LSP1_YEAST - dbPTM
LSP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LSP1_YEAST
UniProt AC Q12230
Protein Name Sphingolipid long chain base-responsive protein LSP1
Gene Name LSP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 341
Subcellular Localization Cytoplasm, cell cortex . Localizes at eisosomes, structures which colocalize with sites of protein and lipid endocytosis.
Protein Description Together with PIL1, main component of eisosomes, structures at the cell periphery underneath the plasma membrane that mark the site of endocytosis. Negative regulator of cell wall integrity (CWI) in unstressed cells, probably by inhibiting protein kinase PKH1/PHK2 activity and regulating their downstream CWI pathways PKC1-MAP kinase pathway and protein kinase YPK1 pathway. Activity may be regulated by the transient increase of sphingolipid long chain bases (LCBs) during heat stress..
Protein Sequence MHRTYSLRNQRAPTAAELQAPPPPPSSTKSKFFGKASIASSFRKNAAGNFGPELARKLSQLVKTEKGVLRAMEVVASERREAAKQLSLWGADNDDDVSDVTDKLGVLIYELGELQDQFIDKYDQYRVTLKSIRNIEASVQPSRDRKEKITDEIAHLKYKDPQSTKIPVLEQELVRAEAESLVAEAQLSNITREKLKAAYSYMFDSLRELSEKFALIAGYGKALLELLDDSPVTPGEARPAYDGYEASRQIIMDAESALESWTLDMAAVKPTLSFHQTVDDVYEDEDGEEEEEPEIQNGDIPGQVVEEEEVEWTTEVPVDDEAHEADHHVSQNGHTSGSENI
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
4Phosphorylation----MHRTYSLRNQR
----CCCCCCCCCCC		11.6421440633
5Phosphorylation---MHRTYSLRNQRA
---CCCCCCCCCCCC		12.9819823750
6Phosphorylation--MHRTYSLRNQRAP
--CCCCCCCCCCCCC		21.9028152593
14PhosphorylationLRNQRAPTAAELQAP
CCCCCCCCHHHHCCC		37.2022369663
26PhosphorylationQAPPPPPSSTKSKFF
CCCCCCCCCCCCHHC		57.3122369663
27PhosphorylationAPPPPPSSTKSKFFG
CCCCCCCCCCCHHCC		45.7022369663
28PhosphorylationPPPPPSSTKSKFFGK
CCCCCCCCCCHHCCH		43.6122369663
30PhosphorylationPPPSSTKSKFFGKAS
CCCCCCCCHHCCHHH		34.4828889911
352-HydroxyisobutyrylationTKSKFFGKASIASSF
CCCHHCCHHHHHHHH		33.53-
35AcetylationTKSKFFGKASIASSF
CCCHHCCHHHHHHHH		33.5325381059
37PhosphorylationSKFFGKASIASSFRK
CHHCCHHHHHHHHHH		23.3627214570
40PhosphorylationFGKASIASSFRKNAA
CCHHHHHHHHHHCCC		28.4821440633
41PhosphorylationGKASIASSFRKNAAG
CHHHHHHHHHHCCCC		21.7624909858
442-HydroxyisobutyrylationSIASSFRKNAAGNFG
HHHHHHHHCCCCCCC		49.26-
57UbiquitinationFGPELARKLSQLVKT
CCHHHHHHHHHHHHH		47.0523749301
59PhosphorylationPELARKLSQLVKTEK
HHHHHHHHHHHHHHH		25.2219823750
63AcetylationRKLSQLVKTEKGVLR
HHHHHHHHHHHHHHH		60.6024489116
66AcetylationSQLVKTEKGVLRAME
HHHHHHHHHHHHHHH		60.6024489116
77PhosphorylationRAMEVVASERREAAK
HHHHHHHHHHHHHHH		21.7421440633
87PhosphorylationREAAKQLSLWGADND
HHHHHHHHHCCCCCC		21.4124909858
98PhosphorylationADNDDDVSDVTDKLG
CCCCCCHHHHHHHHH		33.1029136822
101PhosphorylationDDDVSDVTDKLGVLI
CCCHHHHHHHHHHHH		32.1924961812
1302-HydroxyisobutyrylationDQYRVTLKSIRNIEA
HHHEEHHHHHHCCHH		34.18-
130AcetylationDQYRVTLKSIRNIEA
HHHEEHHHHHHCCHH		34.1825381059
