SYEM_HUMAN - dbPTM
SYEM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYEM_HUMAN
UniProt AC Q5JPH6
Protein Name Probable glutamate--tRNA ligase, mitochondrial
Gene Name EARS2
Organism Homo sapiens (Human).
Sequence Length 523
Subcellular Localization Mitochondrion matrix.
Protein Description Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu)..
Protein Sequence MAALLRRLLQRERPSAASGRPVGRREANLGTDAGVAVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRGGPAGPYQQSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRLEQVVPAFQDLVYGWNRHEVASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQRLVSNESQRRQLVGKLQVLVEEAFGCQLQNRDVLNPVYVERILLLRQGHICRLQDLVSPVYSYLWTRPAVGRAQLDAISEKVDVIAKRVLGLLERSSMSLTQDMLNGELKKLSEGLEGTKYSNVMKLLRMALSGQQQGPPVAEMMLALGPKEVRERIQKVVSS
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
44PhosphorylationVRVRFAPSPTGFLHL
EEEEECCCCCCCEEC		31.5020068231
46PhosphorylationVRFAPSPTGFLHLGG
EEECCCCCCCEECCH		44.9220068231
56PhosphorylationLHLGGLRTALYNYIF
EECCHHHHHHHHHHH		26.5118452278
59PhosphorylationGGLRTALYNYIFAKK
CHHHHHHHHHHHCHH		11.9418452278
61PhosphorylationLRTALYNYIFAKKYQ
HHHHHHHHHHCHHCC		5.4818452278
67PhosphorylationNYIFAKKYQGSFILR
HHHHCHHCCCEEEEE		19.8722210691
91UbiquitinationVPGAAENIEDMLEWA
CCCHHHCHHHHHHHC		3.4124816145
108MethylationPPDESPRRGGPAGPY
CCCCCCCCCCCCCCC		58.78-
134PhosphorylationATEALLKTGAAYPCF
HHHHHHHCCCCCCCC		31.8326074081
138PhosphorylationLLKTGAAYPCFCSPQ
HHHCCCCCCCCCCHH		10.4526074081
143PhosphorylationAAYPCFCSPQRLELL
CCCCCCCCHHHHHHH		12.1025159151
160UbiquitinationEALRNHQTPRYDNRC
HHHHCCCCCCCCHHH		11.3724816145
178UbiquitinationSQEQVAQKLAKDPKP
CHHHHHHHHHCCCCH		40.4529967540
178AcetylationSQEQVAQKLAKDPKP
CHHHHHHHHHCCCCH		40.4525953088
184UbiquitinationQKLAKDPKPAIRFRL
HHHHCCCCHHHHHHH		58.1624816145
256SuccinylationEWLVSTAKHLLLYQA
HHHHHHHHHHHHHHH		34.57-
256SuccinylationEWLVSTAKHLLLYQA
HHHHHHHHHHHHHHH		34.57-
326PhosphorylationAENQMGRTLPELITQ
HHCCHHCCHHHHHHH		40.7224043423
332PhosphorylationRTLPELITQFNLTQV
CCHHHHHHHCCCCCC		39.4724043423
337PhosphorylationLITQFNLTQVTCHSA
HHHHCCCCCCCCCHH		23.3024043423
340PhosphorylationQFNLTQVTCHSALLD
HCCCCCCCCCHHHHC		8.4924043423
343PhosphorylationLTQVTCHSALLDLEK
CCCCCCCHHHHCHHH		23.8224043423
387UbiquitinationVEEAFGCQLQNRDVL
HHHHHCCCCCCCCCC		46.6021890473
393UbiquitinationCQLQNRDVLNPVYVE
CCCCCCCCCCHHHHH		5.1323503661
398PhosphorylationRDVLNPVYVERILLL
CCCCCHHHHHHHHHH		9.61-
4472-HydroxyisobutyrylationEKVDVIAKRVLGLLE
HHHHHHHHHHHHHHH		31.73-
447AcetylationEKVDVIAKRVLGLLE
HHHHHHHHHHHHHHH		31.7325953088
456UbiquitinationVLGLLERSSMSLTQD
HHHHHHHHCCCHHHH		22.4821890473
462UbiquitinationRSSMSLTQDMLNGEL
HHCCCHHHHHHHHHH		39.1323503661
470UbiquitinationDMLNGELKKLSEGLE
HHHHHHHHHHHHCCC		47.57-
470AcetylationDMLNGELKKLSEGLE
HHHHHHHHHHHHCCC		47.5719809829
473PhosphorylationNGELKKLSEGLEGTK
HHHHHHHHHCCCCCH		38.2022985185
480UbiquitinationSEGLEGTKYSNVMKL
HHCCCCCHHHHHHHH		58.5021890473
480MalonylationSEGLEGTKYSNVMKL
HHCCCCCHHHHHHHH		58.5026320211
486MalonylationTKYSNVMKLLRMALS
CHHHHHHHHHHHHHC		39.8426320211
486UbiquitinationTKYSNVMKLLRMALS
CHHHHHHHHHHHHHC		39.8423503661
486AcetylationTKYSNVMKLLRMALS
CHHHHHHHHHHHHHC		39.8419608861
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 SYEM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of SYEM_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614924Combined oxidative phosphorylation deficiency 12 (COXPD12)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYEM_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-486, AND MASS SPECTROMETRY.

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