SLN1_YEAST - dbPTM
SLN1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SLN1_YEAST
UniProt AC P39928
Protein Name Osmosensing histidine protein kinase SLN1
Gene Name SLN1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1220
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Histidine kinase that acts as an osmosensor at the plasma membrane. Part of the bifurcated SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which controls activity of the HOG1 pathway and gene expression in response to changes in the osmolarity of the extracellular environment. Under normal osmotic conditions, the histidine kinase autophosphorylates His-576. This phosphate is subsequently transferred to Asp-1144, from where it is relayed to 'His-64' of the phosphorelay intermediate protein YPD1. Under high osmolarity conditions, the histidine kinase is no longer active..
Protein Sequence MRFGLPSKLELTPPFRIGIRTQLTALVSIVALGSLIILAVTTGVYFTSNYKNLRSDRLYIAAQLKSSQIDQTLNYLYYQAYYLASRDALQSSLTSYVAGNKSADNWVDSLSVIQKFLSSSNLFYVAKVYDSSFNAVLNATNNGTGDLIPEDVLDSLFPLSTDTPLPSSLETIGILTDPVLNSTDYLMSMSLPIFANPSIILTDSRVYGYITIIMSAEGLKSVFNDTTALEHSTIAIISAVYNSQGKASGYHFVFPPYGSRSDLPQKVFSIKNDTFISSAFRNGKGGSLKQTNILSTRNTALGYSPCSFNLVNWVAIVSQPESVFLSPATKLAKIITGTVIAIGVFVILLTLPLAHWAVQPIVRLQKATELITEGRGLRPSTPRTISRASSFKRGFSSGFAVPSSLLQFNTAEAGSTTSVSGHGGSGHGSGAAFSANSSMKSAINLGNEKMSPPEEENKIPNNHTDAKISMDGSLNHDLLGPHSLRHNDTDRSSNRSHILTTSANLTEARLPDYRRLFSDELSDLTETFNTMTDALDQHYALLEERVRARTKQLEAAKIEAEAANEAKTVFIANISHELRTPLNGILGMTAISMEETDVNKIRNSLKLIFRSGELLLHILTELLTFSKNVLQRTKLEKRDFCITDVALQIKSIFGKVAKDQRVRLSISLFPNLIRTMVLWGDSNRIIQIVMNLVSNALKFTPVDGTVDVRMKLLGEYDKELSEKKQYKEVYIKKGTEVTENLETTDKYDLPTLSNHRKSVDLESSATSLGSNRDTSTIQEEITKRNTVANESIYKKVNDREKASNDDVSSIVSTTTSSYDNAIFNSQFNKAPGSDDEEGGNLGRPIENPKTWVISIEVEDTGPGIDPSLQESVFHPFVQGDQTLSRQYGGTGLGLSICRQLANMMHGTMKLESKVGVGSKFTFTLPLNQTKEISFADMEFPFEDEFNPESRKNRRVKFSVAKSIKSRQSTSSVATPATNRSSLTNDVLPEVRSKGKHETKDVGNPNMGREEKNDNGGLEQLQEKNIKPSICLTGAEVNEQNSLSSKHRSRHEGLGSVNLDRPFLQSTGTATSSRNIPTVKDDDKNETSVKILVVEDNHVNQEVIKRMLNLEGIENIELACDGQEAFDKVKELTSKGENYNMIFMDVQMPKVDGLLSTKMIRRDLGYTSPIVALTAFADDSNIKECLESGMNGFLSKPIKRPKLKTILTEFCAAYQGKKNNK
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
100N-linked_GlycosylationLTSYVAGNKSADNWV
HHHHHHCCCCCCCHH		25.93-
118PhosphorylationSVIQKFLSSSNLFYV
HHHHHHHCCCCCEEE		34.5528889911
138N-linked_GlycosylationSSFNAVLNATNNGTG
CCHHHHHHCCCCCCC		37.81-
142N-linked_GlycosylationAVLNATNNGTGDLIP
HHHHCCCCCCCCCCC		45.08-
181N-linked_GlycosylationILTDPVLNSTDYLMS
EECCCCCCCCHHHHH		43.00-
224N-linked_GlycosylationEGLKSVFNDTTALEH
HHHHHHHCCCCHHHH		43.49-
272N-linked_GlycosylationQKVFSIKNDTFISSA
CEEEEECCCCEEHHH		52.46-
274PhosphorylationVFSIKNDTFISSAFR
EEEECCCCEEHHHHH		32.0628889911
277PhosphorylationIKNDTFISSAFRNGK
ECCCCEEHHHHHCCC		16.0627017623
