SYRC_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SYRC_MOUSE
• UniProt AC: Q9D0I9
• Protein Name: Arginine--tRNA ligase, cytoplasmic
• Gene Name: Rars
• Organism: Mus musculus (Mouse).
• Sequence Length: 660
• Subcellular Localization: Cytoplasm . Cytoplasm, cytosol .
• Protein Description: Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. [PubMed: 12060739 Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1.]
• Protein Sequence: MDGLVAQCSARLLQQEREIKALTAEIDRLKNCGCLEASPSLEQLREENLKLKYRLNILRRSLQEERRKPTKNMININSRLQEVFGCAIRAAYPDLENPPLIVTPSQQPKFGDYQCNSAMGISQMLKAKEQKVSPREIAENITKHLPNNKYIDKVEIAGPGFINVHLRKDFVSEQLTSLLVNGVQLPVLGDKEKVIVDFSSPNIAKEMHVGHLRSTIIGESMSRLFEFAGYDVLRLNHVGDWGTQFGMLIAHLQDKFPDYLTVSPPIGDLQAFYKESKKRFDADEEFKKRAYQCVVLLQSKNPDIMKAWNLICDVSREEFKKIYDALDITLIERGESFYQDRMKDIVKEFEDKGFVQVDDGRKIVFVPGCSVPLTIVKSDGGYTYDTSDLAAIKQRLFEEKANKIIYVVDNGQAIHFQTIFAAAQMIGWYDPKVTLVTHVGFGVVLGEDKKKFKTRSGETVRLMDLLEEGLKRSMDKLKEKERDKVLTEEELKAAQTSVAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTRIRSIARLANIDEAMLQRAARETKIILDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDYIYELATTFTEFYDSCYCVEKDRQTGKVLKVNMWRMLLCEAVAAVMAKGFDILGIKPVQRM

