SYNC_HUMAN - dbPTM
SYNC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYNC_HUMAN
UniProt AC O43776
Protein Name Asparagine--tRNA ligase, cytoplasmic
Gene Name NARS
Organism Homo sapiens (Human).
Sequence Length 548
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MVLAELYVSDREGSDATGDGTKEKPFKTGLKALMTVGKEPFPTIYVDSQKENERWNVISKSQLKNIKKMWHREQMKSESREKKEAEDSLRREKNLEEAKKITIKNDPSLPEPKCVKIGALEGYRGQRVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLADELCQCYNGVLLSTESSVAVYGMLNLTPKGKQAPGGHELSCDFWELIGLAPAGGADNLINEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPAGSIVHELNPNFQPPKRPFKRMNYSDAIVWLKEHDVKKEDGTFYEFGEDIPEAPERLMTDTINEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP
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
14PhosphorylationYVSDREGSDATGDGT
EEECCCCCCCCCCCC		21.2225159151
22UbiquitinationDATGDGTKEKPFKTG
CCCCCCCCCCCCCHH		70.0833845483
31UbiquitinationKPFKTGLKALMTVGK
CCCCHHHHHHHHCCC		40.6029967540
34SulfoxidationKTGLKALMTVGKEPF
CHHHHHHHHCCCCCC		3.2230846556
38UbiquitinationKALMTVGKEPFPTIY
HHHHHCCCCCCCEEE		58.8529967540
45NitrationKEPFPTIYVDSQKEN
CCCCCEEEECCCCCH		10.73-
502-HydroxyisobutyrylationTIYVDSQKENERWNV
EEEECCCCCHHCCEE		67.47-
50UbiquitinationTIYVDSQKENERWNV
EEEECCCCCHHCCEE		67.4732015554
50AcetylationTIYVDSQKENERWNV
EEEECCCCCHHCCEE		67.4726051181
59PhosphorylationNERWNVISKSQLKNI
HHCCEECCHHHHHHH		23.2129978859
59UbiquitinationNERWNVISKSQLKNI
HHCCEECCHHHHHHH		23.2121890473
60UbiquitinationERWNVISKSQLKNIK
HCCEECCHHHHHHHH		30.9721890473
60UbiquitinationERWNVISKSQLKNIK
HCCEECCHHHHHHHH		30.9722817900
60MalonylationERWNVISKSQLKNIK
HCCEECCHHHHHHHH		30.9726320211
60AcetylationERWNVISKSQLKNIK
HCCEECCHHHHHHHH		30.9725953088
61PhosphorylationRWNVISKSQLKNIKK
CCEECCHHHHHHHHH		33.6726055452
63UbiquitinationNVISKSQLKNIKKMW
EECCHHHHHHHHHHH		6.2222817900
64UbiquitinationVISKSQLKNIKKMWH
ECCHHHHHHHHHHHH		49.3322817900
64AcetylationVISKSQLKNIKKMWH
ECCHHHHHHHHHHHH		49.3325953088
77PhosphorylationWHREQMKSESREKKE
HHHHHHHHHHHHHHH		35.1524719451
81UbiquitinationQMKSESREKKEAEDS
HHHHHHHHHHHHHHH		77.1824816145
82UbiquitinationMKSESREKKEAEDSL
HHHHHHHHHHHHHHH		55.6024816145
83UbiquitinationKSESREKKEAEDSLR
HHHHHHHHHHHHHHH		58.3624816145
88PhosphorylationEKKEAEDSLRREKNL
HHHHHHHHHHHHHCH		18.4529255136
93UbiquitinationEDSLRREKNLEEAKK
HHHHHHHHCHHHHHC		66.0929967540
98UbiquitinationREKNLEEAKKITIKN
HHHCHHHHHCCEECC		14.7423000965
99UbiquitinationEKNLEEAKKITIKND
HHCHHHHHCCEECCC		48.2423000965
992-HydroxyisobutyrylationEKNLEEAKKITIKND
HHCHHHHHCCEECCC		48.24-
100UbiquitinationKNLEEAKKITIKNDP
HCHHHHHCCEECCCC		52.7223000965
100AcetylationKNLEEAKKITIKNDP
HCHHHHHCCEECCCC		52.727677539
102PhosphorylationLEEAKKITIKNDPSL
