dbPTM

ECHP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ECHP_HUMAN
UniProt AC	Q08426
Protein Name	Peroxisomal bifunctional enzyme
Gene Name	EHHADH
Organism	Homo sapiens (Human).
Sequence Length	723
Subcellular Localization	Peroxisome.
Protein Description
Protein Sequence	MAEYTRLHNALALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAPRTFGLTLGHVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDPVEEAIRFAQRVSDQPLESRRLCNKPIQSLPNMDSIFSEALLKMRRQHPGCLAQEACVRAVQAAVQYPYEVGIKKEEELFLYLLQSGQARALQYAFFAERKANKWSTPSGASWKTASARPVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSGPKPRLTSSVKELGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEGSKPEEVDQVLEEFGFKMGPFRVSDLAGLDVGWKSRKGQGLTGPTLLPGTPARKRGNRRYCPIPDVLCELGRFGQKTGKGWYQYDKPLGRIHKPDPWLSKFLSRYRKTHHIEPRTISQDEILERCLYSLINEAFRILGEGIAASPEHIDVVYLHGYGWPRHKGGPMFYASTVGLPTVLEKLQKYYRQNPDIPQLEPSDYLKKLASQGNPPLKEWQSLAGSPSSKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
25	Phosphorylation	NPPVNAISTTLLRDI CCCCCCHHHHHHHHH	16.96	24275569
26	Phosphorylation	PPVNAISTTLLRDIK CCCCCHHHHHHHHHH	18.49	28857561
27	Phosphorylation	PVNAISTTLLRDIKE CCCCHHHHHHHHHHH	19.60	24275569
38	Succinylation	DIKEGLQKAVIDHTI HHHHHHHHHHHHHCE	50.06	-
38	Succinylation	DIKEGLQKAVIDHTI HHHHHHHHHHHHHCE	50.06	-
56	Ubiquitination	VICGAEGKFSAGADI EEECCCCCCCCCCCC	27.87	-
56	Acetylation	VICGAEGKFSAGADI EEECCCCCCCCCCCC	27.87	26051181
67	Phosphorylation	GADIRGFSAPRTFGL CCCCCCCCCCCHHCC	39.94	24719451
153	Phosphorylation	PAALDLITSGRRILA CHHHHHHHHCCHHHH	32.21	-
165	Acetylation	ILADEALKLGILDKV HHHHHHHHHCCHHHH	52.28	20167786
165	Succinylation	ILADEALKLGILDKV HHHHHHHHHCCHHHH	52.28	-
165	Succinylation	ILADEALKLGILDKV HHHHHHHHHCCHHHH	52.28	-
171	Acetylation	LKLGILDKVVNSDPV HHHCCHHHHHCCCHH	44.64	20167786
175	Phosphorylation	ILDKVVNSDPVEEAI CHHHHHCCCHHHHHH	31.51	25072903
195	Phosphorylation	VSDQPLESRRLCNKP HCCCCCHHHHCCCCC	30.31	24275569
219	Acetylation	IFSEALLKMRRQHPG HHHHHHHHHHHHCCC	31.07	71123
219	Succinylation	IFSEALLKMRRQHPG HHHHHHHHHHHHCCC	31.07	-
219	Succinylation	IFSEALLKMRRQHPG HHHHHHHHHHHHCCC	31.07	-
243	Phosphorylation	AVQAAVQYPYEVGIK HHHHHHCCCHHCCCC	10.94	-
250	Acetylation	YPYEVGIKKEEELFL CCHHCCCCCHHHHHH	48.48	-
280	Malonylation	FAERKANKWSTPSGA HHHHHCCCCCCCCCC	47.59	26320211
280	Acetylation	FAERKANKWSTPSGA HHHHHCCCCCCCCCC	47.59	23236377
280	Succinylation	FAERKANKWSTPSGA HHHHHCCCCCCCCCC	47.59	-
280	Succinylation	FAERKANKWSTPSGA HHHHHCCCCCCCCCC	47.59	-
282	Phosphorylation	ERKANKWSTPSGASW HHHCCCCCCCCCCCC	31.86	-
288	Phosphorylation	WSTPSGASWKTASAR CCCCCCCCCCCCCCC	32.41	24719451
290	Malonylation	TPSGASWKTASARPV CCCCCCCCCCCCCCC	31.55	26320211
290	Succinylation	TPSGASWKTASARPV CCCCCCCCCCCCCCC	31.55	-
290	Succinylation	TPSGASWKTASARPV CCCCCCCCCCCCCCC	31.55	-
