dbPTM

SYA_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYA_SCHPO
UniProt AC	O13914
Protein Name	Alanine--tRNA ligase {ECO:0000255\|HAMAP-Rule:MF_03133}
Gene Name	ala1
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	959
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	MTAESEVVNWPANEIRRTFLKYFEDHGHTIVPSSSVIPYDDPTLLFANAGMNQFKPIFLGTVDPSSDFAKLKRACDSQKCIRAGGKHNDLEDVGKDNYHHTMFEMLGNWSFGDYFKKEAIAMAWDLLTNVYGLKKDQLYVTYFGGHEESGLEPDLEARQLWLDIGIDESRVIPGSLKDNFWEMGDQGPCGPCSEIHYDRIGNRTVPELVNMDDPNVLEIWNIVFIQFNREKDGSLRPLPNRHVDTGMGFERLVSVIQNKTSNYDTDVFSPIFAKIQELTNARPYTGKMGDEDVDGIDTAYRVVADHVRTLTFAISDGGVPNNEGRGYVLRRILRRGARYVRKKFGVPIGNFFSRLSLTVVEQMGDFFPELKRKVDDVRELLDEEEESFSRTLDRGEKMFEQYAAAAKKTPSKTLQGNDVWRLYETYGFPVDLTHLMAEEAGIKIDEPGFEAAQARSKEISKQASKGGSSGDDLLVLDVHALGALSKMDDIPETDDVFKHNSVSLKSVIKGIYHKGGFQKSTEGFNSGEQLGLLLDRTNFYAEQGGQEYDTGHIVIDGVADFRVTNVQVYAGYVLHTGFLEYGNLTVNDSVVCEYDEIRRWHLMNNHTVTHILNLALRNTLGDGIDQRGSLVSQEKLRFDFSYKSSIPIDKLLLVENYCNNVIQDNLSVYSKEVALSKAKEINGLRAVFGEVYPDPVRVVCIGVDIDTLLQEPKKPDWTKYSIEFCGGTHCDKSGEIKDFVILEENGIAKGIRRIVAVTSTEANRVSRLANEFDARIAKLEKMPFSPAKEAELKKISVDLSKLVVAAVRKHAMKERIAKITKQVQEHVKAINAAEQKEVVNVVTEYFKENPDMSFVVAKVPISANPKALSFALTYAKKNLKDKSIYLLASDDTKVAHACLVSPEAMKKLTPQEWSQKVCHSIGGRSGGKGDTCQGVGDKPLSIDVAVEEAIEFFQGKLTI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
309	Phosphorylation	VVADHVRTLTFAISD HHHHHHEEEEEEEEC	29.12	25720772
311	Phosphorylation	ADHVRTLTFAISDGG HHHHEEEEEEEECCC	15.48	25720772
387	Phosphorylation	LLDEEEESFSRTLDR HCHHHHHHHHHHHHH	31.62	25720772
389	Phosphorylation	DEEEESFSRTLDRGE HHHHHHHHHHHHHHH	33.37	28889911
521	Phosphorylation	KGGFQKSTEGFNSGE CCCCCCCCCCCCCHH	47.35	25720772

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_SCHPO !!

Functions of PTM Sites

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

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_SCHPO !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of SYA_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of fission yeast."; Wilson-Grady J.T., Villen J., Gygi S.P.; J. Proteome Res. 7:1088-1097(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND MASSSPECTROMETRY.	18257517 [Abstract]