dbPTM

BDH_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BDH_MOUSE
UniProt AC	Q80XN0
Protein Name	D-beta-hydroxybutyrate dehydrogenase, mitochondrial {ECO:0000305}
Gene Name	Bdh1 {ECO:0000312\|MGI:MGI:1919161}
Organism	Mus musculus (Mouse).
Sequence Length	343
Subcellular Localization	Mitochondrion inner membrane . Mitochondrion matrix .
Protein Description
Protein Sequence	MLAARLSRPLSQLPGKALSVRDRENGTRHTLLFYPASFSPDTRRTYASQADAASGKAILITGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGDAGVKELDSLKSDRLRTIQLNVCNSEEVEKAVETIRSGLKDPEKGMWGLVNNAGISTFGEVEFTSMETYKEVAEVNLWGTVRTTKSFLPLLRRAKGRVVNISSMLGRMANPARSPYCITKFGIEAFSDCLRYEMHPLGVKVSVVEPGNFIAATSLYSPERIQAIAKKMWDDLPEVVRKDYGRKYFDEKIAKMETYCNSGSTDTSSVINAVTHALTAATPYTRYHPMDYYWWLRMQIMTHFPGAISDKIYIH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
63	S-palmitoylation	KAILITGCDSGFGFS CEEEEECCCCCCCHH	2.55	28526873
73	Succinylation	GFGFSLAKHLHSKGF CCCHHHHHHHHCCCE	52.58	24315375
73	Acetylation	GFGFSLAKHLHSKGF CCCHHHHHHHHCCCE	52.58	23576753
78	Acetylation	LAKHLHSKGFLVFAG HHHHHHCCCEEEEEE	42.82	23864654
78	Succinylation	LAKHLHSKGFLVFAG HHHHHHCCCEEEEEE	42.82	24315375
86	S-nitrosocysteine	GFLVFAGCLMKDKGD CEEEEEEHEECCCCC	2.77	-
86	S-nitrosylation	GFLVFAGCLMKDKGD CEEEEEEHEECCCCC	2.77	21278135
86	S-palmitoylation	GFLVFAGCLMKDKGD CEEEEEEHEECCCCC	2.77	28526873
89	Acetylation	VFAGCLMKDKGDAGV EEEEHEECCCCCCCC	43.25	23864654
91	Acetylation	AGCLMKDKGDAGVKE EEHEECCCCCCCCCC	53.85	23864654
97	Succinylation	DKGDAGVKELDSLKS CCCCCCCCCHHHCCC	52.20	24315375
97	Glutarylation	DKGDAGVKELDSLKS CCCCCCCCCHHHCCC	52.20	24703693
97	Acetylation	DKGDAGVKELDSLKS CCCCCCCCCHHHCCC	52.20	23576753
103	Glutarylation	VKELDSLKSDRLRTI CCCHHHCCCCCCCEE	55.02	24703693
103	Succinylation	VKELDSLKSDRLRTI CCCHHHCCCCCCCEE	55.02	-
103	Acetylation	VKELDSLKSDRLRTI CCCHHHCCCCCCCEE	55.02	23576753
103	Succinylation	VKELDSLKSDRLRTI CCCHHHCCCCCCCEE	55.02	23806337
115	S-nitrosylation	RTIQLNVCNSEEVEK CEEEEEECCHHHHHH	4.51	21278135
115	S-palmitoylation	RTIQLNVCNSEEVEK CEEEEEECCHHHHHH	4.51	28526873
115	S-nitrosocysteine	RTIQLNVCNSEEVEK CEEEEEECCHHHHHH	4.51	-
122	Acetylation	CNSEEVEKAVETIRS CCHHHHHHHHHHHHH	64.01	23201123
132	Succinylation	ETIRSGLKDPEKGMW HHHHHCCCCHHCCCC	74.82	26388266
132	Acetylation	ETIRSGLKDPEKGMW HHHHHCCCCHHCCCC	74.82	23576753
136	Acetylation	SGLKDPEKGMWGLVN HCCCCHHCCCCEECC	60.50	23954790
177	Acetylation	WGTVRTTKSFLPLLR CCEECCCHHHHHHHH	38.30	23576753
208	Phosphorylation	ANPARSPYCITKFGI CCCCCCCCEEEHHHH	9.57	-
209	S-palmitoylation	NPARSPYCITKFGIE CCCCCCCEEEHHHHH	3.46	28526873
209	S-nitrosylation	NPARSPYCITKFGIE CCCCCCCEEEHHHHH	3.46	21278135
209	S-nitrosocysteine	NPARSPYCITKFGIE CCCCCCCEEEHHHHH	3.46	-
212	Acetylation	RSPYCITKFGIEAFS CCCCEEEHHHHHHHH	22.98	23576753
219	O-linked_Glycosylation	KFGIEAFSDCLRYEM HHHHHHHHHHHHHCC	34.17	-
221	S-palmitoylation	GIEAFSDCLRYEMHP HHHHHHHHHHHCCCC	1.95	28526873
232	Acetylation	EMHPLGVKVSVVEPG CCCCCCCEEEEECCC	27.30	23864654
234	Phosphorylation	HPLGVKVSVVEPGNF CCCCCEEEEECCCCE	18.09	23984901
245	Phosphorylation	PGNFIAATSLYSPER CCCEEEEECCCCHHH	15.39	29472430
246	Phosphorylation	GNFIAATSLYSPERI CCEEEEECCCCHHHH	22.15	29472430
248	Phosphorylation	FIAATSLYSPERIQA EEEEECCCCHHHHHH	23.19	23140645
249	Phosphorylation	IAATSLYSPERIQAI EEEECCCCHHHHHHH	26.10	29472430
258	Acetylation	ERIQAIAKKMWDDLP HHHHHHHHHHHHCCH	36.73	23576753
258	Succinylation	ERIQAIAKKMWDDLP HHHHHHHHHHHHCCH	36.73	24315375
259	Acetylation	RIQAIAKKMWDDLPE HHHHHHHHHHHCCHH	35.88	23576753
259	Succinylation	RIQAIAKKMWDDLPE HHHHHHHHHHHCCHH	35.88	23806337
259	Succinylation	RIQAIAKKMWDDLPE HHHHHHHHHHHCCHH	35.88	-
275	Acetylation	VRKDYGRKYFDEKIA HHHHHCCHHHHHHHH	46.00	23576753
280	Acetylation	GRKYFDEKIAKMETY CCHHHHHHHHCCCHH	50.21	23576753
280	Succinylation	GRKYFDEKIAKMETY CCHHHHHHHHCCCHH	50.21	24315375
283	Succinylation	YFDEKIAKMETYCNS HHHHHHHCCCHHCCC	40.52	24315375
283	Acetylation	YFDEKIAKMETYCNS HHHHHHHCCCHHCCC	40.52	23201123
288	S-nitrosylation	IAKMETYCNSGSTDT HHCCCHHCCCCCCCH	4.22	21278135
288	S-palmitoylation	IAKMETYCNSGSTDT HHCCCHHCCCCCCCH	4.22	28526873
288	S-nitrosocysteine	IAKMETYCNSGSTDT HHCCCHHCCCCCCCH	4.22	-
339	Acetylation	FPGAISDKIYIH--- CCCCCCCCEEEC---	30.53	23201123

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 BDH_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
132	K	Acetylation		23576753
Acetylation of Lys-132 is observed in liver mitochondria from fasted mice but not from fed mice.

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 BDH_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of BDH_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of BDH_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-132 AND LYS-275, AND MASSSPECTROMETRY.	16916647 [Abstract]

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