SYG_YEAST - dbPTM
SYG_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYG_YEAST
UniProt AC P38088
Protein Name Glycine--tRNA ligase 1, mitochondrial
Gene Name GRS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 690
Subcellular Localization Isoform Cytoplasmic: Cytoplasm.
Isoform Mitochondrial: Mitochondrion matrix.
Protein Description Catalyzes the attachment of glycine to tRNA(Gly). Is also able produce diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs (By similarity)..
Protein Sequence MSFFNISRRFYSQIVKKSVKIKRMSVEDIKKARAAVPFNREQLESVLRGRFFYAPAFDLYGGVSGLYDYGPPGCAFQNNIIDAWRKHFILEEDMLEVDCTMLTPYEVLKTSGHVDKFSDWMCRDLKTGEIFRADHLVEEVLEARLKGDQEARGLVEDANAAAKDDAEKKKRKKKVKQIKAVKLDDDVVKEYEEILAKIDGYSGPELGELMEKYDIGNPVTGETLESPRAFNLMFETAIGPSGQLKGYLRPETAQGQFLNFNKLLEFNNSKTPFASASIGKSFRNEISPRAGLLRVREFLMAEIEHFVDPLDKSHPKFNEIKDIKLSFLPRDVQEAGSTEPIVKTVGEAVASRMVDNETLGYFIARIYQFLMKIGVDESKLRFRQHMANEMAHYAADCWDGELKTSYGWIECVGCADRSAYDLTVHSKKTKEKLVVRQKLDNPIEVTKWEIDLTKKLFGPKFRKDAPKVESHLLNMSQDDLASKAELLKANGKFTIKVDGVDGEVELDDKLVKIEQRTKVEHVREYVPSVIEPSFGIGRIIYSVFEHSFWNRPEDNARSVLSFPPLVAPTKVLLVPLSNHKDLVPVTTEVAKILRKSQIPFKIDDSGVSIGKRYARNDELGTPFGVTIDFESAKDHSVTLRERDSTKQVRGSVENVIKAIRDITYNGASWEEGTKDLTPFIAQAEAEAETD
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
7Phosphorylation-MSFFNISRRFYSQI
-CCCHHCCHHHHHHH		20.6430377154
25PhosphorylationSVKIKRMSVEDIKKA
HCCEEECCHHHHHHH		26.7922369663
25AcetylationSVKIKRMSVEDIKKA
HCCEEECCHHHHHHH		26.7922814378
116AcetylationKTSGHVDKFSDWMCR
HCCCCHHHCCHHHHC		45.7524489116
126AcetylationDWMCRDLKTGEIFRA
HHHHCCCCCCCCEEH		59.7924489116
126SuccinylationDWMCRDLKTGEIFRA
HHHHCCCCCCCCEEH		59.7923954790
163SuccinylationEDANAAAKDDAEKKK
HHHHHHCCCHHHHHH		51.9523954790
163AcetylationEDANAAAKDDAEKKK
HHHHHHCCCHHHHHH		51.9524489116
168AcetylationAAKDDAEKKKRKKKV
HCCCHHHHHHHHHHH		66.3724489116
182AcetylationVKQIKAVKLDDDVVK
HHHHHCCCCCHHHHH		51.5724489116
189AcetylationKLDDDVVKEYEEILA
CCCHHHHHHHHHHHH		55.1924489116
197PhosphorylationEYEEILAKIDGYSGP
HHHHHHHHHCCCCCH		37.5721126336
201PhosphorylationILAKIDGYSGPELGE
HHHHHCCCCCHHHHH		13.5022369663
202PhosphorylationLAKIDGYSGPELGEL
HHHHCCCCCHHHHHH		54.0922369663
203PhosphorylationAKIDGYSGPELGELM
HHHCCCCCHHHHHHH		15.9517330950
213PhosphorylationLGELMEKYDIGNPVT
HHHHHHHCCCCCCCC		10.2521440633
220PhosphorylationYDIGNPVTGETLESP
CCCCCCCCCCCCCCC		30.4722369663
223PhosphorylationGNPVTGETLESPRAF
CCCCCCCCCCCCCHH		36.8522369663
226PhosphorylationVTGETLESPRAFNLM
CCCCCCCCCCHHHHE		23.8522369663
236PhosphorylationAFNLMFETAIGPSGQ
HHHHEEEEECCCCCC		16.5922369663
241PhosphorylationFETAIGPSGQLKGYL
EEEECCCCCCCCCCC		33.6822369663
247UbiquitinationPSGQLKGYLRPETAQ
CCCCCCCCCCCCCCC		9.6524961812
252PhosphorylationKGYLRPETAQGQFLN
CCCCCCCCCCCCCCC		27.2824961812
257UbiquitinationPETAQGQFLNFNKLL
CCCCCCCCCCHHHHH		8.4523749301
262AcetylationGQFLNFNKLLEFNNS
CCCCCHHHHHHCCCC		50.7624489116
270AcetylationLLEFNNSKTPFASAS
HHHCCCCCCCCCCCH		63.4424489116
271PhosphorylationLEFNNSKTPFASASI
HHCCCCCCCCCCCHH		24.3722369663
275PhosphorylationNSKTPFASASIGKSF
CCCCCCCCCHHCHHH		23.9522369663
