SYEP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SYEP_HUMAN
• UniProt AC: P07814
• Protein Name: Bifunctional glutamate/proline--tRNA ligase
• Gene Name: EPRS
• Organism: Homo sapiens (Human).
• Sequence Length: 1512
• Subcellular Localization: Cytoplasm, cytosol . Membrane ; Peripheral membrane protein . Translocates from cytosol to membranes upon phosphorylation at Ser-999.
• Protein Description: Multifunctional protein which is primarily part of the aminoacyl-tRNA synthetase multienzyme complex, also know as multisynthetase complex, that catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. [PubMed: 1756734]
• Protein Sequence: MATLSLTVNSGDPPLGALLAVEHVKDDVSISVEEGKENILHVSENVIFTDVNSILRYLARVATTAGLYGSNLMEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNAAWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEKKQDVGKFVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIDSKHRKNPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVGLKPVWYSPKVFIEGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKLNLENKDYKKTTKVTWLAETTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTKVEATKNETSAPFKERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYKEKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPEAKVLFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAEDKDKKKKEKENKSEKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKKEENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDKEALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY

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
6	Ubiquitination	--MATLSLTVNSGDP --CCEEEEEECCCCC	7.53	23000965
9	Ubiquitination	ATLSLTVNSGDPPLG CEEEEEECCCCCCHH	34.73	21890473
29	Phosphorylation	EHVKDDVSISVEEGK EECCCCCEEEHHCCC	19.01	20873877
31	Phosphorylation	VKDDVSISVEEGKEN CCCCCEEEHHCCCCC	18.90	20873877
64	Phosphorylation	YLARVATTAGLYGSN HHHHHHHHHHHCCCC	14.70	-
92	S-nitrosocysteine	SATKLSSCDSFTSTI CCHHHHCCHHHHHHH	4.58	-
92	S-nitrosylation	SATKLSSCDSFTSTI CCHHHHCCHHHHHHH	4.58	19483679
94	Phosphorylation	TKLSSCDSFTSTINE HHHHCCHHHHHHHHH	34.45	28348404
96	Phosphorylation	LSSCDSFTSTINELN HHCCHHHHHHHHHHH	28.98	28348404
97	Phosphorylation	SSCDSFTSTINELNH HCCHHHHHHHHHHHH	25.86	28348404
98	Phosphorylation	SCDSFTSTINELNHC CCHHHHHHHHHHHHH	25.43	28348404
105	S-nitrosocysteine	TINELNHCLSLRTYL HHHHHHHHHHCCHHH	2.41	-
105	S-nitrosylation	TINELNHCLSLRTYL HHHHHHHHHHCCHHH	2.41	19483679
121	Ubiquitination	GNSLSLADLCVWATL CCCCCHHHHHHHHHH	45.99	27667366
139	Acetylation	AAWQEQLKQKKAPVH HHHHHHHHHCCCCHH	60.82	25953088
139	Malonylation	AAWQEQLKQKKAPVH HHHHHHHHHCCCCHH	60.82	26320211
139	Ubiquitination	AAWQEQLKQKKAPVH HHHHHHHHHCCCCHH	60.82	27667366
141	Ubiquitination	WQEQLKQKKAPVHVK HHHHHHHCCCCHHHH	49.68	22817900
142	Ubiquitination	QEQLKQKKAPVHVKR HHHHHHCCCCHHHHH	56.26	22817900
173	Acetylation	KWDVSTTKARVAPEK CCCCCCCCCEECCHH	33.99	25953088
173	Malonylation	KWDVSTTKARVAPEK CCCCCCCCCEECCHH	33.99	32601280
173	Ubiquitination	KWDVSTTKARVAPEK CCCCCCCCCEECCHH	33.99	27667366
181	Acetylation	ARVAPEKKQDVGKFV CEECCHHHCCCCCEE	50.50	26051181
181	Ubiquitination	ARVAPEKKQDVGKFV CEECCHHHCCCCCEE	50.50	24816145
186	Acetylation	EKKQDVGKFVELPGA HHHCCCCCEEECCCC	46.19	25953088
186	Ubiquitination	EKKQDVGKFVELPGA HHHCCCCCEEECCCC	46.19	29967540
195	Sulfoxidation	VELPGAEMGKVTVRF EECCCCCCCEEEEEC	6.62	30846556
197	Acetylation	LPGAEMGKVTVRFPP CCCCCCCEEEEECCC	33.16	25953088
197	Ubiquitination	LPGAEMGKVTVRFPP CCCCCCCEEEEECCC	33.16	29967540
216	Ubiquitination	YLHIGHAKAALLNQH EEEEEEHHHHHHCCC	28.63	29967540
224	Phosphorylation	AALLNQHYQVNFKGK HHHHCCCEEEECCCE	12.37	28152594
229	2-Hydroxyisobutyrylation	QHYQVNFKGKLIMRF CCEEEECCCEEEEEE	50.35	-
229	Acetylation	QHYQVNFKGKLIMRF CCEEEECCCEEEEEE	50.35	25953088
229	Methylation	QHYQVNFKGKLIMRF CCEEEECCCEEEEEE	50.35	-
229	Ubiquitination	QHYQVNFKGKLIMRF CCEEEECCCEEEEEE	50.35	23000965
231	Methylation	YQVNFKGKLIMRFDD EEEECCCEEEEEECC	35.12	-
231	Ubiquitination	YQVNFKGKLIMRFDD EEEECCCEEEEEECC	35.12	23000965
243	Acetylation	FDDTNPEKEKEDFEK ECCCCHHHHHHHHHH	75.29	23749302
243	Malonylation	FDDTNPEKEKEDFEK ECCCCHHHHHHHHHH	75.29	26320211
245	Acetylation	DTNPEKEKEDFEKVI CCCHHHHHHHHHHHH	73.90	23749302
245	Malonylation	DTNPEKEKEDFEKVI CCCHHHHHHHHHHHH	73.90	26320211
256	Ubiquitination	EKVILEDVAMLHIKP HHHHHHHEEEEEECC	2.17	21890473
258	Sulfoxidation	VILEDVAMLHIKPDQ HHHHHEEEEEECCCC	2.55	30846556
262	Ubiquitination	DVAMLHIKPDQFTYT HEEEEEECCCCCEEC	31.62	23000965
277	Sulfoxidation	SDHFETIMKYAEKLI HHHHHHHHHHHHHHH	3.38	30846556
282	2-Hydroxyisobutyrylation	TIMKYAEKLIQEGKA HHHHHHHHHHHHCCC	42.59	-
282	Acetylation	TIMKYAEKLIQEGKA HHHHHHHHHHHHCCC	42.59	23954790
282	Malonylation	TIMKYAEKLIQEGKA HHHHHHHHHHHHCCC	42.59	26320211
282	Ubiquitination	TIMKYAEKLIQEGKA HHHHHHHHHHHHCCC	42.59	23503661
288	2-Hydroxyisobutyrylation	EKLIQEGKAYVDDTP HHHHHHCCCCCCCCH	35.47	-
288	Acetylation	EKLIQEGKAYVDDTP HHHHHHCCCCCCCCH	35.47	26051181
288	Ubiquitination	EKLIQEGKAYVDDTP HHHHHHCCCCCCCCH	35.47	21906983
299	Sulfoxidation	DDTPAEQMKAEREQR CCCHHHHHHHHHHHH	3.15	30846556
300	N6-malonyllysine	DTPAEQMKAEREQRI CCHHHHHHHHHHHHC	46.95	-
300	2-Hydroxyisobutyrylation	DTPAEQMKAEREQRI CCHHHHHHHHHHHHC	46.95	-
300	Acetylation	DTPAEQMKAEREQRI CCHHHHHHHHHHHHC	46.95	19608861
300	Malonylation	DTPAEQMKAEREQRI CCHHHHHHHHHHHHC	46.95	26320211
300	Ubiquitination	DTPAEQMKAEREQRI CCHHHHHHHHHHHHC	46.95	32015554
