAGCAACAGCTA AATCTTCAGCACCTGCATAACTTGCAGCAGCATACGAGAAGTATGACTTCAGCAGATCAT GCCAACGTTTTACAACAACAGCAACAACAACAACAACAACAACAGCAGCAGCAGCAGCAA CAGCAGCAGAGCGCAAGCTTTCAAAATGGCAGTTTGACATCCGATATAAACCAACAAAGC TATTTGAATGGACAACCAGTTCCTTCCACTAGTAATTCAACGTTTCAAAACAATAGGACG CTGACGATGAATTCTGGAGGGTTGCAAGGTATCATAAGCAATGGTTCTCCTAATATCGAC TCGAACACCAATGTAACCATTGCTGTCCCAGATCCCAATAATAACAACGGGAAACAGCTC CAAGGGAAAAACTCTTTAACCAACACTTCAATACTGTCGAGGGCTAGGTCTTCCTTACAA CGTCAAAGACTTGCTCAGCAACAGCAACAACAACAAGATCCTAGATCTCCATTAGTAATA CTGGTCCCTACAGCTGCGCAACCAACAGATATTCTTGCAGCGAGGTTTTCAGCTTGGAGA AATGTCATCAAGTCGGTGATCGTTTACTTAACAGAAATCGCTTCTATTCAGGATGAAATT GTTAGACAGCAACTAAGATTATCACATGCTGTACAATTCCCATTCTTTTCGATCGAGAAT CAATACCAACCAAGCTCGCAGGAGGATAAATCAGTACAAAAGTTTTTTTTGCCATTGGGT AATGGCTCGATACAGGACTTACCAACAATTTTGAACCAGTATCATGAATCCCTAGCATCC AGCGCGTCTAAGGCATCAAGGGAATTGACCAATGATGTTATTCCTCGTTTGGAAGACTTG AGGAGAGATCTAATAGTCAAGATAAAGGAAATAAAATCACTGCAGTCGGATTTCAAAAAT TCTTGTTCCAAAGAGTTACAACAAACAAAACAGGCCATGAAGCAATTTCAGGAGTCTTTA AAGGATGCGCGCTATTCAGTGCCAAAACAAGATCCATTCTTAACCAAGCTGGCGCTTGAT AGACAAATTAAAAAGCAACTTCAGGAGGAAAACTTTCTGCATGAAGCTTTTGATAATTTA GAGACTTCAGGCGCTGAATTAGAAAAAATTGTAGTTATGGAAATTCAAAACTCTTTAACA ATATATGCCAGATTACTGGGACAAGAAGCACAATTGGTTTTCGATATATTGATATCCAAA TTAGATTCTGGATTTTTCAACGTTGACCCACAATTTGAATGGGATAACTTCATTTCAAGG GATCCCAACTTTTTATTGCCTAATCTACCGATGAGGACATTCAAAGAAATCGTTTACAAA TACCAATTCGATCCTTTGACTTATGAAATCAAATCAGGGTTTTTAGAAAGAAGATCAAAA TTTCTAAAATCCTATTCAAAAGGGTATTATGTGCTGACACCGAACTTTTTACATGAATTC AAGACCGCGGACAGAAAAAAAGATTTAGTACCAGTGATGTCGTTAGCATTAAGTGAATGT ACTGTGACGGAACATTCCCGGAAAAACAGTACATCATCACCAAATTCGACTGGTTCGGAT GCTAAGTTTGTGTTGCATGCTAAGCAAAACGGCATAATTCGTCGTGGTCACAATTGGGTT TTTAAAGCCGATTCTTATGAATCAATGATGTCTTGGTTTGATAATTTGAAGATCTTAACA TCTACTTCGAATATACAAGACAAGTATAAATTCATAACACAAAAATTAAACTTGAATTCA GATGGGAAACCCAAGCTAACCAATAACCATACCAGCATTAATAAGTATCAGCTGAGTAAT GCCAATAGCACAATGGTAGAAAATGATGAAAACGATGATATAAATAGTAATTATGTGGGG TCCACGGTAACACCAAAATTGGACAATCAAACAAATACGAATACATCCATGTCTTCATTA CCTGATACTAATGATTCTGAATTACAAGATCAAGTTCCCAATATTTATATTCAAACTCCA ATAAACGATTTCAAATCATAA
Protein Properties
Pfam Domain Function
Protein Residues686
Protein Molecular Weight77994.70313
Protein Theoretical pI8.19
