dbPTM

ALDOA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ALDOA_MOUSE
UniProt AC	P05064
Protein Name	Fructose-bisphosphate aldolase A
Gene Name	Aldoa
Organism	Mus musculus (Mouse).
Sequence Length	364
Subcellular Localization	Cytoplasm, myofibril, sarcomere, I band. Cytoplasm, myofibril, sarcomere, M line. In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca(2+)..
Protein Description	Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein (By similarity)..
Protein Sequence	MPHPYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYIKRALANSLACQGKYTPSGQSGAAASESLFISNHAY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Nitration	---MPHPYPALTPEQ ---CCCCCCCCCHHH	9.71	-
5	Phosphorylation	---MPHPYPALTPEQ ---CCCCCCCCCHHH	9.71	71539
9	Phosphorylation	PHPYPALTPEQKKEL CCCCCCCCHHHHHHH	27.21	25266776
13	Acetylation	PALTPEQKKELSDIA CCCCHHHHHHHHHHH	46.70	109263
13	Malonylation	PALTPEQKKELSDIA CCCCHHHHHHHHHHH	46.70	26320211
14	Acetylation	ALTPEQKKELSDIAH CCCHHHHHHHHHHHH	64.68	21728379
14	Ubiquitination	ALTPEQKKELSDIAH CCCHHHHHHHHHHHH	64.68	-
17	Phosphorylation	PEQKKELSDIAHRIV HHHHHHHHHHHHHHH	28.23	46162127
28	Ubiquitination	HRIVAPGKGILAADE HHHHCCCCCEEEEEC	41.54	-
36	Phosphorylation	GILAADESTGSIAKR CEEEEECCHHHHHHH	38.32	24925903
37	Phosphorylation	ILAADESTGSIAKRL EEEEECCHHHHHHHH	32.66	25521595
39	Phosphorylation	AADESTGSIAKRLQS EEECCHHHHHHHHHH	21.33	24925903
42	Acetylation	ESTGSIAKRLQSIGT CCHHHHHHHHHHHCC	52.55	22826441
42	Malonylation	ESTGSIAKRLQSIGT CCHHHHHHHHHHHCC	52.55	26320211
42	Succinylation	ESTGSIAKRLQSIGT CCHHHHHHHHHHHCC	52.55	23806337
42	Ubiquitination	ESTGSIAKRLQSIGT CCHHHHHHHHHHHCC	52.55	-
46	Phosphorylation	SIAKRLQSIGTENTE HHHHHHHHHCCCCCH	27.81	25521595
49	Phosphorylation	KRLQSIGTENTEENR HHHHHHCCCCCHHHH	25.13	23429704
52	Phosphorylation	QSIGTENTEENRRFY HHHCCCCCHHHHHHH	38.14	25266776
73	S-nitrosocysteine	ADDRVNPCIGGVILF CCCCCCHHHCCEEEE	3.68	-
73	S-nitrosylation	ADDRVNPCIGGVILF CCCCCCHHHCCEEEE	3.68	22588120
87	Ubiquitination	FHETLYQKADDGRPF EEEHHHHHCCCCCCC	39.98	-
99	Acetylation	RPFPQVIKSKGGVVG CCCCCCHHCCCCEEE	47.46	23806337
99	Other	RPFPQVIKSKGGVVG CCCCCCHHCCCCEEE	47.46	-
99	Succinylation	RPFPQVIKSKGGVVG CCCCCCHHCCCCEEE	47.46	23806337
99	Ubiquitination	RPFPQVIKSKGGVVG CCCCCCHHCCCCEEE	47.46	-
100	Phosphorylation	PFPQVIKSKGGVVGI CCCCCHHCCCCEEEE	25.96	54218509
101	Ubiquitination	FPQVIKSKGGVVGIK CCCCHHCCCCEEEEE	55.47	-
108	Acetylation	KGGVVGIKVDKGVVP CCCEEEEEECCCCEE	38.15	23806337
108	Malonylation	KGGVVGIKVDKGVVP CCCEEEEEECCCCEE	38.15	26320211
108	Ubiquitination	KGGVVGIKVDKGVVP CCCEEEEEECCCCEE	38.15	-
111	N6-malonyllysine	VVGIKVDKGVVPLAG EEEEEECCCCEECCC	57.50	-
111	Acetylation	VVGIKVDKGVVPLAG EEEEEECCCCEECCC	57.50	23806337
111	Malonylation	VVGIKVDKGVVPLAG EEEEEECCCCEECCC	57.50	26320211
111	Ubiquitination	VVGIKVDKGVVPLAG EEEEEECCCCEECCC	57.50	-
119	Phosphorylation	GVVPLAGTNGETTTQ CCEECCCCCCCCCCC	34.15	28464351
132	Phosphorylation	TQGLDGLSERCAQYK CCCCCHHHHHHHHHH	28.64	27180971
135	S-nitrosocysteine	LDGLSERCAQYKKDG CCHHHHHHHHHHHCC	2.13	-
