SYC_YEAST - dbPTM
SYC_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYC_YEAST
UniProt AC P53852
Protein Name Cysteine--tRNA ligase
Gene Name YNL247W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 767
Subcellular Localization
Protein Description
Protein Sequence MNIFIKALRRYTIMSTPKIVQPKWKVPTPQAKETVLKLYNSLTRSKVEFIPQSGNRGVTWYSCGPTVYDASHMGHARNYVSIDINRRIIQDYFGYDVQFVQNVTDIDDKIILRARQNYLFDNFVKENDTKFNATVVDKVKTALFQYINKNFTIQGSEIKTIEEFETWLSNADTETLKLENPKFPMHVTAVQNAIESITKGDSMDAEVAFEKVKDVTVPLLDKELGSTISNPEIFRQLPAYWEQKFNDDMLSLNVLPPTVTTRVSEYVPEIIDFVQKIIDNGYAYATSDGSVYFDTLKFDKSPNHDYAKCQPWNKGQLDLINDGEGSLSNFADNGKKSNNDFALWKASKAGEPEWESPWGKGRPGWHIECSVMASDILGSNIDIHSGGIDLAFPHHDNELAQSEARFDNQQWINYFLHTGHLHIEGQKMSKSLKNFITIQEALKKFSPRQLRLAFASVQWNNQLDFKESLIHEVKSFENSMNNFFKTIRALKNDAASAGHISKKFSPLEKELLADFVESESKVHSAFCDNLSTPVALKTLSELVTKSNTYITTAGAALKIEPLIAICSYITKILRIIGFPSRPDNLGWAAQAGSNDGSLGSLEDTVMPYVKCLSTFRDDVRSLAIKKAEPKEFLQLTDKIRNEDLLNLNVALDDRNGQSALIKFLTNDEKLEIVKLNEEKHANELAKKQKKLEQQKLREQKENERKQKAQIKPQDMFKDVTLYSAWDEQGLPTKDKDGNDITKSMTKKLKKQWEQQKKLHEEYFGEDK
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
23AcetylationTPKIVQPKWKVPTPQ
CCCCCCCCCCCCCHH		42.4225381059
28PhosphorylationQPKWKVPTPQAKETV
CCCCCCCCHHHHHHH		30.9021440633
37AcetylationQAKETVLKLYNSLTR
HHHHHHHHHHHHCCC		44.5924489116
41PhosphorylationTVLKLYNSLTRSKVE
HHHHHHHHCCCCCCE		19.9822369663
43PhosphorylationLKLYNSLTRSKVEFI
HHHHHHCCCCCCEEE		32.4922369663
46UbiquitinationYNSLTRSKVEFIPQS
HHHCCCCCCEEECCC		42.3623749301
46AcetylationYNSLTRSKVEFIPQS
HHHCCCCCCEEECCC		42.3624489116
125AcetylationYLFDNFVKENDTKFN
HHHHHCCCCCCCCCC		46.8122865919
1402-HydroxyisobutyrylationATVVDKVKTALFQYI
CCHHHHHHHHHHHHH		33.55-
182AcetylationTLKLENPKFPMHVTA
CEECCCCCCCCHHHH		73.9324489116
222AcetylationVTVPLLDKELGSTIS
CCHHCCCHHHCCCCC		55.6024489116
301PhosphorylationDTLKFDKSPNHDYAK
EEEECCCCCCCCCCC		32.5528889911
326PhosphorylationLINDGEGSLSNFADN
CCCCCCCCHHHCCCC		25.0722369663
328PhosphorylationNDGEGSLSNFADNGK
CCCCCCHHHCCCCCC		31.4422369663
345AcetylationNNDFALWKASKAGEP
CCCCHHHHCCCCCCC		43.5724489116
433AcetylationQKMSKSLKNFITIQE
HHHCHHHHHHHHHHH		57.8324489116
443AcetylationITIQEALKKFSPRQL
HHHHHHHHHCCHHHH		59.8424489116
474AcetylationESLIHEVKSFENSMN
HHHHHHHHHHHHHHH		46.5824489116
485AcetylationNSMNNFFKTIRALKN
HHHHHHHHHHHHHHH		38.6224489116
621PhosphorylationTFRDDVRSLAIKKAE
HCCHHHHHHHHCCCC		23.2321440633
630AcetylationAIKKAEPKEFLQLTD
HHCCCCCHHHHHHHH		53.2424489116
665PhosphorylationSALIKFLTNDEKLEI
EEEEHHHCCCCCCEE		43.7022369663
669AcetylationKFLTNDEKLEIVKLN
HHHCCCCCCEEEECC		55.0424489116
674AcetylationDEKLEIVKLNEEKHA
CCCCEEEECCHHHHH		51.7824489116
679AcetylationIVKLNEEKHANELAK
EEECCHHHHHHHHHH		41.6724489116
735AcetylationQGLPTKDKDGNDITK
CCCCCCCCCCCCCCH		69.9224489116
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 SYC_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYC_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 SYC_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSK1_YEASTPSK1physical
16554755
HOSM_YEASTLYS21physical
16554755
NACA_YEASTEGD2physical
16554755
SYC_YEASTYNL247Wphysical
9523015
MAS5_YEASTYDJ1physical
19536198
SYC_YEASTYNL247Wphysical
22615397
CDC23_YEASTCDC23genetic
27708008
SWC5_YEASTSWC5genetic
27708008
MRM2_YEASTMRM2genetic
27708008
SAC1_YEASTSAC1genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
RS3A2_YEASTRPS1Bgenetic
27708008
CDK1_YEASTCDC28genetic
27708008
ERF3_YEASTSUP35genetic
27708008
TCPZ_YEASTCCT6genetic
27708008
NSE3_YEASTNSE3genetic
27708008
GPI11_YEASTGPI11genetic
27708008
CCA1_YEASTCCA1genetic
27708008
ACT_YEASTACT1genetic
27708008
CP51_YEASTERG11genetic
27708008
CDC12_YEASTCDC12genetic
27708008
TIM44_YEASTTIM44genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
NMT_YEASTNMT1genetic
27708008
DYR_YEASTDFR1genetic
27708008
APC5_YEASTAPC5genetic
27708008
FUN30_YEASTFUN30genetic
27708008
SKT5_YEASTSKT5genetic
27708008
THRC_YEASTTHR4genetic
27708008
TRM3_YEASTTRM3genetic
27708008
HEL2_YEASTHEL2genetic
27708008
MRX8_YEASTYDR336Wgenetic
27708008
PALF_YEASTRIM8genetic
27708008
PHB2_YEASTPHB2genetic
27708008
UPS1_YEASTUPS1genetic
27708008
MMS22_YEASTMMS22genetic
27708008
ECM19_YEASTECM19genetic
27708008
SERC_YEASTSER1genetic
27708008
LIPA_YEASTLIP5genetic
27708008
IRA2_YEASTIRA2genetic
27453043
CDC42_YEASTCDC42genetic
27453043
DCOR_YEASTSPE1genetic
27453043
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYC_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-326; SER-328 ANDTHR-665, 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-326, 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-326, AND MASSSPECTROMETRY.

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