LRE1_YEAST - dbPTM
LRE1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRE1_YEAST
UniProt AC P25579
Protein Name Laminarase-resistance protein LRE1
Gene Name LRE1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 583
Subcellular Localization
Protein Description Overexpression affects chitinase expression, cell separation and budding pattern, and increases trehalose accumulation and heat resistance by inhibiting protein kinase CBK1. Overexpression also suppresses temperature-induced hyperosmosensitivity and sensitivity to cell wall degrading enzymes. Overexpression of both LRE1 and PBN1 confers resistance to laminarinase..
Protein Sequence MPNTHTQHVQISEPNPVNTLSTPSKRGHRHRRSLAISGDFDFLKQPAAIVNLPPPQAAENCPSTAPTAVSSTLSPIRYNRFPCKTNEDAGTLDLPEPRFYPLSPKNNLQTPSPRFFISEEPSFSSPVKGVPDAIINLDDALKTRPRSFKSHRRSESAPPDLEVMVDKGNCAAGSNSMIKEEEDSLIEPESKNEYYEQKLPTALLSPLRPSLCVSEQAIDVDDSALNGSPTHHNHGMQNANARNSNTFNSLKIKGQKQRYYHYTKQLPLTVGCDSQSPKEQRSAASMTINQAMTPSSLAYTPSKLASTPATPVSFYDSNADINLESDNFPLKDNPRYAKDGYPKKCGNSQLNRVLDSDKRQDFSGESRRRRSGSPISHMQHRNLIDNMKGRRNSNTINSIFNYKSQHYEMPYDDMMKNENINAQSMPFSVNGVNNENSIGGVITRADDAPLQHSVVKSCTPDGKEEMNRLKSNDSNEYSKSEGQIRTNSQLSKDILMGEPGDMVDLSSFVNAQRKASNETGDLVFSLSQDDDALKTFHASNSAATSNESWCISDDALGKQAQDSEVRRKRKSKLGLFRHIFSRK
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
19PhosphorylationSEPNPVNTLSTPSKR
CCCCCCCCCCCCCCC		23.4824961812
21PhosphorylationPNPVNTLSTPSKRGH
CCCCCCCCCCCCCCC		35.9128889911
22PhosphorylationNPVNTLSTPSKRGHR
CCCCCCCCCCCCCCC		34.3928889911
24PhosphorylationVNTLSTPSKRGHRHR
CCCCCCCCCCCCCCH		34.7624961812
33PhosphorylationRGHRHRRSLAISGDF
CCCCCHHCEEECCCC		23.3122890988
37PhosphorylationHRRSLAISGDFDFLK
CHHCEEECCCCHHHC		27.0522890988
67PhosphorylationNCPSTAPTAVSSTLS
CCCCCCCCCCCCCCC		36.9121551504
74PhosphorylationTAVSSTLSPIRYNRF
CCCCCCCCCCCCCCC		20.5427017623
103PhosphorylationEPRFYPLSPKNNLQT
CCCCCCCCCCCCCCC		29.3521440633
110PhosphorylationSPKNNLQTPSPRFFI
CCCCCCCCCCCCEEE		28.9724909858
112PhosphorylationKNNLQTPSPRFFISE
CCCCCCCCCCEEECC		31.9024909858
124PhosphorylationISEEPSFSSPVKGVP
ECCCCCCCCCCCCCC		37.7621440633
125PhosphorylationSEEPSFSSPVKGVPD
CCCCCCCCCCCCCCH		31.5328152593
154PhosphorylationSFKSHRRSESAPPDL
CHHHCCCCCCCCCCC		35.5428132839
156PhosphorylationKSHRRSESAPPDLEV
HHCCCCCCCCCCCEE		47.5228132839
249PhosphorylationRNSNTFNSLKIKGQK
CCCCCCCCEEECCCC		27.1827017623
259PhosphorylationIKGQKQRYYHYTKQL
ECCCCCEEEEEECCC		7.6629688323
260PhosphorylationKGQKQRYYHYTKQLP
CCCCCEEEEEECCCC		7.1929688323
262PhosphorylationQKQRYYHYTKQLPLT
CCCEEEEEECCCCEE		10.2629688323
263PhosphorylationKQRYYHYTKQLPLTV
CCEEEEEECCCCEEE		10.0529688323
269PhosphorylationYTKQLPLTVGCDSQS
EECCCCEEECCCCCC		16.9529688323
274PhosphorylationPLTVGCDSQSPKEQR
CEEECCCCCCHHHHH		36.3121551504
276PhosphorylationTVGCDSQSPKEQRSA
EECCCCCCHHHHHHH		41.7221440633
300PhosphorylationTPSSLAYTPSKLAST
CHHHHCCCHHHHCCC		18.5827017623
306PhosphorylationYTPSKLASTPATPVS
CCHHHHCCCCCCCCC		45.4121551504
307PhosphorylationTPSKLASTPATPVSF
CHHHHCCCCCCCCCC		16.0121551504
