dbPTM

SYAC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYAC_HUMAN
UniProt AC	P49588
Protein Name	Alanine--tRNA ligase, cytoplasmic {ECO:0000255\|HAMAP-Rule:MF_03133}
Gene Name	AARS {ECO:0000255\|HAMAP-Rule:MF_03133}
Organism	Homo sapiens (Human).
Sequence Length	968
Subcellular Localization	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). [PubMed: 28493438 Also edits incorrectly charged tRNA(Ala) via its editing domain]
Protein Sequence	MDSTLTASEIRQRFIDFFKRNEHTYVHSSATIPLDDPTLLFANAGMNQFKPIFLNTIDPSHPMAKLSRAANTQKCIRAGGKHNDLDDVGKDVYHHTFFEMLGSWSFGDYFKELACKMALELLTQEFGIPIERLYVTYFGGDEAAGLEADLECKQIWQNLGLDDTKILPGNMKDNFWEMGDTGPCGPCSEIHYDRIGGRDAAHLVNQDDPNVLEIWNLVFIQYNREADGILKPLPKKSIDTGMGLERLVSVLQNKMSNYDTDLFVPYFEAIQKGTGARPYTGKVGAEDADGIDMAYRVLADHARTITVALADGGRPDNTGRGYVLRRILRRAVRYAHEKLNASRGFFATLVDVVVQSLGDAFPELKKDPDMVKDIINEEEVQFLKTLSRGRRILDRKIQSLGDSKTIPGDTAWLLYDTYGFPVDLTGLIAEEKGLVVDMDGFEEERKLAQLKSQGKGAGGEDLIMLDIYAIEELRARGLEVTDDSPKYNYHLDSSGSYVFENTVATVMALRREKMFVEEVSTGQECGVVLDKTCFYAEQGGQIYDEGYLVKVDDSSEDKTEFTVKNAQVRGGYVLHIGTIYGDLKVGDQVWLFIDEPRRRPIMSNHTATHILNFALRSVLGEADQKGSLVAPDRLRFDFTAKGAMSTQQIKKAEEIANEMIEAAKAVYTQDCPLAAAKAIQGLRAVFDETYPDPVRVVSIGVPVSELLDDPSGPAGSLTSVEFCGGTHLRNSSHAGAFVIVTEEAIAKGIRRIVAVTGAEAQKALRKAESLKKCLSVMEAKVKAQTAPNKDVQREIADLGEALATAVIPQWQKDELRETLKSLKKVMDDLDRASKADVQKRVLEKTKQFIDSNPNQPLVILEMESGASAKALNEALKLFKMHSPQTSAMLFTVDNEAGKITCLCQVPQNAANRGLKASEWVQQVSGLMDGKGGGKDVSAQATGKNVGCLQEALQLATSFAQLRLGDVKN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDSTLTAS -------CCCCCCHH	9.18	22223895
1	Sulfoxidation	-------MDSTLTAS -------CCCCCCHH	9.18	21406390
3	Phosphorylation	-----MDSTLTASEI -----CCCCCCHHHH	24.82	20068231
4	Phosphorylation	----MDSTLTASEIR ----CCCCCCHHHHH	24.70	20068231
6	Phosphorylation	--MDSTLTASEIRQR --CCCCCCHHHHHHH	28.38	20068231
8	Phosphorylation	MDSTLTASEIRQRFI CCCCCCHHHHHHHHH	28.46	20068231
19	Acetylation	QRFIDFFKRNEHTYV HHHHHHHHHCCCEEE	55.07	19608861
19	Ubiquitination	QRFIDFFKRNEHTYV HHHHHHHHHCCCEEE	55.07	23000965
19	2-Hydroxyisobutyrylation	QRFIDFFKRNEHTYV HHHHHHHHHCCCEEE	55.07	-
19	Malonylation	QRFIDFFKRNEHTYV HHHHHHHHHCCCEEE	55.07	26320211
19	Ubiquitination	QRFIDFFKRNEHTYV HHHHHHHHHCCCEEE	55.07	21890473
50	Ubiquitination	NAGMNQFKPIFLNTI CCCCCCCCCEECCCC	27.69	29967540
56	Phosphorylation	FKPIFLNTIDPSHPM CCCEECCCCCCCCHH	28.98	20068231
60	Phosphorylation	FLNTIDPSHPMAKLS ECCCCCCCCHHHHHH	36.15	20068231
