ECHA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ECHA_HUMAN
• UniProt AC: P40939
• Protein Name: Trifunctional enzyme subunit alpha, mitochondrial
• Gene Name: HADHA
• Organism: Homo sapiens (Human).
• Sequence Length: 763
• Subcellular Localization: Mitochondrion.
• Protein Description: Bifunctional subunit..
• Protein Sequence: MVACRAIGILSRFSAFRILRSRGYICRNFTGSSALLTRTHINYGVKGDVAVVRINSPNSKVNTLSKELHSEFSEVMNEIWASDQIRSAVLISSKPGCFIAGADINMLAACKTLQEVTQLSQEAQRIVEKLEKSTKPIVAAINGSCLGGGLEVAISCQYRIATKDRKTVLGTPEVLLGALPGAGGTQRLPKMVGVPAALDMMLTGRSIRADRAKKMGLVDQLVEPLGPGLKPPEERTIEYLEEVAITFAKGLADKKISPKRDKGLVEKLTAYAMTIPFVRQQVYKKVEEKVRKQTKGLYPAPLKIIDVVKTGIEQGSDAGYLCESQKFGELVMTKESKALMGLYHGQVLCKKNKFGAPQKDVKHLAILGAGLMGAGIAQVSVDKGLKTILKDATLTALDRGQQQVFKGLNDKVKKKALTSFERDSIFSNLTGQLDYQGFEKADMVIEAVFEDLSLKHRVLKEVEAVIPDHCIFASNTSALPISEIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTEKTSKDTSASAVAVGLKQGKVIIVVKDGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDSLTTSFGFPVGAATLVDEVGVDVAKHVAEDLGKVFGERFGGGNPELLTQMVSKGFLGRKSGKGFYIYQEGVKRKDLNSDMDSILASLKLPPKSEVSSDEDIQFRLVTRFVNEAVMCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRFVDLYGAQKIVDRLKKYEAAYGKQFTPCQLLADHANSPNKKFYQ

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
42	Acetylation	LLTRTHINYGVKGDV EEECCEECCCCCCCE	21.65	-
43	Phosphorylation	LTRTHINYGVKGDVA EECCEECCCCCCCEE	23.77	28152594
46	2-Hydroxyisobutyrylation	THINYGVKGDVAVVR CEECCCCCCCEEEEE	45.06	-
46	Acetylation	THINYGVKGDVAVVR CEECCCCCCCEEEEE	45.06	-
46	Malonylation	THINYGVKGDVAVVR CEECCCCCCCEEEEE	45.06	26320211
46	Succinylation	THINYGVKGDVAVVR CEECCCCCCCEEEEE	45.06	-
46	Succinylation	THINYGVKGDVAVVR CEECCCCCCCEEEEE	45.06	23954790
56	Phosphorylation	VAVVRINSPNSKVNT EEEEEECCCCHHHHH	24.08	27067055
59	Phosphorylation	VRINSPNSKVNTLSK EEECCCCHHHHHHHH	41.17	28857561
60	2-Hydroxyisobutyrylation	RINSPNSKVNTLSKE EECCCCHHHHHHHHH	46.26	-
60	Acetylation	RINSPNSKVNTLSKE EECCCCHHHHHHHHH	46.26	25953088
60	Malonylation	RINSPNSKVNTLSKE EECCCCHHHHHHHHH	46.26	26320211
60	Succinylation	RINSPNSKVNTLSKE EECCCCHHHHHHHHH	46.26	-
60	Succinylation	RINSPNSKVNTLSKE EECCCCHHHHHHHHH	46.26	27452117
60	Ubiquitination	RINSPNSKVNTLSKE EECCCCHHHHHHHHH	46.26	-
63	Phosphorylation	SPNSKVNTLSKELHS CCCHHHHHHHHHHHH	35.08	28857561
66	Acetylation	SKVNTLSKELHSEFS HHHHHHHHHHHHHHH	68.36	25038526
79	Ubiquitination	FSEVMNEIWASDQIR HHHHHHHHHCHHHHH	2.94	-