318	Sumoylation	HRKNPIEKNLQMWEE HCCCHHHHHHHHHHH	64.77	-
318	Acetylation	HRKNPIEKNLQMWEE HCCCHHHHHHHHHHH	64.77	27452117
318	Sumoylation	HRKNPIEKNLQMWEE HCCCHHHHHHHHHHH	64.77	-
327	Acetylation	LQMWEEMKKGSQFGQ HHHHHHHHHCCCCHH	58.21	25953088
328	Acetylation	QMWEEMKKGSQFGQS HHHHHHHHCCCCHHC	63.58	26051181
328	Methylation	QMWEEMKKGSQFGQS HHHHHHHHCCCCHHC	63.58	-
328	Ubiquitination	QMWEEMKKGSQFGQS HHHHHHHHCCCCHHC	63.58	29967540
330	Phosphorylation	WEEMKKGSQFGQSCC HHHHHHCCCCHHCHH	31.08	28258704
335	Phosphorylation	KGSQFGQSCCLRAKI HCCCCHHCHHHEEEE	13.74	28258704
335	Ubiquitination	KGSQFGQSCCLRAKI HCCCCHHCHHHEEEE	13.74	21890473
339	Ubiquitination	FGQSCCLRAKIDMSS CHHCHHHEEEEECCC	21.66	23000965
341	Acetylation	QSCCLRAKIDMSSNN HCHHHEEEEECCCCC	32.57	26051181
341	Ubiquitination	QSCCLRAKIDMSSNN HCHHHEEEEECCCCC	32.57	23000965
345	Phosphorylation	LRAKIDMSSNNGCMR HEEEEECCCCCCCCC	26.60	-
346	Phosphorylation	RAKIDMSSNNGCMRD EEEEECCCCCCCCCC	27.90	20044836
355	Phosphorylation	NGCMRDPTLYRCKIQ CCCCCCCEEEEEEEE	40.48	25849741
357	Phosphorylation	CMRDPTLYRCKIQPH CCCCCEEEEEEEECC	19.22	20044836
360	Acetylation	DPTLYRCKIQPHPRT CCEEEEEEEECCCCC	35.06	25953088
360	Ubiquitination	DPTLYRCKIQPHPRT CCEEEEEEEECCCCC	35.06	29967540
370	Acetylation	PHPRTGNKYNVYPTY CCCCCCCCCEECCCC	39.28	130251
370	Ubiquitination	PHPRTGNKYNVYPTY CCCCCCCCCEECCCC	39.28	-
376	Phosphorylation	NKYNVYPTYDFACPI CCCEECCCCCCCCCC	20.31	26356563
376	Ubiquitination	NKYNVYPTYDFACPI CCCEECCCCCCCCCC	20.31	23000965
377	Phosphorylation	KYNVYPTYDFACPIV CCEECCCCCCCCCCH	12.45	17360941
381	Ubiquitination	YPTYDFACPIVDSIE CCCCCCCCCCHHHHH	2.09	23000965
391	Phosphorylation	VDSIEGVTHALRTTE HHHHHCCCEEHHCCC	16.58	28787133
413	Ubiquitination	FYWIIEALGIRKPYI HHHHHHHHCCCCCCH	3.67	23000965
417	2-Hydroxyisobutyrylation	IEALGIRKPYIWEYS HHHHCCCCCCHHEEE	40.01	-
417	Acetylation	IEALGIRKPYIWEYS HHHHCCCCCCHHEEE	40.01	19608861
417	Malonylation	IEALGIRKPYIWEYS HHHHCCCCCCHHEEE	40.01	26320211
417	Ubiquitination	IEALGIRKPYIWEYS HHHHCCCCCCHHEEE	40.01	21890473
419	Phosphorylation	ALGIRKPYIWEYSRL HHCCCCCCHHEEEEC	23.00	28152594
423	Phosphorylation	RKPYIWEYSRLNLNN CCCCHHEEEECCCCC	5.54	-
431	Phosphorylation	SRLNLNNTVLSKRKL EECCCCCCCCCCCCE	23.04	29255136
434	Phosphorylation	NLNNTVLSKRKLTWF CCCCCCCCCCCEEEE	26.52	29255136
435	2-Hydroxyisobutyrylation	LNNTVLSKRKLTWFV CCCCCCCCCCEEEEE	49.76	-
435	Acetylation	LNNTVLSKRKLTWFV CCCCCCCCCCEEEEE	49.76	25953088
435	Malonylation	LNNTVLSKRKLTWFV CCCCCCCCCCEEEEE	49.76	26320211
435	Ubiquitination	LNNTVLSKRKLTWFV CCCCCCCCCCEEEEE	49.76	23000965
437	Ubiquitination	NTVLSKRKLTWFVNE CCCCCCCCEEEEECC	54.74	23000965
454	Methylation	VDGWDDPRFPTVRGV CCCCCCCCCCCHHHH	58.11	-
461	Ubiquitination	RFPTVRGVLRRGMTV CCCCHHHHHHCCCCH	2.35	22817900
464	Methylation	TVRGVLRRGMTVEGL CHHHHHHCCCCHHHH	34.76	-
465	Ubiquitination	VRGVLRRGMTVEGLK HHHHHHCCCCHHHHH	15.07	22817900
467	Phosphorylation	GVLRRGMTVEGLKQF HHHHCCCCHHHHHHH	20.45	22199227
472	Acetylation	GMTVEGLKQFIAAQG CCCHHHHHHHHHHCC	54.76	25953088
472	Ubiquitination	GMTVEGLKQFIAAQG CCCHHHHHHHHHHCC	54.76	21906983
480	Phosphorylation	QFIAAQGSSRSVVNM HHHHHCCCCCCEEEC	15.53	30257219
481	Phosphorylation	FIAAQGSSRSVVNME HHHHCCCCCCEEECC	35.09	30257219
483	Phosphorylation	AAQGSSRSVVNMEWD HHCCCCCCEEECCHH	32.15	29449344
483	Ubiquitination	AAQGSSRSVVNMEWD HHCCCCCCEEECCHH	32.15	22817900
484	Ubiquitination	AQGSSRSVVNMEWDK HCCCCCCEEECCHHH	3.33	22817900
487	Sulfoxidation	SSRSVVNMEWDKIWA CCCCEEECCHHHHHE	3.58	30846556
497	Acetylation	DKIWAFNKKVIDPVA HHHHEECCHHCCCCH	41.80	23749302
497	Malonylation	DKIWAFNKKVIDPVA HHHHEECCHHCCCCH	41.80	26320211
497	Ubiquitination	DKIWAFNKKVIDPVA HHHHEECCHHCCCCH	41.80	19608861
498	Acetylation	KIWAFNKKVIDPVAP HHHEECCHHCCCCHH	45.59	19608861
498	Malonylation	KIWAFNKKVIDPVAP HHHEECCHHCCCCHH	45.59	26320211
498	Ubiquitination	KIWAFNKKVIDPVAP HHHEECCHHCCCCHH	45.59	19608861
512	Ubiquitination	PRYVALLKKEVIPVN HHHHHHHHCCCCCCC	47.97	21906983
513	Ubiquitination	RYVALLKKEVIPVNV HHHHHHHCCCCCCCC	58.12	29967540
527	Sulfoxidation	VPEAQEEMKEVAKHP CHHHHHHHHHHHHCC	4.39	21406390
528	Acetylation	PEAQEEMKEVAKHPK HHHHHHHHHHHHCCC	52.93	23954790
532	Acetylation	EEMKEVAKHPKNPEV HHHHHHHHCCCCCCC	66.66	25038526
532	Ubiquitination	EEMKEVAKHPKNPEV HHHHHHHHCCCCCCC	66.66	23000965
535	Acetylation	KEVAKHPKNPEVGLK HHHHHCCCCCCCCCC	82.14	19608861
535	Malonylation	KEVAKHPKNPEVGLK HHHHHCCCCCCCCCC	82.14	26320211
535	Ubiquitination	KEVAKHPKNPEVGLK HHHHHCCCCCCCCCC	82.14	23000965
542	2-Hydroxyisobutyrylation	KNPEVGLKPVWYSPK CCCCCCCCCCEECCE	31.43	-
542	Acetylation	KNPEVGLKPVWYSPK CCCCCCCCCCEECCE	31.43	19608861
542	Ubiquitination	KNPEVGLKPVWYSPK CCCCCCCCCCEECCE	31.43	19608861
543	Ubiquitination	NPEVGLKPVWYSPKV CCCCCCCCCEECCEE	27.24	22817900
544	Ubiquitination	PEVGLKPVWYSPKVF CCCCCCCCEECCEEE	7.77	22817900
546	Phosphorylation	VGLKPVWYSPKVFIE CCCCCCEECCEEEEE	18.48	28152594
547	Phosphorylation	GLKPVWYSPKVFIEG CCCCCEECCEEEEEC	11.52	28152594
581	Ubiquitination	LNITKIHKNADGKII CCEEEEEECCCCCEE	58.25	29967540
583	Ubiquitination	ITKIHKNADGKIISL EEEEEECCCCCEEEE	31.56	22817900
586	2-Hydroxyisobutyrylation	IHKNADGKIISLDAK EEECCCCCEEEEEEE	37.10	-
586	Acetylation	IHKNADGKIISLDAK EEECCCCCEEEEEEE	37.10	27452117
586	Ubiquitination	IHKNADGKIISLDAK EEECCCCCEEEEEEE	37.10	29967540
593	2-Hydroxyisobutyrylation	KIISLDAKLNLENKD CEEEEEEEECCCCCC	37.26	-