278PhosphorylationKNDTFISSAFRNGKG
CCCCEEHHHHHCCCC		26.9828889911
368PhosphorylationIVRLQKATELITEGR
HHHHHHHHHHHHCCC		38.0621551504
380PhosphorylationEGRGLRPSTPRTISR
CCCCCCCCCCCHHCC		44.6127017623
381PhosphorylationGRGLRPSTPRTISRA
CCCCCCCCCCHHCCH		21.3320377248
384PhosphorylationLRPSTPRTISRASSF
CCCCCCCHHCCHHHC		25.2220377248
386PhosphorylationPSTPRTISRASSFKR
CCCCCHHCCHHHCCC		22.6028889911
389PhosphorylationPRTISRASSFKRGFS
CCHHCCHHHCCCCCC		34.8920377248
390PhosphorylationRTISRASSFKRGFSS
CHHCCHHHCCCCCCC		33.5320377248
404PhosphorylationSGFAVPSSLLQFNTA
CCCCCCHHHEEEECC		27.3319779198
425PhosphorylationSVSGHGGSGHGSGAA
EECCCCCCCCCCCCC		32.0119779198
441PhosphorylationSANSSMKSAINLGNE
CCCHHHHHHHHCCCC		26.2422369663
451PhosphorylationNLGNEKMSPPEEENK
HCCCCCCCCHHHHCC		48.6619779198
469PhosphorylationNHTDAKISMDGSLNH
CCCCCEECCCCCCCC		15.3225704821
473PhosphorylationAKISMDGSLNHDLLG
CEECCCCCCCCCCCC		23.0225752575
483PhosphorylationHDLLGPHSLRHNDTD
CCCCCCHHHCCCCCC		30.1728889911
489PhosphorylationHSLRHNDTDRSSNRS
HHHCCCCCCCCCCCC		38.3319779198
492PhosphorylationRHNDTDRSSNRSHIL
CCCCCCCCCCCCCEE		34.4719779198
493PhosphorylationHNDTDRSSNRSHILT
CCCCCCCCCCCCEEE		36.8419779198
496PhosphorylationTDRSSNRSHILTTSA
CCCCCCCCCEEECCC		21.0919779198
502PhosphorylationRSHILTTSANLTEAR
CCCEEECCCCCCCCC		15.2128889911
518PhosphorylationPDYRRLFSDELSDLT
HHHHHHHHHHHHHHH		34.4627017623
530PhosphorylationDLTETFNTMTDALDQ
HHHHHHHHHHHHHHH		19.7727017623
532PhosphorylationTETFNTMTDALDQHY
HHHHHHHHHHHHHHH		18.9727017623
576PhosphorylationVFIANISHELRTPLN
EEEEECCHHHCCCCC		34.028808622
580PhosphorylationNISHELRTPLNGILG
ECCHHHCCCCCCCCC		44.7619779198
589PhosphorylationLNGILGMTAISMEET
CCCCCCCCEEECCHH		21.0219779198
758PhosphorylationTLSNHRKSVDLESSA
CCCCCCCCCCCCCCC		22.3320377248
763PhosphorylationRKSVDLESSATSLGS
CCCCCCCCCCHHCCC		32.3522369663
764PhosphorylationKSVDLESSATSLGSN
CCCCCCCCCHHCCCC		26.6222369663
766PhosphorylationVDLESSATSLGSNRD
CCCCCCCHHCCCCCC		26.8220377248
767PhosphorylationDLESSATSLGSNRDT
CCCCCCHHCCCCCCH		30.3722369663
770PhosphorylationSSATSLGSNRDTSTI
CCCHHCCCCCCHHHH		33.7022369663
774PhosphorylationSLGSNRDTSTIQEEI
HCCCCCCHHHHHHHH		25.2422369663
775PhosphorylationLGSNRDTSTIQEEIT
CCCCCCHHHHHHHHH		28.0020377248
776PhosphorylationGSNRDTSTIQEEITK
CCCCCHHHHHHHHHH		28.8622369663
782PhosphorylationSTIQEEITKRNTVAN
HHHHHHHHHHCCCCC		27.5122369663
786PhosphorylationEEITKRNTVANESIY
HHHHHHCCCCCHHHH		25.6521440633
791PhosphorylationRNTVANESIYKKVND
HCCCCCHHHHHHHHH		30.9021440633
794UbiquitinationVANESIYKKVNDREK
CCCHHHHHHHHHHHH		48.8823749301
795UbiquitinationANESIYKKVNDREKA
CCHHHHHHHHHHHHH		29.3322817900
803PhosphorylationVNDREKASNDDVSSI
HHHHHHHCCCCHHHH		52.4327214570
833PhosphorylationQFNKAPGSDDEEGGN
HCCCCCCCCCCCCCC		40.6122369663
