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Protein

Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1

Gene

SLM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Together 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.4 Publications

GO - Molecular functioni

  • phosphatidylinositol-4,5-bisphosphate binding Source: SGD
  • sphingolipid binding Source: SGD

GO - Biological processi

  • actin cytoskeleton organization Source: SGD
  • actin filament bundle assembly Source: SGD
  • eisosome assembly Source: SGD
  • endosomal transport Source: SGD
  • establishment of protein localization to plasma membrane Source: SGD
  • establishment or maintenance of actin cytoskeleton polarity Source: SGD
  • regulation of cell growth Source: SGD
  • TOR signaling Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-31361-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1
Alternative name(s):
Synthetic lethal with MSS4 protein 1
TORC2 effector protein SLM1
Gene namesi
Name:SLM1
Synonyms:LIT2
Ordered Locus Names:YIL105C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL105C.
SGDiS000001367. SLM1.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: GOC
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi477 – 4782RR → AA in SLM1-PHM2; reduces phosphoinositide binding by 95%; when associated with A-487. 1 Publication
Mutagenesisi483 – 4831K → A in SLM1-PHM1; reduces phosphoinositide binding by 80% and causes mislocalization to the cytoplasm; when associated with A-487. 2 Publications
Mutagenesisi487 – 4871K → A in SLM1-PHM1; reduces phosphoinositide binding by 80% and causes mislocalization to the cytoplasm; when associated with A-483. In SLM1-PHM2; reduces phosphoinositide binding by 95%; when associated with 477-AA-478. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 686686Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1PRO_0000202965Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei145 – 1451PhosphoserineCombined sources
Modified residuei150 – 1501PhosphoserineCombined sources
Modified residuei153 – 1531PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by the target of rapamycin complex 2 (TORC2) and dephosphorylated by serine/threonine-protein phosphatase 2B (calcineurin).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40485.
PeptideAtlasiP40485.

PTM databases

iPTMnetiP40485.

Interactioni

Subunit structurei

Heterodimer of SLM1-SLM2. Binds phosphatidylinositol 4,5-bisphosphate, which is required for function. Interacts with the TORC2 subunits AVO2, BIT61 and TOR2. Interacts with the calcineurin catalytic subunits CNA1 and CNA2.4 Publications

Protein-protein interaction databases

BioGridi34886. 122 interactions.
DIPiDIP-1353N.
IntActiP40485. 25 interactions.
MINTiMINT-387224.

Structurei

Secondary structure

1
686
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi470 – 47910Combined sources
Turni480 – 4834Combined sources
Beta strandi484 – 4929Combined sources
Beta strandi494 – 5029Combined sources
Turni505 – 5073Combined sources
Beta strandi512 – 5165Combined sources
Helixi517 – 5193Combined sources
Beta strandi520 – 5256Combined sources
Beta strandi530 – 5334Combined sources
Beta strandi542 – 55312Combined sources
Beta strandi558 – 5625Combined sources
Helixi566 – 57914Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NSUX-ray2.00A/B469-583[»]
4A5KX-ray1.76A/B/C/D469-583[»]
4A6FX-ray1.68A/B469-583[»]
4A6HX-ray1.45A/B/C/D469-583[»]
4A6KX-ray1.80A/B/C/D469-583[»]
ProteinModelPortaliP40485.
SMRiP40485. Positions 469-581.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini468 – 581114PHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili296 – 38186Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi673 – 6786PXIXIT-like, required for interaction with CNA1 and CNA2, and calcineurin-dependent dephosphorylation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi45 – 6319Poly-GlnAdd
BLAST
Compositional biasi133 – 1364Poly-Asn
Compositional biasi166 – 1727Poly-Gln

Sequence similaritiesi

Contains 1 PH domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00390000002928.
HOGENOMiHOG000066129.
InParanoidiP40485.
OMAiMVENDEN.
OrthoDBiEOG7FZ06S.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR033191. Slm1/Slm2.
[Graphical view]
PANTHERiPTHR31941:SF7. PTHR31941:SF7. 1 hit.
PfamiPF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40485-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:686
Mass (Da):77,995
Last modified:February 1, 1995 - v1
Checksum:i849C82CC0960014B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38125 Genomic DNA. Translation: CAA86275.1.
BK006942 Genomic DNA. Translation: DAA08448.1.
PIRiS48467.
RefSeqiNP_012161.1. NM_001179453.1.

Genome annotation databases

EnsemblFungiiYIL105C; YIL105C; YIL105C.
GeneIDi854701.
KEGGisce:YIL105C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38125 Genomic DNA. Translation: CAA86275.1.
BK006942 Genomic DNA. Translation: DAA08448.1.
PIRiS48467.
RefSeqiNP_012161.1. NM_001179453.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NSUX-ray2.00A/B469-583[»]
4A5KX-ray1.76A/B/C/D469-583[»]
4A6FX-ray1.68A/B469-583[»]
4A6HX-ray1.45A/B/C/D469-583[»]
4A6KX-ray1.80A/B/C/D469-583[»]
ProteinModelPortaliP40485.
SMRiP40485. Positions 469-581.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34886. 122 interactions.
DIPiDIP-1353N.
IntActiP40485. 25 interactions.
MINTiMINT-387224.

PTM databases

iPTMnetiP40485.

Proteomic databases

MaxQBiP40485.
PeptideAtlasiP40485.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL105C; YIL105C; YIL105C.
GeneIDi854701.
KEGGisce:YIL105C.

Organism-specific databases

EuPathDBiFungiDB:YIL105C.
SGDiS000001367. SLM1.

Phylogenomic databases

GeneTreeiENSGT00390000002928.
HOGENOMiHOG000066129.
InParanoidiP40485.
OMAiMVENDEN.
OrthoDBiEOG7FZ06S.

Enzyme and pathway databases

BioCyciYEAST:G3O-31361-MONOMER.

Miscellaneous databases

PROiP40485.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR033191. Slm1/Slm2.
[Graphical view]
PANTHERiPTHR31941:SF7. PTHR31941:SF7. 1 hit.
PfamiPF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  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.
  5. "Genome-wide analysis of membrane targeting by S.cerevisiae pleckstrin homology domains."
    Yu J.W., Mendrola J.M., Audhya A., Singh S., Keleti D., DeWald D.B., Murray D., Emr S.D., Lemmon M.A.
    Mol. Cell 13:677-688(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHOINOSITIDE-BINDING, SUBCELLULAR LOCATION.
  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.
  7. "Mutual antagonism of TOR and calcineurin signaling."
    Mulet J.M., Martin D.E., Loewith R., Hall M.N.
    J. Biol. Chem. 281:33000-33007(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CNA1 AND TOR2.
  8. "Slm1 and slm2 are novel substrates of the calcineurin phosphatase required for heat stress-induced endocytosis of the yeast uracil permease."
    Bultynck G., Heath V.L., Majeed A.P., Galan J.-M., Haguenauer-Tsapis R., Cyert M.S.
    Mol. Cell. Biol. 26:4729-4745(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEPHOSPHORYLATION BY CALCINEURIN, INTERACTION WITH CNA1 AND CNA2.
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-150 AND SER-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSLM1_YEAST
AccessioniPrimary (citable) accession number: P40485
Secondary accession number(s): D6VVI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 8, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5190 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.