dbPTM

MDHC_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MDHC_MOUSE
UniProt AC	P14152
Protein Name	Malate dehydrogenase, cytoplasmic
Gene Name	Mdh1
Organism	Mus musculus (Mouse).
Sequence Length	334
Subcellular Localization	Cytoplasm.
Protein Description
Protein Sequence	MSEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLLDITPMMGVLDGVLMELQDCALPLLQDVIATDKEEIAFKDLDVAVLVGSMPRREGMERKDLLKANVKIFKSQGTALEKYAKKSVKVIVVGNPANTNCLTASKSAPSIPKENFSCLTRLDHNRAKSQIALKLGVTADDVKNVIIWGNHSSTQYPDVNHAKVKLQGKEVGVYEALKDDSWLKGEFITTVQQRGAAVIKARKLSSAMSAAKAIADHIRDIWFGTPEGEFVSMGVISDGNSYGVPDDLLYSFPVVIKNKTWKFVEGLPINDFSREKMDLTAKELTEEKETAFEFLSSA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSEPIRVLV ------CCCCEEEEE	52.67	-
22	Phosphorylation	QIAYSLLYSIGNGSV HHHHHHHHHCCCCCC	11.97	-
23	Phosphorylation	IAYSLLYSIGNGSVF HHHHHHHHCCCCCCC	24.80	-
28	Phosphorylation	LYSIGNGSVFGKDQP HHHCCCCCCCCCCCC	20.48	-
89	Phosphorylation	DVAVLVGSMPRREGM CEEEHCCCCCCCCCC	20.38	29899451
103	Acetylation	MERKDLLKANVKIFK CCHHHHHHHHHHHHH	45.25	23864654
103	Malonylation	MERKDLLKANVKIFK CCHHHHHHHHHHHHH	45.25	26320211
103	Ubiquitination	MERKDLLKANVKIFK CCHHHHHHHHHHHHH	45.25	-
107	Acetylation	DLLKANVKIFKSQGT HHHHHHHHHHHHCCH	42.08	23864654
107	Malonylation	DLLKANVKIFKSQGT HHHHHHHHHHHHCCH	42.08	26320211
107	Succinylation	DLLKANVKIFKSQGT HHHHHHHHHHHHCCH	42.08	23954790
110	Ubiquitination	KANVKIFKSQGTALE HHHHHHHHHCCHHHH	45.39	-
110	Succinylation	KANVKIFKSQGTALE HHHHHHHHHCCHHHH	45.39	-
110	Succinylation	KANVKIFKSQGTALE HHHHHHHHHCCHHHH	45.39	23806337
110	Glutarylation	KANVKIFKSQGTALE HHHHHHHHHCCHHHH	45.39	24703693
110	Acetylation	KANVKIFKSQGTALE HHHHHHHHHCCHHHH	45.39	22826441
110	Malonylation	KANVKIFKSQGTALE HHHHHHHHHCCHHHH	45.39	26073543
111	Phosphorylation	ANVKIFKSQGTALEK HHHHHHHHCCHHHHH	24.08	25521595
114	Phosphorylation	KIFKSQGTALEKYAK HHHHHCCHHHHHHHC	22.04	22324799
118	Ubiquitination	SQGTALEKYAKKSVK HCCHHHHHHHCCCCE	51.89	-
118	Acetylation	SQGTALEKYAKKSVK HCCHHHHHHHCCCCE	51.89	23576753
118	Malonylation	SQGTALEKYAKKSVK HCCHHHHHHHCCCCE	51.89	26320211
119	Phosphorylation	QGTALEKYAKKSVKV CCHHHHHHHCCCCEE	17.80	-
121	Acetylation	TALEKYAKKSVKVIV HHHHHHHCCCCEEEE	42.35	-
122	Acetylation	ALEKYAKKSVKVIVV HHHHHHCCCCEEEEE	52.92	22826441
125	Ubiquitination	KYAKKSVKVIVVGNP HHHCCCCEEEEECCC	33.08	22790023
