dbPTM

HCDH_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HCDH_MOUSE
UniProt AC	Q61425
Protein Name	Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
Gene Name	Hadh
Organism	Mus musculus (Mouse).
Sequence Length	314
Subcellular Localization	Mitochondrion matrix.
Protein Description	Plays an essential role in the mitochondrial beta-oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA..
Protein Sequence	MAFVTRQFLRSMSSSSSASAAAKKILIKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLKRMAKKKFTENPKAGDEFVEKTLSCLSTSTDAASVVHSTDLVVEAIVENLKLKNELFQRLDKFAAEHTIFASNTSSLQITNIANATTRQDRFAGLHFFNPVPMMKLVEVIKTPMTSQKTFESLVDFCKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLHERGDASKEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFILDGWHEMEPENPLFQPSPSMNNLVAQKKLGKKTGEGFYKYK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	VTRQFLRSMSSSSSA HHHHHHHHCCCCCCH	25.76	27087446
13	Phosphorylation	RQFLRSMSSSSSASA HHHHHHCCCCCCHHH	28.45	25521595
14	Phosphorylation	QFLRSMSSSSSASAA HHHHHCCCCCCHHHH	26.12	25521595
15	Phosphorylation	FLRSMSSSSSASAAA HHHHCCCCCCHHHHH	22.47	23737553
16	Phosphorylation	LRSMSSSSSASAAAK HHHCCCCCCHHHHHH	31.69	25521595
17	Phosphorylation	RSMSSSSSASAAAKK HHCCCCCCHHHHHHH	28.35	23984901
19	Phosphorylation	MSSSSSASAAAKKIL CCCCCCHHHHHHHHH	22.01	26643407
68	Malonylation	DILAKSKKGIEESLK HHHHHCHHCHHHHHH	72.68	26320211
68	Acetylation	DILAKSKKGIEESLK HHHHHCHHCHHHHHH	72.68	24062335
68	Glutarylation	DILAKSKKGIEESLK HHHHHCHHCHHHHHH	72.68	24703693
73	Phosphorylation	SKKGIEESLKRMAKK CHHCHHHHHHHHHHH	26.80	23737553
75	Succinylation	KGIEESLKRMAKKKF HCHHHHHHHHHHHHH	49.78	26388266
75	Glutarylation	KGIEESLKRMAKKKF HCHHHHHHHHHHHHH	49.78	24703693
75	Malonylation	KGIEESLKRMAKKKF HCHHHHHHHHHHHHH	49.78	26320211
75	Acetylation	KGIEESLKRMAKKKF HCHHHHHHHHHHHHH	49.78	23576753
80	Succinylation	SLKRMAKKKFTENPK HHHHHHHHHHCCCCC	43.51	23806337
80	Acetylation	SLKRMAKKKFTENPK HHHHHHHHHHCCCCC	43.51	23806337
80	Succinylation	SLKRMAKKKFTENPK HHHHHHHHHHCCCCC	43.51	-
80	Glutarylation	SLKRMAKKKFTENPK HHHHHHHHHHCCCCC	43.51	24703693
81	Malonylation	LKRMAKKKFTENPKA HHHHHHHHHCCCCCC	57.73	26320211
81	Succinylation	LKRMAKKKFTENPKA HHHHHHHHHCCCCCC	57.73	-
81	Succinylation	LKRMAKKKFTENPKA HHHHHHHHHCCCCCC	57.73	23806337
81	Glutarylation	LKRMAKKKFTENPKA HHHHHHHHHCCCCCC	57.73	24703693
81	Acetylation	LKRMAKKKFTENPKA HHHHHHHHHCCCCCC	57.73	23576753
87	Succinylation	KKFTENPKAGDEFVE HHHCCCCCCHHHHHH	76.28	-
87	Malonylation	KKFTENPKAGDEFVE HHHCCCCCCHHHHHH	76.28	26320211
87	Glutarylation	KKFTENPKAGDEFVE HHHCCCCCCHHHHHH	76.28	24703693
87	Succinylation	KKFTENPKAGDEFVE HHHCCCCCCHHHHHH	76.28	23806337
