dbPTM

LDHA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LDHA_MOUSE
UniProt AC	P06151
Protein Name	L-lactate dehydrogenase A chain
Gene Name	Ldha
Organism	Mus musculus (Mouse).
Sequence Length	332
Subcellular Localization	Cytoplasm.
Protein Description
Protein Sequence	MATLKDQLIVNLLKEEQAPQNKITVVGVGAVGMACAISILMKDLADELALVDVMEDKLKGEMMDLQHGSLFLKTPKIVSSKDYCVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNIVKYSPHCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHALSCHGWVLGEHGDSSVPVWSGVNVAGVSLKSLNPELGTDADKEQWKEVHKQVVDSAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPISTMIKGLYGINEDVFLSVPCILGQNGISDVVKVTLTPEEEARLKKSADTLWGIQKELQF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATLKDQLI ------CCCHHHHHH	22.95	23806337
3	Phosphorylation	-----MATLKDQLIV -----CCCHHHHHHH	32.80	29514104
5	Ubiquitination	---MATLKDQLIVNL ---CCCHHHHHHHHH	38.79	-
5	Acetylation	---MATLKDQLIVNL ---CCCHHHHHHHHH	38.79	23806337
5	Malonylation	---MATLKDQLIVNL ---CCCHHHHHHHHH	38.79	26073543
5	Succinylation	---MATLKDQLIVNL ---CCCHHHHHHHHH	38.79	-
5	Succinylation	---MATLKDQLIVNL ---CCCHHHHHHHHH	38.79	23806337
14	Acetylation	QLIVNLLKEEQAPQN HHHHHHHHHCCCCCC	63.47	22826441
14	Ubiquitination	QLIVNLLKEEQAPQN HHHHHHHHHCCCCCC	63.47	-
14	Succinylation	QLIVNLLKEEQAPQN HHHHHHHHHCCCCCC	63.47	23806337
38	Phosphorylation	VGMACAISILMKDLA HHHHHHHHHHHHHHH	7.37	20139300
57	Acetylation	LVDVMEDKLKGEMMD HHHHHHHHHCCCCEE	38.50	22733758
57	Ubiquitination	LVDVMEDKLKGEMMD HHHHHHHHHCCCCEE	38.50	-
59	Succinylation	DVMEDKLKGEMMDLQ HHHHHHHCCCCEECC	59.57	23806337
59	Ubiquitination	DVMEDKLKGEMMDLQ HHHHHHHCCCCEECC	59.57	-
59	Acetylation	DVMEDKLKGEMMDLQ HHHHHHHCCCCEECC	59.57	23806337
69	Phosphorylation	MMDLQHGSLFLKTPK CEECCCCCEEECCCC	17.52	24899341
73	Ubiquitination	QHGSLFLKTPKIVSS CCCCEEECCCCCCCC	56.28	-
76	Succinylation	SLFLKTPKIVSSKDY CEEECCCCCCCCCCE	62.06	23806337
76	Acetylation	SLFLKTPKIVSSKDY CEEECCCCCCCCCCE	62.06	23806337
76	Ubiquitination	SLFLKTPKIVSSKDY CEEECCCCCCCCCCE	62.06	-
79	Phosphorylation	LKTPKIVSSKDYCVT ECCCCCCCCCCEEEE	34.83	22210690
80	Phosphorylation	KTPKIVSSKDYCVTA CCCCCCCCCCEEEEC	20.74	22210690
81	Succinylation	TPKIVSSKDYCVTAN CCCCCCCCCEEEECC	45.25	23806337
81	Ubiquitination	TPKIVSSKDYCVTAN CCCCCCCCCEEEECC	45.25	-
81	Acetylation	TPKIVSSKDYCVTAN CCCCCCCCCEEEECC	45.25	23806337
81	Malonylation	TPKIVSSKDYCVTAN CCCCCCCCCEEEECC	45.25	26320211