HHHHHCCEECCCCCC		34.4824719451
103UbiquitinationEEAKKITIKNDPSLP
HHHHCCEECCCCCCC		4.4621890473
104UbiquitinationEAKKITIKNDPSLPE
HHHCCEECCCCCCCC		46.8021890473
104UbiquitinationEAKKITIKNDPSLPE
HHHCCEECCCCCCCC		46.8023000965
104AcetylationEAKKITIKNDPSLPE
HHHCCEECCCCCCCC		46.8025953088
113UbiquitinationDPSLPEPKCVKIGAL
CCCCCCCCEEEEEEE		50.4229967540
113AcetylationDPSLPEPKCVKIGAL
CCCCCCCCEEEEEEE		50.427677549
116UbiquitinationLPEPKCVKIGALEGY
CCCCCEEEEEEECCC		44.91-
116UbiquitinationLPEPKCVKIGALEGY
CCCCCEEEEEEECCC		44.91-
123PhosphorylationKIGALEGYRGQRVKV
EEEEECCCCCCEEEE		11.3828152594
124MethylationIGALEGYRGQRVKVF
EEEECCCCCCEEEEE		45.70115484487
1292-HydroxyisobutyrylationGYRGQRVKVFGWVHR
CCCCCEEEEEEHHHH		33.75-
129UbiquitinationGYRGQRVKVFGWVHR
CCCCCEEEEEEHHHH		33.75-
129AcetylationGYRGQRVKVFGWVHR
CCCCCEEEEEEHHHH		33.7526051181
129UbiquitinationGYRGQRVKVFGWVHR
CCCCCEEEEEEHHHH		33.75-
141UbiquitinationVHRLRRQGKNLMFLV
HHHHHHCCCCEEEEE		21.0024816145
142UbiquitinationHRLRRQGKNLMFLVL
HHHHHCCCCEEEEEE		38.2724816145
243UbiquitinationMIRGENMSKILKARS
EEECCCHHHHHHHHH		28.2922817900
244UbiquitinationIRGENMSKILKARSM
EECCCHHHHHHHHHH		41.0921906983
244AcetylationIRGENMSKILKARSM
EECCCHHHHHHHHHH		41.0919608861
246UbiquitinationGENMSKILKARSMVT
CCCHHHHHHHHHHHH		4.0022817900
247UbiquitinationENMSKILKARSMVTR
CCHHHHHHHHHHHHH		45.2722817900
250PhosphorylationSKILKARSMVTRCFR
HHHHHHHHHHHHHHH		23.5929900121
253PhosphorylationLKARSMVTRCFRDHF
HHHHHHHHHHHHHHH		17.0629900121
289PhosphorylationATLFKLDYFGEEAFL
EEEEEECCCCCCEEE		24.7425332170
384UbiquitinationLNPNFQPPKRPFKRM
CCCCCCCCCCCCCCC		34.2121890473
385UbiquitinationNPNFQPPKRPFKRMN
CCCCCCCCCCCCCCC		78.4021890473
393PhosphorylationRPFKRMNYSDAIVWL
CCCCCCCHHHEEEEE		9.8920068231
394PhosphorylationPFKRMNYSDAIVWLK
CCCCCCHHHEEEEEH		18.6320068231
400UbiquitinationYSDAIVWLKEHDVKK
HHHEEEEEHHHCCCC		3.0221963094
4012-HydroxyisobutyrylationSDAIVWLKEHDVKKE
HHEEEEEHHHCCCCC		36.97-
401UbiquitinationSDAIVWLKEHDVKKE
HHEEEEEHHHCCCCC		36.9721906983
405UbiquitinationVWLKEHDVKKEDGTF
EEEHHHCCCCCCCCE		11.7122817900
406UbiquitinationWLKEHDVKKEDGTFY
EEHHHCCCCCCCCEE		57.4122817900
407UbiquitinationLKEHDVKKEDGTFYE
EHHHCCCCCCCCEEE		61.9721906983
413PhosphorylationKKEDGTFYEFGEDIP
CCCCCCEEECCCCCC		15.3627642862
427SulfoxidationPEAPERLMTDTINEP
CCCCHHHCCCCCCCC		3.9021406390
428PhosphorylationEAPERLMTDTINEPI
CCCHHHCCCCCCCCE		34.2825690035
430PhosphorylationPERLMTDTINEPILL
CHHHCCCCCCCCEEE		19.2825690035
438GlutathionylationINEPILLCRFPVEIK
CCCCEEEECCCEEEH		3.6522555962
444UbiquitinationLCRFPVEIKSFYMQR
EECCCEEEHEEEHHH		4.6321890473
445UbiquitinationCRFPVEIKSFYMQRC
ECCCEEEHEEEHHHC		22.4722817900
451MethylationIKSFYMQRCPEDSRL