67	Phosphorylation	SHPMAKLSRAANTQK CCHHHHHHHHHHHHH	21.11	20068231
74	Ubiquitination	SRAANTQKCIRAGGK HHHHHHHHHHHCCCC	29.59	24816145
74	2-Hydroxyisobutyrylation	SRAANTQKCIRAGGK HHHHHHHHHHHCCCC	29.59	-
81	Acetylation	KCIRAGGKHNDLDDV HHHHCCCCCCCHHHC	38.01	7306885
81	Ubiquitination	KCIRAGGKHNDLDDV HHHHCCCCCCCHHHC	38.01	21906983
117	Sulfoxidation	FKELACKMALELLTQ HHHHHHHHHHHHHHH	5.31	28183972
178	Sulfoxidation	MKDNFWEMGDTGPCG CCCCCCCCCCCCCCC	4.25	30846556
192	Phosphorylation	GPCSEIHYDRIGGRD CCCCHHCCCCCCCCC	16.75	25147952
198	Methylation	HYDRIGGRDAAHLVN CCCCCCCCCHHHHCC	25.78	-
231	Ubiquitination	READGILKPLPKKSI HHCCCCCCCCCCCCC	42.46	33845483
231	Acetylation	READGILKPLPKKSI HHCCCCCCCCCCCCC	42.46	23236377
231	Succinylation	READGILKPLPKKSI HHCCCCCCCCCCCCC	42.46	23954790
235	2-Hydroxyisobutyrylation	GILKPLPKKSIDTGM CCCCCCCCCCCCCCC	67.83	-
236	Ubiquitination	ILKPLPKKSIDTGMG CCCCCCCCCCCCCCC	51.18	24816145
236	2-Hydroxyisobutyrylation	ILKPLPKKSIDTGMG CCCCCCCCCCCCCCC	51.18	-
237	Phosphorylation	LKPLPKKSIDTGMGL CCCCCCCCCCCCCCH	31.64	21406692
240	Phosphorylation	LPKKSIDTGMGLERL CCCCCCCCCCCHHHH	27.65	20068231
242	Sulfoxidation	KKSIDTGMGLERLVS CCCCCCCCCHHHHHH	6.34	21406390
249	Phosphorylation	MGLERLVSVLQNKMS CCHHHHHHHHHHHCC	23.00	20873877
254	Ubiquitination	LVSVLQNKMSNYDTD HHHHHHHHCCCCCCC	30.64	29967540
255	Sulfoxidation	VSVLQNKMSNYDTDL HHHHHHHCCCCCCCC	4.05	30846556
272	Ubiquitination	PYFEAIQKGTGARPY HHHHHHHCCCCCCCC	52.94	29967540
282	Ubiquitination	GARPYTGKVGAEDAD CCCCCCCCCCCCCCC	29.69	24816145
293	Sulfoxidation	EDADGIDMAYRVLAD CCCCCCCHHHHHHHH	3.14	30846556
304	Phosphorylation	VLADHARTITVALAD HHHHHCCEEEEEECC	23.06	28857561
306	Phosphorylation	ADHARTITVALADGG HHHCCEEEEEECCCC	10.10	28857561
320	Methylation	GRPDNTGRGYVLRRI CCCCCCCHHHHHHHH	31.09	-
322	Phosphorylation	PDNTGRGYVLRRILR CCCCCHHHHHHHHHH	8.58	68712887
338	Ubiquitination	AVRYAHEKLNASRGF HHHHHHHHHHCCCCH	36.85	24816145
338	2-Hydroxyisobutyrylation	AVRYAHEKLNASRGF HHHHHHHHHHCCCCH	36.85	-
338	Acetylation	AVRYAHEKLNASRGF HHHHHHHHHHCCCCH	36.85	27452117
356	Phosphorylation	LVDVVVQSLGDAFPE HHHHHHHHHHHHCHH	23.78	22210691
366	Acetylation	DAFPELKKDPDMVKD HHCHHHHCCHHHHHH	83.53	23749302
366	Ubiquitination	DAFPELKKDPDMVKD HHCHHHHCCHHHHHH	83.53	-
372	Ubiquitination	KKDPDMVKDIINEEE HCCHHHHHHHCCHHH	36.25	-
384	Ubiquitination	EEEVQFLKTLSRGRR HHHHHHHHHHHHHHH	49.02	23000965
384	Acetylation	EEEVQFLKTLSRGRR HHHHHHHHHHHHHHH	49.02	27452117