593	Ubiquitination	KIISLDAKLNLENKD CEEEEEEEECCCCCC	37.26	29967540
599	Acetylation	AKLNLENKDYKKTTK EEECCCCCCCCCCEE	53.73	23749302
599	Malonylation	AKLNLENKDYKKTTK EEECCCCCCCCCCEE	53.73	26320211
599	Ubiquitination	AKLNLENKDYKKTTK EEECCCCCCCCCCEE	53.73	29967540
601	Phosphorylation	LNLENKDYKKTTKVT ECCCCCCCCCCEEEE	18.92	28152594
602	Acetylation	NLENKDYKKTTKVTW CCCCCCCCCCEEEEE	54.50	25953088
606	Ubiquitination	KDYKKTTKVTWLAET CCCCCCEEEEEEEEC	42.79	21890473
613	O-linked_Glycosylation	KVTWLAETTHALPIP EEEEEEECCCCCCCC	20.48	23301498
617	Ubiquitination	LAETTHALPIPVICV EEECCCCCCCCEEEE	2.83	23000965
631	O-linked_Glycosylation	VTYEHLITKPVLGKD EEEHHHHCCCCCCCC	35.34	23301498
637	Acetylation	ITKPVLGKDEDFKQY HCCCCCCCCHHHHHH	54.50	19608861
637	Malonylation	ITKPVLGKDEDFKQY HCCCCCCCCHHHHHH	54.50	32601280
642	Acetylation	LGKDEDFKQYVNKNS CCCCHHHHHHHCCCC	53.71	26051181
642	Malonylation	LGKDEDFKQYVNKNS CCCCHHHHHHHCCCC	53.71	26320211
642	Ubiquitination	LGKDEDFKQYVNKNS CCCCHHHHHHHCCCC	53.71	32015554
644	Phosphorylation	KDEDFKQYVNKNSKH CCHHHHHHHCCCCCC	13.43	28152594
647	Ubiquitination	DFKQYVNKNSKHEEL HHHHHHCCCCCCHHH	53.18	27667366
650	Acetylation	QYVNKNSKHEELMLG HHHCCCCCCHHHHCC	65.51	27452117
660	Glutathionylation	ELMLGDPCLKDLKKG HHHCCCCCHHHCCCC	9.80	22555962
662	Acetylation	MLGDPCLKDLKKGDI HCCCCCHHHCCCCCC	68.67	25953088
666	Ubiquitination	PCLKDLKKGDIIQLQ CCHHHCCCCCCEEEE	69.94	29967540
684	Phosphorylation	FFICDQPYEPVSPYS EEECCCCCCCCCCCC	27.51	21945579
688	Phosphorylation	DQPYEPVSPYSCKEA CCCCCCCCCCCCCCC	28.92	21945579
690	Phosphorylation	PYEPVSPYSCKEAPC CCCCCCCCCCCCCCE	21.13	21945579
691	Phosphorylation	YEPVSPYSCKEAPCV CCCCCCCCCCCCCEE	23.30	21945579
693	Acetylation	PVSPYSCKEAPCVLI CCCCCCCCCCCEEEE	51.47	26051181
697	Glutathionylation	YSCKEAPCVLIYIPD CCCCCCCEEEEEECC	5.12	22555962
708	Acetylation	YIPDGHTKEMPTSGS EECCCCCCCCCCCCC	46.47	26051181
708	Malonylation	YIPDGHTKEMPTSGS EECCCCCCCCCCCCC	46.47	26320211
708	Ubiquitination	YIPDGHTKEMPTSGS EECCCCCCCCCCCCC	46.47	32015554
712	Phosphorylation	GHTKEMPTSGSKEKT CCCCCCCCCCCCCCC	44.39	20068231
713	Phosphorylation	HTKEMPTSGSKEKTK CCCCCCCCCCCCCCE	34.89	20068231
715	Phosphorylation	KEMPTSGSKEKTKVE CCCCCCCCCCCCEEE	37.09	20068231
716	Ubiquitination	EMPTSGSKEKTKVEA CCCCCCCCCCCEEEE	67.75	33845483
718	Ubiquitination	PTSGSKEKTKVEATK CCCCCCCCCEEEECC	58.33	-
719	Phosphorylation	TSGSKEKTKVEATKN CCCCCCCCEEEECCC	41.22	20068231
720	Acetylation	SGSKEKTKVEATKNE CCCCCCCEEEECCCC	49.50	26051181
720	Ubiquitination	SGSKEKTKVEATKNE CCCCCCCEEEECCCC	49.50	33845483
725	2-Hydroxyisobutyrylation	KTKVEATKNETSAPF CCEEEECCCCCCCCC	60.89	-
725	Acetylation	KTKVEATKNETSAPF CCEEEECCCCCCCCC	60.89	26051181
725	Ubiquitination	KTKVEATKNETSAPF CCEEEECCCCCCCCC	60.89	32015554
729	Phosphorylation	EATKNETSAPFKERP EECCCCCCCCCCCCC	27.97	25627689
733	Acetylation	NETSAPFKERPTPSL CCCCCCCCCCCCCCC	52.32	26051181
733	Ubiquitination	NETSAPFKERPTPSL CCCCCCCCCCCCCCC	52.32	32015554
737	Phosphorylation	APFKERPTPSLNNNC CCCCCCCCCCCCCCC	31.56	23663014
739	Phosphorylation	FKERPTPSLNNNCTT CCCCCCCCCCCCCCC	46.32	25159151
741	Phosphorylation	ERPTPSLNNNCTTSE CCCCCCCCCCCCCCC	41.84	18669648
744	Glutathionylation	TPSLNNNCTTSEDSL CCCCCCCCCCCCCEE	4.83	22555962
745	Phosphorylation	PSLNNNCTTSEDSLV CCCCCCCCCCCCEEE	35.16	25159151
746	Phosphorylation	SLNNNCTTSEDSLVL CCCCCCCCCCCEEEE	32.11	25159151
747	Phosphorylation	LNNNCTTSEDSLVLY CCCCCCCCCCEEEEE	22.66	25159151
750	Phosphorylation	NCTTSEDSLVLYNRV CCCCCCCEEEEEEEE	19.14	25159151
754	Phosphorylation	SEDSLVLYNRVAVQG CCCEEEEEEEEEECC	8.08	28152594
782	Acetylation	EDVDAAVKQLLSLKA HHHHHHHHHHHHHHH	30.42	23236377
782	Neddylation	EDVDAAVKQLLSLKA HHHHHHHHHHHHHHH	30.42	32015554
782	Ubiquitination	EDVDAAVKQLLSLKA HHHHHHHHHHHHHHH	30.42	23000965
786	Phosphorylation	AAVKQLLSLKAEYKE HHHHHHHHHHHHHHH	36.09	24719451
788	2-Hydroxyisobutyrylation	VKQLLSLKAEYKEKT HHHHHHHHHHHHHHH	35.48	-
788	Acetylation	VKQLLSLKAEYKEKT HHHHHHHHHHHHHHH	35.48	19608861
788	Malonylation	VKQLLSLKAEYKEKT HHHHHHHHHHHHHHH	35.48	26320211
788	Succinylation	VKQLLSLKAEYKEKT HHHHHHHHHHHHHHH	35.48	23954790
788	Ubiquitination	VKQLLSLKAEYKEKT HHHHHHHHHHHHHHH	35.48	23000965
794	2-Hydroxyisobutyrylation	LKAEYKEKTGQEYKP HHHHHHHHHCCCCCC	54.53	-
800	Acetylation	EKTGQEYKPGNPPAE HHHCCCCCCCCCCHH	45.77	26051181
800	Malonylation	EKTGQEYKPGNPPAE HHHCCCCCCCCCCHH	45.77	26320211
800	Phosphorylation	EKTGQEYKPGNPPAE HHHCCCCCCCCCCHH	45.77	18669648
808	Phosphorylation	PGNPPAEIGQNISSN CCCCCHHHCCCCCCC	8.16	18669648
810	Phosphorylation	NPPAEIGQNISSNSS CCCHHHCCCCCCCCC	50.15	18669648
811	Phosphorylation	PPAEIGQNISSNSSA CCHHHCCCCCCCCCC	30.78	18669648
813	Phosphorylation	AEIGQNISSNSSASI HHHCCCCCCCCCCHH	30.89	25159151
814	Phosphorylation	EIGQNISSNSSASIL HHCCCCCCCCCCHHH	36.61	30576142
816	Phosphorylation	GQNISSNSSASILES CCCCCCCCCCHHHHC	29.27	26657352
817	Phosphorylation	QNISSNSSASILESK CCCCCCCCCHHHHCC	30.22	30576142
819	Phosphorylation	ISSNSSASILESKSL CCCCCCCHHHHCCHH	29.65	30576142
823	Phosphorylation	SSASILESKSLYDEV CCCHHHHCCHHHHHH	24.89	23186163
825	Phosphorylation	ASILESKSLYDEVAA CHHHHCCHHHHHHHH	41.25	29978859
826	Phosphorylation	SILESKSLYDEVAAQ HHHHCCHHHHHHHHH	7.79	18669648
827	Phosphorylation	ILESKSLYDEVAAQG HHHCCHHHHHHHHHC	19.69	28796482
835	Ubiquitination	DEVAAQGEVVRKLKA HHHHHHCHHHHHHHC	26.26	21963094
