dbPTM

ALDOA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ALDOA_HUMAN
UniProt AC	P04075
Protein Name	Fructose-bisphosphate aldolase A
Gene Name	ALDOA
Organism	Homo sapiens (Human).
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	MPYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFVSNHAY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MPYQYPALTP -----CCCCCCCCCH	21.27	27273156
5	Phosphorylation	---MPYQYPALTPEQ ---CCCCCCCCCHHH	5.66	27273156
9	Phosphorylation	PYQYPALTPEQKKEL CCCCCCCCHHHHHHH	27.21	19664994
13	Acetylation	PALTPEQKKELSDIA CCCCHHHHHHHHHHH	46.70	16916647
13	Malonylation	PALTPEQKKELSDIA CCCCHHHHHHHHHHH	46.70	26320211
13	Succinylation	PALTPEQKKELSDIA CCCCHHHHHHHHHHH	46.70	23954790
13	Ubiquitination	PALTPEQKKELSDIA CCCCHHHHHHHHHHH	46.70	-
14	Acetylation	ALTPEQKKELSDIAH CCCHHHHHHHHHHHH	64.68	30583241
14	Malonylation	ALTPEQKKELSDIAH CCCHHHHHHHHHHHH	64.68	26320211
14	Ubiquitination	ALTPEQKKELSDIAH CCCHHHHHHHHHHHH	64.68	21890473
17	Phosphorylation	PEQKKELSDIAHRIV HHHHHHHHHHHHHHH	28.23	20068231
28	Acetylation	HRIVAPGKGILAADE HHHHCCCCCEEEEEC	41.54	26051181
28	Ubiquitination	HRIVAPGKGILAADE HHHHCCCCCEEEEEC	41.54	21890473
36	Phosphorylation	GILAADESTGSIAKR CEEEEECCHHHHHHH	38.32	29255136
37	Phosphorylation	ILAADESTGSIAKRL EEEEECCHHHHHHHH	32.66	29255136
39	Phosphorylation	AADESTGSIAKRLQS EEECCHHHHHHHHHH	21.33	19664994
42	Sumoylation	ESTGSIAKRLQSIGT CCHHHHHHHHHHHCC	52.55	-
42	Acetylation	ESTGSIAKRLQSIGT CCHHHHHHHHHHHCC	52.55	19608861
42	Malonylation	ESTGSIAKRLQSIGT CCHHHHHHHHHHHCC	52.55	26320211
42	Sumoylation	ESTGSIAKRLQSIGT CCHHHHHHHHHHHCC	52.55	19608861
42	Ubiquitination	ESTGSIAKRLQSIGT CCHHHHHHHHHHHCC	52.55	20639865
46	Phosphorylation	SIAKRLQSIGTENTE HHHHHHHHHCCCCCH	27.81	29255136
49	Phosphorylation	KRLQSIGTENTEENR HHHHHHCCCCCHHHH	25.13	30266825
52	Phosphorylation	QSIGTENTEENRRFY HHHCCCCCHHHHHHH	38.14	23927012
53 (in isoform 2)	Phosphorylation	-	65.93	30622161
56	Methylation	TENTEENRRFYRQLL CCCCHHHHHHHHHHH	33.11	-
57	Phosphorylation	ENTEENRRFYRQLLL CCCHHHHHHHHHHHH	44.52	27642862
57 (in isoform 2)	Phosphorylation	-	44.52	30622161
59 (in isoform 2)	Phosphorylation	-	8.81	20068231
65	Phosphorylation	FYRQLLLTADDRVNP HHHHHHHCCCCCCCH	28.19	20068231
69	Methylation	LLLTADDRVNPCIGG HHHCCCCCCCHHHCC	30.57	-
71	Phosphorylation	LTADDRVNPCIGGVI HCCCCCCCHHHCCEE	26.98	27251275
73	S-nitrosocysteine	ADDRVNPCIGGVILF CCCCCCHHHCCEEEE	3.68	-
73	S-nitrosylation	ADDRVNPCIGGVILF CCCCCCHHHCCEEEE	3.68	22178444
73	S-palmitoylation	ADDRVNPCIGGVILF CCCCCCHHHCCEEEE	3.68	29575903
83	Phosphorylation	GVILFHETLYQKADD CEEEEEEHHHHHCCC	23.38	22673903
85	Phosphorylation	ILFHETLYQKADDGR EEEEEHHHHHCCCCC	18.52	22673903
87	Acetylation	FHETLYQKADDGRPF EEEHHHHHCCCCCCC	39.98	25953088
87	Ubiquitination	FHETLYQKADDGRPF EEEHHHHHCCCCCCC	39.98	-