131PhosphorylationQYRVTLKSIRNIEAS
HHEEHHHHHHCCHHH		29.8723749301
138PhosphorylationSIRNIEASVQPSRDR
HHHCCHHHCCCCCCH		14.4327214570
142PhosphorylationIEASVQPSRDRKEKI
CHHHCCCCCCHHHHH		29.7127214570
148AcetylationPSRDRKEKITDEIAH
CCCCHHHHHHHHHHH		54.6724489116
157AcetylationTDEIAHLKYKDPQST
HHHHHHHHCCCCCCC		40.1524489116
159AcetylationEIAHLKYKDPQSTKI
HHHHHHCCCCCCCCC		62.4424489116
165AcetylationYKDPQSTKIPVLEQE
CCCCCCCCCCHHHHH		50.7024489116
180PhosphorylationLVRAEAESLVAEAQL
HHHHHHHHHHHHHHH		34.8827214570
212AcetylationSLRELSEKFALIAGY
HHHHHHHHHHHHHHH		32.3424489116
230PhosphorylationLLELLDDSPVTPGEA
HHHHHCCCCCCCCCC		22.4222369663
233PhosphorylationLLDDSPVTPGEARPA
HHCCCCCCCCCCCCC		29.0322369663
241PhosphorylationPGEARPAYDGYEASR
CCCCCCCCCCHHHHH		16.7522369663
244PhosphorylationARPAYDGYEASRQII
CCCCCCCHHHHHHHH		12.8622369663
247PhosphorylationAYDGYEASRQIIMDA
CCCCHHHHHHHHHCH		16.8722369663
273PhosphorylationAAVKPTLSFHQTVDD
HHCCCCEEEECCHHC		24.1428889911
336PhosphorylationVSQNGHTSGSENI--
CCCCCCCCCCCCC--		34.3528889911
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 LSP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LSP1_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 LSP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FAB1_YEASTFAB1physical
16554755
CDC20_YEASTCDC20physical
16554755
BCK1_YEASTBCK1physical
16554755
MRP8_YEASTMRP8physical
16554755
PIL1_YEASTPIL1physical
16496001
FLC1_YEASTFLC1physical
18467557
CET1_YEASTCET1genetic
19269370
HSP71_YEASTSSA1physical
19536198
ACAC_YEASTACC1physical
19269952
COPA_YEASTCOP1physical
19269952
COPB_YEASTSEC26physical
19269952
COPB2_YEASTSEC27physical
19269952
PIL1_YEASTPIL1physical
19269952
YG3A_YEASTYGR130Cphysical
19269952
EIS1_YEASTEIS1physical
19269952
SEG1_YEASTSEG1physical
19269952
BUD27_YEASTBUD27genetic
20093466
MAL12_YEASTMAL12genetic
20093466
DCOR_YEASTSPE1genetic
20093466
NST1_YEASTNST1genetic
20093466
SFL1_YEASTSFL1genetic
20093466
HAP5_YEASTHAP5genetic
20093466
PIL1_YEASTPIL1physical
20526336
TOR2_YEASTTOR2genetic
20526336
IPK1_YEASTIPK1genetic
21987634
SRO7_YEASTSRO7genetic
21987634
LSP1_YEASTLSP1physical
22123866
FLC1_YEASTFLC1physical
22615397
PIL1_YEASTPIL1physical
25863055
LSP1_YEASTLSP1physical
25863055
GPR1_YEASTGPR1genetic
27708008
MED5_YEASTNUT1genetic
27708008
DAL81_YEASTDAL81genetic
27708008
VPS24_YEASTVPS24genetic
27708008
DCOR_YEASTSPE1genetic
27708008
EAF7_YEASTEAF7genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LSP1_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-26; SER-27; THR-233;SER-273 AND SER-336, AND MASS 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-230 AND THR-233, 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 THR-233, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233, AND MASSSPECTROMETRY.

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