dbPTM

ANXA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ANXA2_HUMAN
UniProt AC	P07355
Protein Name	Annexin A2
Gene Name	ANXA2
Organism	Homo sapiens (Human).
Sequence Length	339
Subcellular Localization	Secreted, extracellular space, extracellular matrix, basement membrane . Melanosome . In the lamina beneath the plasma membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Translocated from the cytoplasm to the
Protein Description	Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9. [PubMed: 18799458]
Protein Sequence	MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNAQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSTVHEILC ------CCCHHHHHH	38.85	-
2	O-linked_Glycosylation	------MSTVHEILC ------CCCHHHHHH	38.85	23301498
2	Phosphorylation	------MSTVHEILC ------CCCHHHHHH	38.85	23401153
3	Phosphorylation	-----MSTVHEILCK -----CCCHHHHHHH	25.28	30266825
9	Glutathionylation	STVHEILCKLSLEGD CCHHHHHHHHHCCCC	5.24	22833525
9	S-palmitoylation	STVHEILCKLSLEGD CCHHHHHHHHHCCCC	5.24	29575903
10	Acetylation	TVHEILCKLSLEGDH CHHHHHHHHHCCCCC	37.35	23954790
10	Ubiquitination	TVHEILCKLSLEGDH CHHHHHHHHHCCCCC	37.35	-
12	Phosphorylation	HEILCKLSLEGDHST HHHHHHHHCCCCCCC	15.18	29255136
16	Phosphorylation	CKLSLEGDHSTPPSA HHHHCCCCCCCCCHH	24.16	24719451
18	Phosphorylation	LSLEGDHSTPPSAYG HHCCCCCCCCCHHHC	47.55	29255136
19	O-linked_Glycosylation	SLEGDHSTPPSAYGS HCCCCCCCCCHHHCC	35.48	OGP
19	Phosphorylation	SLEGDHSTPPSAYGS HCCCCCCCCCHHHCC	35.48	29255136
20	Phosphorylation	LEGDHSTPPSAYGSV CCCCCCCCCHHHCCE	24.70	-
20 (in isoform 2)	Phosphorylation	-	24.70	8898866
21	Phosphorylation	EGDHSTPPSAYGSVK CCCCCCCCHHHCCEE	31.51	-
21 (in isoform 2)	Phosphorylation	-	31.51	17081983
22	Phosphorylation	GDHSTPPSAYGSVKA CCCCCCCHHHCCEEE	35.01	29255136
24	Phosphorylation	HSTPPSAYGSVKAYT CCCCCHHHCCEEEEC	17.80	29255136
26	Phosphorylation	TPPSAYGSVKAYTNF CCCHHHCCEEEECCC	14.04	29255136
28	Acetylation	PSAYGSVKAYTNFDA CHHHCCEEEECCCCH	37.06	26051181
28	Ubiquitination	PSAYGSVKAYTNFDA CHHHCCEEEECCCCH	37.06	21906983
28 (in isoform 2)	Ubiquitination	-	37.06	-
30	Nitration	AYGSVKAYTNFDAER HHCCEEEECCCCHHH	9.12	-
30	Phosphorylation	AYGSVKAYTNFDAER HHCCEEEECCCCHHH	9.12	21945579
30 (in isoform 2)	Phosphorylation	-	9.12	29743597
31	Phosphorylation	YGSVKAYTNFDAERD HCCEEEECCCCHHHH	33.98	21945579
36	Phosphorylation	AYTNFDAERDALNIE EECCCCHHHHCCCHH	53.60	27642862
37	Phosphorylation	YTNFDAERDALNIET ECCCCHHHHCCCHHH	35.90	27642862
40	Phosphorylation	FDAERDALNIETAIK CCHHHHCCCHHHHHH	8.54	27642862
42	Phosphorylation	AERDALNIETAIKTK HHHHCCCHHHHHHCC	5.31	27642862