87	Acetylation	KKFTENPKAGDEFVE HHHCCCCCCHHHHHH	76.28	23576753
95	Acetylation	AGDEFVEKTLSCLST CHHHHHHHHHHHHHC	49.84	23806337
95	Succinylation	AGDEFVEKTLSCLST CHHHHHHHHHHHHHC	49.84	23806337
96	Phosphorylation	GDEFVEKTLSCLSTS HHHHHHHHHHHHHCC	15.48	23984901
98	Phosphorylation	EFVEKTLSCLSTSTD HHHHHHHHHHHCCCC	20.46	23984901
99	S-nitrosylation	FVEKTLSCLSTSTDA HHHHHHHHHHCCCCH	3.80	21278135
99	S-palmitoylation	FVEKTLSCLSTSTDA HHHHHHHHHHCCCCH	3.80	28526873
99	S-nitrosocysteine	FVEKTLSCLSTSTDA HHHHHHHHHHCCCCH	3.80	-
99	Glutathionylation	FVEKTLSCLSTSTDA HHHHHHHHHHCCCCH	3.80	24333276
101	Phosphorylation	EKTLSCLSTSTDAAS HHHHHHHHCCCCHHH	25.33	23984901
102	Phosphorylation	KTLSCLSTSTDAASV HHHHHHHCCCCHHHH	23.77	23984901
103	Phosphorylation	TLSCLSTSTDAASVV HHHHHHCCCCHHHHH	22.40	23984901
104	Phosphorylation	LSCLSTSTDAASVVH HHHHHCCCCHHHHHH	29.73	23984901
108	Phosphorylation	STSTDAASVVHSTDL HCCCCHHHHHHCCHH	26.79	23984901
112	Phosphorylation	DAASVVHSTDLVVEA CHHHHHHCCHHHHHH	16.41	23984901
113	Phosphorylation	AASVVHSTDLVVEAI HHHHHHCCHHHHHHH	20.62	23984901
125	Acetylation	EAIVENLKLKNELFQ HHHHHHHHHHHHHHH	69.83	23576753
125	Succinylation	EAIVENLKLKNELFQ HHHHHHHHHHHHHHH	69.83	23806337
127	Acetylation	IVENLKLKNELFQRL HHHHHHHHHHHHHHH	46.95	23576753
136	Succinylation	ELFQRLDKFAAEHTI HHHHHHHHHHHHCCE	41.30	-
136	Ubiquitination	ELFQRLDKFAAEHTI HHHHHHHHHHHHCCE	41.30	-
136	Acetylation	ELFQRLDKFAAEHTI HHHHHHHHHHHHCCE	41.30	23576753
136	Succinylation	ELFQRLDKFAAEHTI HHHHHHHHHHHHCCE	41.30	23806337
179	Succinylation	FNPVPMMKLVEVIKT CCCCCCHHHHHHHCC	43.03	23806337
179	Acetylation	FNPVPMMKLVEVIKT CCCCCCHHHHHHHCC	43.03	23576753
179	Malonylation	FNPVPMMKLVEVIKT CCCCCCHHHHHHHCC	43.03	26073543
185	Succinylation	MKLVEVIKTPMTSQK HHHHHHHCCCCCCHH	52.32	23806337
185	Acetylation	MKLVEVIKTPMTSQK HHHHHHHCCCCCCHH	52.32	23576753
185	Glutarylation	MKLVEVIKTPMTSQK HHHHHHHCCCCCCHH	52.32	24703693
185	Succinylation	MKLVEVIKTPMTSQK HHHHHHHCCCCCCHH	52.32	-
185	Malonylation	MKLVEVIKTPMTSQK HHHHHHHCCCCCCHH	52.32	26320211
186	Phosphorylation	KLVEVIKTPMTSQKT HHHHHHCCCCCCHHH	13.73	-
192	Succinylation	KTPMTSQKTFESLVD CCCCCCHHHHHHHHH	55.75	23806337
192	Acetylation	KTPMTSQKTFESLVD CCCCCCHHHHHHHHH	55.75	23576753
192	Glutarylation	KTPMTSQKTFESLVD CCCCCCHHHHHHHHH	55.75	24703693
192	Succinylation	KTPMTSQKTFESLVD CCCCCCHHHHHHHHH	55.75	-
196	Phosphorylation	TSQKTFESLVDFCKT CCHHHHHHHHHHHHH	29.51	22817900
201	S-nitrosocysteine	FESLVDFCKTLGKHP HHHHHHHHHHHCCCC	2.59	-
201	S-nitrosylation	FESLVDFCKTLGKHP HHHHHHHHHHHCCCC	2.59	21278135
201	S-palmitoylation	FESLVDFCKTLGKHP HHHHHHHHHHHCCCC	2.59	28526873
