SYFA_YEAST - dbPTM
SYFA_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYFA_YEAST
UniProt AC P15625
Protein Name Phenylalanine--tRNA ligase alpha subunit
Gene Name FRS2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 503
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MSDFQLEILKKLDELDEIKSTLATFPQHGSQDVLSALNSLKAHNKLEFSKVDTVTYDLTKEGAQILNEGSYEIKLVKLIQELGQLQIKDVMSKLGPQVGKVGQARAFKNGWIAKNASNELELSAKLQNTDLNELTDETQSILAQIKNNSHLDSIDAKILNDLKKRKLIAQGKITDFNVTKGPEFSTDLTKLETDLTSDMVSTNAYKDLKFKPYNFNSQGVQISSGALHPLNKVREEFRQIFFSMGFTEMPSNQYVETGFWNFDALYVPQQHPARDLQDTFYIKDPLTADLPDDKTYMDNIKAVHEQGRFGSIGYRYNWKPEECQKLVLRTHSTAISARMLHDLAKDPKPTRLFSIDRVFRNEAVDATHLAEFHQVEGVLADYNITLGDLIKFMEEFFERMGVTGLRFKPTYNPYTEPSMEIFSWHEGLQKWVEIGNSGMFRPEMLESMGLPKDLRVLGWGLSLERPTMIKYKVQNIRELLGHKVSLDFIETNPAARLDEDLYE
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
2Acetylation------MSDFQLEIL
------CCHHHHHHH		47.329298649
2Phosphorylation------MSDFQLEIL
------CCHHHHHHH		47.3228152593
39PhosphorylationDVLSALNSLKAHNKL
HHHHHHHHHHHHCCC		31.9028889911
41AcetylationLSALNSLKAHNKLEF
HHHHHHHHHHCCCCC		47.6324489116
60AcetylationTVTYDLTKEGAQILN
EEEEECCHHHHHHHC		62.5424489116
88AcetylationELGQLQIKDVMSKLG
HHCCCCHHHHHHHHC		31.1724489116
93AcetylationQIKDVMSKLGPQVGK
CHHHHHHHHCCCCCC		39.0924489116
117PhosphorylationGWIAKNASNELELSA
CEECCCCCCHHHHHH		39.9828889911
149PhosphorylationLAQIKNNSHLDSIDA
HHHHHCCCCCHHCCH		34.5228889911
157AcetylationHLDSIDAKILNDLKK
CCHHCCHHHHHHHHH		43.9324489116
163SuccinylationAKILNDLKKRKLIAQ
HHHHHHHHHCCEEEE		54.0923954790
172SuccinylationRKLIAQGKITDFNVT
CCEEEECCCCCCCCC		30.2823954790
1722-HydroxyisobutyrylationRKLIAQGKITDFNVT
CCEEEECCCCCCCCC		30.28-
185PhosphorylationVTKGPEFSTDLTKLE
CCCCCCCCCCHHHHC		21.2527017623
190AcetylationEFSTDLTKLETDLTS
CCCCCHHHHCCCCCC		52.1824489116
193PhosphorylationTDLTKLETDLTSDMV
CCHHHHCCCCCCCCC		46.9027017623
196PhosphorylationTKLETDLTSDMVSTN
HHHCCCCCCCCCCCC		26.0319779198
197PhosphorylationKLETDLTSDMVSTNA
HHCCCCCCCCCCCCC		30.8819779198
201PhosphorylationDLTSDMVSTNAYKDL
CCCCCCCCCCCCCCC		14.8728889911
202PhosphorylationLTSDMVSTNAYKDLK
CCCCCCCCCCCCCCC		16.6828889911
205PhosphorylationDMVSTNAYKDLKFKP
CCCCCCCCCCCCCCC		13.7024961812
206SuccinylationMVSTNAYKDLKFKPY
CCCCCCCCCCCCCCC		54.9223954790
206AcetylationMVSTNAYKDLKFKPY
CCCCCCCCCCCCCCC		54.9224489116
206UbiquitinationMVSTNAYKDLKFKPY
CCCCCCCCCCCCCCC		54.9223749301
209AcetylationTNAYKDLKFKPYNFN
CCCCCCCCCCCCCCC		62.5724489116
211AcetylationAYKDLKFKPYNFNSQ
CCCCCCCCCCCCCCC		45.0324489116
217PhosphorylationFKPYNFNSQGVQISS
CCCCCCCCCCEEECC		24.9528889911
232UbiquitinationGALHPLNKVREEFRQ
CCCCCHHHHHHHHHH		50.8023749301
232AcetylationGALHPLNKVREEFRQ
CCCCCHHHHHHHHHH		50.8024489116
283AcetylationLQDTFYIKDPLTADL
CCCCEEECCCCCCCC		41.7524489116
283SuccinylationLQDTFYIKDPLTADL
CCCCEEECCCCCCCC		41.7523954790
283UbiquitinationLQDTFYIKDPLTADL
CCCCEEECCCCCCCC		41.7524961812
301AcetylationKTYMDNIKAVHEQGR
CCHHHHHHHHHHCCC		51.0824489116
311PhosphorylationHEQGRFGSIGYRYNW
HHCCCCCCCCCCCCC		15.3228889911
319AcetylationIGYRYNWKPEECQKL
CCCCCCCCHHHHHHH		38.6222865919
325AcetylationWKPEECQKLVLRTHS
CCHHHHHHHHHHHHH		52.8224489116
325UbiquitinationWKPEECQKLVLRTHS
CCHHHHHHHHHHHHH		52.8222817900
330PhosphorylationCQKLVLRTHSTAISA
HHHHHHHHHHHHHHH		18.9329688323
332PhosphorylationKLVLRTHSTAISARM
HHHHHHHHHHHHHHH		20.9423749301
333PhosphorylationLVLRTHSTAISARML
HHHHHHHHHHHHHHH		22.0229688323
336PhosphorylationRTHSTAISARMLHDL