44	Phosphorylation	RDALNIETAIKTKGV HHCCCHHHHHHCCCC	29.86	21815630
46 (in isoform 2)	Ubiquitination	-	8.32	-
47	Acetylation	LNIETAIKTKGVDEV CCHHHHHHCCCCCEE	41.54	23236377
47	Ubiquitination	LNIETAIKTKGVDEV CCHHHHHHCCCCCEE	41.54	21906983
48	Phosphorylation	NIETAIKTKGVDEVT CHHHHHHCCCCCEEE	27.24	21609022
49	Acetylation	IETAIKTKGVDEVTI HHHHHHCCCCCEEEE	52.51	21466224
49	Phosphorylation	IETAIKTKGVDEVTI HHHHHHCCCCCEEEE	52.51	27251275
49	Sumoylation	IETAIKTKGVDEVTI HHHHHHCCCCCEEEE	52.51	25114211
49	Ubiquitination	IETAIKTKGVDEVTI HHHHHHCCCCCEEEE	52.51	21906983
55	Phosphorylation	TKGVDEVTIVNILTN CCCCCEEEEEEEECC	19.70	20068231
61	Phosphorylation	VTIVNILTNRSNAQR EEEEEEECCCCCHHH	25.45	63753367
65 (in isoform 2)	Ubiquitination	-	36.53	-
67 (in isoform 2)	Ubiquitination	-	48.06	-
75	Phosphorylation	RQDIAFAYQRRTKKE HHHHHHHHHHHCHHH	8.97	28152594
79	Phosphorylation	AFAYQRRTKKELASA HHHHHHHCHHHHHHH	48.97	27251275
80	Malonylation	FAYQRRTKKELASAL HHHHHHCHHHHHHHH	42.30	26320211
81	Malonylation	AYQRRTKKELASALK HHHHHCHHHHHHHHH	58.30	26320211
81	Ubiquitination	AYQRRTKKELASALK HHHHHCHHHHHHHHH	58.30	-
85	Phosphorylation	RTKKELASALKSALS HCHHHHHHHHHHHHC	46.92	30266825
88	Ubiquitination	KELASALKSALSGHL HHHHHHHHHHHCCCH	33.14	-
89	Phosphorylation	ELASALKSALSGHLE HHHHHHHHHHCCCHH	34.98	34801879
92	Phosphorylation	SALKSALSGHLETVI HHHHHHHCCCHHHHH	24.71	28450419
93	Phosphorylation	ALKSALSGHLETVIL HHHHHHCCCHHHHHH	30.19	-
97	Phosphorylation	ALSGHLETVILGLLK HHCCCHHHHHHHHHC	21.14	28450419
99 (in isoform 2)	Ubiquitination	-	3.09	-
103	Phosphorylation	ETVILGLLKTPAQYD HHHHHHHHCCHHHCC	5.72	27251275
104	Acetylation	TVILGLLKTPAQYDA HHHHHHHCCHHHCCH	58.46	23954790
104	Ubiquitination	TVILGLLKTPAQYDA HHHHHHHCCHHHCCH	58.46	21906983
105	Phosphorylation	VILGLLKTPAQYDAS HHHHHHCCHHHCCHH	24.67	21815630
109	Phosphorylation	LLKTPAQYDASELKA HHCCHHHCCHHHHHH	18.64	23927012
110	Phosphorylation	LKTPAQYDASELKAS HCCHHHCCHHHHHHH	31.38	27251275
112	Phosphorylation	TPAQYDASELKASMK CHHHCCHHHHHHHHC	40.33	22199227
115	Acetylation	QYDASELKASMKGLG HCCHHHHHHHHCCCC	34.07	23954790
115	Ubiquitination	QYDASELKASMKGLG HCCHHHHHHHHCCCC	34.07	21906983
117	Phosphorylation	DASELKASMKGLGTD CHHHHHHHHCCCCCC	21.31	23927012
118	Sulfoxidation	ASELKASMKGLGTDE HHHHHHHHCCCCCCH	4.82	28183972
119	Acetylation	SELKASMKGLGTDED HHHHHHHCCCCCCHH	48.79	26051181
119	Malonylation	SELKASMKGLGTDED HHHHHHHCCCCCCHH	48.79	26320211
119	Succinylation	SELKASMKGLGTDED HHHHHHHCCCCCCHH	48.79	23954790
119	Ubiquitination	SELKASMKGLGTDED HHHHHHHCCCCCCHH	48.79	-
122	Acetylation	KASMKGLGTDEDSLI HHHHCCCCCCHHHHH	39.53	19608861