135	S-nitrosylation	LDGLSERCAQYKKDG CCHHHHHHHHHHHCC	2.13	21278135
139	Acetylation	SERCAQYKKDGADFA HHHHHHHHHCCHHHH	32.10	22361389
147	Acetylation	KDGADFAKWRCVLKI HCCHHHHEEEEEEEE	34.85	109331
147	Ubiquitination	KDGADFAKWRCVLKI HCCHHHHEEEEEEEE	34.85	-
150	Glutathionylation	ADFAKWRCVLKIGEH HHHHEEEEEEEECCC	4.01	24333276
153	Acetylation	AKWRCVLKIGEHTPS HEEEEEEEECCCCHH	28.41	21728379
153	Ubiquitination	AKWRCVLKIGEHTPS HEEEEEEEECCCCHH	28.41	-
158	Phosphorylation	VLKIGEHTPSALAIM EEEECCCCHHHHHHH	18.03	26745281
160	Phosphorylation	KIGEHTPSALAIMEN EECCCCHHHHHHHHC	36.75	26745281
174	Nitrated tyrosine	NANVLARYASICQQN CHHHHHHHHHHHHHC	10.09	-
174	Nitration	NANVLARYASICQQN CHHHHHHHHHHHHHC	10.09	-
174	Phosphorylation	NANVLARYASICQQN CHHHHHHHHHHHHHC	10.09	26239621
176	Phosphorylation	NVLARYASICQQNGI HHHHHHHHHHHHCCC	18.24	81018239
178	S-nitrosocysteine	LARYASICQQNGIVP HHHHHHHHHHCCCCC	2.93	-
178	Glutathionylation	LARYASICQQNGIVP HHHHHHHHHHCCCCC	2.93	24333276
178	S-nitrosylation	LARYASICQQNGIVP HHHHHHHHHHCCCCC	2.93	24895380
200	Acetylation	PDGDHDLKRCQYVTE CCCCCCHHHHHHHHH	58.13	69921
200	Ubiquitination	PDGDHDLKRCQYVTE CCCCCCHHHHHHHHH	58.13	-
202	S-nitrosocysteine	GDHDLKRCQYVTEKV CCCCHHHHHHHHHHH	3.06	-
202	S-nitrosylation	GDHDLKRCQYVTEKV CCCCHHHHHHHHHHH	3.06	21278135
204	Phosphorylation	HDLKRCQYVTEKVLA CCHHHHHHHHHHHHH	16.99	25521595
208	Ubiquitination	RCQYVTEKVLAAVYK HHHHHHHHHHHHHHH	32.93	-
214	Phosphorylation	EKVLAAVYKALSDHH HHHHHHHHHHHCCCC	5.94	28542873
218	Phosphorylation	AAVYKALSDHHVYLE HHHHHHHCCCCEEEE	39.49	46162133
223	Phosphorylation	ALSDHHVYLEGTLLK HHCCCCEEEECEEEC	8.48	65333
227	Phosphorylation	HHVYLEGTLLKPNMV CCEEEECEEECCCCC	21.39	46162145
230	Ubiquitination	YLEGTLLKPNMVTPG EEECEEECCCCCCCC	37.14	-
240	S-nitrosocysteine	MVTPGHACTQKFSNE CCCCCCCCCCCCCCH	3.25	-
240	Glutathionylation	MVTPGHACTQKFSNE CCCCCCCCCCCCCCH	3.25	24333276
240	S-nitrosylation	MVTPGHACTQKFSNE CCCCCCCCCCCCCCH	3.25	21278135
241	Phosphorylation	VTPGHACTQKFSNEE CCCCCCCCCCCCCHH	35.26	28464351
245	Phosphorylation	HACTQKFSNEEIAMA CCCCCCCCCHHHHHH	50.82	28542873
253	Phosphorylation	NEEIAMATVTALRRT CHHHHHHHHHHHHHH	12.81	22210690
255	Phosphorylation	EIAMATVTALRRTVP HHHHHHHHHHHHHCC	18.67	22210690
260	Phosphorylation	TVTALRRTVPPAVTG HHHHHHHHCCCCCCE	30.81	25293948
266	Phosphorylation	RTVPPAVTGVTFLSG HHCCCCCCEEEEECC	28.21	25293948
269	Phosphorylation	PPAVTGVTFLSGGQS CCCCCEEEEECCCCC	21.87	25293948
272	Phosphorylation	VTGVTFLSGGQSEEE CCEEEEECCCCCHHH	36.36	26745281
276	Phosphorylation	TFLSGGQSEEEASIN EEECCCCCHHHHEEE	50.69	26745281
281	Phosphorylation	GQSEEEASINLNAIN CCCHHHHEEECCCHH	18.45	25293948
290	S-nitrosocysteine	NLNAINKCPLLKPWA ECCCHHCCCCCCCEE	2.19	-
290	S-nitrosylation	NLNAINKCPLLKPWA ECCCHHCCCCCCCEE	2.19	20925432
294	Acetylation	INKCPLLKPWALTFS HHCCCCCCCEEEEEE	46.31	21728379
294	Succinylation	INKCPLLKPWALTFS HHCCCCCCCEEEEEE	46.31	23806337
299	Phosphorylation	LLKPWALTFSYGRAL CCCCEEEEEEHHHHH	11.64	46162151
301	Phosphorylation	KPWALTFSYGRALQA CCEEEEEEHHHHHHH	22.80	26643407
