SYTM_HUMAN - dbPTM
SYTM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYTM_HUMAN
UniProt AC Q9BW92
Protein Name Threonine--tRNA ligase, mitochondrial
Gene Name TARS2
Organism Homo sapiens (Human).
Sequence Length 718
Subcellular Localization Mitochondrion matrix.
Protein Description Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain..
Protein Sequence MALYQRWRCLRLQGLQACRLHTAVVSTPPRWLAERLGLFEELWAAQVKRLASMAQKEPRTIKISLPGGQKIDAVAWNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLGAAAEQFLGAVLCRGPSTEYGFYHDFFLGKERTIRGSELPVLERICQELTAAARPFRRLEASRDQLRQLFKDNPFKLHLIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGLKLLSNSSSLWRSSGAPETLQRVSGISFPTTELLRVWEAWREEAELRDHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPGSDRPPSSQSDDSTRHITDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSFRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGQAGALERPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDADSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDLPEAVQRLVELQNTRVPNAEEIF
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
52PhosphorylationAQVKRLASMAQKEPR
HHHHHHHHHHCCCCC		21.1724827421
56UbiquitinationRLASMAQKEPRTIKI
HHHHHHCCCCCEEEE		61.21-
56UbiquitinationRLASMAQKEPRTIKI
HHHHHHCCCCCEEEE		61.21-
62UbiquitinationQKEPRTIKISLPGGQ
CCCCCEEEEECCCCC		26.15-
70UbiquitinationISLPGGQKIDAVAWN
EECCCCCEEEEEEEC		45.92-
124PhosphorylationLRFLTFDSPEGKAVF
CEEEEECCCCCCEEE		22.2121815630
159PhosphorylationCRGPSTEYGFYHDFF
CCCCCCCCCCCCCEE		16.7829496907
162PhosphorylationPSTEYGFYHDFFLGK
CCCCCCCCCCEECCC		8.9829496907
169UbiquitinationYHDFFLGKERTIRGS
CCCEECCCCEECCCC		46.2821890473
169UbiquitinationYHDFFLGKERTIRGS
CCCEECCCCEECCCC		46.2821890473
176PhosphorylationKERTIRGSELPVLER
CCEECCCCHHHHHHH		26.5522210691
210UbiquitinationDQLRQLFKDNPFKLH
HHHHHHHHCCCCEEE		66.25-
215UbiquitinationLFKDNPFKLHLIEEK
HHHCCCCEEEEEEEE		35.9321890473
222UbiquitinationKLHLIEEKVTGPTAT
EEEEEEEECCCCCEE		32.10-
262PhosphorylationKLLSNSSSLWRSSGA
EECCCCCCHHHCCCC		31.6024719451
266PhosphorylationNSSSLWRSSGAPETL
CCCCHHHCCCCCHHH		22.8824719451
267PhosphorylationSSSLWRSSGAPETLQ
CCCHHHCCCCCHHHH		30.3328857561
329PhosphorylationCFFLPRGTRVYNALV
EEEECCCHHHHHHHH		20.4522210691
332PhosphorylationLPRGTRVYNALVAFI
ECCCHHHHHHHHHHH		7.4522210691
343PhosphorylationVAFIRAEYAHRGFSE
HHHHHHHHHHCCCCC		13.5122210691
349PhosphorylationEYAHRGFSEVKTPTL
HHHHCCCCCCCCCCE		44.2822210691
352UbiquitinationHRGFSEVKTPTLFST
HCCCCCCCCCCEEEE		44.74-
388PhosphorylationPGSDRPPSSQSDDST
CCCCCCCCCCCCCCC		43.6326471730
389PhosphorylationGSDRPPSSQSDDSTR
CCCCCCCCCCCCCCC		39.2026471730
390UbiquitinationSDRPPSSQSDDSTRH
CCCCCCCCCCCCCCC		56.04-
391PhosphorylationDRPPSSQSDDSTRHI
CCCCCCCCCCCCCCC		45.3826471730
394PhosphorylationPSSQSDDSTRHITDT
CCCCCCCCCCCCCCC		32.1226471730
395PhosphorylationSSQSDDSTRHITDTL
CCCCCCCCCCCCCCE		33.0126471730
405UbiquitinationITDTLALKPMNCPAH
CCCCEECCCCCCCHH		36.29-
429MethylationSWRELPLRLADFGAL
CHHHCCCHHHHHHHH		26.37115918233
442UbiquitinationALHRAEASGGLGGLT
HHHHHHHCCCCCHHC		25.5421890473
489PhosphorylationVYAVLGFSFRLALST
HHHHHCHHHHHHHCC		13.9924719451
520UbiquitinationQVLKQALKEFGEPWD
HHHHHHHHHHCCCCC		54.75-
530PhosphorylationGEPWDLNSGDGAFYG
CCCCCCCCCCCCCCC		45.63-
536PhosphorylationNSGDGAFYGPKIDVH
CCCCCCCCCCEEEEE		31.80-
572UbiquitinationLRFDLQYKGQAGALE
EEEECEECCCCCCCC		31.4221890473
643PhosphorylationLRAAGLVSDLDADSG
HHHCCCCCCCCCCCC		37.1820860994
652PhosphorylationLDADSGLTLSRRIRR
CCCCCCCCHHHHHHH		26.6424719451
654PhosphorylationADSGLTLSRRIRRAQ
CCCCCCHHHHHHHHH		17.8020860994
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 SYTM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYTM_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 SYTM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SYTM_HUMAN !!
Drug and Disease Associations
Kegg Disease
OMIM Disease
615918Combined oxidative phosphorylation deficiency 21 (COXPD21)
Kegg Drug
DrugBank
DB00156L-Threonine
Regulatory Network of SYTM_HUMAN

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Related Literatures of Post-Translational Modification

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