845	Phosphorylation	RKLKAEKSPKAKINE HHHHCCCCCCHHHHH	24.12	26055452
849	Ubiquitination	AEKSPKAKINEAVEC CCCCCCHHHHHHHHH	52.79	23000965
856	S-nitrosocysteine	KINEAVECLLSLKAQ HHHHHHHHHHHHHHH	3.58	-
856	Glutathionylation	KINEAVECLLSLKAQ HHHHHHHHHHHHHHH	3.58	22555962
856	S-nitrosylation	KINEAVECLLSLKAQ HHHHHHHHHHHHHHH	3.58	22178444
859	Phosphorylation	EAVECLLSLKAQYKE HHHHHHHHHHHHHHH	18.18	21406692
861	2-Hydroxyisobutyrylation	VECLLSLKAQYKEKT HHHHHHHHHHHHHHH	30.02	-
861	Acetylation	VECLLSLKAQYKEKT HHHHHHHHHHHHHHH	30.02	23954790
861	Malonylation	VECLLSLKAQYKEKT HHHHHHHHHHHHHHH	30.02	26320211
861	Ubiquitination	VECLLSLKAQYKEKT HHHHHHHHHHHHHHH	30.02	23000965
863	Ubiquitination	CLLSLKAQYKEKTGK HHHHHHHHHHHHHCC	48.52	22817900
864	Phosphorylation	LLSLKAQYKEKTGKE HHHHHHHHHHHHCCC	26.44	-
865	Ubiquitination	LSLKAQYKEKTGKEY HHHHHHHHHHHCCCC	40.43	23000965
867	Ubiquitination	LKAQYKEKTGKEYIP HHHHHHHHHCCCCCC	59.43	23000965
868	Phosphorylation	KAQYKEKTGKEYIPG HHHHHHHHCCCCCCC	55.36	26074081
872	Phosphorylation	KEKTGKEYIPGQPPL HHHHCCCCCCCCCCC	18.85	23927012
880	Phosphorylation	IPGQPPLSQSSDSSP CCCCCCCCCCCCCCC	33.52	29255136
882	Phosphorylation	GQPPLSQSSDSSPTR CCCCCCCCCCCCCCC	32.51	29255136
883	Phosphorylation	QPPLSQSSDSSPTRN CCCCCCCCCCCCCCC	33.60	29255136
885	Phosphorylation	PLSQSSDSSPTRNSE CCCCCCCCCCCCCCC	39.92	29255136
886	Phosphorylation	LSQSSDSSPTRNSEP CCCCCCCCCCCCCCC	34.97	19664994
888	Phosphorylation	QSSDSSPTRNSEPAG CCCCCCCCCCCCCCC	44.42	29255136
891	Phosphorylation	DSSPTRNSEPAGLET CCCCCCCCCCCCCCC	41.48	20201521
898	Phosphorylation	SEPAGLETPEAKVLF CCCCCCCCCCHHHHH	31.32	25159151
902	Ubiquitination	GLETPEAKVLFDKVA CCCCCCHHHHHHHHH	37.50	23000965
907	Acetylation	EAKVLFDKVASQGEV CHHHHHHHHHHCCHH	32.16	25953088
907	Malonylation	EAKVLFDKVASQGEV CHHHHHHHHHHCCHH	32.16	26320211
907	Ubiquitination	EAKVLFDKVASQGEV CHHHHHHHHHHCCHH	32.16	23000965
909	Ubiquitination	KVLFDKVASQGEVVR HHHHHHHHHCCHHHH	11.24	21890473
910	Phosphorylation	VLFDKVASQGEVVRK HHHHHHHHCCHHHHH	41.53	25159151
915	Ubiquitination	VASQGEVVRKLKTEK HHHCCHHHHHHHCCC	3.77	23000965
925	Ubiquitination	LKTEKAPKDQVDIAV HHCCCCCHHHHHHHH	66.70	32015554
928	Phosphorylation	EKAPKDQVDIAVQEL CCCCHHHHHHHHHHH	9.13	18669648
939	Acetylation	VQELLQLKAQYKSLI HHHHHHHHHHHHHHH	22.08	26822725
939	Ubiquitination	VQELLQLKAQYKSLI HHHHHHHHHHHHHHH	22.08	23000965
943	Malonylation	LQLKAQYKSLIGVEY HHHHHHHHHHHCCEE	27.06	26320211
943	Ubiquitination	LQLKAQYKSLIGVEY HHHHHHHHHHHCCEE	27.06	23000965
944	Phosphorylation	QLKAQYKSLIGVEYK HHHHHHHHHHCCEEE	21.93	21945579
950	Phosphorylation	KSLIGVEYKPVSATG HHHHCCEEECCCCCC	20.41	21945579
951	Acetylation	SLIGVEYKPVSATGA HHHCCEEECCCCCCC	25.99	23954790
951	Malonylation	SLIGVEYKPVSATGA HHHCCEEECCCCCCC	25.99	32601280
951	Ubiquitination	SLIGVEYKPVSATGA HHHCCEEECCCCCCC	25.99	33845483
954	Phosphorylation	GVEYKPVSATGAEDK CCEEECCCCCCCCCH	28.74	21945579
956	Phosphorylation	EYKPVSATGAEDKDK EEECCCCCCCCCHHH	29.44	21945579
961	Acetylation	SATGAEDKDKKKKEK CCCCCCCHHHHHHHH	64.05	23236377
973	Ubiquitination	KEKENKSEKQNKPQK HHHHCHHHHCCCCCC	61.34	23000965
977	Ubiquitination	NKSEKQNKPQKQNDG CHHHHCCCCCCCCCC	46.46	21890473
980	Ubiquitination	EKQNKPQKQNDGQRK HHCCCCCCCCCCCCC	60.64	29967540
987	Ubiquitination	KQNDGQRKDPSKNQG CCCCCCCCCCCCCCC	67.13	22817900
990	Phosphorylation	DGQRKDPSKNQGGGL CCCCCCCCCCCCCCC	55.14	29214152
991	Methylation	GQRKDPSKNQGGGLS CCCCCCCCCCCCCCC	59.69	-
991	Ubiquitination	GQRKDPSKNQGGGLS CCCCCCCCCCCCCCC	59.69	21906983
998	Phosphorylation	KNQGGGLSSSGAGEG CCCCCCCCCCCCCCC	26.23	29255136
999	Phosphorylation	NQGGGLSSSGAGEGQ CCCCCCCCCCCCCCC	37.52	29255136
1000	Phosphorylation	QGGGLSSSGAGEGQG CCCCCCCCCCCCCCC	29.32	29255136
1009	2-Hydroxyisobutyrylation	AGEGQGPKKQTRLGL CCCCCCCHHHCCCCC	65.42	-
1009	Acetylation	AGEGQGPKKQTRLGL CCCCCCCHHHCCCCC	65.42	26051181
1009	Ubiquitination	AGEGQGPKKQTRLGL CCCCCCCHHHCCCCC	65.42	21906983
1010	Ubiquitination	GEGQGPKKQTRLGLE CCCCCCHHHCCCCCH	61.10	22817900
1012	Phosphorylation	GQGPKKQTRLGLEAK CCCCHHHCCCCCHHH	36.42	20068231
1019	Ubiquitination	TRLGLEAKKEENLAD CCCCCHHHHHHCHHH	51.87	29967540
1020	Acetylation	RLGLEAKKEENLADW CCCCHHHHHHCHHHH	76.84	26051181
1020	Ubiquitination	RLGLEAKKEENLADW CCCCHHHHHHCHHHH	76.84	29967540
1028	Phosphorylation	EENLADWYSQVITKS HHCHHHHHHHCCCHH	6.97	27642862
1035	Phosphorylation	YSQVITKSEMIEYHD HHHCCCHHHHEEEEC	24.60	25072903
1040	Phosphorylation	TKSEMIEYHDISGCY CHHHHEEEECCCCCE	8.22	25072903
1044	Phosphorylation	MIEYHDISGCYILRP HEEEECCCCCEECHH	28.94	25072903
1047	Phosphorylation	YHDISGCYILRPWAY EECCCCCEECHHHHH	13.40	25072903
1054	Phosphorylation	YILRPWAYAIWEAIK EECHHHHHHHHHHHH	8.51	25072903
1069	Ubiquitination	DFFDAEIKKLGVENC HHHHHHHHHHCCCCC	33.19	22817900
1070	Ubiquitination	FFDAEIKKLGVENCY HHHHHHHHHCCCCCC	57.02	22817900
1076	Glutathionylation	KKLGVENCYFPMFVS HHHCCCCCCHHEECC	2.04	22555962
1080	Sulfoxidation	VENCYFPMFVSQSAL CCCCCHHEECCHHHH	3.57	30846556
1083	O-linked_Glycosylation	CYFPMFVSQSALEKE CCHHEECCHHHHHHH	13.73	23301498
1091	2-Hydroxyisobutyrylation	QSALEKEKTHVADFA HHHHHHHHCCHHCCC	55.81	-
1091	Acetylation	QSALEKEKTHVADFA HHHHHHHHCCHHCCC	55.81	25953088
1091	Ubiquitination	QSALEKEKTHVADFA HHHHHHHHCCHHCCC	55.81	29967540
1109	Acetylation	AWVTRSGKTELAEPI EEEECCCCCCCCCCE	39.82	26051181
1109	Malonylation	AWVTRSGKTELAEPI EEEECCCCCCCCCCE	39.82	26320211
