Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Miscellaneous

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "An in vivo map of the yeast protein interactome."
    Tarassov K., Messier V., Landry C.R., Radinovic S., Serna Molina M.M., Shames I., Malitskaya Y., Vogel J., Bussey H., Michnick S.W.
    Science 320:1465-1470(2008) [PubMed] [Europe PMC] [Abstract]
  • "High-quality binary protein interaction map of the yeast interactome network."
    Yu H., Braun P., Yildirim M.A., Lemmens I., Venkatesan K., Sahalie J., Hirozane-Kishikawa T., Gebreab F., Li N., Simonis N., Hao T., Rual J.F., Dricot A., Vazquez A., Murray R.R., Simon C., Tardivo L., Tam S.

    , Svrzikapa N., Fan C., de Smet A.S., Motyl A., Hudson M.E., Park J., Xin X., Cusick M.E., Moore T., Boone C., Snyder M., Roth F.P., Barabasi A.L., Tavernier J., Hill D.E., Vidal M.
    Science 322:104-110(2008) [PubMed] [Europe PMC] [Abstract]
  • "Plasma membrane recruitment and activation of the AGC kinase Ypk1 is mediated by target of rapamycin complex 2 (TORC2) and its effector proteins Slm1 and Slm2."
    Niles B.J., Mogri H., Hill A., Vlahakis A., Powers T.
    Proc Natl Acad Sci U S A 109:1536-1541(2012) [PubMed] [Europe PMC] [Abstract]
  • "The role of structural pleiotropy and regulatory evolution in the retention of heteromers of paralogs."
    Marchant A., Cisneros A.F., Dube A.K., Gagnon-Arsenault I., Ascencio D., Jain H., Aube S., Eberlein C., Evans-Yamamoto D., Yachie N., Landry C.R.
    Elife 8:0-0(2019) [PubMed] [Europe PMC] [Abstract]
• phosphatidylinositol-4,5-bisphosphate binding Source: SGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.6

    "The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-bisphosphate and TORC2."
    Fadri M., Daquinag A., Wang S., Xue T., Kunz J.
    Mol. Biol. Cell 16:1883-1900(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, PHOSPHOINOSITIDE-BINDING, INTERACTION WITH AVO2; BIT2; BIT61 AND TOR2, SUBCELLULAR LOCATION, MUTAGENESIS OF 477-ARG-ARG-478; LYS-483 AND LYS-487.
  • "A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae."
    Gallego O., Betts M.J., Gvozdenovic-Jeremic J., Maeda K., Matetzki C., Aguilar-Gurrieri C., Beltran-Alvarez P., Bonn S., Fernandez-Tornero C., Jensen L.J., Kuhn M., Trott J., Rybin V., Muller C.W., Bork P., Kaksonen M., Russell R.B., Gavin A.C.
    Mol Syst Biol 6:430-430(2010) [PubMed] [Europe PMC] [Abstract]
• sphingolipid binding Source: SGDInferred from direct assayⁱ
  • "A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae."
    Gallego O., Betts M.J., Gvozdenovic-Jeremic J., Maeda K., Matetzki C., Aguilar-Gurrieri C., Beltran-Alvarez P., Bonn S., Fernandez-Tornero C., Jensen L.J., Kuhn M., Trott J., Rybin V., Muller C.W., Bork P., Kaksonen M., Russell R.B., Gavin A.C.
    Mol Syst Biol 6:430-430(2010) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• actin cytoskeleton organization Source: SGD <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • Ref.4

    "Genome-wide lethality screen identifies new PI4,5P2 effectors that regulate the actin cytoskeleton."
    Audhya A., Loewith R., Parsons A.B., Gao L., Tabuchi M., Zhou H., Boone C., Hall M.N., Emr S.D.
    EMBO J. 23:3747-3757(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION BY TORC2, MUTAGENESIS OF LYS-483 AND LYS-487, INTERACTION WITH SLM2 AND AVO2.
  • Ref.6