913UbiquitinationGTMKLESKVGVGSKF
CEEEEECCCCCCCEE		33.3623749301
962PhosphorylationVKFSVAKSIKSRQST
EEEEHHHHHHCCCCC		26.0528889911
965PhosphorylationSVAKSIKSRQSTSSV
EHHHHHHCCCCCCCC		33.6021440633
968PhosphorylationKSIKSRQSTSSVATP
HHHHCCCCCCCCCCC		29.1921440633
969PhosphorylationSIKSRQSTSSVATPA
HHHCCCCCCCCCCCC		19.3821440633
970PhosphorylationIKSRQSTSSVATPAT
HHCCCCCCCCCCCCC		28.2321440633
971PhosphorylationKSRQSTSSVATPATN
HCCCCCCCCCCCCCC		18.8323749301
974PhosphorylationQSTSSVATPATNRSS
CCCCCCCCCCCCCHH		15.9921440633
977PhosphorylationSSVATPATNRSSLTN
CCCCCCCCCCHHCCC		32.1621440633
980PhosphorylationATPATNRSSLTNDVL
CCCCCCCHHCCCCCH		31.5917563356
981PhosphorylationTPATNRSSLTNDVLP
CCCCCCHHCCCCCHH		35.6621440633
983PhosphorylationATNRSSLTNDVLPEV
CCCCHHCCCCCHHHH		31.1819779198
1041PhosphorylationAEVNEQNSLSSKHRS
CCCCCCCCCCHHHHH		29.3520377248
1043PhosphorylationVNEQNSLSSKHRSRH
CCCCCCCCHHHHHHC		36.8420377248
1044PhosphorylationNEQNSLSSKHRSRHE
CCCCCCCHHHHHHCC		37.4620377248
1055PhosphorylationSRHEGLGSVNLDRPF
HHCCCCCCCCCCCHH		16.9319779198
1065PhosphorylationLDRPFLQSTGTATSS
CCCHHHHCCCCCCCC		30.8324961812
1066PhosphorylationDRPFLQSTGTATSSR
CCHHHHCCCCCCCCC		26.1224961812
1068PhosphorylationPFLQSTGTATSSRNI
HHHHCCCCCCCCCCC		27.1824961812
1070PhosphorylationLQSTGTATSSRNIPT
HHCCCCCCCCCCCCC		27.3724961812
1071PhosphorylationQSTGTATSSRNIPTV
HCCCCCCCCCCCCCC		25.4924961812
1072PhosphorylationSTGTATSSRNIPTVK
CCCCCCCCCCCCCCC		25.6224961812
1077PhosphorylationTSSRNIPTVKDDDKN
CCCCCCCCCCCCCCC		36.0724961812
1144PhosphorylationNYNMIFMDVQMPKVD
CEEEEEEECCCCCCC		19.428808622
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 SLN1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLN1_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 SLN1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COPA_YEASTCOP1physical
11805837
YPD1_YEASTYPD1physical
15628880
YPD1_YEASTYPD1physical
9882653
MOG1_YEASTMOG1physical
15590828
DJP1_YEASTDJP1physical
15590828
YPD1_YEASTYPD1physical
12455952
SKN7_YEASTSKN7physical
12455952
SKN7_YEASTSKN7physical
11073911
SSK1_YEASTSSK1physical
11073911
PP2C1_YEASTPTC1genetic
11113180
PP2C2_YEASTPTC2genetic
11113180
PP2C3_YEASTPTC3genetic
11113180
PTP2_YEASTPTP2genetic
8808622
SKN7_YEASTSKN7genetic
9843501
SKN7_YEASTSKN7genetic
11854400
SHO1_YEASTSHO1genetic
9148959
PP2C3_YEASTPTC3genetic
8183345
PTP2_YEASTPTP2genetic
8183345
PP2C1_YEASTPTC1genetic
8183345
HOG1_YEASTHOG1genetic
15448699
SIC1_YEASTSIC1genetic
15448699
YPD1_YEASTYPD1physical
17559414
MPR1_SCHPOmpr1physical
17559414
SLT2_YEASTSLT2genetic
19269370
KHSE_YEASTTHR1genetic
19269370
SWE1_YEASTSWE1genetic
19269370
CTK1_YEASTCTK1genetic
19269370
FPK1_YEASTFPK1genetic
19269370
FRK1_YEASTFRK1genetic
19269370
SSK1_YEASTSSK1genetic
18573873
