SLM1_YEAST - dbPTM
SLM1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SLM1_YEAST
UniProt AC P40485
Protein Name Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1
Gene Name SLM1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 686
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side . Localizes to cortical punctate structures. Correct localization requires phosphatidylinositol 4,5-bisphosphate and functional TORC2.
Protein Description 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..
Protein Sequence MSKNNTMTSAVSDMLSQQQLNLQHLHNLQQHTRSMTSADHANVLQQQQQQQQQQQQQQQQQQQSASFQNGSLTSDINQQSYLNGQPVPSTSNSTFQNNRTLTMNSGGLQGIISNGSPNIDSNTNVTIAVPDPNNNNGKQLQGKNSLTNTSILSRARSSLQRQRLAQQQQQQQDPRSPLVILVPTAAQPTDILAARFSAWRNVIKSVIVYLTEIASIQDEIVRQQLRLSHAVQFPFFSIENQYQPSSQEDKSVQKFFLPLGNGSIQDLPTILNQYHESLASSASKASRELTNDVIPRLEDLRRDLIVKIKEIKSLQSDFKNSCSKELQQTKQAMKQFQESLKDARYSVPKQDPFLTKLALDRQIKKQLQEENFLHEAFDNLETSGAELEKIVVMEIQNSLTIYARLLGQEAQLVFDILISKLDSGFFNVDPQFEWDNFISRDPNFLLPNLPMRTFKEIVYKYQFDPLTYEIKSGFLERRSKFLKSYSKGYYVLTPNFLHEFKTADRKKDLVPVMSLALSECTVTEHSRKNSTSSPNSTGSDAKFVLHAKQNGIIRRGHNWVFKADSYESMMSWFDNLKILTSTSNIQDKYKFITQKLNLNSDGKPKLTNNHTSINKYQLSNANSTMVENDENDDINSNYVGSTVTPKLDNQTNTNTSMSSLPDTNDSELQDQVPNIYIQTPINDFKS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
143UbiquitinationNGKQLQGKNSLTNTS
CCCCCCCCCCCCHHH		30.3323749301
145PhosphorylationKQLQGKNSLTNTSIL
CCCCCCCCCCHHHHH		39.8022369663
147PhosphorylationLQGKNSLTNTSILSR
CCCCCCCCHHHHHHH		35.9522369663
149PhosphorylationGKNSLTNTSILSRAR
CCCCCCHHHHHHHHH		16.3522369663
150PhosphorylationKNSLTNTSILSRARS
CCCCCHHHHHHHHHH		24.4922369663
153PhosphorylationLTNTSILSRARSSLQ
CCHHHHHHHHHHHHH		23.4022369663
157PhosphorylationSILSRARSSLQRQRL
HHHHHHHHHHHHHHH		34.1224909858
158PhosphorylationILSRARSSLQRQRLA
HHHHHHHHHHHHHHH		23.9824909858
250AcetylationQPSSQEDKSVQKFFL
CCCCCCCCCCCEEEE		52.3425381059
313PhosphorylationVKIKEIKSLQSDFKN
HHHHHHHHHHHHHCH		36.9819795423
346PhosphorylationSLKDARYSVPKQDPF
HHHHCCCCCCCCCHH		26.7923749301
487UbiquitinationKFLKSYSKGYYVLTP
HHHHHHCCCEEEECH		42.5717644757
501UbiquitinationPNFLHEFKTADRKKD
HHHHHHHCCCCCCCC		39.5617644757
530PhosphorylationTEHSRKNSTSSPNST
CCHHHCCCCCCCCCC		32.4728889911
531PhosphorylationEHSRKNSTSSPNSTG
CHHHCCCCCCCCCCC		42.4930377154
532PhosphorylationHSRKNSTSSPNSTGS
HHHCCCCCCCCCCCC		43.5525521595
533PhosphorylationSRKNSTSSPNSTGSD
HHCCCCCCCCCCCCC		28.3425752575
536PhosphorylationNSTSSPNSTGSDAKF
CCCCCCCCCCCCCEE		37.2128889911
537PhosphorylationSTSSPNSTGSDAKFV
CCCCCCCCCCCCEEE		47.5527717283
539PhosphorylationSSPNSTGSDAKFVLH
CCCCCCCCCCEEEEE		34.1930377154
542AcetylationNSTGSDAKFVLHAKQ
CCCCCCCEEEEEHHH		40.7824489116
581PhosphorylationDNLKILTSTSNIQDK
HCCEEHHCCCCHHHH		26.7927214570
600PhosphorylationTQKLNLNSDGKPKLT
HHCCCCCCCCCCCCC		51.4021440633
611PhosphorylationPKLTNNHTSINKYQL
CCCCCCCCCCCEEEE		33.1621440633