    "The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-bisphosphate and TORC2."
    Fadri M., Daquinag A., Wang S., Xue T., Kunz J.
    Mol. Biol. Cell 16:1883-1900(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, PHOSPHOINOSITIDE-BINDING, INTERACTION WITH AVO2; BIT2; BIT61 AND TOR2, SUBCELLULAR LOCATION, MUTAGENESIS OF 477-ARG-ARG-478; LYS-483 AND LYS-487.
• actin filament bundle assembly Source: SGDInferred from genetic interactionⁱ
  • Ref.6

    "The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-bisphosphate and TORC2."
    Fadri M., Daquinag A., Wang S., Xue T., Kunz J.
    Mol. Biol. Cell 16:1883-1900(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, PHOSPHOINOSITIDE-BINDING, INTERACTION WITH AVO2; BIT2; BIT61 AND TOR2, SUBCELLULAR LOCATION, MUTAGENESIS OF 477-ARG-ARG-478; LYS-483 AND LYS-487.
• eisosome assembly Source: SGDInferred from genetic interactionⁱ
  • "Requirements of Slm proteins for proper eisosome organization, endocytic trafficking and recycling in the yeast Saccharomyces cerevisiae."
    Kamble C., Jain S., Murphy E., Kim K.
    J Biosci 36:79-96(2011) [PubMed] [Europe PMC] [Abstract]
• endosomal transport Source: SGDInferred from genetic interactionⁱ
  • "Requirements of Slm proteins for proper eisosome organization, endocytic trafficking and recycling in the yeast Saccharomyces cerevisiae."
    Kamble C., Jain S., Murphy E., Kim K.
    J Biosci 36:79-96(2011) [PubMed] [Europe PMC] [Abstract]
• establishment or maintenance of actin cytoskeleton polarity Source: SGDInferred from physical interactionⁱ
  • Ref.6

    "The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-bisphosphate and TORC2."
    Fadri M., Daquinag A., Wang S., Xue T., Kunz J.
    Mol. Biol. Cell 16:1883-1900(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, PHOSPHOINOSITIDE-BINDING, INTERACTION WITH AVO2; BIT2; BIT61 AND TOR2, SUBCELLULAR LOCATION, MUTAGENESIS OF 477-ARG-ARG-478; LYS-483 AND LYS-487.
• protein localization to plasma membrane Source: SGDInferred from genetic interactionⁱ
  • "Plasma membrane recruitment and activation of the AGC kinase Ypk1 is mediated by target of rapamycin complex 2 (TORC2) and its effector proteins Slm1 and Slm2."
    Niles B.J., Mogri H., Hill A., Vlahakis A., Powers T.
    Proc Natl Acad Sci U S A 109:1536-1541(2012) [PubMed] [Europe PMC] [Abstract]
• regulation of cell growth Source: SGDInferred from genetic interactionⁱ
  • Ref.6

    "The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-bisphosphate and TORC2."
    Fadri M., Daquinag A., Wang S., Xue T., Kunz J.
    Mol. Biol. Cell 16:1883-1900(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, PHOSPHOINOSITIDE-BINDING, INTERACTION WITH AVO2; BIT2; BIT61 AND TOR2, SUBCELLULAR LOCATION, MUTAGENESIS OF 477-ARG-ARG-478; LYS-483 AND LYS-487.
• TORC2 signaling Source: InterPro
• TOR signaling Source: SGDInferred from physical interactionⁱ
  • Ref.6

    "The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-bisphosphate and TORC2."
    Fadri M., Daquinag A., Wang S., Xue T., Kunz J.
    Mol. Biol. Cell 16:1883-1900(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, PHOSPHOINOSITIDE-BINDING, INTERACTION WITH AVO2; BIT2; BIT61 AND TOR2, SUBCELLULAR LOCATION, MUTAGENESIS OF 477-ARG-ARG-478; LYS-483 AND LYS-487.