277PhosphorylationKTPFASASIGKSFRN
CCCCCCCHHCHHHHC		29.4022369663
280AcetylationFASASIGKSFRNEIS
CCCCHHCHHHHCCCC		44.7624489116
280UbiquitinationFASASIGKSFRNEIS
CCCCHHCHHHHCCCC		44.76-
320UbiquitinationSHPKFNEIKDIKLSF
CCCCHHHCCCCEEEE		5.2223749301
321AcetylationHPKFNEIKDIKLSFL
CCCHHHCCCCEEEEC		47.4224489116
324AcetylationFNEIKDIKLSFLPRD
HHHCCCCEEEECCCC		48.4924489116
343UbiquitinationGSTEPIVKTVGEAVA
CCCCCCHHHHHHHHH		37.91-
343AcetylationGSTEPIVKTVGEAVA
CCCCCCHHHHHHHHH		37.9124489116
378PhosphorylationMKIGVDESKLRFRQH
HHHCCCHHHHHHHHH		32.3123749301
379AcetylationKIGVDESKLRFRQHM
HHCCCHHHHHHHHHH		41.4524489116
426PhosphorylationAYDLTVHSKKTKEKL
CEECEECCCCCCCEE		31.3528889911
427AcetylationYDLTVHSKKTKEKLV
EECEECCCCCCCEEE		49.9722865919
438AcetylationEKLVVRQKLDNPIEV
CEEEEEEECCCCEEE		47.4424489116
447AcetylationDNPIEVTKWEIDLTK
CCCEEEEEEEEEHHH		48.2624489116
453PhosphorylationTKWEIDLTKKLFGPK
EEEEEEHHHHHHCCH		23.5319779198
454AcetylationKWEIDLTKKLFGPKF
EEEEEHHHHHHCCHH		55.5724489116
460UbiquitinationTKKLFGPKFRKDAPK
HHHHHCCHHCCCCHH		59.1724961812
460AcetylationTKKLFGPKFRKDAPK
HHHHHCCHHCCCCHH		59.1724489116
467AcetylationKFRKDAPKVESHLLN
HHCCCCHHHHHHHHC		61.4224489116
470PhosphorylationKDAPKVESHLLNMSQ
CCCHHHHHHHHCCCH		23.5621440633
476PhosphorylationESHLLNMSQDDLASK
HHHHHCCCHHHHHHH		29.4123749301
483AcetylationSQDDLASKAELLKAN
CHHHHHHHHHHHHHC		40.0324489116
488AcetylationASKAELLKANGKFTI
HHHHHHHHHCCEEEE		53.0524489116
505PhosphorylationDGVDGEVELDDKLVK
CCCCCEEEECCCEEE		42.0218407956
509AcetylationGEVELDDKLVKIEQR
CEEEECCCEEEEHHH		55.6424489116
512AcetylationELDDKLVKIEQRTKV
EECCCEEEEHHHHCC		51.4624489116
528PhosphorylationHVREYVPSVIEPSFG
HHHHHCCCHHCCCCC		26.1922369663
533PhosphorylationVPSVIEPSFGIGRII
CCCHHCCCCCHHHHH		24.2630377154
558PhosphorylationRPEDNARSVLSFPPL
CCCCCCCCHHCCCCC		25.6221440633
570AcetylationPPLVAPTKVLLVPLS
CCCCCCCEEEEEECC		29.8124489116
588UbiquitinationDLVPVTTEVAKILRK
CCCCCHHHHHHHHHH		30.9823749301
601SuccinylationRKSQIPFKIDDSGVS
HHCCCCEEECCCCCC		39.6123954790
601AcetylationRKSQIPFKIDDSGVS
HHCCCCEEECCCCCC		39.6124489116
605PhosphorylationIPFKIDDSGVSIGKR
CCEEECCCCCCCCCC		37.0328889911
608PhosphorylationKIDDSGVSIGKRYAR
EECCCCCCCCCCEEC		29.2028889911
611SuccinylationDSGVSIGKRYARNDE
CCCCCCCCCEECCCC		40.3323954790
611AcetylationDSGVSIGKRYARNDE
CCCCCCCCCEECCCC		40.3324489116
611UbiquitinationDSGVSIGKRYARNDE
CCCCCCCCCEECCCC		40.33-
631PhosphorylationGVTIDFESAKDHSVT
EEEEECHHCCCCEEE		40.3819779198
638PhosphorylationSAKDHSVTLRERDST
HCCCCEEEEEECCCC		24.1019779198
644PhosphorylationVTLRERDSTKQVRGS
EEEEECCCCHHHCHH		43.6630377154
651PhosphorylationSTKQVRGSVENVIKA
CCHHHCHHHHHHHHH		18.7228889911
654PhosphorylationQVRGSVENVIKAIRD
HHCHHHHHHHHHHHH		38.3621126336
657AcetylationGSVENVIKAIRDITY
HHHHHHHHHHHHCCC		33.2224489116
666PhosphorylationIRDITYNGASWEEGT
HHHCCCCCCCCCCCC		15.5819795423
677PhosphorylationEEGTKDLTPFIAQAE
CCCCCCCHHHHHHHH		26.7021126336
689PhosphorylationQAEAEAETD------
HHHHHHCCC------		54.8025521595
