dbPTM

ANXA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ANXA1_HUMAN
UniProt AC	P04083
Protein Name	Annexin A1
Gene Name	ANXA1
Organism	Homo sapiens (Human).
Sequence Length	346
Subcellular Localization	Nucleus . Cytoplasm . Cell projection, cilium . Cell membrane . Membrane Peripheral membrane protein . Endosome membrane Peripheral membrane protein . Basolateral cell membrane . Apical cell membrane . Lateral cell membrane . Secreted . Secreted, extr
Protein Description	Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity. [PubMed: 8425544 Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response (By similarity Promotes resolution of inflammation and wound healing]
Protein Sequence	MAMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAMVSEFLK ------CCHHHHHHH	13.69	3303336
3	Sulfoxidation	-----MAMVSEFLKQ -----CCHHHHHHHH	3.09	28465586
5	Phosphorylation	---MAMVSEFLKQAW ---CCHHHHHHHHHH	15.00	26846344
21	Phosphorylation	IENEEQEYVQTVKSS CCCCHHHHHHHHHHC	9.50	20007894
24	Phosphorylation	EEQEYVQTVKSSKGG CHHHHHHHHHHCCCC	21.62	28796482
26	Ubiquitination	QEYVQTVKSSKGGPG HHHHHHHHHCCCCCC	53.02	21906983
27	Phosphorylation	EYVQTVKSSKGGPGS HHHHHHHHCCCCCCC	32.71	19625660
28	Phosphorylation	YVQTVKSSKGGPGSA HHHHHHHCCCCCCCC	29.60	1956339
29	Ubiquitination	VQTVKSSKGGPGSAV HHHHHHCCCCCCCCC	74.99	-
29	Malonylation	VQTVKSSKGGPGSAV HHHHHHCCCCCCCCC	74.99	26320211
29	Acetylation	VQTVKSSKGGPGSAV HHHHHHCCCCCCCCC	74.99	26051181
34	Phosphorylation	SSKGGPGSAVSPYPT HCCCCCCCCCCCCCC	28.73	30266825
37	Phosphorylation	GGPGSAVSPYPTFNP CCCCCCCCCCCCCCC	20.59	22167270
37	O-linked_Glycosylation	GGPGSAVSPYPTFNP CCCCCCCCCCCCCCC	20.59	6357859
39	Phosphorylation	PGSAVSPYPTFNPSS CCCCCCCCCCCCCCC	13.85	30266825
41	Phosphorylation	SAVSPYPTFNPSSDV CCCCCCCCCCCCCHH	30.15	30266825
41	O-linked_Glycosylation	SAVSPYPTFNPSSDV CCCCCCCCCCCCCHH	30.15	OGP
45	Phosphorylation	PYPTFNPSSDVAALH CCCCCCCCCHHHHHH	40.03	25159151
46	Phosphorylation	YPTFNPSSDVAALHK CCCCCCCCHHHHHHH	37.04	25159151
53	Acetylation	SDVAALHKAIMVKGV CHHHHHHHHHHCCCC	40.22	23954790
53	Ubiquitination	SDVAALHKAIMVKGV CHHHHHHHHHHCCCC	40.22	21906983
58	Acetylation	LHKAIMVKGVDEATI HHHHHHCCCCCHHHH	35.52	-
58	Ubiquitination	LHKAIMVKGVDEATI HHHHHHCCCCCHHHH	35.52	21906983
64	Phosphorylation	VKGVDEATIIDILTK CCCCCHHHHHHHHHH	19.20	46164621
70	Phosphorylation	ATIIDILTKRNNAQR HHHHHHHHHCCHHHH	28.43	46164627
71	Acetylation	TIIDILTKRNNAQRQ HHHHHHHHCCHHHHH	50.08	23236377
71	Ubiquitination	TIIDILTKRNNAQRQ HHHHHHHHCCHHHHH	50.08	21906983
81	Ubiquitination	NAQRQQIKAAYLQET HHHHHHHHHHHHHHH	23.72	21906983
84	Phosphorylation	RQQIKAAYLQETGKP HHHHHHHHHHHHCCC	17.49	28152594
88	Phosphorylation	KAAYLQETGKPLDET HHHHHHHHCCCHHHH	37.23	28152594
90	Acetylation	AYLQETGKPLDETLK HHHHHHCCCHHHHHH	50.23	23954790
90	Ubiquitination	AYLQETGKPLDETLK HHHHHHCCCHHHHHH	50.23	906983
90	Malonylation	AYLQETGKPLDETLK HHHHHHCCCHHHHHH	50.23	26320211
95	Phosphorylation	TGKPLDETLKKALTG HCCCHHHHHHHHHCC	43.47	72261247
97	Acetylation	KPLDETLKKALTGHL CCHHHHHHHHHCCCH	43.34	23954790