117	Phosphorylation	CKTLQEVTQLSQEAQ HHHHHHHHHHHHHHH	24.04	-
120	O-linked_Glycosylation	LQEVTQLSQEAQRIV HHHHHHHHHHHHHHH	19.02	32119511
120	Phosphorylation	LQEVTQLSQEAQRIV HHHHHHHHHHHHHHH	19.02	-
127	Ubiquitination	SQEAQRIVEKLEKST HHHHHHHHHHHHHCC	6.05	-
129	2-Hydroxyisobutyrylation	EAQRIVEKLEKSTKP HHHHHHHHHHHCCCC	51.56	-
129	Acetylation	EAQRIVEKLEKSTKP HHHHHHHHHHHCCCC	51.56	19608861
129	Ubiquitination	EAQRIVEKLEKSTKP HHHHHHHHHHHCCCC	51.56	19608861
143	Ubiquitination	PIVAAINGSCLGGGL CEEEEECCCCCCCHH	17.39	-
163	Acetylation	CQYRIATKDRKTVLG EEEEEECCCCCEEEC	46.65	6570153
166	Acetylation	RIATKDRKTVLGTPE EEECCCCCEEECCHH	53.79	25038526
166	Malonylation	RIATKDRKTVLGTPE EEECCCCCEEECCHH	53.79	26320211
166	Succinylation	RIATKDRKTVLGTPE EEECCCCCEEECCHH	53.79	-
166	Succinylation	RIATKDRKTVLGTPE EEECCCCCEEECCHH	53.79	-
166	Ubiquitination	RIATKDRKTVLGTPE EEECCCCCEEECCHH	53.79	-
167	Phosphorylation	IATKDRKTVLGTPEV EECCCCCEEECCHHH	23.12	21406692
171	Phosphorylation	DRKTVLGTPEVLLGA CCCEEECCHHHHHCC	16.47	21406692
185	Phosphorylation	ALPGAGGTQRLPKMV CCCCCCCCCCCCHHH	15.03	21406692
191	Sulfoxidation	GTQRLPKMVGVPAAL CCCCCCHHHCCCHHH	2.75	28465586
202	Acetylation	PAALDMMLTGRSIRA CHHHHHHHHCCCHHH	3.54	-
203	Phosphorylation	AALDMMLTGRSIRAD HHHHHHHHCCCHHHH	16.80	21406692
206	Phosphorylation	DMMLTGRSIRADRAK HHHHHCCCHHHHHHH	20.12	21406692
208	Acetylation	MLTGRSIRADRAKKM HHHCCCHHHHHHHHC	31.51	-
213	Succinylation	SIRADRAKKMGLVDQ CHHHHHHHHCCHHHH	44.16	-
213	Succinylation	SIRADRAKKMGLVDQ CHHHHHHHHCCHHHH	44.16	-
214	2-Hydroxyisobutyrylation	IRADRAKKMGLVDQL HHHHHHHHCCHHHHH	36.90	-
214	Acetylation	IRADRAKKMGLVDQL HHHHHHHHCCHHHHH	36.90	25038526
214	Malonylation	IRADRAKKMGLVDQL HHHHHHHHCCHHHHH	36.90	26320211
214	Succinylation	IRADRAKKMGLVDQL HHHHHHHHCCHHHHH	36.90	-
214	Succinylation	IRADRAKKMGLVDQL HHHHHHHHCCHHHHH	36.90	27452117
214	Ubiquitination	IRADRAKKMGLVDQL HHHHHHHHCCHHHHH	36.90	-
216	Acetylation	ADRAKKMGLVDQLVE HHHHHHCCHHHHHCC	31.28	-
216	Ubiquitination	ADRAKKMGLVDQLVE HHHHHHCCHHHHHCC	31.28	21890473
230	Succinylation	EPLGPGLKPPEERTI CCCCCCCCCCHHHHH	65.52	-
230	Succinylation	EPLGPGLKPPEERTI CCCCCCCCCCHHHHH	65.52	-
230	Ubiquitination	EPLGPGLKPPEERTI CCCCCCCCCCHHHHH	65.52	-
239	Phosphorylation	PEERTIEYLEEVAIT CHHHHHHHHHHHHHH	18.63	-
249	Acetylation	EVAITFAKGLADKKI HHHHHHHHCCCCCCC	50.71	25825284
249	Succinylation	EVAITFAKGLADKKI HHHHHHHHCCCCCCC	50.71	-
249	Succinylation	EVAITFAKGLADKKI HHHHHHHHCCCCCCC	50.71	-