122	Ubiquitination	KASMKGLGTDEDSLI HHHHCCCCCCHHHHH	39.53	19608861
122 (in isoform 2)	Ubiquitination	-	39.53	-
123	Phosphorylation	ASMKGLGTDEDSLIE HHHCCCCCCHHHHHH	41.06	23927012
127	Phosphorylation	GLGTDEDSLIEIICS CCCCCHHHHHHHHHH	29.24	20201521
130	Phosphorylation	TDEDSLIEIICSRTN CCHHHHHHHHHHCCH	31.43	27251275
133	S-nitrosocysteine	DSLIEIICSRTNQEL HHHHHHHHHCCHHHH	2.50	-
133	Acetylation	DSLIEIICSRTNQEL HHHHHHHHHCCHHHH	2.50	19608861
133	Glutathionylation	DSLIEIICSRTNQEL HHHHHHHHHCCHHHH	2.50	22833525
133	S-nitrosylation	DSLIEIICSRTNQEL HHHHHHHHHCCHHHH	2.50	22178444
133	S-palmitoylation	DSLIEIICSRTNQEL HHHHHHHHHCCHHHH	2.50	29575903
133 (in isoform 2)	Ubiquitination	-	2.50	-
134	Phosphorylation	SLIEIICSRTNQELQ HHHHHHHHCCHHHHH	31.56	46164657
136	Phosphorylation	IEIICSRTNQELQEI HHHHHHCCHHHHHHH	25.59	20873877
137 (in isoform 2)	Ubiquitination	-	32.02	-
141	Phosphorylation	SRTNQELQEINRVYK HCCHHHHHHHHHHHH	49.09	-
145	Phosphorylation	QELQEINRVYKEMYK HHHHHHHHHHHHHHC	38.51	27251275
147	Phosphorylation	LQEINRVYKEMYKTD HHHHHHHHHHHHCCH	9.67	20068231
148	Acetylation	QEINRVYKEMYKTDL HHHHHHHHHHHCCHH	32.90	25825284
148	Malonylation	QEINRVYKEMYKTDL HHHHHHHHHHHCCHH	32.90	26320211
148	Ubiquitination	QEINRVYKEMYKTDL HHHHHHHHHHHCCHH	32.90	19608861
148 (in isoform 1)	Ubiquitination	-	32.90	21890473
151	S-nitrosocysteine	NRVYKEMYKTDLEKD HHHHHHHHCCHHHHH	16.30	-
151	Phosphorylation	NRVYKEMYKTDLEKD HHHHHHHHCCHHHHH	16.30	30622161
152	Acetylation	RVYKEMYKTDLEKDI HHHHHHHCCHHHHHH	33.96	25825284
152	Malonylation	RVYKEMYKTDLEKDI HHHHHHHCCHHHHHH	33.96	26320211
152	Ubiquitination	RVYKEMYKTDLEKDI HHHHHHHCCHHHHHH	33.96	19608861
153	O-linked_Glycosylation	VYKEMYKTDLEKDII HHHHHHCCHHHHHHH	28.47	23301498
153	Phosphorylation	VYKEMYKTDLEKDII HHHHHHCCHHHHHHH	28.47	20068231
157	Acetylation	MYKTDLEKDIISDTS HHCCHHHHHHHCCCC	62.62	23954790
157	Ubiquitination	MYKTDLEKDIISDTS HHCCHHHHHHHCCCC	62.62	21906983
161	Phosphorylation	DLEKDIISDTSGDFR HHHHHHHCCCCHHHH	34.86	30266825
163	Phosphorylation	EKDIISDTSGDFRKL HHHHHCCCCHHHHHH	28.02	30266825
164	Phosphorylation	KDIISDTSGDFRKLM HHHHCCCCHHHHHHH	41.16	30266825
165	Phosphorylation	DIISDTSGDFRKLMV HHHCCCCHHHHHHHH	39.92	-
166	Acetylation	IISDTSGDFRKLMVA HHCCCCHHHHHHHHH	39.69	19608861
166	Ubiquitination	IISDTSGDFRKLMVA HHCCCCHHHHHHHHH	39.69	21890473
166 (in isoform 2)	Ubiquitination	-	39.69	21890473
169	Malonylation	DTSGDFRKLMVALAK CCCHHHHHHHHHHHC	40.71	26320211
169	Methylation	DTSGDFRKLMVALAK CCCHHHHHHHHHHHC	40.71	-
169	Ubiquitination	DTSGDFRKLMVALAK CCCHHHHHHHHHHHC	40.71	-