392	Ubiquitination	TLSRGRRILDRKIQS HHHHHHHHHHHHHHH	4.52	21890473
396	Ubiquitination	GRRILDRKIQSLGDS HHHHHHHHHHHCCCC	44.77	29967540
396	2-Hydroxyisobutyrylation	GRRILDRKIQSLGDS HHHHHHHHHHHCCCC	44.77	-
399	Phosphorylation	ILDRKIQSLGDSKTI HHHHHHHHCCCCCCC	37.48	25159151
403	Phosphorylation	KIQSLGDSKTIPGDT HHHHCCCCCCCCCCC	29.87	21815630
405	Phosphorylation	QSLGDSKTIPGDTAW HHCCCCCCCCCCCEE	36.03	22210691
410	Phosphorylation	SKTIPGDTAWLLYDT CCCCCCCCEEEEEEC	26.16	22210691
415	Phosphorylation	GDTAWLLYDTYGFPV CCCEEEEEECCCCCC	12.22	22210691
425	Phosphorylation	YGFPVDLTGLIAEEK CCCCCCHHHHHHCCC	26.02	22210691
438	Sulfoxidation	EKGLVVDMDGFEEER CCCEEECCCCHHHHH	3.52	21406390
451	Ubiquitination	ERKLAQLKSQGKGAG HHHHHHHHHCCCCCC	28.75	27667366
468	Phosphorylation	DLIMLDIYAIEELRA CEEEEEEEHHHHHHH	10.95	27642862
481	Phosphorylation	RARGLEVTDDSPKYN HHCCCCCCCCCCCCE	25.39	29255136
484	Phosphorylation	GLEVTDDSPKYNYHL CCCCCCCCCCCEEEE	26.54	29255136
486	Ubiquitination	EVTDDSPKYNYHLDS CCCCCCCCCEEEECC	50.51	-
487	Phosphorylation	VTDDSPKYNYHLDSS CCCCCCCCEEEECCC	25.08	29449344
489	Phosphorylation	DDSPKYNYHLDSSGS CCCCCCEEEECCCCC	10.73	29449344
493	Phosphorylation	KYNYHLDSSGSYVFE CCEEEECCCCCEEEE	42.85	29449344
494	Phosphorylation	YNYHLDSSGSYVFEN CEEEECCCCCEEEEC	31.27	29449344
496	Phosphorylation	YHLDSSGSYVFENTV EEECCCCCEEEECHH	21.77	29449344
497	Phosphorylation	HLDSSGSYVFENTVA EECCCCCEEEECHHH	16.81	29449344
502	Phosphorylation	GSYVFENTVATVMAL CCEEEECHHHHHHHH	12.34	29449344
505	Phosphorylation	VFENTVATVMALRRE EEECHHHHHHHHHHH	13.38	29449344
513	Ubiquitination	VMALRREKMFVEEVS HHHHHHHHCEEEECC	35.51	-
514	Sulfoxidation	MALRREKMFVEEVST HHHHHHHCEEEECCC	3.79	30846556
532	Phosphorylation	CGVVLDKTCFYAEQG EEEEEECEEEEEECC	13.91	24260401
535	Phosphorylation	VLDKTCFYAEQGGQI EEECEEEEEECCCEE	16.04	24260401
543	Phosphorylation	AEQGGQIYDEGYLVK EECCCEEEEEEEEEE	10.47	28796482
547	Phosphorylation	GQIYDEGYLVKVDDS CEEEEEEEEEECCCC	13.28	28060719
554	Phosphorylation	YLVKVDDSSEDKTEF EEEECCCCCCCCCEE	31.03	23401153
555	Phosphorylation	LVKVDDSSEDKTEFT EEECCCCCCCCCEEE	57.73	29255136
558	Ubiquitination	VDDSSEDKTEFTVKN CCCCCCCCCEEEEEC	46.00	30230243
558	Acetylation	VDDSSEDKTEFTVKN CCCCCCCCCEEEEEC	46.00	23236377
559	Phosphorylation	DDSSEDKTEFTVKNA CCCCCCCCEEEEECC	48.96	30108239
562	Phosphorylation	SEDKTEFTVKNAQVR CCCCCEEEEECCEEE	25.08	30108239
564	Ubiquitination	DKTEFTVKNAQVRGG CCCEEEEECCEEECC	43.43	21906983