257	Phosphorylation	GLADKKISPKRDKGL CCCCCCCCCCCCCCH	32.99	23312004
259	Acetylation	ADKKISPKRDKGLVE CCCCCCCCCCCCHHH	67.45	2403921
262	2-Hydroxyisobutyrylation	KISPKRDKGLVEKLT CCCCCCCCCHHHHHH	59.17	-
262	Acetylation	KISPKRDKGLVEKLT CCCCCCCCCHHHHHH	59.17	25038526
269	Phosphorylation	KGLVEKLTAYAMTIP CCHHHHHHHHHHHHH	28.79	24505115
283	Phosphorylation	PFVRQQVYKKVEEKV HHHHHHHHHHHHHHH	10.76	28258704
285	Acetylation	VRQQVYKKVEEKVRK HHHHHHHHHHHHHHH	36.87	30582557
289	2-Hydroxyisobutyrylation	VYKKVEEKVRKQTKG HHHHHHHHHHHHCCC	33.56	-
289	Acetylation	VYKKVEEKVRKQTKG HHHHHHHHHHHHCCC	33.56	23749302
292	Malonylation	KVEEKVRKQTKGLYP HHHHHHHHHCCCCCC	66.36	26320211
294	Phosphorylation	EEKVRKQTKGLYPAP HHHHHHHCCCCCCCC	30.07	24719451
295	Acetylation	EKVRKQTKGLYPAPL HHHHHHCCCCCCCCC	44.41	19608861
295	Malonylation	EKVRKQTKGLYPAPL HHHHHHCCCCCCCCC	44.41	26320211
295	Succinylation	EKVRKQTKGLYPAPL HHHHHHCCCCCCCCC	44.41	27452117
298	Phosphorylation	RKQTKGLYPAPLKII HHHCCCCCCCCCEEE	13.15	24719451
303	2-Hydroxyisobutyrylation	GLYPAPLKIIDVVKT CCCCCCCEEEEEECC	36.23	-
303	Acetylation	GLYPAPLKIIDVVKT CCCCCCCEEEEEECC	36.23	19608861
303	Malonylation	GLYPAPLKIIDVVKT CCCCCCCEEEEEECC	36.23	30639696
303	Succinylation	GLYPAPLKIIDVVKT CCCCCCCEEEEEECC	36.23	-
303	Succinylation	GLYPAPLKIIDVVKT CCCCCCCEEEEEECC	36.23	21890473
303	Ubiquitination	GLYPAPLKIIDVVKT CCCCCCCEEEEEECC	36.23	21890473
303	Ubiquitination	GLYPAPLKIIDVVKT CCCCCCCEEEEEECC	36.23	21890473
303	Ubiquitination	GLYPAPLKIIDVVKT CCCCCCCEEEEEECC	36.23	21890473
303	Ubiquitination	GLYPAPLKIIDVVKT CCCCCCCEEEEEECC	36.23	21890473
309	2-Hydroxyisobutyrylation	LKIIDVVKTGIEQGS CEEEEEECCCCCCCC	40.66	-
309	Acetylation	LKIIDVVKTGIEQGS CEEEEEECCCCCCCC	40.66	26051181
309	Ubiquitination	LKIIDVVKTGIEQGS CEEEEEECCCCCCCC	40.66	-
310	Phosphorylation	KIIDVVKTGIEQGSD EEEEEECCCCCCCCC	31.61	27251275
316	Phosphorylation	KTGIEQGSDAGYLCE CCCCCCCCCCCCEEC	24.79	28152594
320	Phosphorylation	EQGSDAGYLCESQKF CCCCCCCCEECCCCC	15.20	27251275
322	Glutathionylation	GSDAGYLCESQKFGE CCCCCCEECCCCCCC	3.39	22555962
322	S-nitrosylation	GSDAGYLCESQKFGE CCCCCCEECCCCCCC	3.39	2212679
324	Phosphorylation	DAGYLCESQKFGELV CCCCEECCCCCCCEE	37.36	27251275
326	Acetylation	GYLCESQKFGELVMT CCEECCCCCCCEEEE	65.69	23954790
326	Malonylation	GYLCESQKFGELVMT CCEECCCCCCCEEEE	65.69	26320211
326	Succinylation	GYLCESQKFGELVMT CCEECCCCCCCEEEE	65.69	-
