TRP_YEAST - dbPTM
TRP_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRP_YEAST
UniProt AC P00931
Protein Name Tryptophan synthase
Gene Name TRP5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 707
Subcellular Localization
Protein Description
Protein Sequence MSEQLRQTFANAKKENRNALVTFMTAGYPTVKDTVPILKGFQDGGVDIIELGMPFSDPIADGPTIQLSNTVALQNGVTLPQTLEMVSQARNEGVTVPIILMGYYNPILNYGEERFIQDAAKAGANGFIIVDLPPEEALKVRNYINDNGLSLIPLVAPSTTDERLELLSHIADSFVYVVSRMGTTGVQSSVASDLDELISRVRKYTKDTPLAVGFGVSTREHFQSVGSVADGVVIGSKIVTLCGDAPEGKRYDVAKEYVQGILNGAKHKVLSKDEFFAFQKESLKSANVKKEILDEFDENHKHPIRFGDFGGQYVPEALHACLRELEKGFDEAVADPTFWEDFKSLYSYIGRPSSLHKAERLTEHCQGAQIWLKREDLNHTGSHKINNALAQVLLAKRLGKKNVIAETGAGQHGVATATACAKFGLTCTVFMGAEDVRRQALNVFRMRILGAKVIAVTNGTKTLRDATSEAFRFWVTNLKTTYYVVGSAIGPHPYPTLVRTFQSVIGKETKEQFAAMNNGKLPDAVVACVGGGSNSTGMFSPFEHDTSVKLLGVEAGGDGVDTKFHSATLTAGRPGVFHGVKTYVLQDSDGQVHDTHSVSAGLDYPGVGPELAYWKSTGRAQFIAATDAQALLGFKLLSQLEGIIPALESSHAVYGACELAKTMKPDQHLVINISGRGDKDVQSVAEVLPKLGPKIGWDLRFEEDPSA
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
13SuccinylationRQTFANAKKENRNAL
HHHHHHHHHHHHHHE		61.5023954790
22PhosphorylationENRNALVTFMTAGYP
HHHHHEEEEHHCCCC		14.4522369663
25PhosphorylationNALVTFMTAGYPTVK
HHEEEEHHCCCCCHH		16.8522369663
28PhosphorylationVTFMTAGYPTVKDTV
EEEHHCCCCCHHHHH		8.0222369663
30PhosphorylationFMTAGYPTVKDTVPI
EHHCCCCCHHHHHHH		31.5322369663
32AcetylationTAGYPTVKDTVPILK
HCCCCCHHHHHHHHH		50.5924489116
168PhosphorylationDERLELLSHIADSFV
HHHHHHHHHHHHHCH		26.0228889911
203AcetylationELISRVRKYTKDTPL
HHHHHHHHHCCCCCC		55.1824489116
206AcetylationSRVRKYTKDTPLAVG
HHHHHHCCCCCCEEE		57.4224489116
224PhosphorylationSTREHFQSVGSVADG
CHHHHHHHHCCCCCC		27.7419779198
249UbiquitinationCGDAPEGKRYDVAKE
CCCCCCCCCHHHHHH		46.2323749301
255AcetylationGKRYDVAKEYVQGIL
CCCHHHHHHHHHHHH		49.8024489116
266UbiquitinationQGILNGAKHKVLSKD
HHHHCCCCCEECCHH		45.4117644757
2682-HydroxyisobutyrylationILNGAKHKVLSKDEF
HHCCCCCEECCHHHH		44.13-
268UbiquitinationILNGAKHKVLSKDEF
HHCCCCCEECCHHHH		44.1317644757
268AcetylationILNGAKHKVLSKDEF
HHCCCCCEECCHHHH		44.1324489116
272UbiquitinationAKHKVLSKDEFFAFQ
CCCEECCHHHHHHHH		58.0517644757
272AcetylationAKHKVLSKDEFFAFQ
CCCEECCHHHHHHHH		58.0524489116
280AcetylationDEFFAFQKESLKSAN
HHHHHHHHHHHHCCC		42.7024489116
280UbiquitinationDEFFAFQKESLKSAN
HHHHHHHHHHHHCCC		42.7017644757
301AcetylationDEFDENHKHPIRFGD
HHHHHCCCCCCCCCC		63.7624489116
327AcetylationACLRELEKGFDEAVA
HHHHHHHHCCCHHHC		76.9924489116
327UbiquitinationACLRELEKGFDEAVA
HHHHHHHHCCCHHHC		76.9917644757
343UbiquitinationPTFWEDFKSLYSYIG
CCHHHHHHHHHHHHC		52.4517644757