612PhosphorylationKLTNNHTSINKYQLS
CCCCCCCCCCEEEEC		19.3325005228
619PhosphorylationSINKYQLSNANSTMV
CCCEEEECCCCCCEE		20.5524961812
623PhosphorylationYQLSNANSTMVENDE
EEECCCCCCEECCCC		18.5724961812
624PhosphorylationQLSNANSTMVENDEN
EECCCCCCEECCCCC		25.6624961812
636PhosphorylationDENDDINSNYVGSTV
CCCCCCCCCCCCCEE		29.8528152593
638PhosphorylationNDDINSNYVGSTVTP
CCCCCCCCCCCEECC		13.1521440633
641PhosphorylationINSNYVGSTVTPKLD
CCCCCCCCEECCCCC		15.0628889911
642PhosphorylationNSNYVGSTVTPKLDN
CCCCCCCEECCCCCC		23.5924961812
644PhosphorylationNYVGSTVTPKLDNQT
CCCCCEECCCCCCCC		18.1325752575
651PhosphorylationTPKLDNQTNTNTSMS
CCCCCCCCCCCCCHH		50.7121440633
653PhosphorylationKLDNQTNTNTSMSSL
CCCCCCCCCCCHHCC		43.1721440633
655PhosphorylationDNQTNTNTSMSSLPD
CCCCCCCCCHHCCCC		24.6221440633
658PhosphorylationTNTNTSMSSLPDTND
CCCCCCHHCCCCCCC		28.6128889911
659PhosphorylationNTNTSMSSLPDTNDS
CCCCCHHCCCCCCCH		34.9728889911
663PhosphorylationSMSSLPDTNDSELQD
CHHCCCCCCCHHHHH		38.7021551504
666PhosphorylationSLPDTNDSELQDQVP
CCCCCCCHHHHHHCC		42.1321551504
679PhosphorylationVPNIYIQTPINDFKS
CCCEEEECCCHHCCC		19.3127214570
686PhosphorylationTPINDFKS-------
CCCHHCCC-------		45.5128889911
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SLM1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLM1_YEAST !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SLM1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DMC1_YEASTDMC1physical
10688190
SHE2_YEASTSHE2physical
10688190
SLM2_YEASTSLM2physical
10688190
SLM2_YEASTSLM2physical
15372071
AVO2_YEASTAVO2physical
15372071
AVO2_YEASTAVO2physical
15689497
BIT61_YEASTBIT61physical
15689497
BIT2_YEASTBIT2physical
15689497
TOR2_YEASTTOR2physical
15689497
SLM2_YEASTSLM2genetic
15689497
INP51_YEASTINP51genetic
15689497
RHO1_YEASTRHO1genetic
15689497
RHO2_YEASTRHO2genetic
15689497
KPC1_YEASTPKC1genetic
15372071
MSS4_YEASTMSS4genetic
15372071
SEC4_YEASTSEC4genetic
15372071
SAC7_YEASTSAC7genetic
15372071
TOR2_YEASTTOR2physical
16959779
CSG2_YEASTCSG2genetic
17101780
LCB4_YEASTLCB4genetic
17101780
ELO2_YEASTELO2genetic
17101780
SLM2_YEASTSLM2genetic
17101780
KPC1_YEASTPKC1genetic
15689497
SLM1_YEASTSLM1physical
18467557
SFK1_YEASTSFK1physical
18467557
MID2_YEASTMID2physical
18467557
PDR12_YEASTPDR12physical
18467557
SLM1_YEASTSLM1physical
18719252
ATG17_YEASTATG17physical
18719252
TOR2_YEASTTOR2physical
18552287
AVO2_YEASTAVO2physical
18552287
TUS1_YEASTTUS1physical
18552287
MBA1_YEASTMBA1genetic
20093466
YCE9_YEASTYCL049Cgenetic
20093466
VMS1_YEASTVMS1genetic
20093466
YD132_YEASTYDR132Cgenetic
20093466
MNN10_YEASTMNN10genetic
20093466
PEX10_YEASTPEX10genetic
20093466
YEW0_YEASTCOM2genetic
20093466
YEY6_YEASTYER156Cgenetic
20093466
MED5_YEASTNUT1genetic
20093466
PEX8_YEASTPEX8genetic
20093466
DRN1_YEASTDRN1genetic
20093466
PCP1_YEASTPCP1genetic
20093466
ELP2_YEASTELP2genetic
