dbPTM

SYRC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYRC_HUMAN
UniProt AC	P54136
Protein Name	Arginine--tRNA ligase, cytoplasmic
Gene Name	RARS
Organism	Homo sapiens (Human).
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: 25288775 Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1]
Protein Sequence	MDVLVSECSARLLQQEEEIKSLTAEIDRLKNCGCLGASPNLEQLQEENLKLKYRLNILRKSLQAERNKPTKNMINIISRLQEVFGHAIKAAYPDLENPPLLVTPSQQAKFGDYQCNSAMGISQMLKTKEQKVNPREIAENITKHLPDNECIEKVEIAGPGFINVHLRKDFVSEQLTSLLVNGVQLPALGENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDVLRLNHVGDWGTQFGMLIAHLQDKFPDYLTVSPPIGDLQVFYKESKKRFDTEEEFKKRAYQCVVLLQGKNPDITKAWKLICDVSRQELNKIYDALDVSLIERGESFYQDRMNDIVKEFEDRGFVQVDDGRKIVFVPGCSIPLTIVKSDGGYTYDTSDLAAIKQRLFEEKADMIIYVVDNGQSVHFQTIFAAAQMIGWYDPKVTRVFHAGFGVVLGEDKKKFKTRSGETVRLMDLLGEGLKRSMDKLKEKERDKVLTAEELNAAQTSVAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTRIRSIARLANIDEEMLQKAARETKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDYIYELATAFTEFYDSCYCVEKDRQTGKILKVNMWRMLLCEAVAAVMAKGFDILGIKPVQRM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDVLVSEC -------CCHHHHHH	7.89	22223895
6	Phosphorylation	--MDVLVSECSARLL --CCHHHHHHHHHHH	28.82	20860994
20	Ubiquitination	LQQEEEIKSLTAEID HHCHHHHHHHHHHHH	42.57	21890473
20	2-Hydroxyisobutyrylation	LQQEEEIKSLTAEID HHCHHHHHHHHHHHH	42.57	-
20	Ubiquitination	LQQEEEIKSLTAEID HHCHHHHHHHHHHHH	42.57	22053931
20 (in isoform 1)	Ubiquitination	-	42.57	21890473
20	Ubiquitination	LQQEEEIKSLTAEID HHCHHHHHHHHHHHH	42.57	21890473
21	Phosphorylation	QQEEEIKSLTAEIDR HCHHHHHHHHHHHHH	36.29	25159151
30	2-Hydroxyisobutyrylation	TAEIDRLKNCGCLGA HHHHHHHHCCCCCCC	51.60	-
30	Acetylation	TAEIDRLKNCGCLGA HHHHHHHHCCCCCCC	51.60	26051181
30	Ubiquitination	TAEIDRLKNCGCLGA HHHHHHHHCCCCCCC	51.60	32015554
38	Phosphorylation	NCGCLGASPNLEQLQ CCCCCCCCCCHHHHH	16.72	25159151
50	Acetylation	QLQEENLKLKYRLNI HHHHHCHHHHHHHHH	55.29	25953088
50	Ubiquitination	QLQEENLKLKYRLNI HHHHHCHHHHHHHHH	55.29	32015554
60	Acetylation	YRLNILRKSLQAERN HHHHHHHHHHHHHHC	52.66	19608861
61	Phosphorylation	RLNILRKSLQAERNK HHHHHHHHHHHHHCC	21.19	26699800
71	Ubiquitination	AERNKPTKNMINIIS HHHCCCCHHHHHHHH	53.71	24816145
73	Sulfoxidation	RNKPTKNMINIISRL HCCCCHHHHHHHHHH	2.37	28183972
103	Phosphorylation	ENPPLLVTPSQQAKF CCCCEEECHHHHCCC	19.72	25850435
105	Phosphorylation	PPLLVTPSQQAKFGD CCEEECHHHHCCCCC	26.09	25850435
115	Glutathionylation	AKFGDYQCNSAMGIS CCCCCCCCHHHHHHH	3.37	22555962