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
1	Acetylation	-------MDGLVAQC -------CCHHHHHH	9.23	-
20	Acetylation	LQQEREIKALTAEID HHHHHHHHHHHHHHH	32.37	23954790
20	Malonylation	LQQEREIKALTAEID HHHHHHHHHHHHHHH	32.37	26320211
20	Ubiquitination	LQQEREIKALTAEID HHHHHHHHHHHHHHH	32.37	27667366
38	Phosphorylation	NCGCLEASPSLEQLR CCCCCCCCCCHHHHH	12.97	28066266
40	Phosphorylation	GCLEASPSLEQLREE CCCCCCCCHHHHHHH	41.88	26824392
61	Phosphorylation	RLNILRRSLQEERRK HHHHHHHHHHHHHCC	28.15	29514104
86	S-nitrosocysteine	RLQEVFGCAIRAAYP HHHHHHCHHHHHHCC	1.61	-
86	S-nitrosylation	RLQEVFGCAIRAAYP HHHHHHCHHHHHHCC	1.61	21278135
86	Glutathionylation	RLQEVFGCAIRAAYP HHHHHHCHHHHHHCC	1.61	24333276
86	S-palmitoylation	RLQEVFGCAIRAAYP HHHHHHCHHHHHHCC	1.61	28526873
115	Glutathionylation	PKFGDYQCNSAMGIS CCCCCCCCHHHHHHH	3.37	24333276
143	Acetylation	EIAENITKHLPNNKY HHHHHHHHHCCCCCE	39.07	23236377
143	Malonylation	EIAENITKHLPNNKY HHHHHHHHHCCCCCE	39.07	26320211
149	Acetylation	TKHLPNNKYIDKVEI HHHCCCCCEEEEEEE	50.66	23954790
205	Ubiquitination	FSSPNIAKEMHVGHL CCCCCHHHHCCCCHH	52.34	-
205	Acetylation	FSSPNIAKEMHVGHL CCCCCHHHHCCCCHH	52.34	23236377
205	Malonylation	FSSPNIAKEMHVGHL CCCCCHHHHCCCCHH	52.34	26320211
230	Phosphorylation	RLFEFAGYDVLRLNH HHHHHCCCCEEECCC	10.23	-
278	Malonylation	AFYKESKKRFDADEE HHHHHHHHCCCCCHH	68.52	26320211
278	Ubiquitination	AFYKESKKRFDADEE HHHHHHHHCCCCCHH	68.52	-
287	Acetylation	FDADEEFKKRAYQCV CCCCHHHHHHHHHHH	44.63	23954790
312	S-palmitoylation	MKAWNLICDVSREEF HHHHHHHHHCCHHHH	4.81	28526873
347	Acetylation	DRMKDIVKEFEDKGF HHHHHHHHHHHHCCC	57.95	23954790
362	Acetylation	VQVDDGRKIVFVPGC EEECCCCEEEEECCC	49.07	22826441
362	Ubiquitination	VQVDDGRKIVFVPGC EEECCCCEEEEECCC	49.07	22790023
369	S-nitrosocysteine	KIVFVPGCSVPLTIV EEEEECCCCCEEEEE	2.80	-
369	S-nitrosylation	KIVFVPGCSVPLTIV EEEEECCCCCEEEEE	2.80	21278135
369	S-palmitoylation	KIVFVPGCSVPLTIV EEEEECCCCCEEEEE	2.80	28526873
369	Glutathionylation	KIVFVPGCSVPLTIV EEEEECCCCCEEEEE	2.80	24333276
370	Phosphorylation	IVFVPGCSVPLTIVK EEEECCCCCEEEEEE	32.46	23984901
374	Phosphorylation	PGCSVPLTIVKSDGG CCCCCEEEEEECCCC	20.04	23984901
377	Malonylation	SVPLTIVKSDGGYTY CCEEEEEECCCCCEE	38.69	26073543
378	Phosphorylation	VPLTIVKSDGGYTYD CEEEEEECCCCCEEE	30.50	29514104
382	Phosphorylation	IVKSDGGYTYDTSDL EEECCCCCEEEHHHH	13.99	22210690
383	Phosphorylation	VKSDGGYTYDTSDLA EECCCCCEEEHHHHH	20.42	30635358
384	Phosphorylation	KSDGGYTYDTSDLAA ECCCCCEEEHHHHHH	14.56	22817900
386	Phosphorylation	DGGYTYDTSDLAAIK CCCCEEEHHHHHHHH	17.46	30635358
387	Phosphorylation	GGYTYDTSDLAAIKQ CCCEEEHHHHHHHHH	27.94	30635358
393	Ubiquitination	TSDLAAIKQRLFEEK HHHHHHHHHHHHHHH	25.33	22790023
393	Acetylation	TSDLAAIKQRLFEEK HHHHHHHHHHHHHHH	25.33	23954790
456	Phosphorylation	KKKFKTRSGETVRLM HHHCCCCCCCCHHHH	46.33	29514104
476	Acetylation	GLKRSMDKLKEKERD HHHHHHHHHHHHHHH	53.47	6568861
478	Acetylation	KRSMDKLKEKERDKV HHHHHHHHHHHHHHC	72.91	6569101
502	Glutathionylation	QTSVAYGCIKYADLS HHHHHHCCHHHHCCC	1.26	24333276
502	S-nitrosylation	QTSVAYGCIKYADLS HHHHHHCCHHHHCCC	1.26	21278135
502	S-nitrosocysteine	QTSVAYGCIKYADLS HHHHHHCCHHHHCCC	1.26	-
502	S-palmitoylation	QTSVAYGCIKYADLS HHHHHHCCHHHHCCC	1.26	28526873
504	Acetylation	SVAYGCIKYADLSHN HHHHCCHHHHCCCCC	38.16	22826441
530	Phosphorylation	MLDDRGNTAAYLLYA HHCCCCCHHHHHHHH	18.58	25367039
533	Phosphorylation	DRGNTAAYLLYAFTR CCCCHHHHHHHHHHH	8.52	25367039
536	Phosphorylation	NTAAYLLYAFTRIRS CHHHHHHHHHHHHHH	9.32	22817900
539	Phosphorylation	AYLLYAFTRIRSIAR HHHHHHHHHHHHHHH	19.60	25367039
563	Acetylation	QRAARETKIILDHEK HHHHHHCCEEECCHH	24.01	23954790
626	Malonylation	EKDRQTGKVLKVNMW ECCCCCCCEEEHHHH	48.02	26320211
629	Acetylation	RQTGKVLKVNMWRML CCCCCEEEHHHHHHH	34.25	22826441
629	Malonylation	RQTGKVLKVNMWRML CCCCCEEEHHHHHHH	34.25	26320211
638	S-nitrosocysteine	NMWRMLLCEAVAAVM HHHHHHHHHHHHHHH	2.51	-
638	S-nitrosylation	NMWRMLLCEAVAAVM HHHHHHHHHHHHHHH	2.51	22178444

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SYRC_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SYRC_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SYRC_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of SYRC_MOUSE !!

Drug and Disease Associations

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