170	Acetylation	TSGDFRKLMVALAKG CCHHHHHHHHHHHCC	2.66	19608861
170	Ubiquitination	TSGDFRKLMVALAKG CCHHHHHHHHHHHCC	2.66	19608861
170 (in isoform 2)	Ubiquitination	-	2.66	-
171	Phosphorylation	SGDFRKLMVALAKGR CHHHHHHHHHHHCCC	1.53	-
171	Sulfoxidation	SGDFRKLMVALAKGR CHHHHHHHHHHHCCC	1.53	30846556
175	Acetylation	RKLMVALAKGRRAED HHHHHHHHCCCCCCC	11.52	19608861
175	Ubiquitination	RKLMVALAKGRRAED HHHHHHHHCCCCCCC	11.52	19608861
175 (in isoform 2)	Ubiquitination	-	11.52	-
176	Acetylation	KLMVALAKGRRAEDG HHHHHHHCCCCCCCC	54.52	23236377
176	Malonylation	KLMVALAKGRRAEDG HHHHHHHCCCCCCCC	54.52	26320211
176	Succinylation	KLMVALAKGRRAEDG HHHHHHHCCCCCCCC	54.52	23954790
176	Ubiquitination	KLMVALAKGRRAEDG HHHHHHHCCCCCCCC	54.52	-
179	Phosphorylation	VALAKGRRAEDGSVI HHHHCCCCCCCCCCC	51.50	27251275
182	Phosphorylation	AKGRRAEDGSVIDYE HCCCCCCCCCCCCCE	54.40	27251275
184	Phosphorylation	GRRAEDGSVIDYELI CCCCCCCCCCCCEEC	28.37	30266825
187 (in isoform 2)	Ubiquitination	-	28.79	-
188	Phosphorylation	EDGSVIDYELIDQDA CCCCCCCCEECCCCH	11.08	23927012
194 (in isoform 2)	Ubiquitination	-	39.56	-
199	Phosphorylation	DQDARDLYDAGVKRK CCCHHHHHHHCCCCC	14.18	27273156
202	Phosphorylation	ARDLYDAGVKRKGTD HHHHHHHCCCCCCCC	23.68	27251275
204	Acetylation	DLYDAGVKRKGTDVP HHHHHCCCCCCCCCC	47.69	26051181
204	Ubiquitination	DLYDAGVKRKGTDVP HHHHHCCCCCCCCCC	47.69	21906983
206	Phosphorylation	YDAGVKRKGTDVPKW HHHCCCCCCCCCCHH	61.52	27642862
212	Acetylation	RKGTDVPKWISIMTE CCCCCCCHHHHHHCC	57.94	23954790
212	Ubiquitination	RKGTDVPKWISIMTE CCCCCCCHHHHHHCC	57.94	21906983
215	Phosphorylation	TDVPKWISIMTERSV CCCCHHHHHHCCCCC	12.75	9403753
217	Phosphorylation	VPKWISIMTERSVPH CCHHHHHHCCCCCHH	2.25	-
217	Sulfoxidation	VPKWISIMTERSVPH CCHHHHHHCCCCCHH	2.25	30846556
218	Phosphorylation	PKWISIMTERSVPHL CHHHHHHCCCCCHHH	26.95	82570423
221	Phosphorylation	ISIMTERSVPHLQKV HHHHCCCCCHHHHHH	33.49	30266825
222 (in isoform 2)	Ubiquitination	-	4.30	-
227	Acetylation	RSVPHLQKVFDRYKS CCCHHHHHHHHHHHC	51.75	23954790
227	Methylation	RSVPHLQKVFDRYKS CCCHHHHHHHHHHHC	51.75	19608861
227	Succinylation	RSVPHLQKVFDRYKS CCCHHHHHHHHHHHC	51.75	23954790
227	Ubiquitination	RSVPHLQKVFDRYKS CCCHHHHHHHHHHHC	51.75	19608861
227 (in isoform 1)	Ubiquitination	-	51.75	21890473
230 (in isoform 2)	Ubiquitination	-	56.86	-
232	Phosphorylation	LQKVFDRYKSYSPYD HHHHHHHHHCCCHHH	13.21	23312004
233	Acetylation	QKVFDRYKSYSPYDM HHHHHHHHCCCHHHH	43.76	25825284
233	Malonylation	QKVFDRYKSYSPYDM HHHHHHHHCCCHHHH	43.76	26320211
233	Phosphorylation	QKVFDRYKSYSPYDM HHHHHHHHCCCHHHH	43.76	27251275
233	Ubiquitination	QKVFDRYKSYSPYDM HHHHHHHHCCCHHHH	43.76	-