326	Succinylation	GYLCESQKFGELVMT CCEECCCCCCCEEEE	65.69	-
332	Sulfoxidation	QKFGELVMTKESKAL CCCCCEEEEHHHHHH	7.47	21406390
333	Phosphorylation	KFGELVMTKESKALM CCCCEEEEHHHHHHH	24.95	29759185
334	Acetylation	FGELVMTKESKALMG CCCEEEEHHHHHHHH	41.73	25953088
334	Malonylation	FGELVMTKESKALMG CCCEEEEHHHHHHHH	41.73	26320211
334	Succinylation	FGELVMTKESKALMG CCCEEEEHHHHHHHH	41.73	-
334	Succinylation	FGELVMTKESKALMG CCCEEEEHHHHHHHH	41.73	23954790
334	Ubiquitination	FGELVMTKESKALMG CCCEEEEHHHHHHHH	41.73	-
337	Acetylation	LVMTKESKALMGLYH EEEEHHHHHHHHHHC	46.78	25038526
337	Malonylation	LVMTKESKALMGLYH EEEEHHHHHHHHHHC	46.78	26320211
350	2-Hydroxyisobutyrylation	YHGQVLCKKNKFGAP HCCEEEECCCCCCCC	56.04	-
350	Acetylation	YHGQVLCKKNKFGAP HCCEEEECCCCCCCC	56.04	23954790
350	Malonylation	YHGQVLCKKNKFGAP HCCEEEECCCCCCCC	56.04	26320211
350	Succinylation	YHGQVLCKKNKFGAP HCCEEEECCCCCCCC	56.04	-
350	Succinylation	YHGQVLCKKNKFGAP HCCEEEECCCCCCCC	56.04	27452117
350	Ubiquitination	YHGQVLCKKNKFGAP HCCEEEECCCCCCCC	56.04	-
351	Acetylation	HGQVLCKKNKFGAPQ CCEEEECCCCCCCCH	65.46	2402799
353	Acetylation	QVLCKKNKFGAPQKD EEEECCCCCCCCHHH	54.80	19608861
353	Ubiquitination	QVLCKKNKFGAPQKD EEEECCCCCCCCHHH	54.80	19608861
359	Acetylation	NKFGAPQKDVKHLAI CCCCCCHHHHHHHHH	64.53	19608861
359	Malonylation	NKFGAPQKDVKHLAI CCCCCCHHHHHHHHH	64.53	26320211
359	Succinylation	NKFGAPQKDVKHLAI CCCCCCHHHHHHHHH	64.53	23954790
359	Ubiquitination	NKFGAPQKDVKHLAI CCCCCCHHHHHHHHH	64.53	19608861
362	2-Hydroxyisobutyrylation	GAPQKDVKHLAILGA CCCHHHHHHHHHHCC	42.93	-
362	Acetylation	GAPQKDVKHLAILGA CCCHHHHHHHHHHCC	42.93	25038526
383	Acetylation	IAQVSVDKGLKTILK EEEEECCCCHHHHHH	65.08	25038526
383	Malonylation	IAQVSVDKGLKTILK EEEEECCCCHHHHHH	65.08	26320211
383	Ubiquitination	IAQVSVDKGLKTILK EEEEECCCCHHHHHH	65.08	-
386	2-Hydroxyisobutyrylation	VSVDKGLKTILKDAT EECCCCHHHHHHHCC	42.03	-
386	Malonylation	VSVDKGLKTILKDAT EECCCCHHHHHHHCC	42.03	26320211
387	Phosphorylation	SVDKGLKTILKDATL ECCCCHHHHHHHCCC	36.26	-
390	2-Hydroxyisobutyrylation	KGLKTILKDATLTAL CCHHHHHHHCCCHHH	41.27	-
390	Acetylation	KGLKTILKDATLTAL CCHHHHHHHCCCHHH	41.27	20167786
390	Succinylation	KGLKTILKDATLTAL CCHHHHHHHCCCHHH	41.27	23954790
390	Ubiquitination	KGLKTILKDATLTAL CCHHHHHHHCCCHHH	41.27	-
393	Phosphorylation	KTILKDATLTALDRG HHHHHHCCCHHHHHH	34.47	28857561
395	Phosphorylation	ILKDATLTALDRGQQ HHHHCCCHHHHHHHH	22.33	21815630
399	Methylation	ATLTALDRGQQQVFK CCCHHHHHHHHHHHH	45.75	-