84	S-palmitoylation	IVSSKDYCVTANSKL CCCCCCEEEECCCEE	2.92	28526873
84	S-nitrosocysteine	IVSSKDYCVTANSKL CCCCCCEEEECCCEE	2.92	-
84	Glutathionylation	IVSSKDYCVTANSKL CCCCCCEEEECCCEE	2.92	24333276
84	S-nitrosylation	IVSSKDYCVTANSKL CCCCCCEEEECCCEE	2.92	21278135
95	Phosphorylation	NSKLVIITAGARQQE CCEEEEEECCCCCCH	14.12	28542873
105	Phosphorylation	ARQQEGESRLNLVQR CCCCHHCHHHHHHHH	53.58	28464351
118	Succinylation	QRNVNIFKFIIPNIV HHHHCCHHHHCCCHH	31.68	23806337
118	Succinylation	QRNVNIFKFIIPNIV HHHHCCHHHHCCCHH	31.68	-
118	Acetylation	QRNVNIFKFIIPNIV HHHHCCHHHHCCCHH	31.68	23806337
118	Malonylation	QRNVNIFKFIIPNIV HHHHCCHHHHCCCHH	31.68	26073543
118	Ubiquitination	QRNVNIFKFIIPNIV HHHHCCHHHHCCCHH	31.68	-
126	Succinylation	FIIPNIVKYSPHCKL HHCCCHHHCCCCCEE	35.89	23806337
126	Ubiquitination	FIIPNIVKYSPHCKL HHCCCHHHCCCCCEE	35.89	-
126	Acetylation	FIIPNIVKYSPHCKL HHCCCHHHCCCCCEE	35.89	23806337
126	Malonylation	FIIPNIVKYSPHCKL HHCCCHHHCCCCCEE	35.89	26320211
137	Phosphorylation	HCKLLIVSNPVDILT CCEEEEECCCHHHHH	28.55	23984901
144	Phosphorylation	SNPVDILTYVAWKIS CCCHHHHHHHHHHCC	19.11	20139300
145	Phosphorylation	NPVDILTYVAWKISG CCHHHHHHHHHHCCC	5.68	20139300
155	Acetylation	WKISGFPKNRVIGSG HHCCCCCCCCEECCC	55.94	23806337
155	Malonylation	WKISGFPKNRVIGSG HHCCCCCCCCEECCC	55.94	26320211
155	Succinylation	WKISGFPKNRVIGSG HHCCCCCCCCEECCC	55.94	23806337
161	Phosphorylation	PKNRVIGSGCNLDSA CCCCEECCCCCCCHH	29.11	-
163	Glutathionylation	NRVIGSGCNLDSARF CCEECCCCCCCHHHH	4.97	24333276
163	S-palmitoylation	NRVIGSGCNLDSARF CCEECCCCCCCHHHH	4.97	28526873
163	S-nitrosylation	NRVIGSGCNLDSARF CCEECCCCCCCHHHH	4.97	24926564
163	S-nitrosocysteine	NRVIGSGCNLDSARF CCEECCCCCCCHHHH	4.97	-
167	Phosphorylation	GSGCNLDSARFRYLM CCCCCCCHHHHHHHH	25.22	28542873
172	Phosphorylation	LDSARFRYLMGERLG CCHHHHHHHHCCCCC	9.79	22345495
184	Phosphorylation	RLGVHALSCHGWVLG CCCEEEEECCCEECC	12.59	26060331
213	Phosphorylation	VAGVSLKSLNPELGT ECCEEHHHCCCCCCC	38.38	24899341
220	Phosphorylation	SLNPELGTDADKEQW HCCCCCCCCCCHHHH	40.41	26525534
224	Succinylation	ELGTDADKEQWKEVH CCCCCCCHHHHHHHH	54.23	23954790
224	Malonylation	ELGTDADKEQWKEVH CCCCCCCHHHHHHHH	54.23	26320211
224	Ubiquitination	ELGTDADKEQWKEVH CCCCCCCHHHHHHHH	54.23	-
224	Acetylation	ELGTDADKEQWKEVH CCCCCCCHHHHHHHH	54.23	23806337
228	Malonylation	DADKEQWKEVHKQVV CCCHHHHHHHHHHHH	49.94	26320211