97	Ubiquitination	KPLDETLKKALTGHL CCHHHHHHHHHCCCH	43.34	-
97	Malonylation	KPLDETLKKALTGHL CCHHHHHHHHHCCCH	43.34	26320211
98	Acetylation	PLDETLKKALTGHLE CHHHHHHHHHCCCHH	52.30	19814793
98	Ubiquitination	PLDETLKKALTGHLE CHHHHHHHHHCCCHH	52.30	21906983
101	Phosphorylation	ETLKKALTGHLEEVV HHHHHHHCCCHHHHH	27.67	101661403
113	Ubiquitination	EVVLALLKTPAQFDA HHHHHHHHCHHHCCH	54.00	-
114	Phosphorylation	VVLALLKTPAQFDAD HHHHHHHCHHHCCHH	24.67	21815630
128	Ubiquitination	DELRAAMKGLGTDED HHHHHHHHCCCCCHH	46.38	21906983
128	Acetylation	DELRAAMKGLGTDED HHHHHHHHCCCCCHH	46.38	26051181
132	Phosphorylation	AAMKGLGTDEDTLIE HHHHCCCCCHHHHHH	41.06	22617229
136	Phosphorylation	GLGTDEDTLIEILAS CCCCCHHHHHHHHHH	27.82	27422710
143	Phosphorylation	TLIEILASRTNKEIR HHHHHHHHCCCHHHH	35.87	63722251
156	Phosphorylation	IRDINRVYREELKRD HHHHHHHHHHHHHHH	14.74	28152594
161	Acetylation	RVYREELKRDLAKDI HHHHHHHHHHHHHHC	47.33	19608861
161	Ubiquitination	RVYREELKRDLAKDI HHHHHHHHHHHHHHC	47.33	19608861
166	Acetylation	ELKRDLAKDITSDTS HHHHHHHHHCCCCCC	57.89	23954790
166	Ubiquitination	ELKRDLAKDITSDTS HHHHHHHHHCCCCCC	57.89	21890473
166	Malonylation	ELKRDLAKDITSDTS HHHHHHHHHCCCCCC	57.89	26320211
169	Phosphorylation	RDLAKDITSDTSGDF HHHHHHCCCCCCHHH	30.59	29255136
170	Phosphorylation	DLAKDITSDTSGDFR HHHHHCCCCCCHHHH	38.94	29255136
172	Phosphorylation	AKDITSDTSGDFRNA HHHCCCCCCHHHHHH	34.08	29255136
173	Phosphorylation	KDITSDTSGDFRNAL HHCCCCCCHHHHHHH	41.16	29255136
182	Phosphorylation	DFRNALLSLAKGDRS HHHHHHHHHHCCCCC	27.42	23403867
185	Acetylation	NALLSLAKGDRSEDF HHHHHHHCCCCCCCC	67.64	23954790
185	Ubiquitination	NALLSLAKGDRSEDF HHHHHHHCCCCCCCC	67.64	21906983
185	Malonylation	NALLSLAKGDRSEDF HHHHHHHCCCCCCCC	67.64	26320211
189	Phosphorylation	SLAKGDRSEDFGVNE HHHCCCCCCCCCCCH	46.38	27050516
201	Phosphorylation	VNEDLADSDARALYE CCHHHCHHHHHHHHH	27.80	30624053
207	Phosphorylation	DSDARALYEAGERRK HHHHHHHHHHHHHCC	11.62	27273156
214	Sumoylation	YEAGERRKGTDVNVF HHHHHHCCCCCCCCC	72.83	-
214	Ubiquitination	YEAGERRKGTDVNVF HHHHHHCCCCCCCCC	72.83	21906983
214	Sumoylation	YEAGERRKGTDVNVF HHHHHHCCCCCCCCC	72.83	28112733
216	Phosphorylation	AGERRKGTDVNVFNT HHHHCCCCCCCCCCH	39.55	20873877
223	Phosphorylation	TDVNVFNTILTTRSY CCCCCCCHHHHCCCH	13.10	27050516
226	Phosphorylation	NVFNTILTTRSYPQL CCCCHHHHCCCHHHH	19.13	46164615
230	Phosphorylation	TILTTRSYPQLRRVF HHHHCCCHHHHHHHH	7.54	22817900
239	Acetylation	QLRRVFQKYTKYSKH HHHHHHHHHHCCCCC	43.34	19608861
239	Ubiquitination	QLRRVFQKYTKYSKH HHHHHHHHHHCCCCC	43.34	19608861
240	Phosphorylation	LRRVFQKYTKYSKHD HHHHHHHHHCCCCCC	9.55	22817900
242	Acetylation	RVFQKYTKYSKHDMN HHHHHHHCCCCCCHH	44.42	26051181
243	Phosphorylation	VFQKYTKYSKHDMNK HHHHHHCCCCCCHHH	18.36	28258704
244	Phosphorylation	FQKYTKYSKHDMNKV HHHHHCCCCCCHHHH	25.68	28258704
245	Acetylation	QKYTKYSKHDMNKVL HHHHCCCCCCHHHHH	40.30	25825284
250	Acetylation	YSKHDMNKVLDLELK CCCCCHHHHHCEEEC	37.22	25825284
250	Ubiquitination	YSKHDMNKVLDLELK CCCCCHHHHHCEEEC	37.22	19608861
257	Ubiquitination	KVLDLELKGDIEKCL HHHCEEECCCHHHHH	45.20	21906983
