ECHB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ECHB_HUMAN
• UniProt AC: P55084
• Protein Name: Trifunctional enzyme subunit beta, mitochondrial
• Gene Name: HADHB
• Organism: Homo sapiens (Human).
• Sequence Length: 474
• Subcellular Localization: Mitochondrion . Mitochondrion inner membrane . Mitochondrion outer membrane . Endoplasmic reticulum .
• Protein Sequence: MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAPAVQTKTKKTLAKPNIRNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGQRLSLISKFRFNFLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSDVVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK

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
22	Phosphorylation	SKWALRFSIRPLSCS CHHHHHEECCCCCCC	15.97	29496963
40	Phosphorylation	RAAPAVQTKTKKTLA HCCCCCCCCCCCCCC	33.80	23612710
42	Phosphorylation	APAVQTKTKKTLAKP CCCCCCCCCCCCCCC	40.95	23612710
48	2-Hydroxyisobutyrylation	KTKKTLAKPNIRNVV CCCCCCCCCCCCCEE	41.53	-
48	Malonylation	KTKKTLAKPNIRNVV CCCCCCCCCCCCCEE	41.53	26320211
50	Acetylation	KKTLAKPNIRNVVVV CCCCCCCCCCCEEEE	45.18	-
50	Ubiquitination	KKTLAKPNIRNVVVV CCCCCCCCCCCEEEE	45.18	-
50	Acetylation	KKTLAKPNIRNVVVV CCCCCCCCCCCEEEE	45.18	19608861
50	Ubiquitination	KKTLAKPNIRNVVVV CCCCCCCCCCCEEEE	45.18	19608861
67	Phosphorylation	VRTPFLLSGTSYKDL CCCCEECCCCCHHHC	42.02	27251275
69	Phosphorylation	TPFLLSGTSYKDLMP CCEECCCCCHHHCCH	26.05	28857561
70	Phosphorylation	PFLLSGTSYKDLMPH CEECCCCCHHHCCHH	33.44	28857561
71	Phosphorylation	FLLSGTSYKDLMPHD EECCCCCHHHCCHHH	14.36	27251275
72	Ubiquitination	LLSGTSYKDLMPHDL ECCCCCHHHCCHHHH	44.12	21890473
72	2-Hydroxyisobutyrylation	LLSGTSYKDLMPHDL ECCCCCHHHCCHHHH	44.12	-
72	Acetylation	LLSGTSYKDLMPHDL ECCCCCHHHCCHHHH	44.12	19608861
72	Malonylation	LLSGTSYKDLMPHDL ECCCCCHHHCCHHHH	44.12	26320211
72	Succinylation	LLSGTSYKDLMPHDL ECCCCCHHHCCHHHH	44.12	-
72	Succinylation	LLSGTSYKDLMPHDL ECCCCCHHHCCHHHH	44.12	-
72	Ubiquitination	LLSGTSYKDLMPHDL ECCCCCHHHCCHHHH	44.12	21890473
75	Sulfoxidation	GTSYKDLMPHDLARA CCCHHHCCHHHHHHH	3.87	28183972
91	Phosphorylation	LTGLLHRTSVPKEVV HHHHHHHCCCCHHHH	24.27	-
95	Acetylation	LHRTSVPKEVVDYII HHHCCCCHHHHHHHH	62.07	25038526
100	Phosphorylation	VPKEVVDYIIFGTVI CCHHHHHHHHHHHHH	5.59	-
111	Acetylation	GTVIQEVKTSNVARE HHHHHHHHCCHHHHH	45.54	25038526
166	Acetylation	VIVAGGVELMSDVPI EEEECCEEECCCCCC	41.87	-
166	Acetylation	VIVAGGVELMSDVPI EEEECCEEECCCCCC	41.87	19608861
179	Acetylation	PIRHSRKMRKLMLDL CCCCCHHHHHHHHHH	4.43	-
181	Acetylation	RHSRKMRKLMLDLNK CCCHHHHHHHHHHHH	34.45	21339330
181	Malonylation	RHSRKMRKLMLDLNK CCCHHHHHHHHHHHH	34.45	26320211
188	2-Hydroxyisobutyrylation	KLMLDLNKAKSMGQR HHHHHHHHHHHHHHH	65.57	-
188	Acetylation	KLMLDLNKAKSMGQR HHHHHHHHHHHHHHH	65.57	19608861
188	Malonylation	KLMLDLNKAKSMGQR HHHHHHHHHHHHHHH	65.57	26320211
188	Succinylation	KLMLDLNKAKSMGQR HHHHHHHHHHHHHHH	65.57	-
188	Succinylation	KLMLDLNKAKSMGQR HHHHHHHHHHHHHHH	65.57	27452117