126	Ubiquitination	MGISQMLKTKEQKVN HHHHHHHHCCCCCCC	52.81	32015554
133 (in isoform 2)	Ubiquitination	-	36.63	21890473
143	Trimethylation	EIAENITKHLPDNEC HHHHHHHHHCCCCHH	39.07	-
143	Acetylation	EIAENITKHLPDNEC HHHHHHHHHCCCCHH	39.07	25953088
143	Methylation	EIAENITKHLPDNEC HHHHHHHHHCCCCHH	39.07	-
143	Ubiquitination	EIAENITKHLPDNEC HHHHHHHHHCCCCHH	39.07	29967540
150	Glutathionylation	KHLPDNECIEKVEIA HHCCCCHHEEEEEEC	6.45	22555962
153	Acetylation	PDNECIEKVEIAGPG CCCHHEEEEEECCCC	25.84	26051181
193	Ubiquitination	PALGENKKVIVDFSS CCCCCCCEEEEECCC	49.10	29967540
199	Phosphorylation	KKVIVDFSSPNIAKE CEEEEECCCCCHHHH	40.18	25627689
200	Phosphorylation	KVIVDFSSPNIAKEM EEEEECCCCCHHHHC	23.20	25159151
202 (in isoform 2)	Ubiquitination	-	49.12	21890473
205	Ubiquitination	FSSPNIAKEMHVGHL CCCCCHHHHCCHHHH	52.34	21890473
205	Acetylation	FSSPNIAKEMHVGHL CCCCCHHHHCCHHHH	52.34	23954790
205	Malonylation	FSSPNIAKEMHVGHL CCCCCHHHHCCHHHH	52.34	26320211
205	Ubiquitination	FSSPNIAKEMHVGHL CCCCCHHHHCCHHHH	52.34	23000965
205 (in isoform 1)	Ubiquitination	-	52.34	21890473
205	Ubiquitination	FSSPNIAKEMHVGHL CCCCCHHHHCCHHHH	52.34	21890473
207	Sulfoxidation	SPNIAKEMHVGHLRS CCCHHHHCCHHHHHH	2.82	30846556
215	Phosphorylation	HVGHLRSTIIGESIS CHHHHHHHHHHHHHH	15.35	21712546
230	Phosphorylation	RLFEFAGYDVLRLNH HHHHHCCCCEEECCC	10.23	-
263	Phosphorylation	FPDYLTVSPPIGDLQ CCCCEEECCCCCCCH	21.52	-
274	Ubiquitination	GDLQVFYKESKKRFD CCCHHHHHHHHHCCC	44.01	22817900
274 (in isoform 1)	Ubiquitination	-	44.01	21890473
275 (in isoform 2)	Ubiquitination	-	57.31	21890473
277	Ubiquitination	QVFYKESKKRFDTEE HHHHHHHHHCCCCHH	49.40	22817900
278	Malonylation	VFYKESKKRFDTEEE HHHHHHHHCCCCHHH	68.52	26320211
278	Ubiquitination	VFYKESKKRFDTEEE HHHHHHHHCCCCHHH	68.52	22817900
279	Methylation	FYKESKKRFDTEEEF HHHHHHHCCCCHHHH	38.11	115490337
282	Phosphorylation	ESKKRFDTEEEFKKR HHHHCCCCHHHHHHH	42.45	20068231
287	2-Hydroxyisobutyrylation	FDTEEEFKKRAYQCV CCCHHHHHHHHHHHE	44.63	-
287	Acetylation	FDTEEEFKKRAYQCV CCCHHHHHHHHHHHE	44.63	23954790
287	Ubiquitination	FDTEEEFKKRAYQCV CCCHHHHHHHHHHHE	44.63	24816145
288	Acetylation	DTEEEFKKRAYQCVV CCHHHHHHHHHHHEE	47.81	25953088
290 (in isoform 2)	Ubiquitination	-	13.97	21890473
291	Phosphorylation	EEFKKRAYQCVVLLQ HHHHHHHHHHEEEEC	13.38	28152594
293	Glutathionylation	FKKRAYQCVVLLQGK HHHHHHHHEEEECCC	1.17	22555962
300	2-Hydroxyisobutyrylation	CVVLLQGKNPDITKA HEEEECCCCCCHHHH	52.96	-