257	Acetylation	KVLDLELKGDIEKCL HHHCEEECCCHHHHH	45.20	26051181
263	S-palmitoylation	LKGDIEKCLTAIVKC ECCCHHHHHHHHHHH	2.37	29575903
269	Acetylation	KCLTAIVKCATSKPA HHHHHHHHHHHCCHH	16.43	26051181
274	Methylation	IVKCATSKPAFFAEK HHHHHHCCHHHHHHH	35.69	-
274	Ubiquitination	IVKCATSKPAFFAEK HHHHHHCCHHHHHHH	35.69	-
274	Acetylation	IVKCATSKPAFFAEK HHHHHHCCHHHHHHH	35.69	25953088
281	Methylation	KPAFFAEKLHQAMKG CHHHHHHHHHHHHCC	48.08	19608861
281	Acetylation	KPAFFAEKLHQAMKG CHHHHHHHHHHHHCC	48.08	25825284
281	Ubiquitination	KPAFFAEKLHQAMKG CHHHHHHHHHHHHCC	48.08	19608861
287	Ubiquitination	EKLHQAMKGVGTRHK HHHHHHHCCCCHHHH	54.16	21906983
287	Acetylation	EKLHQAMKGVGTRHK HHHHHHHCCCCHHHH	54.16	25953088
294	Acetylation	KGVGTRHKALIRIMV CCCCHHHHHHHHHHH	41.41	25825284
302	Phosphorylation	ALIRIMVSRSEIDMN HHHHHHHCCCCCCHH	16.83	22468782
308	Sulfoxidation	VSRSEIDMNDIKAFY HCCCCCCHHHHHHHH	6.28	30846556
312	Acetylation	EIDMNDIKAFYQKMY CCCHHHHHHHHHHHH	34.99	19608861
312	Ubiquitination	EIDMNDIKAFYQKMY CCCHHHHHHHHHHHH	34.99	19608861
312	Sumoylation	EIDMNDIKAFYQKMY CCCHHHHHHHHHHHH	34.99	19608861
312	Malonylation	EIDMNDIKAFYQKMY CCCHHHHHHHHHHHH	34.99	26320211
317	Ubiquitination	DIKAFYQKMYGISLC HHHHHHHHHHHHHHH	23.78	-
318	Sulfoxidation	IKAFYQKMYGISLCQ HHHHHHHHHHHHHHH	1.87	28465586
319	Phosphorylation	KAFYQKMYGISLCQA HHHHHHHHHHHHHHH	20.53	28152594
322	Phosphorylation	YQKMYGISLCQAILD HHHHHHHHHHHHHHH	20.80	28152594
324	S-nitrosocysteine	KMYGISLCQAILDET HHHHHHHHHHHHHHC	1.73	-
324	S-nitrosylation	KMYGISLCQAILDET HHHHHHHHHHHHHHC	1.73	22178444
332	Ubiquitination	QAILDETKGDYEKIL HHHHHHCCCCHHHHH	47.97	-
332	Sumoylation	QAILDETKGDYEKIL HHHHHHCCCCHHHHH	47.97	25114211
335	Phosphorylation	LDETKGDYEKILVAL HHHCCCCHHHHHHHH	27.99	46164633
337	Ubiquitination	ETKGDYEKILVALCG HCCCCHHHHHHHHCC	34.80	-
343	S-nitrosocysteine	EKILVALCGGN---- HHHHHHHCCCC----	4.77	-
343	S-nitrosylation	EKILVALCGGN---- HHHHHHHCCCC----	4.77	22178444
343	S-palmitoylation	EKILVALCGGN---- HHHHHHHCCCC----	4.77	29575903

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
5	S	Phosphorylation	Kinase	CHAK1	Q96QT4	PSP
21	Y	Phosphorylation	Kinase	EGFR	P00533	Uniprot
21	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
21	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
21	Y	Phosphorylation	Kinase	SRC	P12931	PSP
21	Y	Phosphorylation	Kinase	ABL1	P00519	PhosphoELM
24	T	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
24	T	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
27	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
27	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
27	S	Phosphorylation	Kinase	PKC	-	Uniprot
27	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
28	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
28	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
28	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
28	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
216	T	Phosphorylation	Kinase	PRKG1	Q13976	GPS
216	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
216	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