569	Methylation	TVKNAQVRGGYVLHI EEECCEEECCEEEEE	22.27	-
572	Phosphorylation	NAQVRGGYVLHIGTI CCEEECCEEEEEEEE	11.58	28152594
578	Phosphorylation	GYVLHIGTIYGDLKV CEEEEEEEEECCEEC	15.49	28152594
580	Phosphorylation	VLHIGTIYGDLKVGD EEEEEEEECCEECCC	12.39	28152594
603	Phosphorylation	PRRRPIMSNHTATHI CCCCCCCCCCHHHHH	26.61	30257219
606	Phosphorylation	RPIMSNHTATHILNF CCCCCCCHHHHHHHH	37.19	20068231
608	Phosphorylation	IMSNHTATHILNFAL CCCCCHHHHHHHHHH	15.59	30257219
625	Ubiquitination	VLGEADQKGSLVAPD HHCCCCCCCCCCCCC	51.52	22817900
625	2-Hydroxyisobutyrylation	VLGEADQKGSLVAPD HHCCCCCCCCCCCCC	51.52	-
625	Malonylation	VLGEADQKGSLVAPD HHCCCCCCCCCCCCC	51.52	26320211
625	Acetylation	VLGEADQKGSLVAPD HHCCCCCCCCCCCCC	51.52	26051181
627	Phosphorylation	GEADQKGSLVAPDRL CCCCCCCCCCCCCEE	27.06	28188228
633	Methylation	GSLVAPDRLRFDFTA CCCCCCCEEECCEEC	27.06	-
635	Methylation	LVAPDRLRFDFTAKG CCCCCEEECCEECCC	29.95	-
641	Ubiquitination	LRFDFTAKGAMSTQQ EECCEECCCCCCHHH	44.11	29967540
644	Sulfoxidation	DFTAKGAMSTQQIKK CEECCCCCCHHHHHH	6.41	30846556
650	Ubiquitination	AMSTQQIKKAEEIAN CCCHHHHHHHHHHHH	41.41	27667366
650	2-Hydroxyisobutyrylation	AMSTQQIKKAEEIAN CCCHHHHHHHHHHHH	41.41	-
651	Ubiquitination	MSTQQIKKAEEIANE CCHHHHHHHHHHHHH	63.76	29967540
659	Sulfoxidation	AEEIANEMIEAAKAV HHHHHHHHHHHHHHH	3.17	21406390
664	Ubiquitination	NEMIEAAKAVYTQDC HHHHHHHHHHHCCCC	45.49	29967540
667	Phosphorylation	IEAAKAVYTQDCPLA HHHHHHHHCCCCHHH	11.98	28796482
668	Phosphorylation	EAAKAVYTQDCPLAA HHHHHHHCCCCHHHH	16.01	28152594
671	Glutathionylation	KAVYTQDCPLAAAKA HHHHCCCCHHHHHHH	1.82	22555962
677	Ubiquitination	DCPLAAAKAIQGLRA CCHHHHHHHHHHHHH	41.10	21906983
677	2-Hydroxyisobutyrylation	DCPLAAAKAIQGLRA CCHHHHHHHHHHHHH	41.10	-
677	Acetylation	DCPLAAAKAIQGLRA CCHHHHHHHHHHHHH	41.10	25953088
683	Methylation	AKAIQGLRAVFDETY HHHHHHHHHHHCCCC	35.21	-
685	Ubiquitination	AIQGLRAVFDETYPD HHHHHHHHHCCCCCC	5.13	21890473
689	Phosphorylation	LRAVFDETYPDPVRV HHHHHCCCCCCCCEE	42.05	28152594
690	Phosphorylation	RAVFDETYPDPVRVV HHHHCCCCCCCCEEE	12.00	28152594
690	Nitration	RAVFDETYPDPVRVV HHHHCCCCCCCCEEE	12.00	-
747	Ubiquitination	VTEEAIAKGIRRIVA ECHHHHHCCCHHHHH	49.08	21906983
762	Ubiquitination	VTGAEAQKALRKAES HCCHHHHHHHHHHHH	57.34	23000965
762	2-Hydroxyisobutyrylation	VTGAEAQKALRKAES HCCHHHHHHHHHHHH	57.34	-
762	Acetylation	VTGAEAQKALRKAES HCCHHHHHHHHHHHH	57.34	25953088
766	Ubiquitination	EAQKALRKAESLKKC HHHHHHHHHHHHHHH	58.31	23000965