300	Acetylation	CVVLLQGKNPDITKA HEEEECCCCCCHHHH	52.96	26051181
300	Ubiquitination	CVVLLQGKNPDITKA HEEEECCCCCCHHHH	52.96	-
306	Acetylation	GKNPDITKAWKLICD CCCCCHHHHHHHHHH	53.21	26051181
306	Ubiquitination	GKNPDITKAWKLICD CCCCCHHHHHHHHHH	53.21	29967540
309	Acetylation	PDITKAWKLICDVSR CCHHHHHHHHHHHCH	32.60	25953088
321	Ubiquitination	VSRQELNKIYDALDV HCHHHHHHHHHHHCH	56.09	29967540
321 (in isoform 2)	Ubiquitination	-	56.09	21890473
329	Phosphorylation	IYDALDVSLIERGES HHHHHCHHHHHCCCC	24.24	26270265
338	Phosphorylation	IERGESFYQDRMNDI HHCCCCHHHHHHHHH	20.84	-
341	Methylation	GESFYQDRMNDIVKE CCCHHHHHHHHHHHH	15.41	115490329
342	Sulfoxidation	ESFYQDRMNDIVKEF CCHHHHHHHHHHHHH	7.70	21406390
347	2-Hydroxyisobutyrylation	DRMNDIVKEFEDRGF HHHHHHHHHHHHCCC	57.95	-
347	Acetylation	DRMNDIVKEFEDRGF HHHHHHHHHHHHCCC	57.95	26051181
347	Ubiquitination	DRMNDIVKEFEDRGF HHHHHHHHHHHHCCC	57.95	21906983
347 (in isoform 1)	Ubiquitination	-	57.95	21890473
352	Methylation	IVKEFEDRGFVQVDD HHHHHHHCCCEEECC	33.00	115490321
362	Ubiquitination	VQVDDGRKIVFVPGC EEECCCCEEEEECCC	49.07	21890473
362	Neddylation	VQVDDGRKIVFVPGC EEECCCCEEEEECCC	49.07	32015554
362	Ubiquitination	VQVDDGRKIVFVPGC EEECCCCEEEEECCC	49.07	23000965
362 (in isoform 1)	Ubiquitination	-	49.07	21890473
362	Ubiquitination	VQVDDGRKIVFVPGC EEECCCCEEEEECCC	49.07	21890473
369	S-nitrosocysteine	KIVFVPGCSIPLTIV EEEEECCCCCEEEEE	2.46	-
369	Glutathionylation	KIVFVPGCSIPLTIV EEEEECCCCCEEEEE	2.46	22555962
369	S-nitrosylation	KIVFVPGCSIPLTIV EEEEECCCCCEEEEE	2.46	19483679
369	S-palmitoylation	KIVFVPGCSIPLTIV EEEEECCCCCEEEEE	2.46	29575903
370	Phosphorylation	IVFVPGCSIPLTIVK EEEECCCCCEEEEEE	32.91	28348404
374	Phosphorylation	PGCSIPLTIVKSDGG CCCCCEEEEEECCCC	20.54	28102081
377	Acetylation	SIPLTIVKSDGGYTY CCEEEEEECCCCCEE	38.69	23236377
377	Malonylation	SIPLTIVKSDGGYTY CCEEEEEECCCCCEE	38.69	26320211
377	Ubiquitination	SIPLTIVKSDGGYTY CCEEEEEECCCCCEE	38.69	33845483
378	Phosphorylation	IPLTIVKSDGGYTYD CEEEEEECCCCCEEE	30.50	28152594
382	Phosphorylation	IVKSDGGYTYDTSDL EEECCCCCEEEHHHH	13.99	28152594
383	Phosphorylation	VKSDGGYTYDTSDLA EECCCCCEEEHHHHH	20.42	28152594
384	Phosphorylation	KSDGGYTYDTSDLAA ECCCCCEEEHHHHHH	14.56	28152594
386	Phosphorylation	DGGYTYDTSDLAAIK CCCCEEEHHHHHHHH	17.46	28152594
387	Phosphorylation	GGYTYDTSDLAAIKQ CCCEEEHHHHHHHHH	27.94	28152594
393	Ubiquitination	TSDLAAIKQRLFEEK HHHHHHHHHHHHHHC	25.33	21890473
393	2-Hydroxyisobutyrylation	TSDLAAIKQRLFEEK HHHHHHHHHHHHHHC	25.33	-
393	Acetylation	TSDLAAIKQRLFEEK HHHHHHHHHHHHHHC	25.33	27452117
393	Ubiquitination	TSDLAAIKQRLFEEK HHHHHHHHHHHHHHC	25.33	23000965
393 (in isoform 1)	Ubiquitination	-	25.33	21890473
393	Ubiquitination	TSDLAAIKQRLFEEK HHHHHHHHHHHHHHC	25.33	21890473
399 (in isoform 2)	Ubiquitination	-	46.33	21890473
449	Ubiquitination	GVVLGEDKKKFKTRS CEEECCCHHHCCCCC	54.27	33845483
450 (in isoform 2)	Ubiquitination	-	75.63	21890473
451	Acetylation	VLGEDKKKFKTRSGE EECCCHHHCCCCCCC	58.81	7681275
453	Acetylation	GEDKKKFKTRSGETV CCCHHHCCCCCCCCH	52.49	7681285
459	Phosphorylation	FKTRSGETVRLMDLL CCCCCCCCHHHHHHH	17.91	-
463	Sulfoxidation	SGETVRLMDLLGEGL CCCCHHHHHHHHHHH	2.09	21406390
471	2-Hydroxyisobutyrylation	DLLGEGLKRSMDKLK HHHHHHHHHHHHHHH	53.97	-
471	Ubiquitination	DLLGEGLKRSMDKLK HHHHHHHHHHHHHHH	53.97	21906983
471 (in isoform 1)	Ubiquitination	-	53.97	21890473
472	Dimethylation	LLGEGLKRSMDKLKE HHHHHHHHHHHHHHH	42.11	-
472	Methylation	LLGEGLKRSMDKLKE HHHHHHHHHHHHHHH	42.11	18938727
476	Ubiquitination	GLKRSMDKLKEKERD HHHHHHHHHHHHHHH	53.47	22817900
480	Ubiquitination	SMDKLKEKERDKVLT HHHHHHHHHHHHCCC	57.36	24816145
484	2-Hydroxyisobutyrylation	LKEKERDKVLTAEEL HHHHHHHHCCCHHHH	45.42	-
485 (in isoform 2)	Ubiquitination	-	7.23	21890473
496	Phosphorylation	EELNAAQTSVAYGCI HHHHHHHHHHHHCCH	22.05	28152594
497	Phosphorylation	ELNAAQTSVAYGCIK HHHHHHHHHHHCCHH	7.83	28152594
500	Phosphorylation	AAQTSVAYGCIKYAD HHHHHHHHCCHHHHH	15.46	28152594
502	Glutathionylation	QTSVAYGCIKYADLS HHHHHHCCHHHHHCC	1.26	22555962
504	Acetylation	SVAYGCIKYADLSHN HHHHCCHHHHHCCCC	38.16	26051181
504	Ubiquitination	SVAYGCIKYADLSHN HHHHCCHHHHHCCCC	38.16	21963094
505	Phosphorylation	VAYGCIKYADLSHNR HHHCCHHHHHCCCCC	5.85	28152594
516	Phosphorylation	SHNRLNDYIFSFDKM CCCCCHHEEEEHHHH	11.64	28152594
519	Phosphorylation	RLNDYIFSFDKMLDD CCHHEEEEHHHHHCC	23.99	21712546
522	Acetylation	DYIFSFDKMLDDRGN HEEEEHHHHHCCCCC	39.08	26822725
522	Ubiquitination	DYIFSFDKMLDDRGN HEEEEHHHHHCCCCC	39.08	21906983
522 (in isoform 1)	Ubiquitination	-	39.08	21890473
536	Phosphorylation	NTAAYLLYAFTRIRS CHHHHHHHHHHHHHH	9.32	22817900
554	Sulfoxidation	LANIDEEMLQKAARE HCCCCHHHHHHHHHH	4.52	21406390
557	2-Hydroxyisobutyrylation	IDEEMLQKAARETKI CCHHHHHHHHHHHCC	39.80	-
557	Acetylation	IDEEMLQKAARETKI CCHHHHHHHHHHHCC	39.80	27452117
557	Ubiquitination	IDEEMLQKAARETKI CCHHHHHHHHHHHCC	39.80	21963094