135	Phosphorylation	VVGNPANTNCLTASK EECCCCCCCCCCCCC	29.43	23984901
137	S-nitrosocysteine	GNPANTNCLTASKSA CCCCCCCCCCCCCCC	3.17	-
137	S-nitrosylation	GNPANTNCLTASKSA CCCCCCCCCCCCCCC	3.17	24895380
137	Glutathionylation	GNPANTNCLTASKSA CCCCCCCCCCCCCCC	3.17	24333276
137	S-palmitoylation	GNPANTNCLTASKSA CCCCCCCCCCCCCCC	3.17	28526873
139	Phosphorylation	PANTNCLTASKSAPS CCCCCCCCCCCCCCC	30.96	23984901
141	Phosphorylation	NTNCLTASKSAPSIP CCCCCCCCCCCCCCC	23.16	23984901
142	Ubiquitination	TNCLTASKSAPSIPK CCCCCCCCCCCCCCC	48.44	22790023
146	Phosphorylation	TASKSAPSIPKENFS CCCCCCCCCCCCCCC	51.76	28542873
149	Acetylation	KSAPSIPKENFSCLT CCCCCCCCCCCCHHH	64.72	22826441
149	Ubiquitination	KSAPSIPKENFSCLT CCCCCCCCCCCCHHH	64.72	22790023
154	S-nitrosylation	IPKENFSCLTRLDHN CCCCCCCHHHHCCCC	3.83	24895380
154	S-palmitoylation	IPKENFSCLTRLDHN CCCCCCCHHHHCCCC	3.83	28526873
154	S-nitrosocysteine	IPKENFSCLTRLDHN CCCCCCCHHHHCCCC	3.83	-
154	Glutathionylation	IPKENFSCLTRLDHN CCCCCCCHHHHCCCC	3.83	24333276
164	Acetylation	RLDHNRAKSQIALKL HCCCCHHHCHHHHHH	39.39	22826441
165	Phosphorylation	LDHNRAKSQIALKLG CCCCHHHCHHHHHHC	26.32	25338131
170	Ubiquitination	AKSQIALKLGVTADD HHCHHHHHHCCCHHH	33.89	22790023
179	Acetylation	GVTADDVKNVIIWGN CCCHHHCCEEEEECC	53.11	23954790
179	Ubiquitination	GVTADDVKNVIIWGN CCCHHHCCEEEEECC	53.11	22790023
188	Phosphorylation	VIIWGNHSSTQYPDV EEEECCCCCCCCCCC	38.80	27742792
189	Phosphorylation	IIWGNHSSTQYPDVN EEECCCCCCCCCCCC	16.39	25521595
190	Phosphorylation	IWGNHSSTQYPDVNH EECCCCCCCCCCCCC	34.83	23737553
192	Phosphorylation	GNHSSTQYPDVNHAK CCCCCCCCCCCCCCE	11.07	23737553
199	Acetylation	YPDVNHAKVKLQGKE CCCCCCCEEEECCEE	32.14	22826441
199	Ubiquitination	YPDVNHAKVKLQGKE CCCCCCCEEEECCEE	32.14	22790023
205	Ubiquitination	AKVKLQGKEVGVYEA CEEEECCEEEEEEEE	35.94	-
205	Acetylation	AKVKLQGKEVGVYEA CEEEECCEEEEEEEE	35.94	22733758
205	Malonylation	AKVKLQGKEVGVYEA CEEEECCEEEEEEEE	35.94	26320211
210	Phosphorylation	QGKEVGVYEALKDDS CCEEEEEEEECCCCC	6.91	22817900
214	Ubiquitination	VGVYEALKDDSWLKG EEEEEECCCCCCCCC	67.54	-
214	Succinylation	VGVYEALKDDSWLKG EEEEEECCCCCCCCC	67.54	23806337
214	Acetylation	VGVYEALKDDSWLKG EEEEEECCCCCCCCC	67.54	22826441
214	Succinylation	VGVYEALKDDSWLKG EEEEEECCCCCCCCC	67.54	-
217	Phosphorylation	YEALKDDSWLKGEFI EEECCCCCCCCCCCE	44.43	21082442
