dbPTM

MDHM_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MDHM_MOUSE
UniProt AC	P08249
Protein Name	Malate dehydrogenase, mitochondrial
Gene Name	Mdh2
Organism	Mus musculus (Mouse).
Sequence Length	338
Subcellular Localization	Mitochondrion matrix .
Protein Description
Protein Sequence	MLSALARPAGAALRRSFSTSAQNNAKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGVAADLSHIETRANVKGYLGPEQLPDCLKGCDVVVIPAGVPRKPGMTRDDLFNTNATIVATLTAACAQHCPEAMVCIIANPVNSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANTFVAELKGLDPARVNVPVIGGHAGKTIIPLISQCTPKVDFPQDQLATLTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVDAMNGKEGVVECSFVQSKETECTYFSTPLLLGKKGLEKNLGIGKITPFEEKMIAEAIPELKASIKKGEDFVKNMK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
26	Acetylation	TSAQNNAKVAVLGAS CCCCCCCEEEEEECC	32.61	22733758
26	Succinylation	TSAQNNAKVAVLGAS CCCCCCCEEEEEECC	32.61	24315375
33	O-linked_Glycosylation	KVAVLGASGGIGQPL EEEEEECCCCCCHHH	35.44	-
33	Phosphorylation	KVAVLGASGGIGQPL EEEEEECCCCCCHHH	35.44	23737553
41	Phosphorylation	GGIGQPLSLLLKNSP CCCCHHHHHHHHCCC	24.53	23984901
45	Acetylation	QPLSLLLKNSPLVSR HHHHHHHHCCCCCEE	56.18	22826441
47	Phosphorylation	LSLLLKNSPLVSRLT HHHHHHCCCCCEEEE	20.30	22324799
51	Phosphorylation	LKNSPLVSRLTLYDI HHCCCCCEEEEHHHH	29.29	29472430
54	Phosphorylation	SPLVSRLTLYDIAHT CCCCEEEEHHHHCCC	23.35	26745281
56	Phosphorylation	LVSRLTLYDIAHTPG CCEEEEHHHHCCCCC	10.48	26745281
61	Phosphorylation	TLYDIAHTPGVAADL EHHHHCCCCCHHHCC	16.83	26745281
69	Phosphorylation	PGVAADLSHIETRAN CCHHHCCHHCHHHCC	23.98	22817900
78	Acetylation	IETRANVKGYLGPEQ CHHHCCCCCCCCHHH	41.46	23576753
78	Glutarylation	IETRANVKGYLGPEQ CHHHCCCCCCCCHHH	41.46	24703693
78	Malonylation	IETRANVKGYLGPEQ CHHHCCCCCCCCHHH	41.46	26320211
78	Succinylation	IETRANVKGYLGPEQ CHHHCCCCCCCCHHH	41.46	-
78	Succinylation	IETRANVKGYLGPEQ CHHHCCCCCCCCHHH	41.46	23806337
78	Ubiquitination	IETRANVKGYLGPEQ CHHHCCCCCCCCHHH	41.46	-
80	Phosphorylation	TRANVKGYLGPEQLP HHCCCCCCCCHHHCC	11.63	-
89	S-nitrosocysteine	GPEQLPDCLKGCDVV CHHHCCHHHCCCCEE	3.90	-
89	Glutathionylation	GPEQLPDCLKGCDVV CHHHCCHHHCCCCEE	3.90	24333276
89	S-nitrosylation	GPEQLPDCLKGCDVV CHHHCCHHHCCCCEE	3.90	22178444
89	S-palmitoylation	GPEQLPDCLKGCDVV CHHHCCHHHCCCCEE	3.90	28526873
91	Acetylation	EQLPDCLKGCDVVVI HHCCHHHCCCCEEEE	64.92	23576753
91	Succinylation	EQLPDCLKGCDVVVI HHCCHHHCCCCEEEE	64.92	-
91	Succinylation	EQLPDCLKGCDVVVI HHCCHHHCCCCEEEE	64.92	23806337
93	S-nitrosocysteine	LPDCLKGCDVVVIPA CCHHHCCCCEEEECC	3.25	-
