SYKC_YEAST - dbPTM
SYKC_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYKC_YEAST
UniProt AC P15180
Protein Name Lysine--tRNA ligase, cytoplasmic
Gene Name KRS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 591
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MSQQDNVKAAAEGVANLHLDEATGEMVSKSELKKRIKQRQVEAKKAAKKAAAQPKPASKKKTDLFADLDPSQYFETRSRQIQELRKTHEPNPYPHKFHVSISNPEFLAKYAHLKKGETLPEEKVSIAGRIHAKRESGSKLKFYVLHGDGVEVQLMSQLQDYCDPDSYEKDHDLLKRGDIVGVEGYVGRTQPKKGGEGEVSVFVSRVQLLTPCLHMLPADHFGFKDQETRYRKRYLDLIMNKDARNRFITRSEIIRYIRRFLDQRKFIEVETPMMNVIAGGATAKPFITHHNDLDMDMYMRIAPELFLKQLVVGGLDRVYEIGRQFRNEGIDMTHNPEFTTCEFYQAYADVYDLMDMTELMFSEMVKEITGSYIIKYHPDPADPAKELELNFSRPWKRINMIEELEKVFNVKFPSGDQLHTAETGEFLKKILVDNKLECPPPLTNARMLDKLVGELEDTCINPTFIFGHPQMMSPLAKYSRDQPGLCERFEVFVATKEICNAYTELNDPFDQRARFEEQARQKDQGDDEAQLVDETFCNALEYGLPPTGGWGCGIDRLAMFLTDSNTIREVLLFPTLKPDVLREEVKKEEEN
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------MSQQDNVKA
------CCHHHHHHH		36.2327717283
2Acetylation------MSQQDNVKA
------CCHHHHHHH		36.239298649
8UbiquitinationMSQQDNVKAAAEGVA
CCHHHHHHHHHHHHH		38.2624961812
8AcetylationMSQQDNVKAAAEGVA
CCHHHHHHHHHHHHH		38.2624489116
29AcetylationATGEMVSKSELKKRI
HHCCCCCHHHHHHHH		36.2224489116
30PhosphorylationTGEMVSKSELKKRIK
HCCCCCHHHHHHHHH		40.4328889911
60AcetylationQPKPASKKKTDLFAD
CCCCCCCCCCCCCCC		59.4124489116
62PhosphorylationKPASKKKTDLFADLD
CCCCCCCCCCCCCCC		46.9822369663
71PhosphorylationLFADLDPSQYFETRS
CCCCCCHHHHHHHHH		36.8622890988
73PhosphorylationADLDPSQYFETRSRQ
CCCCHHHHHHHHHHH		14.0222890988
76PhosphorylationDPSQYFETRSRQIQE
CHHHHHHHHHHHHHH		24.8522890988
86UbiquitinationRQIQELRKTHEPNPY
HHHHHHHHHCCCCCC		67.8523749301
96AcetylationEPNPYPHKFHVSISN
CCCCCCCCCEEEECC		32.4324489116
100PhosphorylationYPHKFHVSISNPEFL
CCCCCEEEECCHHHH		16.2421440633
102PhosphorylationHKFHVSISNPEFLAK
CCCEEEECCHHHHHH		38.5322369663
109AcetylationSNPEFLAKYAHLKKG
CCHHHHHHHHHHHCC		45.1524489116
123AcetylationGETLPEEKVSIAGRI
CCCCCHHHHCCCCEE		39.3524489116
136PhosphorylationRIHAKRESGSKLKFY
EEEEECCCCCCEEEE		53.0219823750
138PhosphorylationHAKRESGSKLKFYVL
EEECCCCCCEEEEEE		44.0619823750
143PhosphorylationSGSKLKFYVLHGDGV
CCCCEEEEEEECCCC		10.6619779198
167PhosphorylationDYCDPDSYEKDHDLL
HHCCCCHHHHHHHHH		34.0919779198
224AcetylationPADHFGFKDQETRYR
CCCHHCCCCHHHHHH		59.9024489116
241UbiquitinationYLDLIMNKDARNRFI
HHHHHCCHHHHHCCC		35.0723749301
241AcetylationYLDLIMNKDARNRFI
HHHHHCCHHHHHCCC		35.0724489116
265UbiquitinationRRFLDQRKFIEVETP
HHHHHHCCCEEECCC		45.0923749301
284UbiquitinationIAGGATAKPFITHHN
ECCCCCCCCCCCCCC		35.7923749301
308UbiquitinationIAPELFLKQLVVGGL
HCHHHHHHHHHHCCH		33.9623749301
369PhosphorylationSEMVKEITGSYIIKY
HHHHHHHHCCEEEEE		22.5922369663
371PhosphorylationMVKEITGSYIIKYHP
HHHHHHCCEEEEECC		12.4322369663
372PhosphorylationVKEITGSYIIKYHPD
