SYDC_YEAST - dbPTM
SYDC_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYDC_YEAST
UniProt AC P04802
Protein Name Aspartate--tRNA ligase, cytoplasmic
Gene Name DPS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 557
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MSQDENIVKAVEESAEPAQVILGEDGKPLSKKALKKLQKEQEKQRKKEERALQLEAEREAREKKAAAEDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDKEVLFRARVHNTRQQGATLAFLTLRQQASLIQGLVKANKEGTISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNLEIHITKIYTISETPEALPILLEDASRSEAEAEAAGLPVVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVEEFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFEDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP
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
2Phosphorylation------MSQDENIVK
------CCCHHHHHH		46.4622369663
2Acetylation------MSQDENIVK
------CCCHHHHHH		46.469298649
14PhosphorylationIVKAVEESAEPAQVI
HHHHHHHHCCCCEEE		25.1522369663
27UbiquitinationVILGEDGKPLSKKAL
EEECCCCCCCCHHHH		55.9223749301
27AcetylationVILGEDGKPLSKKAL
EEECCCCCCCCHHHH		55.9224489116
30PhosphorylationGEDGKPLSKKALKKL
CCCCCCCCHHHHHHH		40.4129136822
31SuccinylationEDGKPLSKKALKKLQ
CCCCCCCHHHHHHHH		50.1523954790
31AcetylationEDGKPLSKKALKKLQ
CCCCCCCHHHHHHHH		50.1524489116
72AcetylationAAAEDTAKDNYGKLP
HHHHHHHHHCCCCCC		48.9124489116
77AcetylationTAKDNYGKLPLIQSR
HHHHCCCCCCEECCC		36.2524489116
77SuccinylationTAKDNYGKLPLIQSR
HHHHCCCCCCEECCC		36.2523954790
86PhosphorylationPLIQSRDSDRTGQKR
CEECCCCCCCCCCCE		28.0721440633
95AcetylationRTGQKRVKFVDLDEA
CCCCCEEEEEEHHHC		43.6424489116
103AcetylationFVDLDEAKDSDKEVL
EEEHHHCCCCCHHEE		56.5724489116
105PhosphorylationDLDEAKDSDKEVLFR
EHHHCCCCCHHEEEE		50.2928889911
107AcetylationDEAKDSDKEVLFRAR
HHCCCCCHHEEEEEE		54.3924489116
1072-HydroxyisobutyrylationDEAKDSDKEVLFRAR
HHCCCCCHHEEEEEE		54.39-
142AcetylationSLIQGLVKANKEGTI
HHHHHHHHHCCCCCC		51.8124489116
145AcetylationQGLVKANKEGTISKN
HHHHHHCCCCCCCHH		63.4825381059
151AcetylationNKEGTISKNMVKWAG
CCCCCCCHHHHHHCC		45.2522865919
180UbiquitinationKKVDEPIKSATVQNL
HHCCCCCHHCEEEEE		44.7624961812
196PhosphorylationIHITKIYTISETPEA
EEEEEEEEECCCCCH		22.8421126336
212PhosphorylationPILLEDASRSEAEAE
HHHHHHHCCCHHHHH		48.9730377154
214PhosphorylationLLEDASRSEAEAEAA
HHHHHCCCHHHHHHC		38.3722369663
243PhosphorylationVIDLRTVTNQAIFRI
EEEHHHHCHHHHHHH		22.4728889911
266UbiquitinationREYLATKKFTEVHTP
HHHHHCCCCCCCCCC		53.8423749301
272PhosphorylationKKFTEVHTPKLLGAP
CCCCCCCCCCCCCCC		27.5622369663
284PhosphorylationGAPSEGGSSVFEVTY
CCCCCCCCCCEEEEE		33.9019779198
285PhosphorylationAPSEGGSSVFEVTYF
CCCCCCCCCEEEEEE		33.8219779198
293AcetylationVFEVTYFKGKAYLAQ
CEEEEEECCEEEEEC		49.4324489116
297PhosphorylationTYFKGKAYLAQSPQF
EEECCEEEEECCCCC		13.1722369663
301PhosphorylationGKAYLAQSPQFNKQQ
CEEEEECCCCCCCCC		18.3022369663
306UbiquitinationAQSPQFNKQQLIVAD
ECCCCCCCCCEEEEC		40.4823749301
306AcetylationAQSPQFNKQQLIVAD
ECCCCCCCCCEEEEC		40.4824489116
329PhosphorylationPVFRAENSNTHRHMT
CEEECCCCCCCCCCC		34.3128889911
390AcetylationQYPVEEFKLPKDGKM
CCCCHHCCCCCCCCE		68.1324489116
393AcetylationVEEFKLPKDGKMVRL
CHHCCCCCCCCEEEE		84.9324489116
403UbiquitinationKMVRLTYKEGIEMLR
CEEEEEHHHHHHHHH		44.2023749301
403AcetylationKMVRLTYKEGIEMLR
CEEEEEHHHHHHHHH		44.2024489116
403SuccinylationKMVRLTYKEGIEMLR
CEEEEEHHHHHHHHH		44.2023954790
414SuccinylationEMLRAAGKEIGDFED
HHHHHHCCCCCCHHH		41.2423954790
414UbiquitinationEMLRAAGKEIGDFED
HHHHHHCCCCCCHHH		41.2423749301
414AcetylationEMLRAAGKEIGDFED
HHHHHHCCCCCCHHH		41.2424489116
428AcetylationDLSTENEKFLGKLVR
HCCCCCHHHHHHHHH		58.4324489116
432AcetylationENEKFLGKLVRDKYD
CCHHHHHHHHHCCCC		46.0524489116
437AcetylationLGKLVRDKYDTDFYI
HHHHHHCCCCCCEEE		34.1724489116
438PhosphorylationGKLVRDKYDTDFYIL
HHHHHCCCCCCEEEE		28.5022890988
440PhosphorylationLVRDKYDTDFYILDK
HHHCCCCCCEEEEEC		25.5622890988
443PhosphorylationDKYDTDFYILDKFPL
CCCCCCEEEEECCCC		11.9122890988
481PhosphorylationMRGEEILSGAQRIHD
HCCHHHHHHHHHHHH		37.4328889911
502PhosphorylationRMKAHGLSPEDPGLK
HHHHCCCCCCCCCCH		30.7322369663
546PhosphorylationLKNIRRASLFPRDPK
CCCCHHHHCCCCCCC		28.8217287358
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 SYDC_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYDC_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 SYDC_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPG1_YEASTPSA1physical
16429126
PYR1_YEASTURA2physical
16429126
ELP6_YEASTELP6genetic
19061648
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYDC_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins.";
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.;
Electrophoresis 18:1347-1360(1997).
Cited for: ACETYLATION AT SER-2.
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-14; THR-243; SER-301;SER-502 AND SER-546, 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-14, AND MASSSPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND MASSSPECTROMETRY.
"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-301, 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 SER-301, AND MASSSPECTROMETRY.

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