SYMC_HUMAN - dbPTM
SYMC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYMC_HUMAN
UniProt AC P56192
Protein Name Methionine--tRNA ligase, cytoplasmic
Gene Name MARS
Organism Homo sapiens (Human).
Sequence Length 900
Subcellular Localization Cytoplasm, cytosol .
Protein Description Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA..
Protein Sequence MRLFVSDGVPGCLPVLAAAGRARGRAEVLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLFSTSAICRYFFLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQGKKGEDVLGSVRRALTHIDHSLSRQNCPFLAGETESLADIVLWGALYPLLQDPAYLPEELSALHSWFQTLSTQEPCQRAAETVLKQQGVLALRPYLQKQPQPSPAEGRAVTNEPEEEELATLSEEEIAMAVTAWEKGLESLPPLRPQQNPVLPVAGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYRWFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGKLINAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLPGSDWTPNAQFITRSWLRDGLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWWKNPEQVDLYQFMAKDNVPFHSLVFPCSALGAEDNYTLVSHLIATEYLNYEDGKFSKSRGVGVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRAGMFVSKFFGGYVPEMVLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKGSEADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSILLTNFLCTLPAGHQIGTVSPLFQKLENDQIESLRQRFGGGQAKTSPKPAVVETVTTAKPQQIQALMDEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQLAVAEGKPPEAPKGKKKK
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
6Phosphorylation--MRLFVSDGVPGCL
--CCCCCCCCCCCHH		22.7027362937
12GlutathionylationVSDGVPGCLPVLAAA
CCCCCCCHHHHHHHH		2.9622555962
38GlutathionylationSTVGPEDCVVPFLTR
EECCHHHCEEECCCC		2.9522555962
108UbiquitinationYYLVVQGKKGEDVLG
HHHHHCCCCCHHHHH		40.2822817900
109UbiquitinationYLVVQGKKGEDVLGS
HHHHCCCCCHHHHHH		74.4922817900
109UbiquitinationYLVVQGKKGEDVLGS
HHHHCCCCCHHHHHH		74.49-
116PhosphorylationKGEDVLGSVRRALTH
CCHHHHHHHHHHHHH		14.3220068231
130UbiquitinationHIDHSLSRQNCPFLA
HHCHHHHHCCCCCCC		36.7022817900
141UbiquitinationPFLAGETESLADIVL
CCCCCCCHHHHHHHH		39.1823000965
153PhosphorylationIVLWGALYPLLQDPA
HHHHHHHHHHHCCCC		7.4124275569
161PhosphorylationPLLQDPAYLPEELSA
HHHCCCCCCHHHHHH		28.3324275569
186UbiquitinationQEPCQRAAETVLKQQ
CHHHHHHHHHHHHHH		18.3822505724
191UbiquitinationRAAETVLKQQGVLAL
HHHHHHHHHHCHHHH		35.9221890473
191UbiquitinationRAAETVLKQQGVLAL
HHHHHHHHHHCHHHH		35.9221963094
201PhosphorylationGVLALRPYLQKQPQP
CHHHHHHHHHCCCCC		18.4828152594
204UbiquitinationALRPYLQKQPQPSPA
HHHHHHHCCCCCCCC		62.4421906983
204UbiquitinationALRPYLQKQPQPSPA
HHHHHHHCCCCCCCC		62.4421890473
204AcetylationALRPYLQKQPQPSPA
HHHHHHHCCCCCCCC		62.4426051181
209PhosphorylationLQKQPQPSPAEGRAV
HHCCCCCCCCCCCCC		31.3421815630
227PhosphorylationPEEEELATLSEEEIA
CCHHHHHCCCHHHHH		43.3625338102
229PhosphorylationEEELATLSEEEIAMA
HHHHHCCCHHHHHHH		38.3127251275
235SulfoxidationLSEEEIAMAVTAWEK
CCHHHHHHHHHHHHH		3.6630846556
246PhosphorylationAWEKGLESLPPLRPQ
HHHHHHHHCCCCCCC		51.7420068231
266UbiquitinationPVAGERNVLITSALP
CCCCCCCEEEECCCC		5.2521890473
335AcetylationTPQEICDKYHIIHAD
CHHHHHHHCCEEEEH		34.0327452117
335UbiquitinationTPQEICDKYHIIHAD