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "An in vivo map of the yeast protein interactome."
    Tarassov K., Messier V., Landry C.R., Radinovic S., Serna Molina M.M., Shames I., Malitskaya Y., Vogel J., Bussey H., Michnick S.W.
    Science 320:1465-1470(2008) [PubMed] [Europe PMC] [Abstract]
  • "High-quality binary protein interaction map of the yeast interactome network."
    Yu H., Braun P., Yildirim M.A., Lemmens I., Venkatesan K., Sahalie J., Hirozane-Kishikawa T., Gebreab F., Li N., Simonis N., Hao T., Rual J.F., Dricot A., Vazquez A., Murray R.R., Simon C., Tardivo L., Tam S.

    , Svrzikapa N., Fan C., de Smet A.S., Motyl A., Hudson M.E., Park J., Xin X., Cusick M.E., Moore T., Boone C., Snyder M., Roth F.P., Barabasi A.L., Tavernier J., Hill D.E., Vidal M.
    Science 322:104-110(2008) [PubMed] [Europe PMC] [Abstract]
  • "Plasma membrane recruitment and activation of the AGC kinase Ypk1 is mediated by target of rapamycin complex 2 (TORC2) and its effector proteins Slm1 and Slm2."
    Niles B.J., Mogri H., Hill A., Vlahakis A., Powers T.
    Proc Natl Acad Sci U S A 109:1536-1541(2012) [PubMed] [Europe PMC] [Abstract]
  • "The role of structural pleiotropy and regulatory evolution in the retention of heteromers of paralogs."
    Marchant A., Cisneros A.F., Dube A.K., Gagnon-Arsenault I., Ascencio D., Jain H., Aube S., Eberlein C., Evans-Yamamoto D., Yachie N., Landry C.R.
    Elife 8:0-0(2019) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Coiled coil

Motif

Compositional bias

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MSKNNTMTSA VSDMLSQQQL NLQHLHNLQQ HTRSMTSADH ANVLQQQQQQ 
        60         70         80         90        100
QQQQQQQQQQ QQQSASFQNG SLTSDINQQS YLNGQPVPST SNSTFQNNRT 
       110        120        130        140        150
LTMNSGGLQG IISNGSPNID SNTNVTIAVP DPNNNNGKQL QGKNSLTNTS 
       160        170        180        190        200
ILSRARSSLQ RQRLAQQQQQ QQDPRSPLVI LVPTAAQPTD ILAARFSAWR 
       210        220        230        240        250
NVIKSVIVYL TEIASIQDEI VRQQLRLSHA VQFPFFSIEN QYQPSSQEDK 
       260        270        280        290        300
SVQKFFLPLG NGSIQDLPTI LNQYHESLAS SASKASRELT NDVIPRLEDL 
       310        320        330        340        350
RRDLIVKIKE IKSLQSDFKN SCSKELQQTK QAMKQFQESL KDARYSVPKQ 
       360        370        380        390        400
DPFLTKLALD RQIKKQLQEE NFLHEAFDNL ETSGAELEKI VVMEIQNSLT 
       410        420        430        440        450
IYARLLGQEA QLVFDILISK LDSGFFNVDP QFEWDNFISR DPNFLLPNLP 
       460        470        480        490        500
MRTFKEIVYK YQFDPLTYEI KSGFLERRSK FLKSYSKGYY VLTPNFLHEF 
       510        520        530        540        550
KTADRKKDLV PVMSLALSEC TVTEHSRKNS TSSPNSTGSD AKFVLHAKQN 
       560        570        580        590        600
GIIRRGHNWV FKADSYESMM SWFDNLKILT STSNIQDKYK FITQKLNLNS 
       610        620        630        640        650
DGKPKLTNNH TSINKYQLSN ANSTMVENDE NDDINSNYVG STVTPKLDNQ 
       660        670        680 
TNTNTSMSSL PDTNDSELQD QVPNIYIQTP INDFKS                

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. Yeast
   Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
3. Yeast chromosome IX
   Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names