1109	Ubiquitination	AWVTRSGKTELAEPI EEEECCCCCCCCCCE	39.82	22817900
1110	Phosphorylation	WVTRSGKTELAEPIA EEECCCCCCCCCCEE	39.49	20068231
1121	Phosphorylation	EPIAIRPTSETVMYP CCEEECCCCCCCCCH	29.37	20068231
1122	Phosphorylation	PIAIRPTSETVMYPA CEEECCCCCCCCCHH	33.67	20068231
1124	Phosphorylation	AIRPTSETVMYPAYA EECCCCCCCCCHHHH	15.44	29978859
1126	Sulfoxidation	RPTSETVMYPAYAKW CCCCCCCCCHHHHHH	4.30	30846556
1127	Phosphorylation	PTSETVMYPAYAKWV CCCCCCCCHHHHHHH	4.75	20068231
1130	Phosphorylation	ETVMYPAYAKWVQSH CCCCCHHHHHHHHHC	12.29	29978859
1132	2-Hydroxyisobutyrylation	VMYPAYAKWVQSHRD CCCHHHHHHHHHCCC	34.91	-
1132	Acetylation	VMYPAYAKWVQSHRD CCCHHHHHHHHHCCC	34.91	26051181
1132	Ubiquitination	VMYPAYAKWVQSHRD CCCHHHHHHHHHCCC	34.91	22817900
1136	Phosphorylation	AYAKWVQSHRDLPIK HHHHHHHHCCCCCCC	15.75	29978859
1143	Acetylation	SHRDLPIKLNQWCNV HCCCCCCCHHHHHCE	39.17	26051181
1143	Ubiquitination	SHRDLPIKLNQWCNV HCCCCCCCHHHHHCE	39.17	23000965
1152	Dimethylation	NQWCNVVRWEFKHPQ HHHHCEEEEEECCCC	23.95	-
1152	Methylation	NQWCNVVRWEFKHPQ HHHHCEEEEEECCCC	23.95	24129315
1156	Acetylation	NVVRWEFKHPQPFLR CEEEEEECCCCCCCC	42.75	23749302
1156	Ubiquitination	NVVRWEFKHPQPFLR CEEEEEECCCCCCCC	42.75	19608861
1207	Ubiquitination	LLAIPVVKGRKTEKE HHCCEEECCCCCCCH	53.91	-
1221	Phosphorylation	EKFAGGDYTTTIEAF HHCCCCCCEEEHHHH	14.84	-
1222	Phosphorylation	KFAGGDYTTTIEAFI HCCCCCCEEEHHHHH	23.39	-
1250	Methylation	HLGQNFSKMFEIVFE CCCCCHHHHEEHHHC	43.39	-
1251	Sulfoxidation	LGQNFSKMFEIVFED CCCCHHHHEEHHHCC	3.36	21406390
1269	Phosphorylation	PGEKQFAYQNSWGLT CCCCCCCEECCCCCC	14.98	28152594
1272	Phosphorylation	KQFAYQNSWGLTTRT CCCCEECCCCCCCCE	13.65	28152594
1278	Methylation	NSWGLTTRTIGVMTM CCCCCCCCEEEEEEE	21.07	-
1279	Phosphorylation	SWGLTTRTIGVMTMV CCCCCCCEEEEEEEE	21.71	-
1301	S-palmitoylation	VLPPRVACVQVVIIP CCCCCEEEEEEEEEC	1.69	29575903
1309	S-palmitoylation	VQVVIIPCGITNALS EEEEEECCCHHHCCC	4.30	29575903
1336	Phosphorylation	DYRRRLLSVNIRVRA HHHHHHHEEEEEEEC	20.08	30266825
1349	Phosphorylation	RADLRDNYSPGWKFN ECCCCCCCCCCCCCC	22.11	20873877
1350	Phosphorylation	ADLRDNYSPGWKFNH CCCCCCCCCCCCCCC	24.16	23663014
1354	Acetylation	DNYSPGWKFNHWELK CCCCCCCCCCCEEEC	42.05	27452117
1354	Methylation	DNYSPGWKFNHWELK CCCCCCCCCCCEEEC	42.05	-
1361	2-Hydroxyisobutyrylation	KFNHWELKGVPIRLE CCCCEEECCCCEEEE	46.47	-
1361	Acetylation	KFNHWELKGVPIRLE CCCCEEECCCCEEEE	46.47	26051181
1361	Succinylation	KFNHWELKGVPIRLE CCCCEEECCCCEEEE	46.47	23954790
1361	Ubiquitination	KFNHWELKGVPIRLE CCCCEEECCCCEEEE	46.47	21963094
1375	2-Hydroxyisobutyrylation	EVGPRDMKSCQFVAV EECCCCCCCCEEEEE	52.98	-
1375	Acetylation	EVGPRDMKSCQFVAV EECCCCCCCCEEEEE	52.98	25953088
1375	Malonylation	EVGPRDMKSCQFVAV EECCCCCCCCEEEEE	52.98	26320211
1375	Ubiquitination	EVGPRDMKSCQFVAV EECCCCCCCCEEEEE	52.98	23000965
1377	Glutathionylation	GPRDMKSCQFVAVRR CCCCCCCCEEEEEEC	2.80	22555962
1377	S-nitrosylation	GPRDMKSCQFVAVRR CCCCCCCCEEEEEEC	2.80	2212679
1389	Acetylation	VRRDTGEKLTVAENE EECCCCCCEEEECCH	51.29	23954790
1389	Malonylation	VRRDTGEKLTVAENE EECCCCCCEEEECCH	51.29	26320211
1389	Ubiquitination	VRRDTGEKLTVAENE EECCCCCCEEEECCH	51.29	22817900
1417	Phosphorylation	VTLFTRASEDLKTHM HHEEEECCCHHHHCE	28.49	26437602
1421	2-Hydroxyisobutyrylation	TRASEDLKTHMVVAN EECCCHHHHCEEEEC	49.02	-
1421	Acetylation	TRASEDLKTHMVVAN EECCCHHHHCEEEEC	49.02	25953088
1424	Sulfoxidation	SEDLKTHMVVANTME CCHHHHCEEEECCHH	2.91	30846556
1430	Sulfoxidation	HMVVANTMEDFQKIL CEEEECCHHHHHHHH	4.70	30846556
1435	2-Hydroxyisobutyrylation	NTMEDFQKILDSGKI CCHHHHHHHHHCCCE	45.27	-
1435	Acetylation	NTMEDFQKILDSGKI CCHHHHHHHHHCCCE	45.27	26051181
1435	Ubiquitination	NTMEDFQKILDSGKI CCHHHHHHHHHCCCE	45.27	23000965
1441	Acetylation	QKILDSGKIVQIPFC HHHHHCCCEEEECCC	43.59	26051181
1441	Ubiquitination	QKILDSGKIVQIPFC HHHHHCCCEEEECCC	43.59	23000965
1453	Glutathionylation	PFCGEIDCEDWIKKT CCCCEECHHHHHHHH	6.67	22555962
1458	Acetylation	IDCEDWIKKTTARDQ ECHHHHHHHHCCCCC	39.55	25953088
1458	Ubiquitination	IDCEDWIKKTTARDQ ECHHHHHHHHCCCCC	39.55	32015554
1460	Phosphorylation	CEDWIKKTTARDQDL HHHHHHHHCCCCCCC	22.23	21406692
1461	Phosphorylation	EDWIKKTTARDQDLE HHHHHHHCCCCCCCC	28.68	21406692
1473	Phosphorylation	DLEPGAPSMGAKSLC CCCCCCCCCCCCEEE	29.34	21406692
1474	Sulfoxidation	LEPGAPSMGAKSLCI CCCCCCCCCCCEEEE	6.19	21406390
1477	Acetylation	GAPSMGAKSLCIPFK CCCCCCCCEEEEECC	37.93	26051181
1477	Ubiquitination	GAPSMGAKSLCIPFK CCCCCCCCEEEEECC	37.93	32015554
1478	Phosphorylation	APSMGAKSLCIPFKP CCCCCCCEEEEECCC	28.12	27080861
1480	Glutathionylation	SMGAKSLCIPFKPLC CCCCCEEEEECCCCC	4.85	22555962
1480	S-palmitoylation	SMGAKSLCIPFKPLC CCCCCEEEEECCCCC	4.85	29575903
1484	Acetylation	KSLCIPFKPLCELQP CEEEEECCCCCCCCC	31.55	26051181
1484	Ubiquitination	KSLCIPFKPLCELQP CEEEEECCCCCCCCC	31.55	33845483
1487	S-palmitoylation	CIPFKPLCELQPGAK EEECCCCCCCCCCCE	7.14	29575903
1494	Ubiquitination	CELQPGAKCVCGKNP CCCCCCCEEEECCCH	32.87	33845483
1499	Ubiquitination	GAKCVCGKNPAKYYT CCEEEECCCHHHEEE	55.41	23000965
1503	Acetylation	VCGKNPAKYYTLFGR EECCCHHHEEEECCC	39.79	19608861
1503	Ubiquitination	VCGKNPAKYYTLFGR EECCCHHHEEEECCC	39.79	23000965
1504	Phosphorylation	CGKNPAKYYTLFGRS ECCCHHHEEEECCCC	12.09	28152594
1505	Phosphorylation	GKNPAKYYTLFGRSY CCCHHHEEEECCCCC	9.03	28152594
1506	Phosphorylation	KNPAKYYTLFGRSY- CCHHHEEEECCCCC-	16.72	28152594
1510	Methylation	KYYTLFGRSY----- HEEEECCCCC-----	26.00	-