228	Succinylation	DADKEQWKEVHKQVV CCCHHHHHHHHHHHH	49.94	23954790
228	Ubiquitination	DADKEQWKEVHKQVV CCCHHHHHHHHHHHH	49.94	-
228	Acetylation	DADKEQWKEVHKQVV CCCHHHHHHHHHHHH	49.94	22826441
232	Malonylation	EQWKEVHKQVVDSAY HHHHHHHHHHHHHHH	50.38	26320211
232	Succinylation	EQWKEVHKQVVDSAY HHHHHHHHHHHHHHH	50.38	23806337
232	Acetylation	EQWKEVHKQVVDSAY HHHHHHHHHHHHHHH	50.38	23806337
232	Ubiquitination	EQWKEVHKQVVDSAY HHHHHHHHHHHHHHH	50.38	-
237	Phosphorylation	VHKQVVDSAYEVIKL HHHHHHHHHHHHHHC	22.57	20139300
239	Phosphorylation	KQVVDSAYEVIKLKG HHHHHHHHHHHHCCC	18.06	27566939
243	Succinylation	DSAYEVIKLKGYTSW HHHHHHHHCCCCCHH	49.69	23806337
243	Ubiquitination	DSAYEVIKLKGYTSW HHHHHHHHCCCCCHH	49.69	-
243	Malonylation	DSAYEVIKLKGYTSW HHHHHHHHCCCCCHH	49.69	26320211
243	Acetylation	DSAYEVIKLKGYTSW HHHHHHHHCCCCCHH	49.69	23806337
247	Phosphorylation	EVIKLKGYTSWAIGL HHHHCCCCCHHHHHC	8.94	28576409
293	S-palmitoylation	DVFLSVPCILGQNGI CEEEECCEECCCCCC	3.62	28526873
293	S-nitrosylation	DVFLSVPCILGQNGI CEEEECCEECCCCCC	3.62	21278135
293	Glutathionylation	DVFLSVPCILGQNGI CEEEECCEECCCCCC	3.62	24333276
293	S-nitrosocysteine	DVFLSVPCILGQNGI CEEEECCEECCCCCC	3.62	-
307	Phosphorylation	ISDVVKVTLTPEEEA CCCEEEEECCHHHHH	21.13	25777480
309	Phosphorylation	DVVKVTLTPEEEARL CEEEEECCHHHHHHH	21.20	26824392
318	Succinylation	EEEARLKKSADTLWG HHHHHHHHHHHHHHH	56.31	23806337
318	Succinylation	EEEARLKKSADTLWG HHHHHHHHHHHHHHH	56.31	-
318	Malonylation	EEEARLKKSADTLWG HHHHHHHHHHHHHHH	56.31	26320211
318	Ubiquitination	EEEARLKKSADTLWG HHHHHHHHHHHHHHH	56.31	-
318	Acetylation	EEEARLKKSADTLWG HHHHHHHHHHHHHHH	56.31	23806337
319	Phosphorylation	EEARLKKSADTLWGI HHHHHHHHHHHHHHH	29.77	22210690
322	Phosphorylation	RLKKSADTLWGIQKE HHHHHHHHHHHHHHH	24.91	22210690
328	Acetylation	DTLWGIQKELQF--- HHHHHHHHHHCC---	59.48	22826441
328	Ubiquitination	DTLWGIQKELQF--- HHHHHHHHHHCC---	59.48	-

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 LDHA_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LDHA_MOUSE !!

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 LDHA_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of LDHA_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-239, AND MASSSPECTROMETRY.	18034455 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, AND MASSSPECTROMETRY.	17947660 [Abstract]