234	Phosphorylation	KVFDRYKSYSPYDML HHHHHHHCCCHHHHH	23.16	21945579
235	Phosphorylation	VFDRYKSYSPYDMLE HHHHHHCCCHHHHHH	14.98	21945579
236	Phosphorylation	FDRYKSYSPYDMLES HHHHHCCCHHHHHHH	24.87	21945579
238	Nitration	RYKSYSPYDMLESIR HHHCCCHHHHHHHHH	14.19	-
238	Phosphorylation	RYKSYSPYDMLESIR HHHCCCHHHHHHHHH	14.19	21945579
239	Phosphorylation	YKSYSPYDMLESIRK HHCCCHHHHHHHHHH	38.28	27251275
240	Sulfoxidation	KSYSPYDMLESIRKE HCCCHHHHHHHHHHH	3.54	30846556
243	Phosphorylation	SPYDMLESIRKEVKG CHHHHHHHHHHHHCC	24.59	21945579
245	Acetylation	YDMLESIRKEVKGDL HHHHHHHHHHHCCHH	38.06	19608861
245	Ubiquitination	YDMLESIRKEVKGDL HHHHHHHHHHHCCHH	38.06	21890473
245 (in isoform 2)	Ubiquitination	-	38.06	21890473
246	Ubiquitination	DMLESIRKEVKGDLE HHHHHHHHHHCCHHH	66.25	-
249	Ubiquitination	ESIRKEVKGDLENAF HHHHHHHCCHHHHHH	48.04	-
251 (in isoform 2)	Ubiquitination	-	45.12	-
252	Phosphorylation	RKEVKGDLENAFLNL HHHHCCHHHHHHHHH	8.13	27251275
253	Phosphorylation	KEVKGDLENAFLNLV HHHCCHHHHHHHHHH	51.78	17389395
256	Phosphorylation	KGDLENAFLNLVQCI CCHHHHHHHHHHHHH	7.58	27642862
262	Glutathionylation	AFLNLVQCIQNKPLY HHHHHHHHHHCCCCH	2.42	14668336
262	S-nitrosylation	AFLNLVQCIQNKPLY HHHHHHHHHHCCCCH	2.42	25040305
266	Acetylation	LVQCIQNKPLYFADR HHHHHHCCCCHHHHH	21.74	21466224
266	Sumoylation	LVQCIQNKPLYFADR HHHHHHCCCCHHHHH	21.74	-
266	Ubiquitination	LVQCIQNKPLYFADR HHHHHHCCCCHHHHH	21.74	21906983
269	Phosphorylation	CIQNKPLYFADRLYD HHHCCCCHHHHHHHH	12.78	310709061
275	Phosphorylation	LYFADRLYDSMKGKG CHHHHHHHHHHCCCC	13.58	19534553
277	Phosphorylation	FADRLYDSMKGKGTR HHHHHHHHHCCCCCC	14.61	23312004
279	Acetylation	DRLYDSMKGKGTRDK HHHHHHHCCCCCCCH	62.51	19608861
279	Malonylation	DRLYDSMKGKGTRDK HHHHHHHCCCCCCCH	62.51	26320211
279	Ubiquitination	DRLYDSMKGKGTRDK HHHHHHHCCCCCCCH	62.51	19608861
281	Ubiquitination	LYDSMKGKGTRDKVL HHHHHCCCCCCCHHH	52.14	-
296	Phosphorylation	IRIMVSRSEVDMLKI EEEEECHHHHCHHHH	34.17	21712546
297	Acetylation	RIMVSRSEVDMLKIR EEEECHHHHCHHHHH	41.23	19608861
297 (in isoform 2)	Ubiquitination	-	41.23	-
299 (in isoform 2)	Ubiquitination	-	32.42	-
302	Acetylation	RSEVDMLKIRSEFKR HHHHCHHHHHHHHHH	29.45	23954790
302	Ubiquitination	RSEVDMLKIRSEFKR HHHHCHHHHHHHHHH	29.45	21906983
305	Phosphorylation	VDMLKIRSEFKRKYG HCHHHHHHHHHHHHC	51.35	23312004
310	Acetylation	IRSEFKRKYGKSLYY HHHHHHHHHCCCCEE	59.97	25825284
310	Malonylation	IRSEFKRKYGKSLYY HHHHHHHHHCCCCEE	59.97	26320211
313	Acetylation	EFKRKYGKSLYYYIQ HHHHHHCCCCEEEEE	33.91	23954790
313	Malonylation	EFKRKYGKSLYYYIQ HHHHHHCCCCEEEEE	33.91	26320211
313	Methylation	EFKRKYGKSLYYYIQ HHHHHHCCCCEEEEE	33.91	19608861