771	2-Hydroxyisobutyrylation	LRKAESLKKCLSVME HHHHHHHHHHHHHHH	51.20	-
772	Ubiquitination	RKAESLKKCLSVMEA HHHHHHHHHHHHHHH	45.78	24816145
775	Phosphorylation	ESLKKCLSVMEAKVK HHHHHHHHHHHHHHH	28.96	28348404
777	Sulfoxidation	LKKCLSVMEAKVKAQ HHHHHHHHHHHHHHC	3.58	30846556
780	Ubiquitination	CLSVMEAKVKAQTAP HHHHHHHHHHHCCCC	30.84	29967540
780	Acetylation	CLSVMEAKVKAQTAP HHHHHHHHHHHCCCC	30.84	25953088
782	Ubiquitination	SVMEAKVKAQTAPNK HHHHHHHHHCCCCCH	33.79	27667366
785	Phosphorylation	EAKVKAQTAPNKDVQ HHHHHHCCCCCHHHH	49.28	24300666
789	Ubiquitination	KAQTAPNKDVQREIA HHCCCCCHHHHHHHH	59.21	30230243
789	Acetylation	KAQTAPNKDVQREIA HHCCCCCHHHHHHHH	59.21	27452117
804	Phosphorylation	DLGEALATAVIPQWQ HHHHHHHHHHCCHHC	23.47	110745699
812	Ubiquitination	AVIPQWQKDELRETL HHCCHHCHHHHHHHH	50.65	29967540
820	Ubiquitination	DELRETLKSLKKVMD HHHHHHHHHHHHHHH	62.25	27667366
820	Neddylation	DELRETLKSLKKVMD HHHHHHHHHHHHHHH	62.25	32015554
823	Ubiquitination	RETLKSLKKVMDDLD HHHHHHHHHHHHHHH	50.87	22817900
824	Ubiquitination	ETLKSLKKVMDDLDR HHHHHHHHHHHHHHH	48.35	22817900
826	Sulfoxidation	LKSLKKVMDDLDRAS HHHHHHHHHHHHHHH	4.57	30846556
828	Ubiquitination	SLKKVMDDLDRASKA HHHHHHHHHHHHHHH	32.16	21890473
839	Ubiquitination	ASKADVQKRVLEKTK HHHHHHHHHHHHHHH	44.30	24816145
844	Ubiquitination	VQKRVLEKTKQFIDS HHHHHHHHHHHHHHC	57.78	27667366
846	Ubiquitination	KRVLEKTKQFIDSNP HHHHHHHHHHHHCCC	55.04	23503661
854	Ubiquitination	QFIDSNPNQPLVILE HHHHCCCCCCEEEEE	61.42	-
869	Ubiquitination	MESGASAKALNEALK ECCCCCHHHHHHHHH	51.41	32015554
876	Acetylation	KALNEALKLFKMHSP HHHHHHHHHHHHCCC	59.95	19608861
876	Ubiquitination	KALNEALKLFKMHSP HHHHHHHHHHHHCCC	59.95	23000965
876	Malonylation	KALNEALKLFKMHSP HHHHHHHHHHHHCCC	59.95	26320211
879	Ubiquitination	NEALKLFKMHSPQTS HHHHHHHHHCCCCCC	46.25	23000965
879	Malonylation	NEALKLFKMHSPQTS HHHHHHHHHCCCCCC	46.25	26320211
879	Acetylation	NEALKLFKMHSPQTS HHHHHHHHHCCCCCC	46.25	25953088
880	Sulfoxidation	EALKLFKMHSPQTSA HHHHHHHHCCCCCCE	2.72	21406390
882	Phosphorylation	LKLFKMHSPQTSAML HHHHHHCCCCCCEEE	18.40	110745707
886	Phosphorylation	KMHSPQTSAMLFTVD HHCCCCCCEEEEEEE	13.36	110745715
888	Sulfoxidation	HSPQTSAMLFTVDNE CCCCCCEEEEEEECC	2.95	30846556
898	Ubiquitination	TVDNEAGKITCLCQV EEECCCCEEEEEEEC	41.72	29967540
900	Phosphorylation	DNEAGKITCLCQVPQ ECCCCEEEEEEECCH	11.69	310709009
900	Ubiquitination	DNEAGKITCLCQVPQ ECCCCEEEEEEECCH	11.69	21890473
