SYAM_HUMAN - dbPTM
SYAM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYAM_HUMAN
UniProt AC Q5JTZ9
Protein Name Alanine--tRNA ligase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03133}
Gene Name AARS2 {ECO:0000255|HAMAP-Rule:MF_03133}
Organism Homo sapiens (Human).
Sequence Length 985
Subcellular Localization Mitochondrion .
Protein Description Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain..
Protein Sequence MAASVAAAARRLRRAIRRSPAWRGLSHRPLSSEPPAAKASAVRAAFLNFFRDRHGHRLVPSASVRPRGDPSLLFVNAGMNQFKPIFLGTVDPRSEMAGFRRVANSQKCVRAGGHHNDLEDVGRDLSHHTFFEMLGNWAFGGEYFKEEACNMAWELLTQVYGIPEERLWISYFDGDPKAGLDPDLETRDIWLSLGVPASRVLSFGPQENFWEMGDTGPCGPCTEIHYDLAGGVGAPQLVELWNLVFMQHNREADGSLQPLPQRHVDTGMGLERLVAVLQGKHSTYDTDLFSPLLNAIQQGCRAPPYLGRVGVADEGRTDTAYRVVADHIRTLSVCISDGIFPGMSGPPLVLRRILRRAVRFSMEILKAPPGFLGSLVPVVVETLGDAYPELQRNSAQIANLVSEDEAAFLASLERGRRIIDRTLRTLGPSDMFPAEVAWSLSLCGDLGLPLDMVELMLEEKGVQLDSAGLERLAQEEAQHRARQAEPVQKQGLWLDVHALGELQRQGVPPTDDSPKYNYSLRPSGSYEFGTCEAQVLQLYTEDGTAVASVGKGQRCGLLLDRTNFYAEQGGQASDRGYLVRAGQEDVLFPVARAQVCGGFILHEAVAPECLRLGDQVQLHVDEAWRLGCMAKHTATHLLNWALRQTLGPGTEQQGSHLNPEQLRLDVTTQTPLTPEQLRAVENTVQEAVGQDEAVYMEEVPLALTAQVPGLRSLDEVYPDPVRVVSVGVPVAHALDPASQAALQTSVELCCGTHLLRTGAVGDLVIIGDRQLSKGTTRLLAVTGEQAQQARELGQSLAQEVKAATERLSLGSRDVAEALRLSKDIGRLIEAVETAVMPQWQRRELLATVKMLQRRANTAIRKLQMGQAAKKTQELLERHSKGPLIVDTVSAESLSVLVKVVRQLCEQAPSTSVLLLSPQPMGKVLCACQVAQGAMPTFTAEAWALAVCSHMGGKAWGSRVVAQGTGSTTDLEAALSIAQTYALSQL
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
83UbiquitinationNAGMNQFKPIFLGTV
ECCCCCCCCEEEEEC		27.6922817900
280UbiquitinationLVAVLQGKHSTYDTD
HHHHHCCCCCCCCCC		22.78-
300GlutathionylationLNAIQQGCRAPPYLG
HHHHHHCCCCCCCCC		2.6622555962
330PhosphorylationVVADHIRTLSVCISD
HHHHHHHHEEEEECC		23.8422210691
332PhosphorylationADHIRTLSVCISDGI
HHHHHHEEEEECCCC		17.8422210691
336PhosphorylationRTLSVCISDGIFPGM
HHEEEEECCCCCCCC		25.3420068231
344PhosphorylationDGIFPGMSGPPLVLR
CCCCCCCCCCHHHHH		54.8020068231
361PhosphorylationLRRAVRFSMEILKAP
HHHHHHHHHHHHHCC		12.6321406692
374PhosphorylationAPPGFLGSLVPVVVE
CCCCHHHHHHHHHHH		28.4850558273
382PhosphorylationLVPVVVETLGDAYPE
HHHHHHHHHHHCCHH		25.1650558279
387PhosphorylationVETLGDAYPELQRNS
HHHHHHCCHHHHHCH		11.2850558285
402PhosphorylationAQIANLVSEDEAAFL
HHHHHHCCHHHHHHH		42.36110752575
519PhosphorylationDSPKYNYSLRPSGSY
CCCCCCEECCCCCCC		17.7924719451
561MethylationRCGLLLDRTNFYAEQ
CEEEEEECCCCCHHH		31.38-
575MethylationQGGQASDRGYLVRAG
HCCCCCCCCEEEECC		32.91-
580MethylationSDRGYLVRAGQEDVL
CCCCEEEECCCCCCC		30.33-
670PhosphorylationRLDVTTQTPLTPEQL
CCEEECCCCCCHHHH		20.4124719451
673PhosphorylationVTTQTPLTPEQLRAV
EECCCCCCHHHHHHH		26.4422817900
712PhosphorylationAQVPGLRSLDEVYPD
CCCCCCCCCCCCCCC		45.2620068231
717PhosphorylationLRSLDEVYPDPVRVV
CCCCCCCCCCCCEEE		10.4020068231
795O-linked_GlycosylationQARELGQSLAQEVKA
HHHHHHHHHHHHHHH		24.7123301498
801UbiquitinationQSLAQEVKAATERLS
HHHHHHHHHHHHHHC		31.3929967540
819MethylationRDVAEALRLSKDIGR
HHHHHHHHHHHHHHH		43.92-
857PhosphorylationMLQRRANTAIRKLQM
HHHHHHHHHHHHHHH		23.6024114839
892PhosphorylationVDTVSAESLSVLVKV
EEECCHHHHHHHHHH		26.1746156181
894PhosphorylationTVSAESLSVLVKVVR
ECCHHHHHHHHHHHH		23.7646156187
909PhosphorylationQLCEQAPSTSVLLLS
HHHHHCCCCEEEEEC		36.0124043423
910PhosphorylationLCEQAPSTSVLLLSP
HHHHCCCCEEEEECC		23.0724043423
911PhosphorylationCEQAPSTSVLLLSPQ
HHHCCCCEEEEECCC		18.3324043423
916PhosphorylationSTSVLLLSPQPMGKV
CCEEEEECCCCCCHH		22.8124043423
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
673TPhosphorylationKinaseCDK2P24941
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of SYAM_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614096Combined oxidative phosphorylation deficiency 8 (COXPD8)
615889Leukoencephalopathy, progressive, with ovarian failure (LKENP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00160L-Alanine
Regulatory Network of SYAM_HUMAN

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Related Literatures of Post-Translational Modification

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