190	2-Hydroxyisobutyrylation	MLDLNKAKSMGQRLS HHHHHHHHHHHHHHH	42.45	-
190	Acetylation	MLDLNKAKSMGQRLS HHHHHHHHHHHHHHH	42.45	25038526
190	Malonylation	MLDLNKAKSMGQRLS HHHHHHHHHHHHHHH	42.45	26320211
190	Succinylation	MLDLNKAKSMGQRLS HHHHHHHHHHHHHHH	42.45	-
190	Succinylation	MLDLNKAKSMGQRLS HHHHHHHHHHHHHHH	42.45	-
191	Phosphorylation	LDLNKAKSMGQRLSL HHHHHHHHHHHHHHH	32.76	23882029
197	Phosphorylation	KSMGQRLSLISKFRF HHHHHHHHHHHHHCC	26.33	24719451
200	Phosphorylation	GQRLSLISKFRFNFL HHHHHHHHHHCCCHH	30.91	26853621
201	2-Hydroxyisobutyrylation	QRLSLISKFRFNFLA HHHHHHHHHCCCHHC	33.30	-
201	Acetylation	QRLSLISKFRFNFLA HHHHHHHHHCCCHHC	33.30	25825284
201	Malonylation	QRLSLISKFRFNFLA HHHHHHHHHCCCHHC	33.30	26320211
244	Phosphorylation	SRLEQDEYALRSHSL HHHHHHHHHHHHCHH	21.16	-
246	Ubiquitination	LEQDEYALRSHSLAK HHHHHHHHHHCHHHH	5.89	-
247	Methylation	EQDEYALRSHSLAKK HHHHHHHHHCHHHHH	24.93	-
248	Phosphorylation	QDEYALRSHSLAKKA HHHHHHHHCHHHHHH	20.48	26699800
250	Phosphorylation	EYALRSHSLAKKAQD HHHHHHCHHHHHHHH	31.13	26699800
253	2-Hydroxyisobutyrylation	LRSHSLAKKAQDEGL HHHCHHHHHHHHCCC	54.67	-
253	Acetylation	LRSHSLAKKAQDEGL HHHCHHHHHHHHCCC	54.67	6271151
254	2-Hydroxyisobutyrylation	RSHSLAKKAQDEGLL HHCHHHHHHHHCCCC	45.75	-
254	Ubiquitination	RSHSLAKKAQDEGLL HHCHHHHHHHHCCCC	45.75	-
262	Phosphorylation	AQDEGLLSDVVPFKV HHHCCCCCCCCCEEC	33.14	20068231
268	Ubiquitination	LSDVVPFKVPGKDTV CCCCCCEECCCCCCC	41.26	21890473
268	Acetylation	LSDVVPFKVPGKDTV CCCCCCEECCCCCCC	41.26	25038526
268	Ubiquitination	LSDVVPFKVPGKDTV CCCCCCEECCCCCCC	41.26	21890473
269	Acetylation	SDVVPFKVPGKDTVT CCCCCEECCCCCCCC	8.48	-
269	Acetylation	SDVVPFKVPGKDTVT CCCCCEECCCCCCCC	8.48	19608861
271	Acetylation	VVPFKVPGKDTVTKD CCCEECCCCCCCCCC	43.38	-
272	2-Hydroxyisobutyrylation	VPFKVPGKDTVTKDN CCEECCCCCCCCCCC	44.12	-
272	Acetylation	VPFKVPGKDTVTKDN CCEECCCCCCCCCCC	44.12	23954790
272	Malonylation	VPFKVPGKDTVTKDN CCEECCCCCCCCCCC	44.12	26320211
272	Succinylation	VPFKVPGKDTVTKDN CCEECCCCCCCCCCC	44.12	-
272	Succinylation	VPFKVPGKDTVTKDN CCEECCCCCCCCCCC	44.12	27452117
272	Ubiquitination	VPFKVPGKDTVTKDN CCEECCCCCCCCCCC	44.12	-
277	Acetylation	PGKDTVTKDNGIRPS CCCCCCCCCCCCCCC	44.88	25953088
277	Malonylation	PGKDTVTKDNGIRPS CCCCCCCCCCCCCCC	44.88	26320211
284	Phosphorylation	KDNGIRPSSLEQMAK CCCCCCCCHHHHHHH	37.39	24275569
285	Phosphorylation	DNGIRPSSLEQMAKL CCCCCCCHHHHHHHH	38.31	24275569
291	Acetylation	SSLEQMAKLKPAFIK CHHHHHHHHCCCCCC	52.26	23954790
291	Succinylation	SSLEQMAKLKPAFIK CHHHHHHHHCCCCCC	52.26	-
291	Succinylation	SSLEQMAKLKPAFIK CHHHHHHHHCCCCCC	52.26	-
293	Acetylation	LEQMAKLKPAFIKPY HHHHHHHCCCCCCCC	33.33	23954790
293	Malonylation	LEQMAKLKPAFIKPY HHHHHHHCCCCCCCC	33.33	26320211
293	Succinylation	LEQMAKLKPAFIKPY HHHHHHHCCCCCCCC	33.33	-
293	Succinylation	LEQMAKLKPAFIKPY HHHHHHHCCCCCCCC	33.33	-
298	Acetylation	KLKPAFIKPYGTVTA HHCCCCCCCCCEEEE	26.23	25038526
300	Phosphorylation	KPAFIKPYGTVTAAN CCCCCCCCCEEEECC	22.04	20068231