20093466
RSSA1_YEASTRPS0Agenetic
20093466
OSH3_YEASTOSH3genetic
20093466
THP2_YEASTTHP2genetic
20093466
HXT8_YEASTHXT8genetic
20093466
PRM10_YEASTPRM10genetic
20093466
SAC1_YEASTSAC1genetic
20093466
CBT1_YEASTCBT1genetic
20093466
XPOT_YEASTLOS1genetic
20093466
ASH1_YEASTASH1genetic
20093466
KTI12_YEASTKTI12genetic
20093466
HAP4_YEASTHAP4genetic
20093466
MUD2_YEASTMUD2genetic
20093466
PET10_YEASTPET10genetic
20093466
MSC3_YEASTMSC3genetic
20093466
PEX30_YEASTPEX30genetic
20093466
CHS5_YEASTCHS5genetic
20093466
IMDH3_YEASTIMD3genetic
20093466
INP2_YEASTINP2genetic
20093466
YM39_YEASTYMR166Cgenetic
20093466
MKS1_YEASTMKS1genetic
20093466
IPB2_YEASTPBI2genetic
20093466
EF3B_YEASTHEF3genetic
20093466
RCF2_YEASTRCF2genetic
20093466
SHE4_YEASTSHE4genetic
20093466
SNC2_YEASTSNC2genetic
20093466
PP2B2_YEASTCMP2physical
16847337
SLM2_YEASTSLM2genetic
16847337
CSG2_YEASTCSG2genetic
16847337
CANB_YEASTCNB1genetic
16847337
ISC1_YEASTISC1genetic
16847337
SLM2_YEASTSLM2genetic
20526336
SLM2_YEASTSLM2genetic
21451250
SLM2_YEASTSLM2genetic
22307609
SAC7_YEASTSAC7genetic
22307609
YPK1_YEASTYPK1genetic
22307609
YPK1_YEASTYPK1physical
22307609
SLM1_YEASTSLM1physical
22615397
SLM2_YEASTSLM2genetic
23891562
GPI7_YEASTLAS21genetic
23891562
PSD1_YEASTPSD1genetic
23891562
GET2_YEASTGET2genetic
23891562
RGP1_YEASTRGP1genetic
23891562
PFD4_YEASTGIM3genetic
23891562
TSC11_YEASTTSC11physical
24465216
YPK1_YEASTYPK1physical
24465216
RV161_YEASTRVS161genetic
27708008
MRM2_YEASTMRM2genetic
27708008
OSH3_YEASTOSH3genetic
27708008
MSC3_YEASTMSC3genetic
27708008
AVT5_YEASTAVT5genetic
27708008
MBA1_YEASTMBA1genetic
27708008
MTU1_YEASTSLM3genetic
27708008
PEX5_YEASTPEX5genetic
27708008
YEW0_YEASTCOM2genetic
27708008
YEY6_YEASTYER156Cgenetic
27708008
ODPA_YEASTPDA1genetic
27708008
MED5_YEASTNUT1genetic
27708008
PEX8_YEASTPEX8genetic
27708008
ELP2_YEASTELP2genetic
27708008
RSSA1_YEASTRPS0Agenetic
27708008
HSV2_YEASTHSV2genetic
27708008
THP2_YEASTTHP2genetic
27708008
PRM10_YEASTPRM10genetic
27708008
HAP4_YEASTHAP4genetic
27708008
KTI12_YEASTKTI12genetic
27708008
ASH1_YEASTASH1genetic
27708008
CBT1_YEASTCBT1genetic
27708008
PAM17_YEASTPAM17genetic
27708008
YL194_YEASTYLR194Cgenetic
27708008
PEX30_YEASTPEX30genetic
27708008
DCR2_YEASTDCR2genetic
27708008
IMDH3_YEASTIMD3genetic
27708008
INP2_YEASTINP2genetic
27708008
YM39_YEASTYMR166Cgenetic
27708008
EF3B_YEASTHEF3genetic
27708008
SIN3_YEASTSIN3genetic
27708008
SNC2_YEASTSNC2genetic
27708008
FRK1_YEASTFRK1genetic
27708008
MRL1_YEASTMRL1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SLM1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; THR-147; THR-149;SER-150; SER-153; SER-600; SER-641; SER-658 AND SER-686, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-157 ANDSER-158, AND MASS SPECTROMETRY.

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