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
886	S	Phosphorylation	Kinase	CDK5	Q00535	Uniprot
910	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
999	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
999	S	Phosphorylation	Kinase	P70S6K	P23443	PSP
999	S	Phosphorylation	Kinase	P70S6K ISO2	P23443-2	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
886	S	Phosphorylation	In monocytes, the IFN-gamma-induced sequential phosphorylation at Ser-886 and Ser-999 releases EPRS1 from the aminoacyl-tRNA synthetase multienzyme complex, allowing its association with the GAIT complex.	18669648
886	S	Phosphorylation	Phosphorylated at Ser-886 by CDK5.	18669648
999	S	Phosphorylation	In monocytes, the IFN-gamma-induced sequential phosphorylation at Ser-886 and Ser-999 releases EPRS1 from the aminoacyl-tRNA synthetase multienzyme complex, allowing its association with the GAIT complex.	19647514
999	S	Phosphorylation	Phosphorylated at Ser-999 by RPS6KB1; triggers EPRS1 release from the aminoacyl-tRNA synthetase multienzyme complex.	19647514
999	S	Phosphorylation	Phosphorylation at Ser-999 by RPS6KB1, is also induced by insulin through activation of the mTORC1 signaling pathway and promotes the interaction of EPRS1 with SLC27A1.	19647514
999	S	Phosphorylation	Phosphorylation at Ser-999 is specifically required for the RPL13A-mediated interaction of the GAIT complex with eIF4G.	19647514