90	Phosphorylation	TLYQKADDGRPFPQV HHHHHCCCCCCCCCC	60.92	27251275
91	Phosphorylation	LYQKADDGRPFPQVI HHHHCCCCCCCCCCH	39.44	27251275
93	Phosphorylation	QKADDGRPFPQVIKS HHCCCCCCCCCCHHC	51.29	27251275
96	Acetylation	DDGRPFPQVIKSKGG CCCCCCCCCHHCCCC	50.36	19608861
96	Ubiquitination	DDGRPFPQVIKSKGG CCCCCCCCCHHCCCC	50.36	19608861
99	Acetylation	RPFPQVIKSKGGVVG CCCCCCHHCCCCEEE	47.46	23236377
99	Malonylation	RPFPQVIKSKGGVVG CCCCCCHHCCCCEEE	47.46	26320211
99	Methylation	RPFPQVIKSKGGVVG CCCCCCHHCCCCEEE	47.46	-
99	Other	RPFPQVIKSKGGVVG CCCCCCHHCCCCEEE	47.46	29775581
99	Ubiquitination	RPFPQVIKSKGGVVG CCCCCCHHCCCCEEE	47.46	-
100	Phosphorylation	PFPQVIKSKGGVVGI CCCCCHHCCCCEEEE	25.96	19764811
101	Methylation	FPQVIKSKGGVVGIK CCCCHHCCCCEEEEE	55.47	-
101	Ubiquitination	FPQVIKSKGGVVGIK CCCCHHCCCCEEEEE	55.47	21906983
108	Sumoylation	KGGVVGIKVDKGVVP CCCEEEEEECCCCEE	38.15	-
108	Acetylation	KGGVVGIKVDKGVVP CCCEEEEEECCCCEE	38.15	19608861
108	Malonylation	KGGVVGIKVDKGVVP CCCEEEEEECCCCEE	38.15	26320211
108	Sumoylation	KGGVVGIKVDKGVVP CCCEEEEEECCCCEE	38.15	19608861
108	Ubiquitination	KGGVVGIKVDKGVVP CCCEEEEEECCCCEE	38.15	21890473
111	N6-malonyllysine	VVGIKVDKGVVPLAG EEEEEECCCCEECCC	57.50	-
111	Acetylation	VVGIKVDKGVVPLAG EEEEEECCCCEECCC	57.50	23954790
111	Malonylation	VVGIKVDKGVVPLAG EEEEEECCCCEECCC	57.50	26320211
111	Ubiquitination	VVGIKVDKGVVPLAG EEEEEECCCCEECCC	57.50	21890473
119	Phosphorylation	GVVPLAGTNGETTTQ CCEECCCCCCCCCCC	34.15	21601212
123	Phosphorylation	LAGTNGETTTQGLDG CCCCCCCCCCCCCCH	36.22	25627689
124	Phosphorylation	AGTNGETTTQGLDGL CCCCCCCCCCCCCHH	16.90	25627689
125	Phosphorylation	GTNGETTTQGLDGLS CCCCCCCCCCCCHHH	28.23	25627689
132	Phosphorylation	TQGLDGLSERCAQYK CCCCCHHHHHHHHHH	28.64	25159151
134	Methylation	GLDGLSERCAQYKKD CCCHHHHHHHHHHHC	20.07	-
138	Phosphorylation	LSERCAQYKKDGADF HHHHHHHHHHCCHHH	11.07	-
139	Acetylation	SERCAQYKKDGADFA HHHHHHHHHCCHHHH	32.10	22361385
139	Ubiquitination	SERCAQYKKDGADFA HHHHHHHHHCCHHHH	32.10	-
140	Ubiquitination	ERCAQYKKDGADFAK HHHHHHHHCCHHHHE	57.36	21906983
147	Acetylation	KDGADFAKWRCVLKI HCCHHHHEEEEEEEE	34.85	21466224
147	Malonylation	KDGADFAKWRCVLKI HCCHHHHEEEEEEEE	34.85	26320211
147	Ubiquitination	KDGADFAKWRCVLKI HCCHHHHEEEEEEEE	34.85	-
153	Acetylation	AKWRCVLKIGEHTPS HEEEEEEEECCCCHH	28.41	23954790
153	Ubiquitination	AKWRCVLKIGEHTPS HEEEEEEEECCCCHH	28.41	21890473
158	Phosphorylation	VLKIGEHTPSALAIM EEEECCCCHHHHHHH	18.03	28450419
160	Phosphorylation	KIGEHTPSALAIMEN EECCCCHHHHHHHHC	36.75	28450419
162	Acetylation	GEHTPSALAIMENAN CCCCHHHHHHHHCHH	3.78	19608861
162	Ubiquitination	GEHTPSALAIMENAN CCCCHHHHHHHHCHH	3.78	19608861
165	Sulfoxidation	TPSALAIMENANVLA CHHHHHHHHCHHHHH	2.43	21406390
174	Phosphorylation	NANVLARYASICQQN CHHHHHHHHHHHHHC	10.09	28450419
176	Phosphorylation	NVLARYASICQQNGI HHHHHHHHHHHHCCC	18.24	81018241