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1 MSKNNTMTSAVSDMLSQQQLNLQHLHNLQQHTRSMTSADHANVLQQQQQQQQQQQQQQQQ QQQSASFQNGSLTSDINQQSYLNGQPVPSTSNSTFQNNRTLTMNSGGLQGIISNGSPNID SNTNVTIAVPDPNNNNGKQLQGKNSLTNTSILSRARSSLQRQRLAQQQQQQQDPRSPLVI LVPTAAQPTDILAARFSAWRNVIKSVIVYLTEIASIQDEIVRQQLRLSHAVQFPFFSIEN QYQPSSQEDKSVQKFFLPLGNGSIQDLPTILNQYHESLASSASKASRELTNDVIPRLEDL RRDLIVKIKEIKSLQSDFKNSCSKELQQTKQAMKQFQESLKDARYSVPKQDPFLTKLALD RQIKKQLQEENFLHEAFDNLETSGAELEKIVVMEIQNSLTIYARLLGQEAQLVFDILISK LDSGFFNVDPQFEWDNFISRDPNFLLPNLPMRTFKEIVYKYQFDPLTYEIKSGFLERRSK FLKSYSKGYYVLTPNFLHEFKTADRKKDLVPVMSLALSECTVTEHSRKNSTSSPNSTGSD AKFVLHAKQNGIIRRGHNWVFKADSYESMMSWFDNLKILTSTSNIQDKYKFITQKLNLNS DGKPKLTNNHTSINKYQLSNANSTMVENDENDDINSNYVGSTVTPKLDNQTNTNTSMSSL PDTNDSELQDQVPNIYIQTPINDFKS
References
External Links
ResourceLink
Saccharomyces Genome Database SLM1
Uniprot IDP40485
Uniprot NameSLM1_YEAST
GenBank Gene IDZ38125
Genebank Protein ID558701
General Reference
  • Churcher, C., Bowman, S., Badcock, K., Bankier, A., Brown, D., Chillingworth, T., Connor, R., Devlin, K., Gentles, S., Hamlin, N., Harris, D., Horsnell, T., Hunt, S., Jagels, K., Jones, M., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Rowley, N., Skelton, J., Smith, V., Barrell, B., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Nature 387:84-87.9169870
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Audhya, A., Loewith, R., Parsons, A. B., Gao, L., Tabuchi, M., Zhou, H., Boone, C., Hall, M. N., Emr, S. D. (2004). "Genome-wide lethality screen identifies new PI4,5P2 effectors that regulate the actin cytoskeleton." EMBO J 23:3747-3757.15372071
  • Yu, J. W., Mendrola, J. M., Audhya, A., Singh, S., Keleti, D., DeWald, D. B., Murray, D., Emr, S. D., Lemmon, M. A. (2004). "Genome-wide analysis of membrane targeting by S. cerevisiae pleckstrin homology domains." Mol Cell 13:677-688.15023338
  • Fadri, M., Daquinag, A., Wang, S., Xue, T., Kunz, J. (2005). "The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-bisphosphate and TORC2." Mol Biol Cell 16:1883-1900.15689497
  • Mulet, J. M., Martin, D. E., Loewith, R., Hall, M. N. (2006). "Mutual antagonism of target of rapamycin and calcineurin signaling." J Biol Chem 281:33000-33007.16959779
  • Bultynck, G., Heath, V. L., Majeed, A. P., Galan, J. M., Haguenauer-Tsapis, R., Cyert, M. S. (2006). "Slm1 and slm2 are novel substrates of the calcineurin phosphatase required for heat stress-induced endocytosis of the yeast uracil permease." Mol Cell Biol 26:4729-4745.16738335
  • Smolka, M. B., Albuquerque, C. P., Chen, S. H., Zhou, H. (2007). "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Proc Natl Acad Sci U S A 104:10364-10369.17563356
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956