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYIC_HUMAN	IARS	physical	9556618
SYRC_HUMAN	RARS	physical	9556618
HS90A_HUMAN	HSP90AA1	physical	10913161
SYK_HUMAN	KARS	physical	22751010
SYIC_HUMAN	IARS	physical	22939629
SYRC_HUMAN	RARS	physical	22939629
SYK_HUMAN	KARS	physical	22939629
SYLC_HUMAN	LARS	physical	22939629
SYQ_HUMAN	QARS	physical	22939629
SYMC_HUMAN	MARS	physical	22939629
GARS_HUMAN	GARS	physical	22939629
TCPA_HUMAN	TCP1	physical	22939629
SYNC_HUMAN	NARS	physical	22939629
TRM1_HUMAN	TRMT1	physical	22939629
TXLNA_HUMAN	TXLNA	physical	22939629
TBB5_HUMAN	TUBB	physical	22939629
UBA1_HUMAN	UBA1	physical	22939629
XPO1_HUMAN	XPO1	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
CMYA5_HUMAN	CMYA5	physical	22863883
SYIC_HUMAN	IARS	physical	22863883
IF2B3_HUMAN	IGF2BP3	physical	22863883
PTBP1_HUMAN	PTBP1	physical	22863883
RFC4_HUMAN	RFC4	physical	22863883
RL23A_HUMAN	RPL23A	physical	22863883
AIMP1_HUMAN	AIMP1	physical	26344197
AIMP2_HUMAN	AIMP2	physical	26344197
ATD3B_HUMAN	ATAD3B	physical	26344197
CALX_HUMAN	CANX	physical	26344197
CLGN_HUMAN	CLGN	physical	26344197
MCA3_HUMAN	EEF1E1	physical	26344197
IDH3A_HUMAN	IDH3A	physical	26344197
IPO9_HUMAN	IPO9	physical	26344197
KDSR_HUMAN	KDSR	physical	26344197
NCLN_HUMAN	NCLN	physical	26344197
NMD3_HUMAN	NMD3	physical	26344197
PSMD2_HUMAN	PSMD2	physical	26344197
RPN2_HUMAN	RPN2	physical	26344197
STOM_HUMAN	STOM	physical	26344197
SYTC2_HUMAN	TARSL2	physical	26344197
TRM6_HUMAN	TRMT6	physical	26344197
XPO1_HUMAN	XPO1	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00172: L-Proline