178	S-palmitoylation	LARYASICQQNGIVP HHHHHHHHHHCCCCC	2.93	29575903
186	Phosphorylation	QQNGIVPIVEPEILP HHCCCCCCCCCCCCC	3.67	27251275
200	Acetylation	PDGDHDLKRCQYVTE CCCCCCHHHHHHHHH	58.13	23954790
200	Succinylation	PDGDHDLKRCQYVTE CCCCCCHHHHHHHHH	58.13	23954790
200	Ubiquitination	PDGDHDLKRCQYVTE CCCCCCHHHHHHHHH	58.13	-
204	Phosphorylation	HDLKRCQYVTEKVLA CCHHHHHHHHHHHHH	16.99	21082442
206	Phosphorylation	LKRCQYVTEKVLAAV HHHHHHHHHHHHHHH	25.75	28152594
208	Acetylation	RCQYVTEKVLAAVYK HHHHHHHHHHHHHHH	32.93	25953088
208	Ubiquitination	RCQYVTEKVLAAVYK HHHHHHHHHHHHHHH	32.93	21890473
212	Phosphorylation	VTEKVLAAVYKALSD HHHHHHHHHHHHHCC	10.87	27251275
214	Phosphorylation	EKVLAAVYKALSDHH HHHHHHHHHHHCCCC	5.94	7998215
215	Methylation	KVLAAVYKALSDHHI HHHHHHHHHHCCCCE	35.93	-
215	Ubiquitination	KVLAAVYKALSDHHI HHHHHHHHHHCCCCE	35.93	-
218	Phosphorylation	AAVYKALSDHHIYLE HHHHHHHCCCCEEEE	39.49	27259358
223	Phosphorylation	ALSDHHIYLEGTLLK HHCCCCEEEECEEEC	8.37	27155012
227	Phosphorylation	HHIYLEGTLLKPNMV CCEEEECEEECCCCC	21.39	25693802
230	Acetylation	YLEGTLLKPNMVTPG EEECEEECCCCCCCC	37.14	23954790
230	Phosphorylation	YLEGTLLKPNMVTPG EEECEEECCCCCCCC	37.14	27251275
230	Ubiquitination	YLEGTLLKPNMVTPG EEECEEECCCCCCCC	37.14	19608861
235	Phosphorylation	LLKPNMVTPGHACTQ EECCCCCCCCCCCCC	16.88	19060867
240	S-nitrosocysteine	MVTPGHACTQKFSHE CCCCCCCCCCCCCHH	3.25	-
240	S-nitrosylation	MVTPGHACTQKFSHE CCCCCCCCCCCCCHH	3.25	22178444
241	Phosphorylation	VTPGHACTQKFSHEE CCCCCCCCCCCCHHH	35.26	19060867
243	Acetylation	PGHACTQKFSHEEIA CCCCCCCCCCHHHHH	30.59	25953088
251	Sulfoxidation	FSHEEIAMATVTALR CCHHHHHHHHHHHHH	3.84	21406390
253	Phosphorylation	HEEIAMATVTALRRT HHHHHHHHHHHHHHH	12.81	-
255	Phosphorylation	EIAMATVTALRRTVP HHHHHHHHHHHHHCC	18.67	26437602
258	Phosphorylation	MATVTALRRTVPPAV HHHHHHHHHHCCCCC	29.75	27251275
260	Phosphorylation	TVTALRRTVPPAVTG HHHHHHHHCCCCCCE	30.81	30278072
266	Phosphorylation	RTVPPAVTGITFLSG HHCCCCCCEEEEECC	25.60	30278072
269	Phosphorylation	PPAVTGITFLSGGQS CCCCCEEEEECCCCC	21.62	26657352
272	Phosphorylation	VTGITFLSGGQSEEE CCEEEEECCCCCHHH	36.36	30278072
276	Phosphorylation	TFLSGGQSEEEASIN EEECCCCCHHHHEEE	50.69	30278072
281	Phosphorylation	GQSEEEASINLNAIN CCCHHHHEEECCHHC	18.45	22199227
284	Acetylation	EEEASINLNAINKCP HHHHEEECCHHCCCC	4.34	19608861
284	Ubiquitination	EEEASINLNAINKCP HHHHEEECCHHCCCC	4.34	19608861
290	S-palmitoylation	NLNAINKCPLLKPWA ECCHHCCCCCCCCEE	2.19	29575903
294	Acetylation	INKCPLLKPWALTFS HCCCCCCCCEEEEEE	46.31	25953088
294	Methylation	INKCPLLKPWALTFS HCCCCCCCCEEEEEE	46.31	23644510
294	Ubiquitination	INKCPLLKPWALTFS HCCCCCCCCEEEEEE	46.31	21906983
299	Phosphorylation	LLKPWALTFSYGRAL CCCCEEEEEEHHHHH	11.64	28152594
301	Phosphorylation	KPWALTFSYGRALQA CCEEEEEEHHHHHHH	22.80	28152594
302	Phosphorylation	PWALTFSYGRALQAS CEEEEEEHHHHHHHH	13.36	28152594