216	T	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	UBE3A	Q05086	PMID:19204938

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ANXA1_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 ANXA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
S10AB_HUMAN	S100A11	physical	8557678
K2C8_HUMAN	KRT8	physical	9459484
UBE3A_HUMAN	UBE3A	physical	19204938
G3P_HUMAN	GAPDH	physical	21900206
KLH23_HUMAN	KLHL23	physical	21900206
APBB1_HUMAN	APBB1	physical	21900206
CSAD_HUMAN	CSAD	physical	21900206
CA123_HUMAN	C1orf123	physical	21900206
RFA1_HUMAN	RPA1	physical	21900206
U119A_HUMAN	UNC119	physical	21900206
OTUB1_HUMAN	OTUB1	physical	21900206
ERG28_HUMAN	C14orf1	physical	21900206
XRCC6_HUMAN	XRCC6	physical	21900206
KMT2B_HUMAN	KMT2B	physical	21900206
TCPH_HUMAN	CCT7	physical	21900206
UB2D1_HUMAN	UBE2D1	physical	21900206
CSN6_HUMAN	COPS6	physical	21900206
LRIF1_HUMAN	LRIF1	physical	21900206
FAF1_HUMAN	FAF1	physical	21900206
ANXA1_HUMAN	ANXA1	genetic	12689596
ANXA5_HUMAN	ANXA5	physical	12689596
NEMO_HUMAN	IKBKG	physical	21383699
RIPK1_HUMAN	RIPK1	physical	21383699
TF65_HUMAN	RELA	physical	21383699
ANXA4_HUMAN	ANXA4	physical	22939629
HMGA1_HUMAN	HMGA1	physical	18850631
MEIS2_HUMAN	MEIS2	physical	25416956
UBP7_HUMAN	USP7	physical	25695607
ACTS_HUMAN	ACTA1	physical	22773844
PA24A_HUMAN	PLA2G4A	physical	17873281
S10AB_HUMAN	S100A11	physical	17932043
PA24A_HUMAN	PLA2G4A	physical	17932043

Drug and Disease Associations

Kegg Disease
H00006	Hairy-cell leukemia
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00288	Amcinonide
DB01234	Dexamethasone
DB00741	Hydrocortisone

Regulatory Network of ANXA1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Characterization by tandem mass spectrometry of structuralmodifications in proteins."; Biemann K., Scoble H.A.; Science 237:992-998(1987). Cited for: ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.	3303336 [Abstract]
"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-161; LYS-239; LYS-250;LYS-281 AND LYS-312, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Phosphorylation of annexin I by TRPM7 channel-kinase."; Dorovkov M.V., Ryazanov A.G.; J. Biol. Chem. 279:50643-50646(2004). Cited for: PHOSPHORYLATION AT SER-5 BY TRPM7.	15485879 [Abstract]
"Location of sites in human lipocortin I that are phosphorylated byprotein tyrosine kinases and protein kinases A and C."; Varticovski L., Chahwala S.B., Whitman M., Cantley L., Schindler D.,Chow E.P., Sinclair L.K., Pepinsky R.B.; Biochemistry 27:3682-3690(1988). Cited for: PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION AT TYR-21 BY EGFR ANDSER-27 BY PKC.	2457390 [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-39 AND TYR-207, AND MASSSPECTROMETRY.	19534553 [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-39 AND TYR-207, AND MASSSPECTROMETRY.	18083107 [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 TYR-21, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-207, AND MASSSPECTROMETRY.	15592455 [Abstract]