SYRC_YEAST - dbPTM
SYRC_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYRC_YEAST
UniProt AC Q05506
Protein Name Arginine--tRNA ligase, cytoplasmic
Gene Name YDR341C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 607
Subcellular Localization Cytoplasm . Cytoplasm, cytosol .
Protein Description Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis..
Protein Sequence MASTANMISQLKKLSIAEPAVAKDSHPDVNIVDLMRNYISQELSKISGVDSSLIFPALEWTNTMERGDLLIPIPRLRIKGANPKDLAVQWAEKFPCGDFLEKVEANGPFIQFFFNPQFLAKLVIPDILTRKEDYGSCKLVENKKVIIEFSSPNIAKPFHAGHLRSTIIGGFLANLYEKLGWEVIRMNYLGDWGKQFGLLAVGFERYGNEEALVKDPIHHLFDVYVRINKDIEEEGDSIPLEQSTNGKAREYFKRMEDGDEEALKIWKRFREFSIEKYIDTYARLNIKYDVYSGESQVSKESMLKAIDLFKEKGLTHEDKGAVLIDLTKFNKKLGKAIVQKSDGTTLYLTRDVGAAMDRYEKYHFDKMIYVIASQQDLHAAQFFEILKQMGFEWAKDLQHVNFGMVQGMSTRKGTVVFLDNILEETKEKMHEVMKKNENKYAQIEHPEEVADLVGISAVMIQDMQGKRINNYEFKWERMLSFEGDTGPYLQYAHSRLRSVERNASGITQEKWINADFSLLKEPAAKLLIRLLGQYPDVLRNAIKTHEPTTVVTYLFKLTHQVSSCYDVLWVAGQTEELATARLALYGAARQVLYNGMRLLGLTPVERM
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------MASTANMIS
------CCCHHHHHH		18.6522814378
3Phosphorylation-----MASTANMISQ
-----CCCHHHHHHH		27.1028152593
4Phosphorylation----MASTANMISQL
----CCCHHHHHHHH		16.7124909858
12SuccinylationANMISQLKKLSIAEP
HHHHHHHHHCCCCCC		43.9923954790
15PhosphorylationISQLKKLSIAEPAVA
HHHHHHCCCCCCCCC		28.7317330950
23AcetylationIAEPAVAKDSHPDVN
CCCCCCCCCCCCCCC		53.8424489116
40PhosphorylationDLMRNYISQELSKIS
HHHHHHHHHHHHHHH		13.7730377154
84AcetylationRIKGANPKDLAVQWA
EECCCCHHHHHHHHH		66.2424489116
1432-HydroxyisobutyrylationSCKLVENKKVIIEFS
CCEEECCCEEEEEEC		34.61-
150PhosphorylationKKVIIEFSSPNIAKP
CEEEEEECCCCCCCC		31.9022369663
151PhosphorylationKVIIEFSSPNIAKPF
EEEEEECCCCCCCCC		27.5622369663
156AcetylationFSSPNIAKPFHAGHL
ECCCCCCCCCCCCHH		44.40-
194UbiquitinationNYLGDWGKQFGLLAV
EECCHHHHHCCEEEE		37.8923749301
214AcetylationGNEEALVKDPIHHLF
CCHHHHHCCHHHHHH		59.6524489116
229UbiquitinationDVYVRINKDIEEEGD
HEEEEECCCHHHCCC		58.6823749301
229AcetylationDVYVRINKDIEEEGD
HEEEEECCCHHHCCC		58.6824489116
237PhosphorylationDIEEEGDSIPLEQST
CHHHCCCCCCCCCCC		36.6423749301
264AcetylationDGDEEALKIWKRFRE
CCCHHHHHHHHHHHH		54.2724489116
276UbiquitinationFREFSIEKYIDTYAR
HHHHCHHHHHHHHHH		45.9224961812
280PhosphorylationSIEKYIDTYARLNIK
CHHHHHHHHHHCCCE		14.9921440633
281PhosphorylationIEKYIDTYARLNIKY
HHHHHHHHHHCCCEE		5.9827017623
287AcetylationTYARLNIKYDVYSGE
HHHHCCCEEEECCCC		34.0324489116
298PhosphorylationYSGESQVSKESMLKA
CCCCCCCCHHHHHHH		24.0619779198
299AcetylationSGESQVSKESMLKAI
CCCCCCCHHHHHHHH		55.7624489116
299UbiquitinationSGESQVSKESMLKAI
CCCCCCCHHHHHHHH		55.7623749301
301PhosphorylationESQVSKESMLKAIDL
CCCCCHHHHHHHHHH		32.9019779198
304AcetylationVSKESMLKAIDLFKE
CCHHHHHHHHHHHHH		34.3524489116
3102-HydroxyisobutyrylationLKAIDLFKEKGLTHE
HHHHHHHHHCCCCCC		66.85-
310AcetylationLKAIDLFKEKGLTHE
HHHHHHHHHCCCCCC		66.8524489116
319AcetylationKGLTHEDKGAVLIDL
CCCCCCCCCEEEEEH		45.8724489116
328AcetylationAVLIDLTKFNKKLGK
EEEEEHHHHHHHHCC		54.9924489116
340AcetylationLGKAIVQKSDGTTLY
HCCEEEECCCCCEEE		39.3524489116
340UbiquitinationLGKAIVQKSDGTTLY
HCCEEEECCCCCEEE		39.3523749301
361AcetylationAAMDRYEKYHFDKMI