309	Phosphorylation	YGRALQASALKAWGG HHHHHHHHHHHHCCC	22.60	30266825
312	N6-malonyllysine	ALQASALKAWGGKKE HHHHHHHHHCCCCHH	41.64	-
312	Acetylation	ALQASALKAWGGKKE HHHHHHHHHCCCCHH	41.64	23954790
312	Malonylation	ALQASALKAWGGKKE HHHHHHHHHCCCCHH	41.64	26320211
312	Methylation	ALQASALKAWGGKKE HHHHHHHHHCCCCHH	41.64	-
312	Ubiquitination	ALQASALKAWGGKKE HHHHHHHHHCCCCHH	41.64	21890473
317	Ubiquitination	ALKAWGGKKENLKAA HHHHCCCCHHHHHHH	53.64	-
318	Ubiquitination	LKAWGGKKENLKAAQ HHHCCCCHHHHHHHH	55.92	21906983
322	Acetylation	GGKKENLKAAQEEYV CCCHHHHHHHHHHHH	53.94	23954790
322	Malonylation	GGKKENLKAAQEEYV CCCHHHHHHHHHHHH	53.94	26320211
322	Methylation	GGKKENLKAAQEEYV CCCHHHHHHHHHHHH	53.94	-
322	Ubiquitination	GGKKENLKAAQEEYV CCCHHHHHHHHHHHH	53.94	21890473
326	Phosphorylation	ENLKAAQEEYVKRAL HHHHHHHHHHHHHHH	46.71	27251275
328	Phosphorylation	LKAAQEEYVKRALAN HHHHHHHHHHHHHHH	15.54	28152594
330	Acetylation	AAQEEYVKRALANSL HHHHHHHHHHHHHHH	30.93	19608861
330	Methylation	AAQEEYVKRALANSL HHHHHHHHHHHHHHH	30.93	24129315
330	Ubiquitination	AAQEEYVKRALANSL HHHHHHHHHHHHHHH	30.93	21890473
336	Phosphorylation	VKRALANSLACQGKY HHHHHHHHHHHCCCC	16.25	28450419
339	S-nitrosocysteine	ALANSLACQGKYTPS HHHHHHHHCCCCCCC	7.13	-
339	Glutathionylation	ALANSLACQGKYTPS HHHHHHHHCCCCCCC	7.13	22555962
339	S-nitrosylation	ALANSLACQGKYTPS HHHHHHHHCCCCCCC	7.13	22178444
339	S-palmitoylation	ALANSLACQGKYTPS HHHHHHHHCCCCCCC	7.13	29575903
342	Acetylation	NSLACQGKYTPSGQA HHHHHCCCCCCCCCH	21.77	25953088
342	Ubiquitination	NSLACQGKYTPSGQA HHHHHCCCCCCCCCH	21.77	2189047
343	Phosphorylation	SLACQGKYTPSGQAG HHHHCCCCCCCCCHH	30.61	28152594
344	Phosphorylation	LACQGKYTPSGQAGA HHHCCCCCCCCCHHC	17.92	28152594
346	Phosphorylation	CQGKYTPSGQAGAAA HCCCCCCCCCHHCCC	35.42	28152594
354	O-linked_Glycosylation	GQAGAAASESLFVSN CCHHCCCCHHHCCCC	24.00	31492838
354	Phosphorylation	GQAGAAASESLFVSN CCHHCCCCHHHCCCC	24.00	17287340
356	Phosphorylation	AGAAASESLFVSNHA HHCCCCHHHCCCCCC	25.31	17287340
360	Phosphorylation	ASESLFVSNHAY--- CCHHHCCCCCCC---	18.63	25693802
363	Phosphorylation	SLFVSNHAY------ HHCCCCCCC------	18.91	27251275
364	Phosphorylation	LFVSNHAY------- HCCCCCCC-------	16.13	25693802
384	Acetylation	--------------------------- ---------------------------		19608861
384	Ubiquitination	--------------------------- ---------------------------		19608861
400	Phosphorylation	------------------------------------------- -------------------------------------------		27251275
414	Phosphorylation	--------------------------------------------------------- ---------------------------------------------------------		27251275
418	Phosphorylation	------------------------------------------------------------- -------------------------------------------------------------		27642862

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_HUMAN !!