93	Glutathionylation	LPDCLKGCDVVVIPA CCHHHCCCCEEEECC	3.25	24333276
93	S-nitrosylation	LPDCLKGCDVVVIPA CCHHHCCCCEEEECC	3.25	24895380
93	S-palmitoylation	LPDCLKGCDVVVIPA CCHHHCCCCEEEECC	3.25	28526873
105	Acetylation	IPAGVPRKPGMTRDD ECCCCCCCCCCCHHH	39.59	24062335
157	Acetylation	ITAEVFKKHGVYNPN EEHHHHHHCCCCCCC	33.84	24062335
157	Glutarylation	ITAEVFKKHGVYNPN EEHHHHHHCCCCCCC	33.84	24703693
165	Acetylation	HGVYNPNKIFGVTTL CCCCCCCCEEEEEHH	40.44	23576753
165	Succinylation	HGVYNPNKIFGVTTL CCCCCCCCEEEEEHH	40.44	23806337
171	Phosphorylation	NKIFGVTTLDIVRAN CCEEEEEHHHHHHHC	21.74	-
185	Acetylation	NTFVAELKGLDPARV CCHHHHHCCCCHHHE	49.27	23576753
185	Glutarylation	NTFVAELKGLDPARV CCHHHHHCCCCHHHE	49.27	24703693
185	Succinylation	NTFVAELKGLDPARV CCHHHHHCCCCHHHE	49.27	-
185	Succinylation	NTFVAELKGLDPARV CCHHHHHCCCCHHHE	49.27	23806337
185	Ubiquitination	NTFVAELKGLDPARV CCHHHHHCCCCHHHE	49.27	-
203	Acetylation	VIGGHAGKTIIPLIS EECCCCCCCHHHHHH	37.02	23864654
203	Succinylation	VIGGHAGKTIIPLIS EECCCCCCCHHHHHH	37.02	-
203	Succinylation	VIGGHAGKTIIPLIS EECCCCCCCHHHHHH	37.02	23806337
204	Phosphorylation	IGGHAGKTIIPLISQ ECCCCCCCHHHHHHH	24.18	26745281
210	Phosphorylation	KTIIPLISQCTPKVD CCHHHHHHHCCCCCC	27.21	26745281
212	S-nitrosocysteine	IIPLISQCTPKVDFP HHHHHHHCCCCCCCC	5.85	-
212	Glutathionylation	IIPLISQCTPKVDFP HHHHHHHCCCCCCCC	5.85	24333276
212	S-nitrosylation	IIPLISQCTPKVDFP HHHHHHHCCCCCCCC	5.85	24895380
212	S-palmitoylation	IIPLISQCTPKVDFP HHHHHHHCCCCCCCC	5.85	28526873
213	Phosphorylation	IPLISQCTPKVDFPQ HHHHHHCCCCCCCCH	20.64	25521595
215	Acetylation	LISQCTPKVDFPQDQ HHHHCCCCCCCCHHH	35.96	23576753
215	Succinylation	LISQCTPKVDFPQDQ HHHHCCCCCCCCHHH	35.96	-
215	Succinylation	LISQCTPKVDFPQDQ HHHHCCCCCCCCHHH	35.96	23806337
235	Phosphorylation	GRIQEAGTEVVKAKA HHHHHHCCEEEHHCC	32.43	25521595
239	N6-malonyllysine	EAGTEVVKAKAGAGS HHCCEEEHHCCCCCC	49.71	-
239	Acetylation	EAGTEVVKAKAGAGS HHCCEEEHHCCCCCC	49.71	23806337
239	Glutarylation	EAGTEVVKAKAGAGS HHCCEEEHHCCCCCC	49.71	24703693
239	Malonylation	EAGTEVVKAKAGAGS HHCCEEEHHCCCCCC	49.71	26073543
239	Succinylation	EAGTEVVKAKAGAGS HHCCEEEHHCCCCCC	49.71	23806337
239	Ubiquitination	EAGTEVVKAKAGAGS HHCCEEEHHCCCCCC	49.71	27667366
241	Glutarylation	GTEVVKAKAGAGSAT CCEEEHHCCCCCCHH	41.45	24703693
241	Malonylation	GTEVVKAKAGAGSAT CCEEEHHCCCCCCHH	41.45	26073543
241	Succinylation	GTEVVKAKAGAGSAT CCEEEHHCCCCCCHH	41.45	26388266
241	Ubiquitination	GTEVVKAKAGAGSAT CCEEEHHCCCCCCHH	41.45	27667366
246	Phosphorylation	KAKAGAGSATLSMAY HHCCCCCCHHHHHHH	19.97	25521595