291	Phosphorylation	PSGASWKTASARPVS CCCCCCCCCCCCCCC	21.42	28857561
293	Phosphorylation	GASWKTASARPVSSV CCCCCCCCCCCCCEE	30.00	28857561
298	Phosphorylation	TASARPVSSVGVVGL CCCCCCCCEEEEEEE	23.22	28857561
299	Phosphorylation	ASARPVSSVGVVGLG CCCCCCCEEEEEEEC	24.11	28857561
307	Phosphorylation	VGVVGLGTMGRGIVI EEEEEECCCCCCHHE	22.84	28258704
330	Malonylation	VIAVDSDKNQLATAN EEEECCCHHHHHHHH	51.01	26320211
330	Acetylation	VIAVDSDKNQLATAN EEEECCCHHHHHHHH	51.01	26051181
341	Phosphorylation	ATANKMITSVLEKEA HHHHHHHHHHHHHHH	14.86	25072903
342	Phosphorylation	TANKMITSVLEKEAS HHHHHHHHHHHHHHH	17.49	28857561
346	Malonylation	MITSVLEKEASKMQQ HHHHHHHHHHHHHHH	55.19	26320211
346	Acetylation	MITSVLEKEASKMQQ HHHHHHHHHHHHHHH	55.19	20167786
350	Acetylation	VLEKEASKMQQSGHP HHHHHHHHHHHCCCC	48.02	-
354	Phosphorylation	EASKMQQSGHPWSGP HHHHHHHCCCCCCCC	23.37	22210691
359	Phosphorylation	QQSGHPWSGPKPRLT HHCCCCCCCCCCCCC	50.06	22817900
367	Phosphorylation	GPKPRLTSSVKELGG CCCCCCCCCHHHHCC	37.41	32142685
450	Phosphorylation	LEVIPSQYSSPTTIA HHHCHHCCCCHHHHH	18.56	32142685
463	Phosphorylation	IATVMNLSKKIKKIG HHHHHCHHHHHHCCC	27.22	32142685
464	Malonylation	ATVMNLSKKIKKIGV HHHHCHHHHHHCCCE	62.78	26320211
464	Acetylation	ATVMNLSKKIKKIGV HHHHCHHHHHHCCCE	62.78	155449
488	Acetylation	GNRMLNPYYNQAYFL CCCCCCHHHCHHHHH	17.61	19608861
532	Acetylation	AGLDVGWKSRKGQGL CCCCCCCCCCCCCCC	34.16	2374969
532	Succinylation	AGLDVGWKSRKGQGL CCCCCCCCCCCCCCC	34.16	-
532	Succinylation	AGLDVGWKSRKGQGL CCCCCCCCCCCCCCC	34.16	-
533	Phosphorylation	GLDVGWKSRKGQGLT CCCCCCCCCCCCCCC	32.49	29759185
535	Malonylation	DVGWKSRKGQGLTGP CCCCCCCCCCCCCCC	63.78	26320211
540	Phosphorylation	SRKGQGLTGPTLLPG CCCCCCCCCCCCCCC	48.19	29759185
543	Phosphorylation	GQGLTGPTLLPGTPA CCCCCCCCCCCCCCC	42.12	29759185
548	Phosphorylation	GPTLLPGTPARKRGN CCCCCCCCCCHHCCC	16.31	25159151
558	Phosphorylation	RKRGNRRYCPIPDVL HHCCCCCCCCCHHHH	10.19	28258704
577	Succinylation	RFGQKTGKGWYQYDK CCCCCCCCCCCCCCC	52.05	-
577	Acetylation	RFGQKTGKGWYQYDK CCCCCCCCCCCCCCC	52.05	6570429
577	Succinylation	RFGQKTGKGWYQYDK CCCCCCCCCCCCCCC	52.05	-
580	Phosphorylation	QKTGKGWYQYDKPLG CCCCCCCCCCCCCCC	13.08	-
582	Phosphorylation	TGKGWYQYDKPLGRI CCCCCCCCCCCCCCC	15.39	-
584	Succinylation	KGWYQYDKPLGRIHK CCCCCCCCCCCCCCC	36.89	-
584	Succinylation	KGWYQYDKPLGRIHK CCCCCCCCCCCCCCC	36.89	-
584	Acetylation	KGWYQYDKPLGRIHK CCCCCCCCCCCCCCC	36.89	19608861
591	Succinylation	KPLGRIHKPDPWLSK CCCCCCCCCCHHHHH	49.06	-
591	Acetylation	KPLGRIHKPDPWLSK CCCCCCCCCCHHHHH	49.06	26051181
591	Succinylation	KPLGRIHKPDPWLSK CCCCCCCCCCHHHHH	49.06	-
598	Acetylation	KPDPWLSKFLSRYRK CCCHHHHHHHHHHHH	48.42	26051181
666	Phosphorylation	HKGGPMFYASTVGLP CCCCCCEEECCCCHH	8.06	-
682	Phosphorylation	VLEKLQKYYRQNPDI HHHHHHHHHHHCCCC	7.30	-