EHEEEHHHCCCCCCC		22.79115484495
459PhosphorylationCPEDSRLTESVDVLM
CCCCCCCCCCCCEEC		25.7120068231
461PhosphorylationEDSRLTESVDVLMPN
CCCCCCCCCCEECCC		20.5520068231
466SulfoxidationTESVDVLMPNVGEIV
CCCCCEECCCCHHHC		1.9730846556
476PhosphorylationVGEIVGGSMRIFDSE
CHHHCCCEEEECCHH		10.0420068231
477SulfoxidationGEIVGGSMRIFDSEE
HHHCCCEEEECCHHH		4.2730846556
482PhosphorylationGSMRIFDSEEILAGY
CEEEECCHHHHHHCH		26.7821082442
489NitrationSEEILAGYKREGIDP
HHHHHHCHHCCCCCC		10.98-
489UbiquitinationSEEILAGYKREGIDP
HHHHHHCHHCCCCCC		10.9823000965
489PhosphorylationSEEILAGYKREGIDP
HHHHHHCHHCCCCCC		10.9828152594
490MalonylationEEILAGYKREGIDPT
HHHHHCHHCCCCCCC		42.9526320211
4902-HydroxyisobutyrylationEEILAGYKREGIDPT
HHHHHCHHCCCCCCC		42.95-
490AcetylationEEILAGYKREGIDPT
HHHHHCHHCCCCCCC		42.9525953088
490UbiquitinationEEILAGYKREGIDPT
HHHHHCHHCCCCCCC		42.9523000965
497PhosphorylationKREGIDPTPYYWYTD
HCCCCCCCCCEEECC		21.8528152594
499PhosphorylationEGIDPTPYYWYTDQR
CCCCCCCCEEECCCC		14.7628152594
500PhosphorylationGIDPTPYYWYTDQRK
CCCCCCCEEECCCCC		7.9828152594
502PhosphorylationDPTPYYWYTDQRKYG
CCCCCEEECCCCCCC		5.5928152594
503PhosphorylationPTPYYWYTDQRKYGT
CCCCEEECCCCCCCC		16.1228152594
506UbiquitinationYYWYTDQRKYGTCPH
CEEECCCCCCCCCCC		36.6521890473
5072-HydroxyisobutyrylationYWYTDQRKYGTCPHG
EEECCCCCCCCCCCC		42.26-
507UbiquitinationYWYTDQRKYGTCPHG
EEECCCCCCCCCCCC		42.2622817900
507AcetylationYWYTDQRKYGTCPHG
EEECCCCCCCCCCCC		42.2625953088
539PhosphorylationHIRDVCLYPRFVQRC
CHHHHHCCHHHHCCC		6.2927273156
547PhosphorylationPRFVQRCTP------
HHHHCCCCC------		33.9322199227
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 SYNC_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYNC_HUMAN !!
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 SYNC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYRC_HUMANRARSphysical
22939629
C1QBP_HUMANC1QBPphysical
22863883
CUL2_HUMANCUL2physical
22863883
IF4B_HUMANEIF4Bphysical
22863883
GANAB_HUMANGANABphysical
22863883
PLAK_HUMANJUPphysical
22863883
PAPOA_HUMANPAPOLAphysical
22863883
PLOD2_HUMANPLOD2physical
22863883
ANM3_HUMANPRMT3physical
22863883
TRUA_HUMANPUS1physical
22863883
RL24_HUMANRPL24physical
22863883
SAMH1_HUMANSAMHD1physical
22863883
SC23A_HUMANSEC23Aphysical
22863883
SF01_HUMANSF1physical
22863883
TRM1_HUMANTRMT1physical
22863883
XPO7_HUMANXPO7physical
22863883
XRCC6_HUMANXRCC6physical
22863883
SYIC_HUMANIARSphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00174L-Asparagine
Regulatory Network of SYNC_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-244, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND MASSSPECTROMETRY.

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