248	Phosphorylation	KAGAGSATLSMAYAG CCCCCCHHHHHHHHH	22.51	27742792
250	Phosphorylation	GAGSATLSMAYAGAR CCCCHHHHHHHHHHH	9.30	28066266
253	Phosphorylation	SATLSMAYAGARFVF CHHHHHHHHHHHHHH	9.27	28066266
261	Phosphorylation	AGARFVFSLVDAMNG HHHHHHHHHHHHHCC	23.37	24759943
269	Acetylation	LVDAMNGKEGVVECS HHHHHCCCCCEEEEE	46.41	23806337
269	Succinylation	LVDAMNGKEGVVECS HHHHHCCCCCEEEEE	46.41	-
269	Succinylation	LVDAMNGKEGVVECS HHHHHCCCCCEEEEE	46.41	23806337
275	S-nitrosocysteine	GKEGVVECSFVQSKE CCCCEEEEEEEECCC	2.30	-
275	Glutathionylation	GKEGVVECSFVQSKE CCCCEEEEEEEECCC	2.30	24333276
275	S-nitrosylation	GKEGVVECSFVQSKE CCCCEEEEEEEECCC	2.30	24895380
275	S-palmitoylation	GKEGVVECSFVQSKE CCCCEEEEEEEECCC	2.30	28526873
276	O-linked_Glycosylation	KEGVVECSFVQSKET CCCEEEEEEEECCCC	18.23	55412669
281	Acetylation	ECSFVQSKETECTYF EEEEEECCCCCCEEE	52.11	23806337
281	Succinylation	ECSFVQSKETECTYF EEEEEECCCCCCEEE	52.11	23806337
283	Phosphorylation	SFVQSKETECTYFST EEEECCCCCCEEEEC	39.85	23984901
285	S-nitrosocysteine	VQSKETECTYFSTPL EECCCCCCEEEECCH	4.95	-
285	Glutathionylation	VQSKETECTYFSTPL EECCCCCCEEEECCH	4.95	24333276
285	S-nitrosylation	VQSKETECTYFSTPL EECCCCCCEEEECCH	4.95	24895380
285	S-palmitoylation	VQSKETECTYFSTPL EECCCCCCEEEECCH	4.95	28526873
286	Phosphorylation	QSKETECTYFSTPLL ECCCCCCEEEECCHH	22.75	23984901
296	Acetylation	STPLLLGKKGLEKNL ECCHHCCCCCHHHCC	43.57	23576753
296	Glutarylation	STPLLLGKKGLEKNL ECCHHCCCCCHHHCC	43.57	24703693
296	Succinylation	STPLLLGKKGLEKNL ECCHHCCCCCHHHCC	43.57	-
296	Succinylation	STPLLLGKKGLEKNL ECCHHCCCCCHHHCC	43.57	23806337
296	Ubiquitination	STPLLLGKKGLEKNL ECCHHCCCCCHHHCC	43.57	-
297	Acetylation	TPLLLGKKGLEKNLG CCHHCCCCCHHHCCC	67.91	24062335
297	Succinylation	TPLLLGKKGLEKNLG CCHHCCCCCHHHCCC	67.91	26388266
301	Acetylation	LGKKGLEKNLGIGKI CCCCCHHHCCCCCCC	63.62	23576753
301	Glutarylation	LGKKGLEKNLGIGKI CCCCCHHHCCCCCCC	63.62	24703693
301	Malonylation	LGKKGLEKNLGIGKI CCCCCHHHCCCCCCC	63.62	26073543
301	Succinylation	LGKKGLEKNLGIGKI CCCCCHHHCCCCCCC	63.62	-
301	Succinylation	LGKKGLEKNLGIGKI CCCCCHHHCCCCCCC	63.62	23806337
301	Ubiquitination	LGKKGLEKNLGIGKI CCCCCHHHCCCCCCC	63.62	27667366
307	N6-malonyllysine	EKNLGIGKITPFEEK HHCCCCCCCCHHHHH	41.30	-
307	Acetylation	EKNLGIGKITPFEEK HHCCCCCCCCHHHHH	41.30	23576753
307	Glutarylation	EKNLGIGKITPFEEK HHCCCCCCCCHHHHH	41.30	24703693
307	Malonylation	EKNLGIGKITPFEEK HHCCCCCCCCHHHHH	41.30	26320211
307	Succinylation	EKNLGIGKITPFEEK HHCCCCCCCCHHHHH	41.30	23806337