CHHHHHHHCCEEEEH		34.0333845483
336PhosphorylationPQEICDKYHIIHADI
HHHHHHHCCEEEEHH		5.7529396449
344PhosphorylationHIIHADIYRWFNISF
CEEEEHHHHHHEEEE		11.4429396449
357PhosphorylationSFDIFGRTTTPQQTK
EEEECCCCCCCCCCH		35.0924043423
358PhosphorylationFDIFGRTTTPQQTKI
EEECCCCCCCCCCHH		34.8124043423
359PhosphorylationDIFGRTTTPQQTKIT
EECCCCCCCCCCHHH		20.6324043423
363PhosphorylationRTTTPQQTKITQDIF
CCCCCCCCHHHHHHH		21.1124043423
364UbiquitinationTTTPQQTKITQDIFQ
CCCCCCCHHHHHHHH		39.1421890473
364UbiquitinationTTTPQQTKITQDIFQ
CCCCCCCHHHHHHHH		39.1421906983
375AcetylationDIFQQLLKRGFVLQD
HHHHHHHHCCCCCHH		60.1025953088
375UbiquitinationDIFQQLLKRGFVLQD
HHHHHHHHCCCCCHH		60.1021890473
3752-HydroxyisobutyrylationDIFQQLLKRGFVLQD
HHHHHHHHCCCCCHH		60.10-
375UbiquitinationDIFQQLLKRGFVLQD
HHHHHHHHCCCCCHH		60.1023000965
376MethylationIFQQLLKRGFVLQDT
HHHHHHHCCCCCHHH		43.69115482603
383PhosphorylationRGFVLQDTVEQLRCE
CCCCCHHHHHHHHHH		17.0028857561
420UbiquitinationARGDQCDKCGKLINA
HCCCCCCHHHHCCCH		53.1422505724
423UbiquitinationDQCDKCGKLINAVEL
CCCCHHHHCCCHHHC		56.52-
429UbiquitinationGKLINAVELKKPQCK
HHCCCHHHCCCCCCC		53.0823000965
431AcetylationLINAVELKKPQCKVC
CCCHHHCCCCCCCCC		49.2325953088
431UbiquitinationLINAVELKKPQCKVC
CCCHHHCCCCCCCCC		49.2332015554
4312-HydroxyisobutyrylationLINAVELKKPQCKVC
CCCHHHCCCCCCCCC		49.23-
441GlutathionylationQCKVCRSCPVVQSSQ
CCCCCCCCCCEECCC		1.2122555962
446PhosphorylationRSCPVVQSSQHLFLD
CCCCCEECCCEEECC		21.9828857561
447PhosphorylationSCPVVQSSQHLFLDL
CCCCEECCCEEECCH		12.4328857561
464UbiquitinationLEKRLEEWLGRTLPG
HHHHHHHHHCCCCCC		8.5021139048
468PhosphorylationLEEWLGRTLPGSDWT
HHHHHCCCCCCCCCC		35.1921406692
472PhosphorylationLGRTLPGSDWTPNAQ
HCCCCCCCCCCCCCE		28.2121406692
475PhosphorylationTLPGSDWTPNAQFIT
CCCCCCCCCCCEEEC		16.2021406692
482PhosphorylationTPNAQFITRSWLRDG
CCCCEEECHHHHCCC		21.6821406692
492UbiquitinationWLRDGLKPRCITRDL
HHCCCCCCCEEECCC		41.2223000965
495UbiquitinationDGLKPRCITRDLKWG
CCCCCCEEECCCCCC		3.6023000965
500UbiquitinationRCITRDLKWGTPVPL
CEEECCCCCCCCCCC		48.1121890473
500UbiquitinationRCITRDLKWGTPVPL
CEEECCCCCCCCCCC		48.1122817900
549PhosphorylationNPEQVDLYQFMAKDN
CHHHCCHHHHHHCCC		8.6727642862
552SulfoxidationQVDLYQFMAKDNVPF
HCCHHHHHHCCCCCC		2.4030846556
589UbiquitinationIATEYLNYEDGKFSK
HHHCCCCCCCCCCCC		16.8927667366
606SulfoxidationGVGVFGDMAQDTGIP
CCEEECHHHHHCCCC		3.5530846556
632UbiquitinationRPEGQDSAFSWTDLL
CCCCCCCCCCHHHHH		15.6916196087
641UbiquitinationSWTDLLLKNNSELLN
CHHHHHHHCCHHHHH		54.7916196087
644PhosphorylationDLLLKNNSELLNNLG
HHHHHCCHHHHHHHH		38.7321712546
655UbiquitinationNNLGNFINRAGMFVS
HHHHHHHHHHHHHHH		24.5016196087
661UbiquitinationINRAGMFVSKFFGGY
HHHHHHHHHHHHCCC		4.5216196087
662PhosphorylationNRAGMFVSKFFGGYV
HHHHHHHHHHHCCCC		16.69-
663UbiquitinationRAGMFVSKFFGGYVP
HHHHHHHHHHCCCCC		39.1423000965
675PhosphorylationYVPEMVLTPDDQRLL
CCCCEEECCCHHHHH		17.17-
698UbiquitinationHYHQLLEKVRIRDAL
HHHHHHHHHHHHHHH		36.4621139048
707PhosphorylationRIRDALRSILTISRH
HHHHHHHHHHHHCCC		23.8523403867
710PhosphorylationDALRSILTISRHGNQ