HHHHHCCEEEEECCC		14.1722369663
375AcetylationITGSYIIKYHPDPAD
HHCCEEEEECCCCCC		28.1324489116
385AcetylationPDPADPAKELELNFS
CCCCCHHHHHCCCCC		69.1224489116
396AcetylationLNFSRPWKRINMIEE
CCCCCCHHHHHHHHH		46.1924489116
411AcetylationLEKVFNVKFPSGDQL
HHHHHCCCCCCCCCC		53.3024489116
428AcetylationAETGEFLKKILVDNK
CCCHHHHHHHHHCCC		42.9924489116
435AcetylationKKILVDNKLECPPPL
HHHHHCCCCCCCCCC		40.9924489116
435UbiquitinationKKILVDNKLECPPPL
HHHHHCCCCCCCCCC		40.9923749301
450UbiquitinationTNARMLDKLVGELED
CCHHHHHHHHHHHHH		40.9023749301
473PhosphorylationFGHPQMMSPLAKYSR
CCCHHHHCHHHHHCC		16.0621440633
577SuccinylationVLLFPTLKPDVLREE
HHHCCCCCHHHHHHH		41.4723954790
577UbiquitinationVLLFPTLKPDVLREE
HHHCCCCCHHHHHHH		41.4723749301
577AcetylationVLLFPTLKPDVLREE
HHHCCCCCHHHHHHH		41.4724489116
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 SYKC_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYKC_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 SYKC_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC48_YEASTCDC48physical
11805826
TFB4_YEASTTFB4physical
11805826
TFB4_YEASTTFB4physical
16429126
GCN20_YEASTGCN20genetic
19061648
LSM3_YEASTLSM3genetic
19061648
CSN5_YEASTRRI1genetic
19061648
TRMB_YEASTTRM8genetic
19061648
SLX5_YEASTSLX5genetic
19061648
EIF3G_YEASTTIF35genetic
19061648
POP7_YEASTPOP7genetic
19061648
RS6A_YEASTRPS6Bgenetic
19061648
RS6B_YEASTRPS6Bgenetic
19061648
GCN1_YEASTGCN1genetic
19061648
PBP1_YEASTPBP1genetic
19061648
LSM1_YEASTLSM1genetic
19061648
TOR1_YEASTTOR1genetic
19061648
MUD2_YEASTMUD2genetic
19061648
TSR3_YEASTTSR3genetic
19061648
NOT3_YEASTNOT3genetic
19061648
TRM9_YEASTTRM9genetic
19061648
NCBP1_YEASTSTO1genetic
19061648
GIS2_YEASTGIS2genetic
19061648
SWM2_YEASTSWM2genetic
19061648
EF1G1_YEASTCAM1genetic
19061648
SGF11_YEASTSGF11genetic
19061648
SN309_YEASTSNT309genetic
19061648
CHD1_YEASTCHD1genetic
19061648
SIN3_YEASTSIN3genetic
19061648
EFTU_YEASTTUF1genetic
19061648
ECM8_YEASTECM8genetic
20093466
THRC_YEASTTHR4genetic
20093466
PAT1_YEASTPAT1genetic
20093466
PDP2_YEASTPTC6genetic
20093466
SAC3_YEASTSAC3genetic
20093466
BLM10_YEASTBLM10genetic
20093466
GCN20_YEASTGCN20genetic
20093466
ELP2_YEASTELP2genetic
20093466
PHB2_YEASTPHB2genetic
20093466
RS27B_YEASTRPS27Bgenetic
20093466
UBA4_YEASTUBA4genetic
20093466
STB5_YEASTSTB5genetic
20093466
APQ12_YEASTAPQ12genetic
20093466
LSM1_YEASTLSM1genetic
20093466
SAC1_YEASTSAC1genetic
20093466
KTI12_YEASTKTI12genetic
20093466
MEH1_YEASTMEH1genetic
20093466
ACE2_YEASTACE2genetic
20093466
RS28B_YEASTRPS28Bgenetic
20093466
VRP1_YEASTVRP1genetic
20093466
ELP1_YEASTIKI3genetic
20093466
YPT7_YEASTYPT7genetic
20093466
LSM7_YEASTLSM7genetic
20093466
MET22_YEASTMET22genetic
20093466
RS28A_YEASTRPS28Agenetic
20093466
ELP4_YEASTELP4genetic
20093466
ELOC_YEASTELC1genetic