HHHHHHHHHCHHHEE		34.7824489116
426AcetylationDNILEETKEKMHEVM
CCHHHHHHHHHHHHH		59.6324489116
474AcetylationRINNYEFKWERMLSF
CCCCEEEEEEEHHCC		35.8824489116
504PhosphorylationRSVERNASGITQEKW
HHHHHCCCCCCHHHH		33.9928889911
510AcetylationASGITQEKWINADFS
CCCCCHHHHHCCCHH		43.4824489116
520AcetylationNADFSLLKEPAAKLL
CCCHHHCCHHHHHHH		67.9324489116
525AcetylationLLKEPAAKLLIRLLG
HCCHHHHHHHHHHHC		46.0324489116
543UbiquitinationDVLRNAIKTHEPTTV
HHHHHHHHCCCCCHH		41.2224961812
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 SYRC_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYRC_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 SYRC_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AATC_YEASTAAT2genetic
21623372
IDH2_YEASTIDH2genetic
21623372
SCS7_YEASTSCS7genetic
21623372
CSG2_YEASTCSG2genetic
21623372
PDX3_YEASTPDX3genetic
21623372
ADE_YEASTAAH1genetic
21623372
FOLE_YEASTMET7genetic
21623372
PYRE_YEASTURA5genetic
21623372
PALA_YEASTRIM20genetic
27708008
TFC3_YEASTTFC3genetic
27708008
LSM2_YEASTLSM2genetic
27708008
CDK1_YEASTCDC28genetic
27708008
PRP5_YEASTPRP5genetic
27708008
APC11_YEASTAPC11genetic
27708008
ERF3_YEASTSUP35genetic
27708008
SMC1_YEASTSMC1genetic
27708008
CDC4_YEASTCDC4genetic
27708008
MCE1_YEASTCEG1genetic
27708008
COPB2_YEASTSEC27genetic
27708008
DAM1_YEASTDAM1genetic
27708008
ZPR1_YEASTZPR1genetic
27708008
MPPA_YEASTMAS2genetic
27708008
CDC12_YEASTCDC12genetic
27708008
STS1_YEASTSTS1genetic
27708008
PRP21_YEASTPRP21genetic
27708008
KTHY_YEASTCDC8genetic
27708008
SED5_YEASTSED5genetic
27708008
BOS1_YEASTBOS1genetic
27708008
SEC22_YEASTSEC22genetic
27708008
EI2BB_YEASTGCD7genetic
27708008
RU1C_YEASTYHC1genetic
27708008
TAD3_YEASTTAD3genetic
27708008
BET5_YEASTBET5genetic
27708008
SEC65_YEASTSEC65genetic
27708008
PDS5_YEASTPDS5genetic
27708008
RPC6_YEASTRPC34genetic
27708008
PRP2_YEASTPRP2genetic
27708008
SGT1_YEASTSGT1genetic
27708008
TYSY_YEASTCDC21genetic
27708008
EI2BG_YEASTGCD1genetic
27708008
NAB3_YEASTNAB3genetic
27708008
HRR25_YEASTHRR25genetic
27708008
PRP4_YEASTPRP4genetic
27708008
ATS1_YEASTATS1genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
GCN20_YEASTGCN20genetic
27708008
MED5_YEASTNUT1genetic
27708008
GCN1_YEASTGCN1genetic
27708008
RTF1_YEASTRTF1genetic
27708008
ELP2_YEASTELP2genetic
27708008
ATG32_YEASTATG32genetic
27708008
DHOM_YEASTHOM6genetic
27708008
FABG_YEASTOAR1genetic
27708008
KTI12_YEASTKTI12genetic
27708008
XPOT_YEASTLOS1genetic
27708008
EMC6_YEASTEMC6genetic
27708008
ELP1_YEASTIKI3genetic
27708008
SAM37_YEASTSAM37genetic
27708008
MOT3_YEASTMOT3genetic
27708008
SCS7_YEASTSCS7genetic
27708008
ELP6_YEASTELP6genetic
27708008
LSM7_YEASTLSM7genetic
27708008
BRE5_YEASTBRE5genetic
27708008
TRM10_YEASTTRM10genetic
27708008
SFL1_YEASTSFL1genetic
27708008
ELP3_YEASTELP3genetic
27708008
ELP4_YEASTELP4genetic
27708008
SUE1_YEASTSUE1genetic
27708008
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYRC_YEAST

loading...

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-15, 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 SER-15, 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-15, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory