dbPTM

SYQ_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYQ_HUMAN
UniProt AC	P47897
Protein Name	Glutamine--tRNA ligase
Gene Name	QARS
Organism	Homo sapiens (Human).
Sequence Length	775
Subcellular Localization	Cytoplasm, cytosol . Cytoplasm .
Protein Description	Glutamine--tRNA ligase. [PubMed: 26869582 Plays a critical role in brain development]
Protein Sequence	MAALDSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLGSTIDKATGILLYGLASRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPEQIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGPKLEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKTPGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQRGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKMDPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQVPNFPADETKGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVESLEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLFQHKNPEDPTEVPGGFLSDLNLASLHVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGKLVFNRTVTLKEDPGKV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAALDSLSL ------CCHHHHHHH	19.41	22223895
6	Phosphorylation	--MAALDSLSLFTSL --CCHHHHHHHHHHC	22.25	20068231
8	Phosphorylation	MAALDSLSLFTSLGL CCHHHHHHHHHHCCC	25.95	28348404
11	Phosphorylation	LDSLSLFTSLGLSEQ HHHHHHHHHCCCCHH	28.47	20068231
12	Phosphorylation	DSLSLFTSLGLSEQK HHHHHHHHCCCCHHH	17.07	28348404
16	Phosphorylation	LFTSLGLSEQKARET HHHHCCCCHHHHHHH	35.86	20068231
23	Phosphorylation	SEQKARETLKNSALS CHHHHHHHHHHHHHH	37.16	26552605
25	Ubiquitination	QKARETLKNSALSAQ HHHHHHHHHHHHHHH	57.17	21906983
25	Malonylation	QKARETLKNSALSAQ HHHHHHHHHHHHHHH	57.17	26320211
25	Ubiquitination	QKARETLKNSALSAQ HHHHHHHHHHHHHHH	57.17	-
27	Phosphorylation	ARETLKNSALSAQLR HHHHHHHHHHHHHHH	29.06	23911959
30	Phosphorylation	TLKNSALSAQLREAA HHHHHHHHHHHHHHH	17.43	23312004
43	Phosphorylation	AATQAQQTLGSTIDK HHHHHHHHHHHHHHH	22.47	29255136
46	Phosphorylation	QAQQTLGSTIDKATG HHHHHHHHHHHHHHH	25.88	29255136
47	Phosphorylation	AQQTLGSTIDKATGI HHHHHHHHHHHHHHH	31.25	29255136
50	Ubiquitination	TLGSTIDKATGILLY HHHHHHHHHHHHHHH	43.95	-
57	Phosphorylation	KATGILLYGLASRLR HHHHHHHHHHHHCCC	13.47	28152594
61	Phosphorylation	ILLYGLASRLRDTRR HHHHHHHHCCCHHHH	36.57	28152594
66	Phosphorylation	LASRLRDTRRLSFLV HHHCCCHHHHHHHHH	15.97	29083192
70	Phosphorylation	LRDTRRLSFLVSYIA CCHHHHHHHHHHHHH	18.09	22617229
74	Phosphorylation	RRLSFLVSYIASKKI HHHHHHHHHHHCCCC	16.99	30108239
74 (in isoform 2)	Phosphorylation	-	16.99	28122231
75	Phosphorylation	RLSFLVSYIASKKIH HHHHHHHHHHCCCCC	7.94	27282143
75 (in isoform 2)	Phosphorylation	-	7.94	28122231
78	Phosphorylation	FLVSYIASKKIHTEP HHHHHHHCCCCCCCH	25.56	23312004
78 (in isoform 2)	Phosphorylation	-	25.56	28122231
80	2-Hydroxyisobutyrylation	VSYIASKKIHTEPQL HHHHHCCCCCCCHHH	36.91	-
82 (in isoform 2)	Phosphorylation	-	32.81	28122231
88	Phosphorylation	IHTEPQLSAALEYVR CCCCHHHHHHHHHHH	13.27	-
93	Phosphorylation	QLSAALEYVRSHPLD HHHHHHHHHHHCCCC	11.30	-
142	Phosphorylation	PQLLVERYHFNMGLL HHHEEEEEECCHHHH	9.39	28258704
155	Ubiquitination	LLMGEARAVLKWADG HHHHHHHHHHHHCCC	20.31	-
158	Acetylation	GEARAVLKWADGKMI HHHHHHHHHCCCCCC	33.46	26051181
163	Ubiquitination	VLKWADGKMIKNEVD HHHHCCCCCCCCCCH	37.69	-
166	Ubiquitination	WADGKMIKNEVDMQV HCCCCCCCCCCHHHH	43.48	-
171	Sulfoxidation	MIKNEVDMQVLHLLG CCCCCCHHHHHHHHC	3.42	21406390
176	Ubiquitination	VDMQVLHLLGPKLEA CHHHHHHHHCHHHHH	5.31	-
180	Ubiquitination	VLHLLGPKLEADLEK HHHHHCHHHHHHHHH	58.10	-
187	2-Hydroxyisobutyrylation	KLEADLEKKFKVAKA HHHHHHHHHHHHHHH	71.46	-
187	Ubiquitination	KLEADLEKKFKVAKA HHHHHHHHHHHHHHH	71.46	-
194	Ubiquitination	KKFKVAKARLEETDR HHHHHHHHHHHHHCC	16.14	-
201	Methylation	ARLEETDRRTAKDVV HHHHHHCCCCHHHHH	45.31	115489755
205	Ubiquitination	ETDRRTAKDVVENGE HHCCCCHHHHHHCCC	50.90	21906983
213	Phosphorylation	DVVENGETADQTLSL HHHHCCCCHHHHHHH	36.61	28555341
217	Phosphorylation	NGETADQTLSLMEQL CCCCHHHHHHHHHHH	20.89	28555341
222	Ubiquitination	DQTLSLMEQLRGEAL HHHHHHHHHHCCHHH	52.32	-
225	Methylation	LSLMEQLRGEALKFH HHHHHHHCCHHHHCC	40.37	115489763
228	Ubiquitination	MEQLRGEALKFHKPG HHHHCCHHHHCCCCC	20.90	-
230	Ubiquitination	QLRGEALKFHKPGEN HHCCHHHHCCCCCCC	53.09	-
233	Ubiquitination	GEALKFHKPGENYKT CHHHHCCCCCCCCCC	58.83	-
239	Ubiquitination	HKPGENYKTPGYVVT CCCCCCCCCCCEEEC	60.88	-
240	Phosphorylation	KPGENYKTPGYVVTP CCCCCCCCCCEEECH	16.16	23312004
243	Ubiquitination	ENYKTPGYVVTPHTM CCCCCCCEEECHHHH	7.92	-
243	Phosphorylation	ENYKTPGYVVTPHTM CCCCCCCEEECHHHH	7.92	23312004
246	Phosphorylation	KTPGYVVTPHTMNLL CCCCEEECHHHHHHH	10.18	23312004
249	Phosphorylation	GYVVTPHTMNLLKQH CEEECHHHHHHHHHH	14.68	23312004
254	Methylation	PHTMNLLKQHLEITG HHHHHHHHHHHEECC	38.55	54411627
254	Ubiquitination	PHTMNLLKQHLEITG HHHHHHHHHHHEECC	38.55	-
281	Ubiquitination	GILHIGHAKAINFNF CEEEEEECEEEEEEC	9.58	-
290	Phosphorylation	AINFNFGYAKANNGI EEEEECEEEECCCCE	10.78	28152594
292	Ubiquitination	NFNFGYAKANNGICF EEECEEEECCCCEEE	43.07	-
309	Acetylation	FDDTNPEKEEAKFFT ECCCCHHHHHHHHHH	63.21	19608861
355	Acetylation	ELIRRGLAYVCHQRG HHHHHHHHHHHHHCC	9.50	-
355	Ubiquitination	ELIRRGLAYVCHQRG HHHHHHHHHHHHHCC	9.50	-
366	Acetylation	HQRGEELKGHNTLPS HHCCCCCCCCCCCCC	62.49	23236377
366	Malonylation	HQRGEELKGHNTLPS HHCCCCCCCCCCCCC	62.49	26320211
366	Ubiquitination	HQRGEELKGHNTLPS HHCCCCCCCCCCCCC	62.49	21906983
370	Phosphorylation	EELKGHNTLPSPWRD CCCCCCCCCCCCCCC	34.08	20873877
373	Phosphorylation	KGHNTLPSPWRDRPM CCCCCCCCCCCCCCH	39.96	20873877
381	Ubiquitination	PWRDRPMEESLLLFE CCCCCCHHHHHHHHH	47.30	-
383	Ubiquitination	RDRPMEESLLLFEAM CCCCHHHHHHHHHHH	15.83	-
392	Ubiquitination	LLFEAMRKGKFSEGE HHHHHHHCCCCCCCC	54.06	-
394	Ubiquitination	FEAMRKGKFSEGEAT HHHHHCCCCCCCCCE	49.07	-
394	2-Hydroxyisobutyrylation	FEAMRKGKFSEGEAT HHHHHCCCCCCCCCE	49.07	-
394	Acetylation	FEAMRKGKFSEGEAT HHHHHCCCCCCCCCE	49.07	25953088
394	Ubiquitination	FEAMRKGKFSEGEAT HHHHHCCCCCCCCCE	49.07	21906983
401	Acetylation	KFSEGEATLRMKLVM CCCCCCCEEEEEEEE	15.59	-
401	Ubiquitination	KFSEGEATLRMKLVM CCCCCCCEEEEEEEE	15.59	-
405	Ubiquitination	GEATLRMKLVMEDGK CCCEEEEEEEEECCC	31.34	-
412	2-Hydroxyisobutyrylation	KLVMEDGKMDPVAYR EEEEECCCCCCEEEE	53.07	-
412	Acetylation	KLVMEDGKMDPVAYR EEEEECCCCCCEEEE	53.07	23954790
412	Malonylation	KLVMEDGKMDPVAYR EEEEECCCCCCEEEE	53.07	26320211
412	Ubiquitination	KLVMEDGKMDPVAYR EEEEECCCCCCEEEE	53.07	21906983
420	Ubiquitination	MDPVAYRVKYTPHHR CCCEEEEEEECCCCC	3.46	-
421	Acetylation	DPVAYRVKYTPHHRT CCEEEEEEECCCCCC	34.11	25953088
421	Ubiquitination	DPVAYRVKYTPHHRT CCEEEEEEECCCCCC	34.11	-
431	Ubiquitination	PHHRTGDKWCIYPTY CCCCCCCEEEECCCC	45.36	-
447	Ubiquitination	YTHCLCDSIEHITHS CCHHHHHHHHHHCHH	28.95	-
477	Phosphorylation	LCNALDVYCPVQWEY HHHHHCEECCEEEEE	7.24	22817900
484	Phosphorylation	YCPVQWEYGRLNLHY ECCEEEEECCEEEEE	12.46	22817900
485	Ubiquitination	CPVQWEYGRLNLHYA CCEEEEECCEEEEEE	18.98	-
491	Phosphorylation	YGRLNLHYAVVSKRK ECCEEEEEEEEEHHH	12.31	21082442
495	Phosphorylation	NLHYAVVSKRKILQL EEEEEEEEHHHHHHH	21.83	28152594
496	2-Hydroxyisobutyrylation	LHYAVVSKRKILQLV EEEEEEEHHHHHHHH	46.21	-
496	Acetylation	LHYAVVSKRKILQLV EEEEEEEHHHHHHHH	46.21	26051181
496	Ubiquitination	LHYAVVSKRKILQLV EEEEEEEHHHHHHHH	46.21	-
498	Acetylation	YAVVSKRKILQLVAT EEEEEHHHHHHHHHH	52.05	30585951
498	Malonylation	YAVVSKRKILQLVAT EEEEEHHHHHHHHHH	52.05	26320211
505	Phosphorylation	KILQLVATGAVRDWD HHHHHHHHCCCCCCC	20.42	20068231
518	Phosphorylation	WDDPRLFTLTALRRR CCCCHHHHHHHHHHC	27.99	22210691
520	Phosphorylation	DPRLFTLTALRRRGF CCHHHHHHHHHHCCC	22.16	20873877
556	Glutathionylation	EPHLLEACVRDVLND CHHHHHHHHHHHHCC	1.56	22555962
564	Phosphorylation	VRDVLNDTAPRAMAV HHHHHCCCHHHHHHH	37.17	20071362
569	Sulfoxidation	NDTAPRAMAVLESLR CCCHHHHHHHHHHCH	2.53	21406390
575	Acetylation	AMAVLESLRVIITNF HHHHHHHCHHHCCCC	3.56	-
575	Ubiquitination	AMAVLESLRVIITNF HHHHHHHCHHHCCCC	3.56	-
586	Acetylation	ITNFPAAKSLDIQVP CCCCCCCCCCCEECC	54.37	23236377
586	Ubiquitination	ITNFPAAKSLDIQVP CCCCCCCCCCCEECC	54.37	21906983
590	Ubiquitination	PAAKSLDIQVPNFPA CCCCCCCEECCCCCC	5.58	-
601	Ubiquitination	NFPADETKGFHQVPF CCCCCCCCCCCCCCC	58.49	-
609	Acetylation	GFHQVPFAPIVFIER CCCCCCCCCEEEEEC	6.19	-
609	Ubiquitination	GFHQVPFAPIVFIER CCCCCCCCCEEEEEC	6.19	-
617	Acetylation	PIVFIERTDFKEEPE CEEEEECCCCCCCCC	32.76	-
617	Ubiquitination	PIVFIERTDFKEEPE CEEEEECCCCCCCCC	32.76	-
620	Acetylation	FIERTDFKEEPEPGF EEECCCCCCCCCCCC	65.07	23954790
620	Malonylation	FIERTDFKEEPEPGF EEECCCCCCCCCCCC	65.07	26320211
620	Ubiquitination	FIERTDFKEEPEPGF EEECCCCCCCCCCCC	65.07	21906983
628	Acetylation	EEPEPGFKRLAWGQP CCCCCCCEECCCCCC	53.03	23749302
628	Malonylation	EEPEPGFKRLAWGQP CCCCCCCEECCCCCC	53.03	26320211
628	Methylation	EEPEPGFKRLAWGQP CCCCCCCEECCCCCC	53.03	11924111
628	Ubiquitination	EEPEPGFKRLAWGQP CCCCCCCEECCCCCC	53.03	-
641	Ubiquitination	QPVGLRHTGYVIELQ CCCCCCCCEEEEEEE	24.63	-
657	Glutathionylation	VVKGPSGCVESLEVT EEECCCCCEEEEEEE	3.44	22555962
673	Ubiquitination	RRADAGEKPKAFIHW ECCCCCCCCCEEEHH	51.40	-
687	Glutathionylation	WVSQPLMCEVRLYER HHCCCHHHHHHHHHH	6.03	22555962
740	2-Hydroxyisobutyrylation	ALAKPFDKFQFERLG HCCCCCCCCCCEECC	41.25	-
740	Acetylation	ALAKPFDKFQFERLG HCCCCCCCCCCEECC	41.25	27452117
740	Ubiquitination	ALAKPFDKFQFERLG HCCCCCCCCCCEECC	41.25	-
748	Ubiquitination	FQFERLGYFSVDPDS CCCEECCCEEECCCC	9.40	-
748	Phosphorylation	FQFERLGYFSVDPDS CCCEECCCEEECCCC	9.40	28152594
758	Acetylation	VDPDSHQGKLVFNRT ECCCCCCCEEEEEEE	21.60	-
758	Ubiquitination	VDPDSHQGKLVFNRT ECCCCCCCEEEEEEE	21.60	-
759	Acetylation	DPDSHQGKLVFNRTV CCCCCCCEEEEEEEE	34.60	25953088
759	Ubiquitination	DPDSHQGKLVFNRTV CCCCCCCEEEEEEEE	34.60	-
763	Ubiquitination	HQGKLVFNRTVTLKE CCCEEEEEEEEEECC	31.10	-
765	Phosphorylation	GKLVFNRTVTLKEDP CEEEEEEEEEECCCC	20.96	29514088
767	Phosphorylation	LVFNRTVTLKEDPGK EEEEEEEEECCCCCC	31.34	29514088
769	Acetylation	FNRTVTLKEDPGKV- EEEEEEECCCCCCC-	51.19	23749302
769	Malonylation	FNRTVTLKEDPGKV- EEEEEEECCCCCCC-	51.19	26320211
769	Ubiquitination	FNRTVTLKEDPGKV- EEEEEEECCCCCCC-	51.19	2190698
774	Ubiquitination	TLKEDPGKV------ EECCCCCCC------	50.59	-

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 SYQ_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRAF2_HUMAN	TRAF2	physical	16189514
A4_HUMAN	APP	physical	21832049
SYRC_HUMAN	RARS	physical	22939629
UBA1_HUMAN	UBA1	physical	22939629
TRM1_HUMAN	TRMT1	physical	22939629
TXLNA_HUMAN	TXLNA	physical	22939629
ZFR_HUMAN	ZFR	physical	22939629
RNF11_HUMAN	RNF11	physical	21988832
AIMP1_HUMAN	AIMP1	physical	22863883
AIMP2_HUMAN	AIMP2	physical	22863883
IF2G_HUMAN	EIF2S3	physical	22863883
ROA1_HUMAN	HNRNPA1	physical	22863883
ROA2_HUMAN	HNRNPA2B1	physical	22863883
SYIC_HUMAN	IARS	physical	22863883
IF2B3_HUMAN	IGF2BP3	physical	22863883
IQGA1_HUMAN	IQGAP1	physical	22863883
CCAR2_HUMAN	CCAR2	physical	22863883
SYMC_HUMAN	MARS	physical	22863883
MRE11_HUMAN	MRE11A	physical	22863883
NMT1_HUMAN	NMT1	physical	22863883
PRS10_HUMAN	PSMC6	physical	22863883
PTBP1_HUMAN	PTBP1	physical	22863883
TBB2A_HUMAN	TUBB2A	physical	22863883
SYVC_HUMAN	VARS	physical	22863883
HTF4_HUMAN	TCF12	physical	25416956
PCH2_HUMAN	TRIP13	physical	25416956
TRAF4_HUMAN	TRAF4	physical	25416956
VP37B_HUMAN	VPS37B	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
DTX2_HUMAN	DTX2	physical	25416956
KLC3_HUMAN	KLC3	physical	25416956
MCA3_HUMAN	EEF1E1	physical	26344197
SYEP_HUMAN	EPRS	physical	26344197
PLEC_HUMAN	PLEC	physical	26344197
TRM6_HUMAN	TRMT6	physical	26344197
SYRC_HUMAN	RARS	physical	28514442
MCA3_HUMAN	EEF1E1	physical	28514442
AIMP2_HUMAN	AIMP2	physical	28514442
AIMP1_HUMAN	AIMP1	physical	28514442
SYDC_HUMAN	DARS	physical	28514442
SYLC_HUMAN	LARS	physical	28514442
SYEP_HUMAN	EPRS	physical	28514442
SYIC_HUMAN	IARS	physical	28514442
SYMC_HUMAN	MARS	physical	28514442
OFD1_HUMAN	OFD1	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615760	Microcephaly, progressive, with seizures and cerebral and cerebellar atrophy (MSCCA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00130	L-Glutamine

Regulatory Network of SYQ_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 ALA-2, 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-309 AND LYS-620, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-491, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-491, AND MASSSPECTROMETRY.	15592455 [Abstract]