406	2-Hydroxyisobutyrylation	RGQQQVFKGLNDKVK HHHHHHHHCCCHHHH	64.73	-
406	Acetylation	RGQQQVFKGLNDKVK HHHHHHHHCCCHHHH	64.73	19608861
406	Malonylation	RGQQQVFKGLNDKVK HHHHHHHHCCCHHHH	64.73	26320211
406	Succinylation	RGQQQVFKGLNDKVK HHHHHHHHCCCHHHH	64.73	-
406	Succinylation	RGQQQVFKGLNDKVK HHHHHHHHCCCHHHH	64.73	27452117
406	Ubiquitination	RGQQQVFKGLNDKVK HHHHHHHHCCCHHHH	64.73	19608861
411	Acetylation	VFKGLNDKVKKKALT HHHCCCHHHHHHHHH	55.68	23749302
411	Malonylation	VFKGLNDKVKKKALT HHHCCCHHHHHHHHH	55.68	26320211
411	Succinylation	VFKGLNDKVKKKALT HHHCCCHHHHHHHHH	55.68	-
411	Succinylation	VFKGLNDKVKKKALT HHHCCCHHHHHHHHH	55.68	-
413	Acetylation	KGLNDKVKKKALTSF HCCCHHHHHHHHHHH	55.06	2402063
413	Malonylation	KGLNDKVKKKALTSF HCCCHHHHHHHHHHH	55.06	26320211
414	Malonylation	GLNDKVKKKALTSFE CCCHHHHHHHHHHHH	46.39	26320211
414	Succinylation	GLNDKVKKKALTSFE CCCHHHHHHHHHHHH	46.39	23954790
415	Malonylation	LNDKVKKKALTSFER CCHHHHHHHHHHHHH	42.80	26320211
415	Succinylation	LNDKVKKKALTSFER CCHHHHHHHHHHHHH	42.80	-
415	Succinylation	LNDKVKKKALTSFER CCHHHHHHHHHHHHH	42.80	27452117
415	Ubiquitination	LNDKVKKKALTSFER CCHHHHHHHHHHHHH	42.80	-
418	Phosphorylation	KVKKKALTSFERDSI HHHHHHHHHHHHHHH	35.91	24641631
419	Phosphorylation	VKKKALTSFERDSIF HHHHHHHHHHHHHHH	26.43	25850435
424	Phosphorylation	LTSFERDSIFSNLTG HHHHHHHHHHHHHHC	31.58	27251275
427	Phosphorylation	FERDSIFSNLTGQLD HHHHHHHHHHHCCCC	29.29	21712546
435	Phosphorylation	NLTGQLDYQGFEKAD HHHCCCCCCCHHHHH	21.09	-
440	Succinylation	LDYQGFEKADMVIEA CCCCCHHHHHHHHHH	47.64	-
440	Succinylation	LDYQGFEKADMVIEA CCCCCHHHHHHHHHH	47.64	-
453	Phosphorylation	EAVFEDLSLKHRVLK HHHHHCCCHHHHHHH	47.93	20068231
455	2-Hydroxyisobutyrylation	VFEDLSLKHRVLKEV HHHCCCHHHHHHHHH	26.45	-
455	Ubiquitination	VFEDLSLKHRVLKEV HHHCCCHHHHHHHHH	26.45	-
460	Acetylation	SLKHRVLKEVEAVIP CHHHHHHHHHHHHCC	57.78	26051181
460	Succinylation	SLKHRVLKEVEAVIP CHHHHHHHHHHHHCC	57.78	-
460	Succinylation	SLKHRVLKEVEAVIP CHHHHHHHHHHHHCC	57.78	-
470	Glutathionylation	EAVIPDHCIFASNTS HHHCCCCEEECCCCC	3.40	22555962
474	Phosphorylation	PDHCIFASNTSALPI CCCEEECCCCCCCCH	29.86	25072903
476	Phosphorylation	HCIFASNTSALPISE CEEECCCCCCCCHHH	16.93	25072903
477	Phosphorylation	CIFASNTSALPISEI EEECCCCCCCCHHHH	31.87	25072903
482	Phosphorylation	NTSALPISEIAAVSK CCCCCCHHHHHHHCC	22.47	25072903
488	Phosphorylation	ISEIAAVSKRPEKVI HHHHHHHCCCCCCEE	20.44	25072903