313	Ubiquitination	EFKRKYGKSLYYYIQ HHHHHHCCCCEEEEE	33.91	19608861
313 (in isoform 1)	Ubiquitination	-	33.91	21890473
314	Phosphorylation	FKRKYGKSLYYYIQQ HHHHHCCCCEEEEEC	19.76	30804295
316	Phosphorylation	RKYGKSLYYYIQQDT HHHCCCCEEEEECCC	11.00	21082442
317	Phosphorylation	KYGKSLYYYIQQDTK HHCCCCEEEEECCCC	10.21	27273156
318	Phosphorylation	YGKSLYYYIQQDTKG HCCCCEEEEECCCCC	4.43	21082442
320	Acetylation	KSLYYYIQQDTKGDY CCCEEEEECCCCCCH	20.98	19608861
320	Ubiquitination	KSLYYYIQQDTKGDY CCCEEEEECCCCCCH	20.98	19608861
320 (in isoform 2)	Ubiquitination	-	20.98	-
323	Phosphorylation	YYYIQQDTKGDYQKA EEEEECCCCCCHHHH	32.37	28152594
324	Acetylation	YYIQQDTKGDYQKAL EEEECCCCCCHHHHH	59.06	23954790
324	Sumoylation	YYIQQDTKGDYQKAL EEEECCCCCCHHHHH	59.06	-
324	Ubiquitination	YYIQQDTKGDYQKAL EEEECCCCCCHHHHH	59.06	2190698
327	Phosphorylation	QQDTKGDYQKALLYL ECCCCCCHHHHHHHH	22.15	28152594
329	Acetylation	DTKGDYQKALLYLCG CCCCCHHHHHHHHCC	34.47	26051181
329	Ubiquitination	DTKGDYQKALLYLCG CCCCCHHHHHHHHCC	34.47	-
331	Acetylation	KGDYQKALLYLCGGD CCCHHHHHHHHCCCC	4.10	19608861
331	Ubiquitination	KGDYQKALLYLCGGD CCCHHHHHHHHCCCC	4.10	21890473
331 (in isoform 2)	Ubiquitination	-	4.10	21890473
332	Phosphorylation	GDYQKALLYLCGGDD CCHHHHHHHHCCCCC	3.52	27251275
333	Phosphorylation	DYQKALLYLCGGDD- CHHHHHHHHCCCCC-	10.78	28152594
334	Phosphorylation	YQKALLYLCGGDD-- HHHHHHHHCCCCC--	1.90	27642862
335	Glutathionylation	QKALLYLCGGDD--- HHHHHHHCCCCC---	3.46	14668336
335	Phosphorylation	QKALLYLCGGDD--- HHHHHHHCCCCC---	3.46	27642862
335	S-palmitoylation	QKALLYLCGGDD--- HHHHHHHCCCCC---	3.46	29575903
336	Phosphorylation	KALLYLCGGDD---- HHHHHHCCCCC----	39.71	27642862
342 (in isoform 2)	Ubiquitination	-		-
347 (in isoform 2)	Ubiquitination	-		-
351	Phosphorylation	------------------- -------------------		27251275

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
12	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
24	Y	Phosphorylation	Kinase	IGF1R	P08069	PSP
24	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
24	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
26	S	Phosphorylation	Kinase	PKCA	P04409	PSP
26	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
26	S	Phosphorylation	Kinase	PKCA	P05696	PSP
26	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
26	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
26	S	Phosphorylation	Kinase	PKC	-	Uniprot
26	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	CBLL1	Q75N03	PMID:31952268