20093466
GGPPS_YEASTBTS1genetic
21623372
FOLE_YEASTMET7genetic
21623372
FCY2_YEASTFCY2genetic
21623372
PDE2_YEASTPDE2genetic
21623372
AROC_YEASTARO2genetic
21623372
THRC_YEASTTHR4genetic
21623372
IPK1_YEASTIPK1genetic
21623372
KTHY_YEASTCDC8genetic
27708008
APT2_YEASTAPT2genetic
27708008
STU1_YEASTSTU1genetic
27708008
PRP6_YEASTPRP6genetic
27708008
STT3_YEASTSTT3genetic
27708008
MET30_YEASTMET30genetic
27708008
PRP19_YEASTPRP19genetic
27708008
SNU56_YEASTSNU56genetic
27708008
MOB2_YEASTMOB2genetic
27708008
CDC20_YEASTCDC20genetic
27708008
ORC6_YEASTORC6genetic
27708008
NTR2_YEASTNTR2genetic
27708008
SED5_YEASTSED5genetic
27708008
TAD3_YEASTTAD3genetic
27708008
BET5_YEASTBET5genetic
27708008
SEC65_YEASTSEC65genetic
27708008
ERB1_YEASTERB1genetic
27708008
CBF3B_YEASTCEP3genetic
27708008
CH10_YEASTHSP10genetic
27708008
TYSY_YEASTCDC21genetic
27708008
APC5_YEASTAPC5genetic
27708008
MYO2_YEASTMYO2genetic
27708008
SEC62_YEASTSEC62genetic
27708008
MEX67_YEASTMEX67genetic
27708008
HRR25_YEASTHRR25genetic
27708008
IPL1_YEASTIPL1genetic
27708008
NIP7_YEASTNIP7genetic
27708008
CET1_YEASTCET1genetic
27708008
NSL1_YEASTNSL1genetic
27708008
RUVB2_YEASTRVB2genetic
27708008
DIB1_YEASTDIB1genetic
27708008
PSB5_YEASTPRE2genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
ICS2_YEASTICS2genetic
27708008
SHG1_YEASTSHG1genetic
27708008
AP3M_YEASTAPM3genetic
27708008
HSP78_YEASTHSP78genetic
27708008
RV167_YEASTRVS167genetic
27708008
AIM11_YEASTAIM11genetic
27708008
ECM32_YEASTECM32genetic
27708008
TFS2_YEASTDST1genetic
27708008
YGL7_YEASTYGL117Wgenetic
27708008
SCM4_YEASTSCM4genetic
27708008
RS23A_YEASTRPS23Agenetic
27708008
RS23B_YEASTRPS23Agenetic
27708008
RSSA1_YEASTRPS0Agenetic
27708008
AIM17_YEASTAIM17genetic
27708008
INM1_YEASTINM1genetic
27708008
STB5_YEASTSTB5genetic
27708008
HPM1_YEASTHPM1genetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
VPS24_YEASTVPS24genetic
27708008
FABG_YEASTOAR1genetic
27708008
ENV10_YEASTENV10genetic
27708008
VRP1_YEASTVRP1genetic
27708008
RL6B_YEASTRPL6Bgenetic
27708008
PET8_YEASTPET8genetic
27708008
PMS1_YEASTPMS1genetic
27708008
LDS2_YEASTLDS2genetic
27708008
WHI5_YEASTWHI5genetic
27708008
HAP5_YEASTHAP5genetic
27708008
VPS4_YEASTVPS4genetic
27708008
ERG3_YEASTERG3genetic
27708008
SST2_YEASTSST2genetic
27708008
NOP12_YEASTNOP12genetic
27708008
NEW1_YEASTNEW1genetic
27708008
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYKC_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-30 AND THR-62, AND MASSSPECTROMETRY.
"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 THR-62, 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 THR-62, 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 THR-62, AND MASSSPECTROMETRY.

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