310PhosphorylationKLASTPATPVSFYDS
HHCCCCCCCCCCCCC		25.9821551504
317PhosphorylationTPVSFYDSNADINLE
CCCCCCCCCCCCCCC		23.6521440633
371PhosphorylationGESRRRRSGSPISHM
CHHHCCCCCCCCCHH		41.6429136822
373PhosphorylationSRRRRSGSPISHMQH
HHCCCCCCCCCHHHH		21.9529136822
393PhosphorylationNMKGRRNSNTINSIF
HCCCCCCCCCHHHHH		33.2722369663
395PhosphorylationKGRRNSNTINSIFNY
CCCCCCCCHHHHHCH		22.7422369663
398PhosphorylationRNSNTINSIFNYKSQ
CCCCCHHHHHCHHCC		25.3828889911
404PhosphorylationNSIFNYKSQHYEMPY
HHHHCHHCCCCCCCH		16.3030377154
411PhosphorylationSQHYEMPYDDMMKNE
CCCCCCCHHHHCCCC		24.2230377154
428PhosphorylationNAQSMPFSVNGVNNE
CCCCCCEEECCCCCC		14.5921440633
453PhosphorylationDDAPLQHSVVKSCTP
CCCCCCCHHHHCCCC		18.6928889911
457PhosphorylationLQHSVVKSCTPDGKE
CCCHHHHCCCCCCHH		16.1820377248
459PhosphorylationHSVVKSCTPDGKEEM
CHHHHCCCCCCHHHH		31.3520377248
471PhosphorylationEEMNRLKSNDSNEYS
HHHHHHHCCCCCCCC		50.9219684113
474PhosphorylationNRLKSNDSNEYSKSE
HHHHCCCCCCCCCCC		35.4921082442
480PhosphorylationDSNEYSKSEGQIRTN
CCCCCCCCCCCCCCC		40.8121440633
506PhosphorylationPGDMVDLSSFVNAQR
CCCCEEHHHHHHHHH		19.7821440633
507PhosphorylationGDMVDLSSFVNAQRK
CCCEEHHHHHHHHHH		40.2829650682
516PhosphorylationVNAQRKASNETGDLV
HHHHHHHHCCCCCEE		37.9322369663
519PhosphorylationQRKASNETGDLVFSL
HHHHHCCCCCEEEEE		40.0022369663
548PhosphorylationSAATSNESWCISDDA
CCCCCCCCEECCHHH		31.3419779198
552PhosphorylationSNESWCISDDALGKQ
CCCCEECCHHHHCHH		26.7128889911
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 LRE1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRE1_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 LRE1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IMP2_YEASTIMP2genetic
14764870
HAC1_YEASTHAC1genetic
23891562
IRE1_YEASTIRE1genetic
23891562
MOB2_YEASTMOB2physical
23954433
CBK1_YEASTCBK1physical
23954433
CDC14_YEASTCDC14physical
23954433
CDK1_YEASTCDC28physical
23954433
CG22_YEASTCLB2physical
23954433
MYO1_YEASTMYO1genetic
23954433
CYK3_YEASTCYK3genetic
23954433
INN1_YEASTINN1genetic
23954433
CHS2_YEASTCHS2genetic
23954433
CBK1_YEASTCBK1genetic
23954433
SLX8_YEASTSLX8genetic
27708008
SCS7_YEASTSCS7genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
ECM21_YEASTECM21genetic
27708008
VPS41_YEASTVPS41genetic
27708008
VFA1_YEASTVFA1genetic
27708008
HAC1_YEASTHAC1genetic
27708008
UBP6_YEASTUBP6genetic
27708008
MED5_YEASTNUT1genetic
27708008
RTF1_YEASTRTF1genetic
27708008
RSSA1_YEASTRPS0Agenetic
27708008
SLT2_YEASTSLT2genetic
27708008
IRE1_YEASTIRE1genetic
27708008
STB5_YEASTSTB5genetic
27708008
BCK1_YEASTBCK1genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
RAD14_YEASTRAD14genetic
27708008
AVT4_YEASTAVT4genetic
27708008
SPS4_YEASTSPS4genetic
27708008
RAD1_YEASTRAD1genetic
27708008
SGF11_YEASTSGF11genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LRE1_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-474 AND SER-516, 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-516, AND MASSSPECTROMETRY.

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