683	Phosphorylation	LEKLQKYYRQNPDIP HHHHHHHHHHCCCCC	16.86	-
703	Phosphorylation	DYLKKLASQGNPPLK HHHHHHHHCCCCCHH	49.40	24275569
710	Succinylation	SQGNPPLKEWQSLAG HCCCCCHHHHHHHCC	63.78	-
710	Acetylation	SQGNPPLKEWQSLAG HCCCCCHHHHHHHCC	63.78	26051181
710	Succinylation	SQGNPPLKEWQSLAG HCCCCCHHHHHHHCC	63.78	-
714	Phosphorylation	PPLKEWQSLAGSPSS CCHHHHHHHCCCCCC	22.66	28857561
718	Phosphorylation	EWQSLAGSPSSKL-- HHHHHCCCCCCCC--	18.92	22199227
720	Phosphorylation	QSLAGSPSSKL---- HHHCCCCCCCC----	41.63	23186163
721	Phosphorylation	SLAGSPSSKL----- HHCCCCCCCC-----	41.16	23186163
722	Succinylation	LAGSPSSKL------ HCCCCCCCC------	63.65	-
722	Acetylation	LAGSPSSKL------ HCCCCCCCC------	63.65	2401677
722	Succinylation	LAGSPSSKL------ HCCCCCCCC------	63.65	-

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 ECHP_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
346	K	Acetylation		20167786
Acetylation is enhanced by up to 80% after treatment either with trichostin A (TSA) or with nicotinamide (NAM) with highest increase on Lys-346.

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 ECHP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRI18_HUMAN	MID1	physical	25416956
TRI27_HUMAN	TRIM27	physical	25416956
TPP2_HUMAN	TPP2	physical	25416956
TRAF1_HUMAN	TRAF1	physical	25416956
BHE40_HUMAN	BHLHE40	physical	25416956
SSNA1_HUMAN	SSNA1	physical	25416956
PNMA1_HUMAN	PNMA1	physical	25416956
TNIP1_HUMAN	TNIP1	physical	25416956
NECA2_HUMAN	NECAB2	physical	25416956
KCTD9_HUMAN	KCTD9	physical	25416956
TRI54_HUMAN	TRIM54	physical	25416956
C102B_HUMAN	CCDC102B	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
TRI41_HUMAN	TRIM41	physical	25416956
ADIP_HUMAN	SSX2IP	physical	25416956
FUND1_HUMAN	FUNDC1	physical	25416956
KCTD6_HUMAN	KCTD6	physical	25416956
ZBTB9_HUMAN	ZBTB9	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615605	Fanconi renotubular syndrome 3 (FRTS3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ECHP_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Regulation of cellular metabolism by protein lysine acetylation."; Zhao S., Xu W., Jiang W., Yu W., Lin Y., Zhang T., Yao J., Zhou L.,Zeng Y., Li H., Li Y., Shi J., An W., Hancock S.M., He F., Qin L.,Chin J., Yang P., Chen X., Lei Q., Xiong Y., Guan K.L.; Science 327:1000-1004(2010). Cited for: ACETYLATION AT LYS-165; LYS-171; LYS-346 AND LYS-584, ENZYMEREGULATION, MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-165; LYS-171;LYS-346 AND LYS-584.	20167786 [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-584, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-359, AND MASSSPECTROMETRY.	17287340 [Abstract]

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