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 SYG_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYG_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 SYG_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EIF3J_YEASTHCR1genetic
19061648
NU170_YEASTNUP170genetic
19061648
RAD52_YEASTRAD52genetic
19061648
MET22_YEASTMET22genetic
21623372
SDHA_YEASTSDH1genetic
21623372
6PGD1_YEASTGND1genetic
21623372
DHOM_YEASTHOM6genetic
21623372
TPS2_YEASTTPS2genetic
21623372
SYG2_YEASTGRS2genetic
22438917
HRT3_YEASTHRT3physical
26297823
AIM11_YEASTAIM11genetic
27708008
ECM32_YEASTECM32genetic
27708008
RL8A_YEASTRPL8Agenetic
27708008
AIM18_YEASTAIM18genetic
27708008
PSMD9_YEASTNAS2genetic
27708008
BFA1_YEASTBFA1genetic
27708008
RS3A2_YEASTRPS1Bgenetic
27708008
MLH1_YEASTMLH1genetic
27708008
PMS1_YEASTPMS1genetic
27708008
YAP4_YEASTCIN5genetic
27708008
BUD21_YEASTBUD21genetic
27708008
ELG1_YEASTELG1genetic
27708008
DGK1_YEASTDGK1genetic
27708008
ALDH6_YEASTALD6genetic
27708008
YP109_YEASTYPL109Cgenetic
27708008
YP153_YEASTYPR153Wgenetic
27708008
RPN6_YEASTRPN6genetic
27708008
RPB1_YEASTRPO21genetic
27708008
RPN5_YEASTRPN5genetic
27708008
TIM22_YEASTTIM22genetic
27708008
TCPA_YEASTTCP1genetic
27708008
SRPR_YEASTSRP101genetic
27708008
PSB3_YEASTPUP3genetic
27708008
RPN11_YEASTRPN11genetic
27708008
PRS8_YEASTRPT6genetic
27708008
RPN1_YEASTRPN1genetic
27708008
BRL1_YEASTBRL1genetic
27708008
ARP3_YEASTARP3genetic
27708008
KCY_YEASTURA6genetic
27708008
PRS7_YEASTRPT1genetic
27708008
SSL1_YEASTSSL1genetic
27708008
CFT2_YEASTCFT2genetic
27708008
CAP_YEASTSRV2genetic
27708008
PRS10_YEASTRPT4genetic
27708008
CET1_YEASTCET1genetic
27708008
PSB5_YEASTPRE2genetic
27708008
RPN7_YEASTRPN7genetic
27708008
NU170_YEASTNUP170genetic
27708008
OCA4_YEASTOCA4genetic
27708008
SLX5_YEASTSLX5genetic
27708008
RL13A_YEASTRPL13Agenetic
27708008
BAP3_YEASTBAP3genetic
27708008
SWF1_YEASTSWF1genetic
27708008
ODO2_YEASTKGD2genetic
27708008
ACL4_YEASTYDR161Wgenetic
27708008
RLA4_YEASTRPP2Bgenetic
27708008
IOC3_YEASTIOC3genetic
27708008
RL24A_YEASTRPL24Agenetic
27708008
RME1_YEASTRME1genetic
27708008
PSA3_YEASTPRE9genetic
27708008
TNA1_YEASTTNA1genetic
27708008
OPI1_YEASTOPI1genetic
27708008
LRP1_YEASTLRP1genetic
27708008
VPS53_YEASTVPS53genetic
27708008
NCA3_YEASTNCA3genetic
27708008
MOG1_YEASTMOG1genetic
27708008
DHOM_YEASTHOM6genetic
27708008
ELF1_YEASTELF1genetic
27708008
XPOT_YEASTLOS1genetic
27708008
MDL1_YEASTMDL1genetic
27708008
NU188_YEASTNUP188genetic
27708008
SUB1_YEASTSUB1genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
OCA1_YEASTOCA1genetic
27708008
ATP23_YEASTATP23genetic
27708008
PHO80_YEASTPHO80genetic
27708008
SPS4_YEASTSPS4genetic
27708008
CHL1_YEASTCHL1genetic
27708008
CHMU_YEASTARO7genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYG_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-226; SER-476; SER-528AND THR-689, 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-226, 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-226, AND MASSSPECTROMETRY.

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