202	Acetylation	ESLVDFCKTLGKHPV HHHHHHHHHHCCCCC	46.94	23576753
202	Succinylation	ESLVDFCKTLGKHPV HHHHHHHHHHCCCCC	46.94	-
202	Succinylation	ESLVDFCKTLGKHPV HHHHHHHHHHCCCCC	46.94	23806337
206	Succinylation	DFCKTLGKHPVSCKD HHHHHHCCCCCCCCC	48.09	23806337
206	Succinylation	DFCKTLGKHPVSCKD HHHHHHCCCCCCCCC	48.09	-
206	Acetylation	DFCKTLGKHPVSCKD HHHHHHCCCCCCCCC	48.09	23806337
211	S-nitrosylation	LGKHPVSCKDTPGFI HCCCCCCCCCCCCCH	4.75	21278135
211	S-palmitoylation	LGKHPVSCKDTPGFI HCCCCCCCCCCCCCH	4.75	26165157
211	S-nitrosocysteine	LGKHPVSCKDTPGFI HCCCCCCCCCCCCCH	4.75	-
212	Succinylation	GKHPVSCKDTPGFIV CCCCCCCCCCCCCHH	58.07	23806337
212	Ubiquitination	GKHPVSCKDTPGFIV CCCCCCCCCCCCCHH	58.07	-
212	Acetylation	GKHPVSCKDTPGFIV CCCCCCCCCCCCCHH	58.07	23576753
212	Succinylation	GKHPVSCKDTPGFIV CCCCCCCCCCCCCHH	58.07	-
212	Glutarylation	GKHPVSCKDTPGFIV CCCCCCCCCCCCCHH	58.07	24703693
212	Malonylation	GKHPVSCKDTPGFIV CCCCCCCCCCCCCHH	58.07	26320211
240	Phosphorylation	LHERGDASKEDIDTA HHHCCCCCHHHHHHH	41.12	22817900
241	Ubiquitination	HERGDASKEDIDTAM HHCCCCCHHHHHHHH	62.21	27667366
241	Succinylation	HERGDASKEDIDTAM HHCCCCCHHHHHHHH	62.21	23806337
241	Succinylation	HERGDASKEDIDTAM HHCCCCCHHHHHHHH	62.21	-
241	Malonylation	HERGDASKEDIDTAM HHCCCCCHHHHHHHH	62.21	26073543
241	Glutarylation	HERGDASKEDIDTAM HHCCCCCHHHHHHHH	62.21	24703693
241	Acetylation	HERGDASKEDIDTAM HHCCCCCHHHHHHHH	62.21	23806337
249	Acetylation	EDIDTAMKLGAGYPM HHHHHHHHHCCCCCC	41.11	22733758
300	Acetylation	MNNLVAQKKLGKKTG HHHHHHHHHHCCCCC	39.98	23576753
300	Succinylation	MNNLVAQKKLGKKTG HHHHHHHHHHCCCCC	39.98	24315375
301	Acetylation	NNLVAQKKLGKKTGE HHHHHHHHHCCCCCC	50.85	2393645
312	Succinylation	KTGEGFYKYK----- CCCCCCCCCC-----	44.28	23806337
312	Glutarylation	KTGEGFYKYK----- CCCCCCCCCC-----	44.28	24703693
312	Acetylation	KTGEGFYKYK----- CCCCCCCCCC-----	44.28	23864654
312	Succinylation	KTGEGFYKYK----- CCCCCCCCCC-----	44.28	-
314	Succinylation	GEGFYKYK------- CCCCCCCC-------	50.11	26388266
314	Acetylation	GEGFYKYK------- CCCCCCCC-------	50.11	6269447

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 HCDH_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
81	K	Succinylation		23806337
Succinylation at Lys-81, adjacent to a coenzyme A binding site.

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 HCDH_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
ALDOA_MOUSE	Aldoa	physical	22496890

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HCDH_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, AND MASS SPECTROMETRY.	16916647 [Abstract]

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