HHHHHHHHHHHHHHH		13.8328889911
437PhosphorylationKWVEIGNSGMFRPEM
HHHHCCCCCCCCHHH		26.8219823750
447PhosphorylationFRPEMLESMGLPKDL
CCHHHHHHCCCCCCC		17.7519823750
470UbiquitinationLERPTMIKYKVQNIR
CCCCHHHHHHHHCHH		28.3523749301
470AcetylationLERPTMIKYKVQNIR
CCCCHHHHHHHHCHH		28.3524489116
472UbiquitinationRPTMIKYKVQNIREL
CCHHHHHHHHCHHHH		32.1322817900
483UbiquitinationIRELLGHKVSLDFIE
HHHHHCCCEEHHHHH		31.5523749301
483AcetylationIRELLGHKVSLDFIE
HHHHHCCCEEHHHHH		31.5524489116
485PhosphorylationELLGHKVSLDFIETN
HHHCCCEEHHHHHCC		27.3327017623
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 SYFA_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYFA_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 SYFA_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYFB_YEASTFRS1physical
16429126
CDC20_YEASTCDC20genetic
27708008
SHE1_YEASTSHE1genetic
27708008
SWC5_YEASTSWC5genetic
27708008
YCQ6_YEASTYCR016Wgenetic
27708008
ATG15_YEASTATG15genetic
27708008
NBP2_YEASTNBP2genetic
27708008
CAJ1_YEASTCAJ1genetic
27708008
RS25A_YEASTRPS25Agenetic
27708008
KSP1_YEASTKSP1genetic
27708008
CYT2_YEASTCYT2genetic
27708008
SHB17_YEASTSHB17genetic
27708008
SEI1_YEASTFLD1genetic
27708008
TSA1_YEASTTSA1genetic
27708008
ATP18_YEASTATP18genetic
27708008
CSI1_YEASTCSI1genetic
27708008
TRI1_YEASTTRI1genetic
27708008
PET8_YEASTPET8genetic
27708008
RL9B_YEASTRPL9Bgenetic
27708008
PMS1_YEASTPMS1genetic
27708008
MKT1_YEASTMKT1genetic
27708008
MSO1_YEASTMSO1genetic
27708008
ELG1_YEASTELG1genetic
27708008
IES4_YEASTIES4genetic
27708008
MUM3_YEASTMUM3genetic
27708008
KPYK2_YEASTPYK2genetic
27708008
ATPN_YEASTATP20genetic
27708008
NAA30_YEASTMAK3genetic
27708008
SPEE_YEASTSPE3genetic
27708008
TFC3_YEASTTFC3genetic
27708008
ALG14_YEASTALG14genetic
27708008
CDK1_YEASTCDC28genetic
27708008
UAP1_YEASTQRI1genetic
27708008
GLE1_YEASTGLE1genetic
27708008
RPC10_YEASTRPC11genetic
27708008
RPC9_YEASTRPC17genetic
27708008
NU192_YEASTNUP192genetic
27708008
PRP21_YEASTPRP21genetic
27708008
KTHY_YEASTCDC8genetic
27708008
RFC2_YEASTRFC2genetic
27708008
PRI2_YEASTPRI2genetic
27708008
BET3_YEASTBET3genetic
27708008
PRP19_YEASTPRP19genetic
27708008
SYFB_YEASTFRS1genetic
27708008
SEC22_YEASTSEC22genetic
27708008
POB3_YEASTPOB3genetic
27708008
BET5_YEASTBET5genetic
27708008
MCM1_YEASTMCM1genetic
27708008
LST8_YEASTLST8genetic
27708008
DPOA_YEASTPOL1genetic
27708008
RPC6_YEASTRPC34genetic
27708008
SEC23_YEASTSEC23genetic
27708008
DEP1_YEASTDEP1genetic
27708008
BRE1_YEASTBRE1genetic
27708008
PAR32_YEASTPAR32genetic
27708008
TRM1_YEASTTRM1genetic
27708008
TYW3_YEASTTYW3genetic
27708008
PHB2_YEASTPHB2genetic
27708008
LRP1_YEASTLRP1genetic
27708008
FMC1_YEASTFMC1genetic
27708008
MOG1_YEASTMOG1genetic
27708008
VPS24_YEASTVPS24genetic
27708008
TYW2_YEASTTRM12genetic
27708008
NU188_YEASTNUP188genetic
27708008
TR732_YEASTTRM732genetic
27708008
SCS7_YEASTSCS7genetic
27708008
DSK2_YEASTDSK2genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
EOS1_YEASTEOS1genetic
27708008
PHO23_YEASTPHO23genetic
27708008
TRM11_YEASTTRM11genetic
27708008
TYW4_YEASTPPM2genetic
27708008
UME1_YEASTUME1genetic
27708008
WDR6_YEASTRTT10genetic
27708008
PLS1_HUMANPLSCR1physical
27107014
GOPC_HUMANGOPCphysical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYFA_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-39 AND SER-117, AND MASSSPECTROMETRY.

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