GLY1_YEAST - dbPTM
GLY1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLY1_YEAST
UniProt AC P37303
Protein Name Low specificity L-threonine aldolase
Gene Name GLY1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 387
Subcellular Localization
Protein Description Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde..
Protein Sequence MTEFELPPKYITAANDLRSDTFTTPTAEMMEAALEASIGDAVYGEDVDTVRLEQTVARMAGKEAGLFCVSGTLSNQIAIRTHLMQPPYSILCDYRAHVYTHEAAGLAILSQAMVVPVVPSNGDYLTLEDIKSHYVPDDGDIHGAPTRLISLENTLHGIVYPLEELVRIKAWCMENGLKLHCDGARIWNAAAQSGVPLKQYGEIFDSISICLSKSMGAPIGSVLVGNLKFVKKATHFRKQQGGGIRQSGMMARMALVNINNDWKSQLLYSHSLAHELAEYCEAKGIPLESPADTNFVFINLKAARMDPDVLVKKGLKYNVKLMGGRVSFHYQVTRDTLEKVKLAISEAFDYAKEHPFDCNGPTQIYRSESTEVDVDGNAIREIKTYKY
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
62UbiquitinationTVARMAGKEAGLFCV
HHHHHCCCCCEEEEE		34.5523749301
131UbiquitinationYLTLEDIKSHYVPDD
EEEHHHHHHCCCCCC		43.4317644757
132PhosphorylationLTLEDIKSHYVPDDG
EEHHHHHHCCCCCCC		22.0027738172
178AcetylationWCMENGLKLHCDGAR
HHHHCCEEEEECCHH		37.2724489116
198UbiquitinationAQSGVPLKQYGEIFD
HHHCCCHHHHHHHHH		35.0917644757
213N6-(pyridoxal phosphate)lysineSISICLSKSMGAPIG
HHHHHHHHCCCCCCC		31.36-
213OtherSISICLSKSMGAPIG
HHHHHHHHCCCCCCC		31.36-
213UbiquitinationSISICLSKSMGAPIG
HHHHHHHHCCCCCCC		31.3617644757
214PhosphorylationISICLSKSMGAPIGS
HHHHHHHCCCCCCCE		21.0521440633
228UbiquitinationSVLVGNLKFVKKATH
EEEECCEEEHEECCC		52.7023749301
228AcetylationSVLVGNLKFVKKATH
EEEECCEEEHEECCC		52.7024489116
231UbiquitinationVGNLKFVKKATHFRK
ECCEEEHEECCCCHH		39.5623793018
232UbiquitinationGNLKFVKKATHFRKQ
CCEEEHEECCCCHHH		53.8922817900
263UbiquitinationVNINNDWKSQLLYSH
EECCCCHHHHHHHCH		31.0517644757
283UbiquitinationLAEYCEAKGIPLESP
HHHHHHHCCCCCCCC		34.7717644757
301UbiquitinationNFVFINLKAARMDPD
CEEEEEEEECCCCHH		35.2023749301
312UbiquitinationMDPDVLVKKGLKYNV
CCHHHHHHCCCEEEE		36.6423749301
312AcetylationMDPDVLVKKGLKYNV
CCHHHHHHCCCEEEE		36.6424489116
313UbiquitinationDPDVLVKKGLKYNVK
CHHHHHHCCCEEEEE		63.0922817900
316UbiquitinationVLVKKGLKYNVKLMG
HHHHCCCEEEEEEEC		43.3722817900
320UbiquitinationKGLKYNVKLMGGRVS
CCCEEEEEEECCEEE		29.1723749301
341UbiquitinationRDTLEKVKLAISEAF
HHHHHHHHHHHHHHH		43.1817644757
352UbiquitinationSEAFDYAKEHPFDCN
HHHHHHHHHCCCCCC		50.7817644757
362PhosphorylationPFDCNGPTQIYRSES
CCCCCCCCEEEECCC		29.0625521595
365PhosphorylationCNGPTQIYRSESTEV
CCCCCEEEECCCCEE		9.7725521595
367PhosphorylationGPTQIYRSESTEVDV
CCCEEEECCCCEEEC		20.9422369663
369PhosphorylationTQIYRSESTEVDVDG
CEEEECCCCEEECCC		30.9822369663
370PhosphorylationQIYRSESTEVDVDGN
EEEECCCCEEECCCC		35.6625521595
383UbiquitinationGNAIREIKTYKY---
CCEEEEEEEECC---		40.8423749301
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 GLY1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLY1_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 GLY1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GYP5_YEASTGYP5physical
15802519
GLYM_YEASTSHM1genetic
8852837
GLYM_YEASTSHM1genetic
8132653
GLYC_YEASTSHM2genetic
8852837
GLYC_YEASTSHM2genetic
8132653
KHSE_YEASTTHR1genetic
16941010
THRC_YEASTTHR4genetic
16941010
GCST_YEASTGCV1genetic
8852837
S2538_YEASTYDL119Cgenetic
26821380
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLY1_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-367; SER-369 ANDTHR-370, AND MASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-370, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery.";
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-228, AND MASSSPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-228, AND MASSSPECTROMETRY.

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