309	Phosphorylation	YGRALQASALKAWGG HHHHHHHHHHHHCCC	22.60	24899341
312	N6-malonyllysine	ALQASALKAWGGKKE HHHHHHHHHCCCCHH	41.64	-
312	Acetylation	ALQASALKAWGGKKE HHHHHHHHHCCCCHH	41.64	23806337
312	Malonylation	ALQASALKAWGGKKE HHHHHHHHHCCCCHH	41.64	26320211
312	Succinylation	ALQASALKAWGGKKE HHHHHHHHHCCCCHH	41.64	23806337
312	Ubiquitination	ALQASALKAWGGKKE HHHHHHHHHCCCCHH	41.64	-
322	Acetylation	GGKKENLKAAQEEYI CCCHHHHHHHHHHHH	53.94	23806337
322	Methylation	GGKKENLKAAQEEYI CCCHHHHHHHHHHHH	53.94	-
322	Succinylation	GGKKENLKAAQEEYI CCCHHHHHHHHHHHH	53.94	23806337
322	Ubiquitination	GGKKENLKAAQEEYI CCCHHHHHHHHHHHH	53.94	-
328	Phosphorylation	LKAAQEEYIKRALAN HHHHHHHHHHHHHHH	15.81	25367039
330	Acetylation	AAQEEYIKRALANSL HHHHHHHHHHHHHHH	30.62	21728379
330	Succinylation	AAQEEYIKRALANSL HHHHHHHHHHHHHHH	30.62	23806337
330	Ubiquitination	AAQEEYIKRALANSL HHHHHHHHHHHHHHH	30.62	-
336	Phosphorylation	IKRALANSLACQGKY HHHHHHHHHHHCCCC	16.25	28542873
339	S-nitrosocysteine	ALANSLACQGKYTPS HHHHHHHHCCCCCCC	7.13	-
339	Glutathionylation	ALANSLACQGKYTPS HHHHHHHHCCCCCCC	7.13	24333276
339	S-nitrosylation	ALANSLACQGKYTPS HHHHHHHHCCCCCCC	7.13	24895380
339	S-palmitoylation	ALANSLACQGKYTPS HHHHHHHHCCCCCCC	7.13	28526873
342	Ubiquitination	NSLACQGKYTPSGQS HHHHHCCCCCCCCCC	21.77	-
343	Phosphorylation	SLACQGKYTPSGQSG HHHHCCCCCCCCCCC	30.61	23984901
344	Phosphorylation	LACQGKYTPSGQSGA HHHCCCCCCCCCCCC	17.92	23984901
346	Phosphorylation	CQGKYTPSGQSGAAA HCCCCCCCCCCCCCC	41.48	26643407
349	Phosphorylation	KYTPSGQSGAAASES CCCCCCCCCCCCCCC	33.65	23984901
354	O-linked_Glycosylation	GQSGAAASESLFISN CCCCCCCCCCEEECC	24.00	136817
354	Phosphorylation	GQSGAAASESLFISN CCCCCCCCCCEEECC	24.00	23984901
356	Phosphorylation	SGAAASESLFISNHA CCCCCCCCEEECCCC	26.53	23984901
360	Phosphorylation	ASESLFISNHAY--- CCCCEEECCCCC---	18.41	25367039
364	Phosphorylation	LFISNHAY------- EEECCCCC-------	16.13	25367039

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 ALDOA_MOUSE !!

Functions of PTM Sites

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

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of ALDOA_MOUSE

Related Literatures of Post-Translational Modification

Nitration
Reference	PubMed
"Endogenously nitrated proteins in mouse brain: links toneurodegenerative disease."; Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,Squier T.C., Bigelow D.J.; Biochemistry 45:8009-8022(2006). Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-174, AND MASS SPECTROMETRY.	16800626 [Abstract]
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-46, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-39, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Quantitative analysis of both protein expression and serine /threonine post-translational modifications through stable isotopelabeling with dithiothreitol."; Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,Hart G.W., Burlingame A.L.; Proteomics 5:388-398(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASSSPECTROMETRY.	15648052 [Abstract]