302	Phosphorylation	AFIKPYGTVTAANSS CCCCCCCEEEECCCC	14.61	20068231
304	Phosphorylation	IKPYGTVTAANSSFL CCCCCEEEECCCCCC	21.64	20068231
308	Phosphorylation	GTVTAANSSFLTDGA CEEEECCCCCCCCCC	20.10	20068231
309	Phosphorylation	TVTAANSSFLTDGAS EEEECCCCCCCCCCC	24.88	20068231
312	Phosphorylation	AANSSFLTDGASAML ECCCCCCCCCCCEEE	30.31	20068231
316	Phosphorylation	SFLTDGASAMLIMAE CCCCCCCCEEEEHHH	21.53	20068231
326	Acetylation	LIMAEEKALAMGYKP EEHHHHHHHHCCCCC	12.11	-
332	Acetylation	KALAMGYKPKAYLRD HHHHCCCCCCHHHCC	34.02	25953088
332	Malonylation	KALAMGYKPKAYLRD HHHHCCCCCCHHHCC	34.02	26320211
332	Succinylation	KALAMGYKPKAYLRD HHHHCCCCCCHHHCC	34.02	-
332	Succinylation	KALAMGYKPKAYLRD HHHHCCCCCCHHHCC	34.02	-
334	Malonylation	LAMGYKPKAYLRDFM HHCCCCCCHHHCCCE	45.57	26320211
336	Phosphorylation	MGYKPKAYLRDFMYV CCCCCCHHHCCCEEE	14.38	-
342	Phosphorylation	AYLRDFMYVSQDPKD HHHCCCEEECCCCCC	9.28	28258704
344	Phosphorylation	LRDFMYVSQDPKDQL HCCCEEECCCCCCCE	16.04	28258704
348	2-Hydroxyisobutyrylation	MYVSQDPKDQLLLGP EEECCCCCCCEECCC	67.41	-
348	Acetylation	MYVSQDPKDQLLLGP EEECCCCCCCEECCC	67.41	23236377
348	Ubiquitination	MYVSQDPKDQLLLGP EEECCCCCCCEECCC	67.41	-
356	Phosphorylation	DQLLLGPTYATPKVL CCEECCCCCCCHHHH	24.80	28152594
357	Phosphorylation	QLLLGPTYATPKVLE CEECCCCCCCHHHHH	16.18	28152594
359	Phosphorylation	LLGPTYATPKVLEKA ECCCCCCCHHHHHHC	17.15	28152594
361	Acetylation	GPTYATPKVLEKAGL CCCCCCHHHHHHCCC	55.91	-
361	Ubiquitination	GPTYATPKVLEKAGL CCCCCCHHHHHHCCC	55.91	-
395	Phosphorylation	ANFKAMDSDWFAENY HHHCCCCCHHHHHHH	24.53	-
408	Ubiquitination	NYMGRKTKVGLPPLE HHCCCCCCCCCCCHH	37.02	-
416	Acetylation	VGLPPLEKFNNWGGS CCCCCHHHCCCCCCC	62.16	25038526
423	Phosphorylation	KFNNWGGSLSLGHPF HCCCCCCCCCCCCCC	15.73	27080861
425	Phosphorylation	NNWGGSLSLGHPFGA CCCCCCCCCCCCCCH	33.72	27080861
447	Acetylation	AAANRLRKEGGQYGL HHHHHHHHCCCCCHH	66.36	25038526
447	Malonylation	AAANRLRKEGGQYGL HHHHHHHHCCCCCHH	66.36	26320211

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ECHB_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 ECHB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HS90B_HUMAN	HSP90AB1	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
OPA1_HUMAN	OPA1	physical	22939629
TBB1_HUMAN	TUBB1	physical	22939629
SUOX_HUMAN	SUOX	physical	21988832
TIM8B_HUMAN	TIMM8B	physical	21988832
AT1A1_HUMAN	ATP1A1	physical	26344197
AT1B1_HUMAN	ATP1B1	physical	26344197
OST48_HUMAN	DDOST	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
GPC1_HUMAN	GPC1	physical	28514442
CQ080_HUMAN	C17orf80	physical	28514442
ECHA_HUMAN	HADHA	physical	28514442
POTEI_HUMAN	POTEI	physical	28514442

Drug and Disease Associations

• Kegg Disease
• H00525: Disorders of fatty-acid oxidation, including: Medium-chain (MC) acyl-CoA dehydrogenase (AD) deficien
• OMIM Disease
• 609015: Mitochondrial trifunctional protein deficiency (MTPD)
• 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-72 AND LYS-188, AND MASSSPECTROMETRY.
PubMed: 19608861