Related Literatures of Post-Translational Modification

Acetylation

"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-300; LYS-417; LYS-498;LYS-535; LYS-542; LYS-637; LYS-788; LYS-1156 AND LYS-1503, AND MASSSPECTROMETRY.
PubMed: 19608861

Malonylation

"The first identification of lysine malonylation substrates and itsregulatory enzyme.";
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.;
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
Cited for: MALONYLATION AT LYS-300.
PubMed: 21908771

N6-malonyllysine

"The first identification of lysine malonylation substrates and itsregulatory enzyme.";
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.;
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
Cited for: MALONYLATION AT LYS-300.
PubMed: 21908771

Phosphorylation

"Phosphorylation of glutamyl-prolyl tRNA synthetase by cyclin-dependent kinase 5 dictates transcript-selective translationalcontrol.";
Arif A., Jia J., Moodt R.A., DiCorleto P.E., Fox P.L.;
Proc. Natl. Acad. Sci. U.S.A. 108:1415-1420(2011).
Cited for: PHOSPHORYLATION AT SER-886.
PubMed: 21220307

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-886 ANDSER-891, AND MASS SPECTROMETRY.
PubMed: 19690332

"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-885 ANDSER-886, AND MASS SPECTROMETRY.
PubMed: 19369195

"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-880; SER-882; SER-883;SER-885; SER-886; THR-888; SER-999 AND SER-1000, AND MASSSPECTROMETRY.
PubMed: 19413330

"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 TYR-872; SER-882; SER-883;SER-885; SER-886; SER-891 AND THR-898, AND MASS SPECTROMETRY.
PubMed: 18669648

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, AND MASSSPECTROMETRY.
PubMed: 18691976

"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886 AND THR-888, ANDMASS SPECTROMETRY.
PubMed: 18220336

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-885; SER-886 ANDSER-891, AND MASS SPECTROMETRY.
PubMed: 17287340

"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, AND MASSSPECTROMETRY.
PubMed: 17924679

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-898 AND SER-1000, ANDMASS SPECTROMETRY.
PubMed: 15302935

"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-898, AND MASSSPECTROMETRY.
PubMed: 16964243