915	Ubiquitination	NAANRGLKASEWVQQ HHHHCCCCHHHHHHH	53.33	23503661
917	Phosphorylation	ANRGLKASEWVQQVS HHCCCCHHHHHHHHH	30.33	27542207
924	Phosphorylation	SEWVQQVSGLMDGKG HHHHHHHHCCCCCCC	23.13	27542207
927	Sulfoxidation	VQQVSGLMDGKGGGK HHHHHCCCCCCCCCC	7.92	30846556
930	Acetylation	VSGLMDGKGGGKDVS HHCCCCCCCCCCCCC	50.55	27452117
930	Ubiquitination	VSGLMDGKGGGKDVS HHCCCCCCCCCCCCC	50.55	22817900
930	Malonylation	VSGLMDGKGGGKDVS HHCCCCCCCCCCCCC	50.55	26320211
934	Ubiquitination	MDGKGGGKDVSAQAT CCCCCCCCCCCHHHC	59.22	22817900
934	2-Hydroxyisobutyrylation	MDGKGGGKDVSAQAT CCCCCCCCCCCHHHC	59.22	-
934	Acetylation	MDGKGGGKDVSAQAT CCCCCCCCCCCHHHC	59.22	26051181
937	Phosphorylation	KGGGKDVSAQATGKN CCCCCCCCHHHCCCC	25.46	20068231
941	Phosphorylation	KDVSAQATGKNVGCL CCCCHHHCCCCCCHH	36.29	20068231
943	Ubiquitination	VSAQATGKNVGCLQE CCHHHCCCCCCHHHH	44.07	29967540

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 SYAC_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBA1_HUMAN	UBA1	physical	22939629
SYIC_HUMAN	IARS	physical	22939629
GARS_HUMAN	GARS	physical	22939629
SYNC_HUMAN	NARS	physical	22939629
SYLC_HUMAN	LARS	physical	22939629
SYDC_HUMAN	DARS	physical	22939629
SYFB_HUMAN	FARSB	physical	22939629
SYQ_HUMAN	QARS	physical	22939629
CYBP_HUMAN	CACYBP	physical	22863883
DPP8_HUMAN	DPP8	physical	22863883
DPP9_HUMAN	DPP9	physical	22863883
EF2K_HUMAN	EEF2K	physical	22863883
IF4A3_HUMAN	EIF4A3	physical	22863883
NIF3L_HUMAN	NIF3L1	physical	22863883
SRP09_HUMAN	SRP9	physical	22863883
TPD52_HUMAN	TPD52	physical	22863883
TPD54_HUMAN	TPD52L2	physical	22863883
SYWC_HUMAN	WARS	physical	22863883
GARS_HUMAN	GARS	physical	26344197
SYIC_HUMAN	IARS	physical	26344197
MSH2_HUMAN	MSH2	physical	26344197
NMD3_HUMAN	NMD3	physical	26344197
PDIA3_HUMAN	PDIA3	physical	26344197
SBDS_HUMAN	SBDS	physical	26344197
STAT1_HUMAN	STAT1	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613287	Charcot-Marie-Tooth disease 2N (CMT2N)
616339	Epileptic encephalopathy, early infantile, 29 (EIEE29)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00160	L-Alanine

Regulatory Network of SYAC_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, 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-19 AND LYS-876, 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-555, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-578 AND TYR-580, ANDMASS SPECTROMETRY.	17081983 [Abstract]