489	Ubiquitination	SEIAAVSKRPEKVIG HHHHHHCCCCCCEEC	66.43	-
493	2-Hydroxyisobutyrylation	AVSKRPEKVIGMHYF HHCCCCCCEECEEEC	41.66	-
493	Ubiquitination	AVSKRPEKVIGMHYF HHCCCCCCEECEEEC	41.66	-
499	Phosphorylation	EKVIGMHYFSPVDKM CCEECEEECCCCCHH	9.25	20068231
501	O-linked_Glycosylation	VIGMHYFSPVDKMQL EECEEECCCCCHHHH	19.49	32119511
501	Phosphorylation	VIGMHYFSPVDKMQL EECEEECCCCCHHHH	19.49	20068231
505	Acetylation	HYFSPVDKMQLLEII EECCCCCHHHHHHHH	28.87	19608861
505	Malonylation	HYFSPVDKMQLLEII EECCCCCHHHHHHHH	28.87	26320211
505	Succinylation	HYFSPVDKMQLLEII EECCCCCHHHHHHHH	28.87	-
505	Succinylation	HYFSPVDKMQLLEII EECCCCCHHHHHHHH	28.87	27452117
506	Sulfoxidation	YFSPVDKMQLLEIIT ECCCCCHHHHHHHHH	2.69	21406390
513	Phosphorylation	MQLLEIITTEKTSKD HHHHHHHHCCCCCCC	34.27	21406692
514	Phosphorylation	QLLEIITTEKTSKDT HHHHHHHCCCCCCCC	25.69	21406692
516	2-Hydroxyisobutyrylation	LEIITTEKTSKDTSA HHHHHCCCCCCCCCC	56.88	-
516	Acetylation	LEIITTEKTSKDTSA HHHHHCCCCCCCCCC	56.88	25038526
519	2-Hydroxyisobutyrylation	ITTEKTSKDTSASAV HHCCCCCCCCCCCCE	70.97	-
519	Acetylation	ITTEKTSKDTSASAV HHCCCCCCCCCCCCE	70.97	23236377
519	Malonylation	ITTEKTSKDTSASAV HHCCCCCCCCCCCCE	70.97	26320211
519	Succinylation	ITTEKTSKDTSASAV HHCCCCCCCCCCCCE	70.97	-
519	Succinylation	ITTEKTSKDTSASAV HHCCCCCCCCCCCCE	70.97	27452117
519	Ubiquitination	ITTEKTSKDTSASAV HHCCCCCCCCCCCCE	70.97	-
521	Phosphorylation	TEKTSKDTSASAVAV CCCCCCCCCCCCEEE	29.90	25072903
522	Phosphorylation	EKTSKDTSASAVAVG CCCCCCCCCCCEEEE	30.29	25072903
524	Phosphorylation	TSKDTSASAVAVGLK CCCCCCCCCEEEEEC	24.04	23911959
531	2-Hydroxyisobutyrylation	SAVAVGLKQGKVIIV CCEEEEECCCEEEEE	51.59	-
531	Acetylation	SAVAVGLKQGKVIIV CCEEEEECCCEEEEE	51.59	25953088
531	Malonylation	SAVAVGLKQGKVIIV CCEEEEECCCEEEEE	51.59	26320211
531	Succinylation	SAVAVGLKQGKVIIV CCEEEEECCCEEEEE	51.59	27452117
531	Ubiquitination	SAVAVGLKQGKVIIV CCEEEEECCCEEEEE	51.59	-
540	2-Hydroxyisobutyrylation	GKVIIVVKDGPGFYT CEEEEEEECCCCCCH	46.18	-
540	Acetylation	GKVIIVVKDGPGFYT CEEEEEEECCCCCCH	46.18	19608861
540	Succinylation	GKVIIVVKDGPGFYT CEEEEEEECCCCCCH	46.18	23954790
546	Phosphorylation	VKDGPGFYTTRCLAP EECCCCCCHHHHHHH	17.08	-
549	Methylation	GPGFYTTRCLAPMMS CCCCCHHHHHHHHHH	12.97	-
550	Glutathionylation	PGFYTTRCLAPMMSE CCCCHHHHHHHHHHH	3.40	22555962
569	2-Hydroxyisobutyrylation	LQEGVDPKKLDSLTT HHCCCCHHHHHHCCC	62.60	-
569	Acetylation	LQEGVDPKKLDSLTT HHCCCCHHHHHHCCC	62.60	23954790