SLN1_YEASTSLN1physical
19618914
YPD1_YEASTYPD1physical
19618914
FPS1_YEASTFPS1genetic
19608606
SSK1_YEASTSSK1genetic
8183345
SSK1_YEASTSSK1genetic
11084293
SKM1_YEASTSKM1physical
21118957
SSK2_YEASTSSK2physical
21118957
TOR1_YEASTTOR1physical
21118957
YPK2_YEASTYPK2physical
21118957
CDC4_YEASTCDC4genetic
21836634
PTP2_YEASTPTP2genetic
21836634
REG1_YEASTREG1genetic
26394309
F16P_YEASTFBP1genetic
27708008
HDA1_YEASTHDA1genetic
27708008
MCM7_YEASTMCM7genetic
27708008
SCC1_YEASTMCD1genetic
27708008
RPB1_YEASTRPO21genetic
27708008
RPN5_YEASTRPN5genetic
27708008
RMRP_YEASTSNM1genetic
27708008
SDA1_YEASTSDA1genetic
27708008
MED6_YEASTMED6genetic
27708008
RFC2_YEASTRFC2genetic
27708008
CDC11_YEASTCDC11genetic
27708008
BET3_YEASTBET3genetic
27708008
SSL1_YEASTSSL1genetic
27708008
MED14_YEASTRGR1genetic
27708008
SC61A_YEASTSEC61genetic
27708008
MCM1_YEASTMCM1genetic
27708008
TYSY_YEASTCDC21genetic
27708008
MED4_YEASTMED4genetic
27708008
NAB3_YEASTNAB3genetic
27708008
MED10_YEASTNUT2genetic
27708008
MNN2_YEASTMNN2genetic
27708008
GAL10_YEASTGAL10genetic
27708008
ETR1_YEASTETR1genetic
27708008
SEC66_YEASTSEC66genetic
27708008
GPR1_YEASTGPR1genetic
27708008
VAM6_YEASTVAM6genetic
27708008
ATG9_YEASTATG9genetic
27708008
MNN10_YEASTMNN10genetic
27708008
WWM1_YEASTWWM1genetic
27708008
DBP3_YEASTDBP3genetic
27708008
MON1_YEASTMON1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
MED20_YEASTSRB2genetic
27708008
HOC1_YEASTHOC1genetic
27708008
NNK1_YEASTNNK1genetic
27708008
LIPB_YEASTLIP2genetic
27708008
FKS1_YEASTFKS1genetic
27708008
VAC14_YEASTVAC14genetic
27708008
GBLP_YEASTASC1genetic
27708008
HFA1_YEASTHFA1genetic
27708008
GAS1_YEASTGAS1genetic
27708008
PHO23_YEASTPHO23genetic
27708008
LSM7_YEASTLSM7genetic
27708008
PFD4_YEASTGIM3genetic
27708008
SIN3_YEASTSIN3genetic
27708008
TRM11_YEASTTRM11genetic
27708008
LIPA_YEASTLIP5genetic
27708008
RUD3_YEASTRUD3genetic
27708008
FABD_YEASTMCT1genetic
27708008
ELP3_YEASTELP3genetic
27708008
MGR2_YEASTMGR2genetic
27708008
RU2A_YEASTLEA1genetic
27708008
ASR1_YEASTASR1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SLN1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Yeast HOG1 MAP kinase cascade is regulated by a multistepphosphorelay mechanism in the SLN1-YPD1-SSK1 two-componentosmosensor.";
Posas F., Wurgler-Murphy S.M., Maeda T., Witten E.A., Thai T.C.,Saito H.;
Cell 86:865-875(1996).
Cited for: FUNCTION, PHOSPHORYLATION AT HIS-576 AND ASP-1144, AND INTERACTIONWITH YPD1.
"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-473 AND SER-833, ANDMASS SPECTROMETRY.
"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-833 AND SER-980, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND MASSSPECTROMETRY.

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