Functions of PTM Sites

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

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PGK1_HUMAN	PGK1	physical	22939629
ALDOC_HUMAN	ALDOC	physical	22939629
CH60_HUMAN	HSPD1	physical	22939629
LEG1_HUMAN	LGALS1	physical	22939629
ALDOB_HUMAN	ALDOB	physical	21988832
ALDOA_HUMAN	ALDOA	physical	21988832
BCAT2_HUMAN	BCAT2	physical	21988832
GALT6_HUMAN	GALNT6	physical	21988832
PIAS4_HUMAN	PIAS4	physical	21988832
CISY_HUMAN	CS	physical	22863883
TNPO3_HUMAN	TNPO3	physical	22863883
ALDOA_HUMAN	ALDOA	physical	25416956
ALDOC_HUMAN	ALDOC	physical	25416956
IFNA4_HUMAN	IFNA4	physical	25416956
THIM_HUMAN	ACAA2	physical	26344197
ACTN4_HUMAN	ACTN4	physical	26344197
ATP5J_HUMAN	ATP5J	physical	26344197
KCRB_HUMAN	CKB	physical	26344197
KCRU_HUMAN	CKMT1B	physical	26344197
KCRS_HUMAN	CKMT2	physical	26344197
DUT_HUMAN	DUT	physical	26344197
ENOA_HUMAN	ENO1	physical	26344197
FABP5_HUMAN	FABP5	physical	26344197
FUMH_HUMAN	FH	physical	26344197
FKBP7_HUMAN	FKBP7	physical	26344197
G3P_HUMAN	GAPDH	physical	26344197
LGUL_HUMAN	GLO1	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
KCAB2_HUMAN	KCNAB2	physical	26344197
LDHA_HUMAN	LDHA	physical	26344197
LKHA4_HUMAN	LTA4H	physical	26344197
NDUS4_HUMAN	NDUFS4	physical	26344197
PGAM2_HUMAN	PGAM2	physical	26344197
PPCE_HUMAN	PREP	physical	26344197
SODM_HUMAN	SOD2	physical	26344197
SUMO4_HUMAN	SUMO4	physical	26344197
TALDO_HUMAN	TALDO1	physical	26344197
UMPS_HUMAN	UMPS	physical	26344197
ALDOC_HUMAN	ALDOC	physical	26496610
DRC1_HUMAN	DRC1	physical	26496610
CARM1_HUMAN	CARM1	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611881	Glycogen storage disease 12 (GSD12)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ALDOA_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-108 AND LYS-330, ANDMASS SPECTROMETRY.	19608861 [Abstract]
"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-13 AND LYS-42, AND MASSSPECTROMETRY.	16916647 [Abstract]
Malonylation
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-111 AND LYS-312.	21908771 [Abstract]
N6-malonyllysine
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-111 AND LYS-312.	21908771 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-39 AND SER-46,AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9; SER-36; THR-37 ANDSER-46, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-235; THR-241; SER-354AND SER-356, AND MASS SPECTROMETRY.	17287340 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC."; Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.; Proteomics 5:3589-3599(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-65, AND MASSSPECTROMETRY.	16097034 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-364, AND MASSSPECTROMETRY.	19534553 [Abstract]
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