HHHHHHHHHCCCCCE		18.4223403867
726UbiquitinationIQVNEPWKRIKGSEA
EEECCCHHHCCCCHH		55.7723000965
726AcetylationIQVNEPWKRIKGSEA
EEECCCHHHCCCCHH		55.7723749302
729UbiquitinationNEPWKRIKGSEADRQ
CCCHHHCCCCHHHHH		61.4923000965
812PhosphorylationLENDQIESLRQRFGG
HCHHHHHHHHHHHCC		30.4026074081
823UbiquitinationRFGGGQAKTSPKPAV
HHCCCCCCCCCCCEE		41.4727667366
824PhosphorylationFGGGQAKTSPKPAVV
HCCCCCCCCCCCEEE		53.9622167270
825PhosphorylationGGGQAKTSPKPAVVE
CCCCCCCCCCCEEEE		30.1622167270
833PhosphorylationPKPAVVETVTTAKPQ
CCCEEEEEECCCCHH		16.1430278072
835PhosphorylationPAVVETVTTAKPQQI
CEEEEEECCCCHHHH		28.5823927012
836PhosphorylationAVVETVTTAKPQQIQ
EEEEEECCCCHHHHH		28.4830278072
838UbiquitinationVETVTTAKPQQIQAL
EEEECCCCHHHHHHH		41.0729967540
850PhosphorylationQALMDEVTKQGNIVR
HHHHHHHHHHCHHHH		18.6624732914
866UbiquitinationLKAQKADKNEVAAEV
HHHHCCCHHHHHHHH		60.9216196087
866MalonylationLKAQKADKNEVAAEV
HHHHCCCHHHHHHHH		60.9226320211
866AcetylationLKAQKADKNEVAAEV
HHHHCCCHHHHHHHH		60.9225953088
875UbiquitinationEVAAEVAKLLDLKKQ
HHHHHHHHHHHHHHH		55.5516196087
881UbiquitinationAKLLDLKKQLAVAEG
HHHHHHHHHHHHHCC		58.8229967540
889AcetylationQLAVAEGKPPEAPKG
HHHHHCCCCCCCCCC		49.2426051181
889UbiquitinationQLAVAEGKPPEAPKG
HHHHHCCCCCCCCCC		49.2416196087
895UbiquitinationGKPPEAPKGKKKK--
CCCCCCCCCCCCC--		85.4016196087
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
209SPhosphorylationKinaseERK1P27361
PSP
229SPhosphorylationKinaseEIF2AK4Q9P2K8
GPS
472SPhosphorylationKinaseEIF2AK4Q9P2K8
GPS
662SPhosphorylationKinaseEIF2AK4Q9P2K8
GPS
825SPhosphorylationKinaseERK1P27361
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYMC_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 SYMC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYQ_HUMANQARSphysical
22939629
SYRC_HUMANRARSphysical
22939629
THIL_HUMANACAT1physical
22939629
TCPG_HUMANCCT3physical
22939629
AIMP1_HUMANAIMP1physical
22863883
AIMP2_HUMANAIMP2physical
22863883
SYIC_HUMANIARSphysical
22863883
AIMP2_HUMANAIMP2physical
26344197
EEA1_HUMANEEA1physical
26344197
MCA3_HUMANEEF1E1physical
26344197
SYEP_HUMANEPRSphysical
26344197
GARS_HUMANGARSphysical
26344197
GFPT1_HUMANGFPT1physical
26344197
SYHC_HUMANHARSphysical
26344197
SYIC_HUMANIARSphysical
26344197
SYK_HUMANKARSphysical
26344197
SYLC_HUMANLARSphysical
26344197
NAA20_HUMANNAA20physical
26344197
NMT1_HUMANNMT1physical
26344197
OXSR1_HUMANOXSR1physical
26344197
SYQ_HUMANQARSphysical
26344197
TRM6_HUMANTRMT6physical
26344197
TRM61_HUMANTRMT61Aphysical
26344197
TXLNA_HUMANTXLNAphysical
26344197
SYVC_HUMANVARSphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615486Infantile liver failure syndrome 2 (ILFS2)
616280Charcot-Marie-Tooth disease 2U (CMT2U)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00134L-Methionine
Regulatory Network of SYMC_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-726, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND MASSSPECTROMETRY.

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