569	Malonylation	LQEGVDPKKLDSLTT HHCCCCHHHHHHCCC	62.60	26320211
569	Succinylation	LQEGVDPKKLDSLTT HHCCCCHHHHHHCCC	62.60	-
569	Succinylation	LQEGVDPKKLDSLTT HHCCCCHHHHHHCCC	62.60	27452117
570	Acetylation	QEGVDPKKLDSLTTS HCCCCHHHHHHCCCC	64.02	25038526
597	Acetylation	EVGVDVAKHVAEDLG HHCHHHHHHHHHHHH	38.16	23236377
605	2-Hydroxyisobutyrylation	HVAEDLGKVFGERFG HHHHHHHHHHHHHHC	41.51	-
605	Acetylation	HVAEDLGKVFGERFG HHHHHHHHHHHHHHC	41.51	23954790
605	Malonylation	HVAEDLGKVFGERFG HHHHHHHHHHHHHHC	41.51	26320211
605	Ubiquitination	HVAEDLGKVFGERFG HHHHHHHHHHHHHHC	41.51	-
620	Phosphorylation	GGNPELLTQMVSKGF CCCHHHHHHHHHCCC	27.52	27251275
624	Phosphorylation	ELLTQMVSKGFLGRK HHHHHHHHCCCCCCC	23.01	24719451
625	Ubiquitination	LLTQMVSKGFLGRKS HHHHHHHCCCCCCCC	42.12	21890473
634	2-Hydroxyisobutyrylation	FLGRKSGKGFYIYQE CCCCCCCCCEEEEEC	53.60	-
634	Succinylation	FLGRKSGKGFYIYQE CCCCCCCCCEEEEEC	53.60	-
634	Succinylation	FLGRKSGKGFYIYQE CCCCCCCCCEEEEEC	53.60	-
634	Ubiquitination	FLGRKSGKGFYIYQE CCCCCCCCCEEEEEC	53.60	-
637	Phosphorylation	RKSGKGFYIYQEGVK CCCCCCEEEEECCCC	13.85	28152594
639	Phosphorylation	SGKGFYIYQEGVKRK CCCCEEEEECCCCHH	6.80	28152594
644	2-Hydroxyisobutyrylation	YIYQEGVKRKDLNSD EEEECCCCHHCCCCC	65.67	-
644	Acetylation	YIYQEGVKRKDLNSD EEEECCCCHHCCCCC	65.67	19608861
644	Malonylation	YIYQEGVKRKDLNSD EEEECCCCHHCCCCC	65.67	26320211
644	Succinylation	YIYQEGVKRKDLNSD EEEECCCCHHCCCCC	65.67	-
644	Succinylation	YIYQEGVKRKDLNSD EEEECCCCHHCCCCC	65.67	27452117
644	Ubiquitination	YIYQEGVKRKDLNSD EEEECCCCHHCCCCC	65.67	-
646	2-Hydroxyisobutyrylation	YQEGVKRKDLNSDMD EECCCCHHCCCCCHH	61.93	-
646	Malonylation	YQEGVKRKDLNSDMD EECCCCHHCCCCCHH	61.93	26320211
646	Succinylation	YQEGVKRKDLNSDMD EECCCCHHCCCCCHH	61.93	-
646	Succinylation	YQEGVKRKDLNSDMD EECCCCHHCCCCCHH	61.93	-
646	Ubiquitination	YQEGVKRKDLNSDMD EECCCCHHCCCCCHH	61.93	-
650	Phosphorylation	VKRKDLNSDMDSILA CCHHCCCCCHHHHHH	41.43	-
652	Sulfoxidation	RKDLNSDMDSILASL HHCCCCCHHHHHHHC	4.34	21406390
660	Acetylation	DSILASLKLPPKSEV HHHHHHCCCCCCCCC	57.35	25038526
664	Acetylation	ASLKLPPKSEVSSDE HHCCCCCCCCCCCCC	58.26	-
664	Succinylation	ASLKLPPKSEVSSDE HHCCCCCCCCCCCCC	58.26	-
664	Succinylation	ASLKLPPKSEVSSDE HHCCCCCCCCCCCCC	58.26	-
665	Phosphorylation	SLKLPPKSEVSSDED HCCCCCCCCCCCCCC	49.34	26437602
668	Phosphorylation	LPPKSEVSSDEDIQF CCCCCCCCCCCCHHH	28.20	-
669	Phosphorylation	PPKSEVSSDEDIQFR CCCCCCCCCCCHHHH	50.63	20833797