307	Ubiquitination	EKNLGIGKITPFEEK HHCCCCCCCCHHHHH	41.30	-
309	Phosphorylation	NLGIGKITPFEEKMI CCCCCCCCHHHHHHH	25.97	22817900
314	Acetylation	KITPFEEKMIAEAIP CCCHHHHHHHHHHHH	28.54	23576753
314	Glutarylation	KITPFEEKMIAEAIP CCCHHHHHHHHHHHH	28.54	24703693
314	Succinylation	KITPFEEKMIAEAIP CCCHHHHHHHHHHHH	28.54	-
314	Succinylation	KITPFEEKMIAEAIP CCCHHHHHHHHHHHH	28.54	23806337
314	Ubiquitination	KITPFEEKMIAEAIP CCCHHHHHHHHHHHH	28.54	-
324	Acetylation	AEAIPELKASIKKGE HHHHHHHHHHHHCCH	38.12	23576753
324	Glutarylation	AEAIPELKASIKKGE HHHHHHHHHHHHCCH	38.12	24703693
324	Succinylation	AEAIPELKASIKKGE HHHHHHHHHHHHCCH	38.12	-
324	Succinylation	AEAIPELKASIKKGE HHHHHHHHHHHHCCH	38.12	23806337
324	Ubiquitination	AEAIPELKASIKKGE HHHHHHHHHHHHCCH	38.12	-
326	Phosphorylation	AIPELKASIKKGEDF HHHHHHHHHHCCHHH	33.10	22817900
328	Acetylation	PELKASIKKGEDFVK HHHHHHHHCCHHHHH	52.83	24062335
328	Succinylation	PELKASIKKGEDFVK HHHHHHHHCCHHHHH	52.83	-
328	Succinylation	PELKASIKKGEDFVK HHHHHHHHCCHHHHH	52.83	23806337
329	N6-malonyllysine	ELKASIKKGEDFVKN HHHHHHHCCHHHHHH	66.90	-
329	Acetylation	ELKASIKKGEDFVKN HHHHHHHCCHHHHHH	66.90	23576753
329	Glutarylation	ELKASIKKGEDFVKN HHHHHHHCCHHHHHH	66.90	24703693
329	Malonylation	ELKASIKKGEDFVKN HHHHHHHCCHHHHHH	66.90	26320211
329	Succinylation	ELKASIKKGEDFVKN HHHHHHHCCHHHHHH	66.90	23806337
335	Acetylation	KKGEDFVKNMK---- HCCHHHHHHCC----	51.85	23576753
335	Glutarylation	KKGEDFVKNMK---- HCCHHHHHHCC----	51.85	24703693
335	Succinylation	KKGEDFVKNMK---- HCCHHHHHHCC----	51.85	-
335	Succinylation	KKGEDFVKNMK---- HCCHHHHHHCC----	51.85	23806337
338	Acetylation	EDFVKNMK------- HHHHHHCC-------	67.59	6566469
338	Glutarylation	EDFVKNMK------- HHHHHHCC-------	67.59	24703693

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 MDHM_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
239	K	Acetylation	23806337
Acetylation of Lys-239 and Lys-314 is observed in liver mitochondria from fasted mice but not from fed mice.
314	K	Acetylation	23806337
Acetylation of Lys-239 and Lys-314 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 MDHM_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CISY_MOUSE	Cs	physical	15809022

Drug and Disease Associations

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

Regulatory Network of MDHM_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-157; LYS-239 AND LYS-314,AND MASS SPECTROMETRY.	16916647 [Abstract]

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