344PhosphorylationTFWEDFKSLYSYIGR
CHHHHHHHHHHHHCC		32.3121440633
353PhosphorylationYSYIGRPSSLHKAER
HHHHCCCHHHHHHHH		44.1421440633
354PhosphorylationSYIGRPSSLHKAERL
HHHCCCHHHHHHHHH		36.8621440633
357AcetylationGRPSSLHKAERLTEH
CCCHHHHHHHHHHHH		58.1824489116
373UbiquitinationQGAQIWLKREDLNHT
CCCEEEEEHHHCCCC		38.4517644757
384N6-(pyridoxal phosphate)lysineLNHTGSHKINNALAQ
CCCCCHHHHHHHHHH		49.15-
384OtherLNHTGSHKINNALAQ
CCCCCHHHHHHHHHH		49.15-
384AcetylationLNHTGSHKINNALAQ
CCCCCHHHHHHHHHH		49.1524489116
384UbiquitinationLNHTGSHKINNALAQ
CCCCCHHHHHHHHHH		49.1517644757
396UbiquitinationLAQVLLAKRLGKKNV
HHHHHHHHHHCCCCE		48.3923749301
396AcetylationLAQVLLAKRLGKKNV
HHHHHHHHHHCCCCE		48.3924489116
400UbiquitinationLLAKRLGKKNVIAET
HHHHHHCCCCEEEEC		45.8522817900
401UbiquitinationLAKRLGKKNVIAETG
HHHHHCCCCEEEECC		55.4322817900
461UbiquitinationIAVTNGTKTLRDATS
EEEECCCCCHHHHCH		47.1323749301
479UbiquitinationRFWVTNLKTTYYVVG
HHHHHCCCCEEEEEC		40.6717644757
507UbiquitinationTFQSVIGKETKEQFA
HHHHHHCHHHHHHHH		51.6022817900
507AcetylationTFQSVIGKETKEQFA
HHHHHHCHHHHHHHH		51.6024489116
510UbiquitinationSVIGKETKEQFAAMN
HHHCHHHHHHHHHHH		51.0823749301
5102-HydroxyisobutyrylationSVIGKETKEQFAAMN
HHHCHHHHHHHHHHH		51.08-
528GlutathionylationLPDAVVACVGGGSNS
CCCCEEEEECCCCCC		1.6522833525
540PhosphorylationSNSTGMFSPFEHDTS
CCCCCCCCCCCCCCC		21.5628889911
562PhosphorylationAGGDGVDTKFHSATL
ECCCCCCCCCEECEE		32.9527214570
563AcetylationGGDGVDTKFHSATLT
CCCCCCCCCEECEEC		36.2924489116
581UbiquitinationPGVFHGVKTYVLQDS
CCEECEEEEEEEECC		38.4417644757
664AcetylationCELAKTMKPDQHLVI
HHHHHHCCCCCEEEE		51.1524489116
679UbiquitinationNISGRGDKDVQSVAE
EECCCCCHHHHHHHH		63.7217644757
683PhosphorylationRGDKDVQSVAEVLPK
CCCHHHHHHHHHHHH		24.1217563356
690UbiquitinationSVAEVLPKLGPKIGW
HHHHHHHHHCCCCCC		63.0124961812
690AcetylationSVAEVLPKLGPKIGW
HHHHHHHHHCCCCCC		63.0124489116
694AcetylationVLPKLGPKIGWDLRF
HHHHHCCCCCCEECC		52.6424489116
706PhosphorylationLRFEEDPSA------
ECCCCCCCC------		59.9622369663
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 TRP_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRP_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 TRP_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XPOT_YEASTLOS1genetic
3031485
SMT3_YEASTSMT3physical
18719252
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRP_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-540 AND SER-683, 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-683, AND MASSSPECTROMETRY.

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