dbPTM

SYA_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYA_ARATH
UniProt AC	P36428
Protein Name	Alanine--tRNA ligase {ECO:0000255\|HAMAP-Rule:MF_03133}
Gene Name	ALATS
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	1003
Subcellular Localization	Mitochondrion. Cytoplasm.
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	MRLVKAASLLISSTKPPSRVFYSSHLRRPFFSHFRFSSSSSTSSSVAVMPGSEPSETQWPAKRVRDTYVDFFRGKGHKFWPSSPVVPHNDPTLLFANAGMNQYKPIFLGTADPNTELSKLSRACNTQKCIRAGGKHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKKEAIEWAWELLTKVYGLPTDRIYATYFGGDEKAGLQPDNEARDIWLKVLPSGRVLPFGCKDNFWEMGDTGPCGPCTEIHYDRIGNRDAASLVNNDDPTCLEIWNLVFIQFNRESDGSLKPLPAKHVDTGMGFERLTSVLQNKMSNYDTDVFMPIFDDIQKATGARPYSGKVGPEDVDRVDMAYRVVADHIRTLSFAIADGSRPGNEGREYVLRRILRRAVRYGKEILKAEEGFFNGLVSSVIRVMGDVFTELKEHEKKITDIIKEEEASFCKTLAKGIEKFRKAGQAVQGNTLSGDDAFILWDTYGFPLDLTQLMAEERGLLVDVDGFNKAMEEARERSRSAQNKQAGGAIVMDADATSTLHKAGVSATDDSFKYIWFQDHESELKAIYTGSTFLESSAASDNVGLVLGSTSFYAEQGGQIFDTGLIEGSFGTFNVCNVQIFGGFVLHIGYLSKETGEVSVGDKVICKVDYERRKLIAPNHTCTHMLNYALKEVLGDHIDQKGSIVLPEKLRFDFSHGKPVDPEDLRRIESIVNKQIKDELDVFSKEAVLSEAKRIKGLRAVFGEVYPDPVRVVSIGRKVEDLLADPENNEWSLLSSEFCGGTHITNTREAKAFALLSEEGIAKGIRRVTAVTTECAFDALNAASLLEREVEDASRAEGSALEKKVSALKSRVDAAIIPAAKKADIRTKIASLQNEVRKAQKKIAEQNLKKSVKLATEAAESAASDGKTFCIIQLDVGLDAAAVREAVSKVMEKKGMSIMVFSTDESTNKAVVCAGVPEKSDQFKPLDVTEWLTTALGPLKGRCGKGKGGLASGQGTDASQVQAALDMASSFASMKLN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4 (in isoform 2)	Phosphorylation	-	5.06	19376835
52	Phosphorylation	SVAVMPGSEPSETQW CEEECCCCCCCCCCC	40.23	30291188
55	Phosphorylation	VMPGSEPSETQWPAK ECCCCCCCCCCCCCH	49.58	30407730
301	Phosphorylation	GMGFERLTSVLQNKM CCCHHHHHHHHHHHH	24.02	30407730
302	Phosphorylation	MGFERLTSVLQNKMS CCHHHHHHHHHHHHC	25.97	30407730
696	Phosphorylation	EDLRRIESIVNKQIK HHHHHHHHHHHHHHH	29.48	25561503

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 SYA_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SYA_ARATH !!

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 SYA_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SYA_ARATH !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SYA_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND MASSSPECTROMETRY.	19376835 [Abstract]