724	Phosphorylation	PFRFVDLYGAQKIVD CEEEHHHHCHHHHHH	13.12	28152594
728	2-Hydroxyisobutyrylation	VDLYGAQKIVDRLKK HHHHCHHHHHHHHHH	44.13	-
728	Acetylation	VDLYGAQKIVDRLKK HHHHCHHHHHHHHHH	44.13	23954790
728	Malonylation	VDLYGAQKIVDRLKK HHHHCHHHHHHHHHH	44.13	26320211
728	Succinylation	VDLYGAQKIVDRLKK HHHHCHHHHHHHHHH	44.13	-
728	Succinylation	VDLYGAQKIVDRLKK HHHHCHHHHHHHHHH	44.13	-
728	Ubiquitination	VDLYGAQKIVDRLKK HHHHCHHHHHHHHHH	44.13	2190698
735	2-Hydroxyisobutyrylation	KIVDRLKKYEAAYGK HHHHHHHHHHHHHCC	53.57	-
735	Acetylation	KIVDRLKKYEAAYGK HHHHHHHHHHHHHCC	53.57	27178108
735	Ubiquitination	KIVDRLKKYEAAYGK HHHHHHHHHHHHHCC	53.57	-
742	Acetylation	KYEAAYGKQFTPCQL HHHHHHCCCCCHHHH	29.57	26051181
742	Malonylation	KYEAAYGKQFTPCQL HHHHHHCCCCCHHHH	29.57	30639696
742	Ubiquitination	KYEAAYGKQFTPCQL HHHHHHCCCCCHHHH	29.57	-
745	Phosphorylation	AAYGKQFTPCQLLAD HHHCCCCCHHHHHHH	22.21	23927012
756	Phosphorylation	LLADHANSPNKKFYQ HHHHHCCCCCCCCCC	30.54	29255136
759	Acetylation	DHANSPNKKFYQ--- HHCCCCCCCCCC---	47.87	25953088
759	Succinylation	DHANSPNKKFYQ--- HHCCCCCCCCCC---	47.87	-
759	Succinylation	DHANSPNKKFYQ--- HHCCCCCCCCCC---	47.87	-
760	Acetylation	HANSPNKKFYQ---- HCCCCCCCCCC----	56.81	155823

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ECHB_HUMAN	HADHB	physical	22939629
STT3B_HUMAN	STT3B	physical	22939629
PLOD3_HUMAN	PLOD3	physical	22939629
MOES_HUMAN	MSN	physical	22939629
ETFA_HUMAN	ETFA	physical	22939629
ZFR_HUMAN	ZFR	physical	22939629
TBB4B_HUMAN	TUBB4B	physical	22939629
HNRH1_HUMAN	HNRNPH1	physical	22939629
NR4A1_HUMAN	NR4A1	physical	21988832
ATLA3_HUMAN	ATL3	physical	26344197
AT1B1_HUMAN	ATP1B1	physical	26344197
ECHB_HUMAN	HADHB	physical	26344197
NDUB8_HUMAN	NDUFB8	physical	26344197
TOM40_HUMAN	TOMM40	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 609015: Mitochondrial trifunctional protein deficiency (MTPD)
• 609016: Long-chain 3-hydroxyl-CoA dehydrogenase deficiency (LCHAD deficiency)
• 609016: Maternal acute fatty liver of pregnancy (AFLP)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

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-129; LYS-295; LYS-303;LYS-326; LYS-353; LYS-359; LYS-406; LYS-505; LYS-540 AND LYS-644, ANDMASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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 SER-756, AND MASSSPECTROMETRY.
PubMed: 17081983