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ANXA2_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 ANXA2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CATB_HUMAN	CTSB	physical	10777578
TPA_HUMAN	PLAT	physical	12468550
APOH_HUMAN	APOH	physical	10809787
S10AA_HUMAN	S100A10	physical	18434302
STAT6_HUMAN	STAT6	physical	20121258
GAG_HV1H2	gag	physical	16501079
A4_HUMAN	APP	physical	21832049
RACK1_HUMAN	GNB2L1	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RL11_HUMAN	RPL11	physical	22939629
MLH1_HUMAN	MLH1	physical	20706999
HMGA1_HUMAN	HMGA1	physical	18850631
DNJC8_HUMAN	DNAJC8	physical	22863883
PA24A_HUMAN	PLA2G4A	physical	14599294
S10AA_HUMAN	S100A10	physical	26186194
ANX13_HUMAN	ANXA13	physical	26186194
EWS_HUMAN	EWSR1	physical	26344197
PCBP2_HUMAN	PCBP2	physical	26344197
PDCD6_HUMAN	PDCD6	physical	26344197
PA24A_HUMAN	PLA2G4A	physical	18065419
S10AA_HUMAN	S100A10	physical	18065419
S10AA_HUMAN	S100A10	physical	28514442
ANX13_HUMAN	ANXA13	physical	28514442
AHNK2_HUMAN	AHNAK2	physical	28514442
KLH42_HUMAN	KLHL42	physical	28514442
STAT3_HUMAN	STAT3	physical	23691485

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00031	Tenecteplase

Regulatory Network of ANXA2_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-104; LYS-115; LYS-148;LYS-152; LYS-157; LYS-227; LYS-279; LYS-302 AND LYS-313, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.	16565220 [Abstract]
"The protein-tyrosine kinase substrate p36 is also a substrate forprotein kinase C in vitro and in vivo."; Gould K.L., Woodgett J.R., Isacke C.M., Hunter T.; Mol. Cell. Biol. 6:2738-2744(1986). Cited for: PHOSPHORYLATION AT SER-26.	2946940 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19, AND MASSSPECTROMETRY.	17924679 [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 THR-19, AND MASSSPECTROMETRY.	17081983 [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-275, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24; TYR-30; TYR-188 ANDTYR-238, AND MASS SPECTROMETRY.	17389395 [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 TYR-24, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24; TYR-30; TYR-188;TYR-199; TYR-238; TYR-316; TYR-317 AND TYR-318, AND MASS SPECTROMETRY.	18083107 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, AND MASSSPECTROMETRY.	15951569 [Abstract]
"An annexin 2 phosphorylation switch mediates p11-dependenttranslocation of annexin 2 to the cell surface."; Deora A.B., Kreitzer G., Jacovina A.T., Hajjar K.A.; J. Biol. Chem. 279:43411-43418(2004). Cited for: PHOSPHORYLATION AT TYR-24, AND MUTAGENESIS OF TYR-24.	15302870 [Abstract]