220	Succinylation	LKDDSWLKGEFITTV CCCCCCCCCCCEECH	50.57	23954790
220	Acetylation	LKDDSWLKGEFITTV CCCCCCCCCCCEECH	50.57	23864654
220	Ubiquitination	LKDDSWLKGEFITTV CCCCCCCCCCCEECH	50.57	-
225	Phosphorylation	WLKGEFITTVQQRGA CCCCCCEECHHHHCH	26.66	28464351
230	Methylation	FITTVQQRGAAVIKA CEECHHHHCHHHHHH	21.45	24129315
236	Malonylation	QRGAAVIKARKLSSA HHCHHHHHHHHHHHH	35.22	26320211
239	Acetylation	AAVIKARKLSSAMSA HHHHHHHHHHHHHHH	58.54	22826441
239	Malonylation	AAVIKARKLSSAMSA HHHHHHHHHHHHHHH	58.54	26320211
241	Phosphorylation	VIKARKLSSAMSAAK HHHHHHHHHHHHHHH	21.06	25521595
242	Phosphorylation	IKARKLSSAMSAAKA HHHHHHHHHHHHHHH	38.13	24925903
245	Phosphorylation	RKLSSAMSAAKAIAD HHHHHHHHHHHHHHH	25.45	25521595
248	Acetylation	SSAMSAAKAIADHIR HHHHHHHHHHHHHHH	39.79	22826441
298	Succinylation	VIKNKTWKFVEGLPI EEECCCEEEECCCCC	44.77	23806337
298	Acetylation	VIKNKTWKFVEGLPI EEECCCEEEECCCCC	44.77	23864654
298	Ubiquitination	VIKNKTWKFVEGLPI EEECCCEEEECCCCC	44.77	-
298	Succinylation	VIKNKTWKFVEGLPI EEECCCEEEECCCCC	44.77	-
298	Malonylation	VIKNKTWKFVEGLPI EEECCCEEEECCCCC	44.77	26320211
309	Phosphorylation	GLPINDFSREKMDLT CCCCCCCCHHHHCCC	42.25	22817900
312	Malonylation	INDFSREKMDLTAKE CCCCCHHHHCCCHHH	36.28	26320211
312	Ubiquitination	INDFSREKMDLTAKE CCCCCHHHHCCCHHH	36.28	-
318	Succinylation	EKMDLTAKELTEEKE HHHCCCHHHHHHHHH	48.28	23806337
318	Succinylation	EKMDLTAKELTEEKE HHHCCCHHHHHHHHH	48.28	-
318	Malonylation	EKMDLTAKELTEEKE HHHCCCHHHHHHHHH	48.28	26320211
318	Acetylation	EKMDLTAKELTEEKE HHHCCCHHHHHHHHH	48.28	23806337
318	Ubiquitination	EKMDLTAKELTEEKE HHHCCCHHHHHHHHH	48.28	-
324	Acetylation	AKELTEEKETAFEFL HHHHHHHHHHHHHHH	54.88	23954790
332	Phosphorylation	ETAFEFLSSA----- HHHHHHHHCC-----	29.55	28833060
333	Phosphorylation	TAFEFLSSA------ HHHHHHHCC------	39.90	28833060

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 MDHC_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
118	K	Acetylation		23576753
Acetylation at Lys-118 dramatically enhances enzymatic activity and promotes adipogenic differentiation.

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 MDHC_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of MDHC_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-210, AND MASSSPECTROMETRY.	18034455 [Abstract]

show