557 (in isoform 1)	Ubiquitination	-	39.80	21890473
563	2-Hydroxyisobutyrylation	QKAARETKILLDHEK HHHHHHHCCCCCCHH	26.97	-
563	Ubiquitination	QKAARETKILLDHEK HHHHHHHCCCCCCHH	26.97	33845483
570	Acetylation	KILLDHEKEWKLGRC CCCCCCHHHHHHHHH	66.51	23236377
570	Ubiquitination	KILLDHEKEWKLGRC CCCCCCHHHHHHHHH	66.51	29967540
573	Acetylation	LDHEKEWKLGRCILR CCCHHHHHHHHHHHH	42.00	26051181
573	Ubiquitination	LDHEKEWKLGRCILR CCCHHHHHHHHHHHH	42.00	27667366
583 (in isoform 2)	Ubiquitination	-	54.33	21890473
629	Acetylation	RQTGKILKVNMWRML CCCCCEEEHHHHHHH	34.73	25953088
638	Glutathionylation	NMWRMLLCEAVAAVM HHHHHHHHHHHHHHH	2.51	22555962
655	Ubiquitination	GFDILGIKPVQRM-- CCCCCCCCCCCCC--	37.02	23000965
655 (in isoform 1)	Ubiquitination	-	37.02	21890473

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 SYRC_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYQ_HUMAN	QARS	physical	10801842
AIMP1_HUMAN	AIMP1	physical	22863883
AIMP2_HUMAN	AIMP2	physical	22863883
ASNA_HUMAN	ASNA1	physical	22863883
DNJA1_HUMAN	DNAJA1	physical	22863883
IF2G_HUMAN	EIF2S3	physical	22863883
IF6_HUMAN	EIF6	physical	22863883
HXK1_HUMAN	HK1	physical	22863883
CCAR2_HUMAN	CCAR2	physical	22863883
SYQ_HUMAN	QARS	physical	22863883
RLA0_HUMAN	RPLP0	physical	22863883
TBB3_HUMAN	TUBB3	physical	22863883
TBB5_HUMAN	TUBB	physical	22863883
AIMP1_HUMAN	AIMP1	physical	26344197
SYDC_HUMAN	DARS	physical	26344197
MCA3_HUMAN	EEF1E1	physical	26344197
SYEP_HUMAN	EPRS	physical	26344197
SYIC_HUMAN	IARS	physical	26344197
SYK_HUMAN	KARS	physical	26344197
SYLC_HUMAN	LARS	physical	26344197
SYMC_HUMAN	MARS	physical	26344197
SYQ_HUMAN	QARS	physical	26344197
AIMP1_HUMAN	AIMP1	physical	28514442
SYLC_HUMAN	LARS	physical	28514442
SYDC_HUMAN	DARS	physical	28514442
SYTC2_HUMAN	TARSL2	physical	28514442
MCA3_HUMAN	EEF1E1	physical	28514442
SYIC_HUMAN	IARS	physical	28514442
NECT2_HUMAN	PVRL2	physical	28514442
SYEP_HUMAN	EPRS	physical	28514442
SYMC_HUMAN	MARS	physical	28514442
AIMP2_HUMAN	AIMP2	physical	28514442
NCPR_HUMAN	POR	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616140	Leukodystrophy, hypomyelinating, 9 (HLD9)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SYRC_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-38, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-60 AND LYS-205, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-38, AND MASS SPECTROMETRY.	19413330 [Abstract]