dbPTM

ANXA1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ANXA1_MOUSE
UniProt AC	P10107
Protein Name	Annexin A1
Gene Name	Anxa1
Organism	Mus musculus (Mouse).
Sequence Length	346
Subcellular Localization	Nucleus . Cytoplasm . Cell projection, cilium . Basolateral cell membrane . Lateral cell membrane . Cell membrane Peripheral membrane protein . Apical cell membrane . Membrane Peripheral membrane protein . Early endosome . Cytoplasmic vesicle membrane
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: 12475898 Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response]
Protein Sequence	MAMVSEFLKQARFLENQEQEYVQAVKSYKGGPGSAVSPYPSFNVSSDVAALHKAIMVKGVDEATIIDILTKRTNAQRQQIKAAYLQENGKPLDEVLRKALTGHLEEVVLAMLKTPAQFDADELRGAMKGLGTDEDTLIEILTTRSNEQIREINRVYREELKRDLAKDITSDTSGDFRKALLALAKGDRCQDLSVNQDLADTDARALYEAGERRKGTDVNVFTTILTSRSFPHLRRVFQNYGKYSQHDMNKALDLELKGDIEKCLTTIVKCATSTPAFFAEKLYEAMKGAGTRHKALIRIMVSRSEIDMNEIKVFYQKKYGISLCQAILDETKGDYEKILVALCGGN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAMVSEFLK ------CCHHHHHHH	13.69	-
5	Phosphorylation	---MAMVSEFLKQAR ---CCHHHHHHHHHH	15.00	28638064
9	Acetylation	AMVSEFLKQARFLEN CHHHHHHHHHHHHHC	47.43	23236377
21	Phosphorylation	LENQEQEYVQAVKSY HHCHHHHHHHHHHHC	9.50	28973931
26	Ubiquitination	QEYVQAVKSYKGGPG HHHHHHHHHCCCCCC	51.59	-
26	Acetylation	QEYVQAVKSYKGGPG HHHHHHHHHCCCCCC	51.59	23236377
27	Phosphorylation	EYVQAVKSYKGGPGS HHHHHHHHCCCCCCC	26.02	20450229
28	Phosphorylation	YVQAVKSYKGGPGSA HHHHHHHCCCCCCCC	14.13	25367039
29	Acetylation	VQAVKSYKGGPGSAV HHHHHHCCCCCCCCC	65.56	23806337
34	Phosphorylation	SYKGGPGSAVSPYPS HCCCCCCCCCCCCCC	28.73	26824392
37	Phosphorylation	GGPGSAVSPYPSFNV CCCCCCCCCCCCCCC	20.59	26824392
39	Phosphorylation	PGSAVSPYPSFNVSS CCCCCCCCCCCCCCH	12.19	25619855
41	Phosphorylation	SAVSPYPSFNVSSDV CCCCCCCCCCCCHHH	24.49	25619855
45	Phosphorylation	PYPSFNVSSDVAALH CCCCCCCCHHHHHHH	23.17	25619855
46	Phosphorylation	YPSFNVSSDVAALHK CCCCCCCHHHHHHHH	31.64	25619855
53	Acetylation	SDVAALHKAIMVKGV HHHHHHHHHHHCCCC	40.22	22826441
58	Acetylation	LHKAIMVKGVDEATI HHHHHHCCCCCHHHH	35.52	23806337
71	Acetylation	TIIDILTKRTNAQRQ HHHHHHHHCCHHHHH	54.50	22826441
90	Acetylation	AYLQENGKPLDEVLR HHHHHCCCCHHHHHH	54.73	23236377
128	Ubiquitination	DELRGAMKGLGTDED HHHHHHHCCCCCCHH	50.91	-
136	Phosphorylation	GLGTDEDTLIEILTT CCCCCHHHHHHHHHC	27.82	62168417
142	Phosphorylation	DTLIEILTTRSNEQI HHHHHHHHCCCHHHH	26.31	25338131
143	Phosphorylation	TLIEILTTRSNEQIR HHHHHHHCCCHHHHH	28.76	21454597
145	Phosphorylation	IEILTTRSNEQIREI HHHHHCCCHHHHHHH	42.50	24719451
161	Acetylation	RVYREELKRDLAKDI HHHHHHHHHHHHHHC	47.33	7676335
166	Acetylation	ELKRDLAKDITSDTS HHHHHHHHHCCCCCC	57.89	23236377
166	Ubiquitination	ELKRDLAKDITSDTS HHHHHHHHHCCCCCC	57.89	-
169	Phosphorylation	RDLAKDITSDTSGDF HHHHHHCCCCCCHHH	30.59	25338131
170	Phosphorylation	DLAKDITSDTSGDFR HHHHHCCCCCCHHHH	38.94	26525534
172	Phosphorylation	AKDITSDTSGDFRKA HHHCCCCCCHHHHHH	34.08	20531401
173	Phosphorylation	KDITSDTSGDFRKAL HHCCCCCCHHHHHHH	41.16	26824392
185	Acetylation	KALLALAKGDRCQDL HHHHHHHCCCCCCCC	63.29	23236377
189	Glutathionylation	ALAKGDRCQDLSVNQ HHHCCCCCCCCCCCC	4.37	24333276
193	Phosphorylation	GDRCQDLSVNQDLAD CCCCCCCCCCCCHHH	27.58	30635358
201	Phosphorylation	VNQDLADTDARALYE CCCCHHHHHHHHHHH	26.42	26525534
207	Phosphorylation	DTDARALYEAGERRK HHHHHHHHHHHHHCC	11.62	21409
242	Acetylation	RVFQNYGKYSQHDMN HHHHHHCCCCCHHHH	31.22	23236377
250	Acetylation	YSQHDMNKALDLELK CCCHHHHHHHCHHHC	43.63	23236377
257	Sumoylation	KALDLELKGDIEKCL HHHCHHHCCCHHHHH	45.20	-
257	Sumoylation	KALDLELKGDIEKCL HHHCHHHCCCHHHHH	45.20	23727357
262	Acetylation	ELKGDIEKCLTTIVK HHCCCHHHHHHHHHH	34.57	22826441
265	Phosphorylation	GDIEKCLTTIVKCAT CCHHHHHHHHHHHCC	24.77	28059163
266	Phosphorylation	DIEKCLTTIVKCATS CHHHHHHHHHHHCCC	15.72	28059163
270	Glutathionylation	CLTTIVKCATSTPAF HHHHHHHHCCCCHHH	3.28	24333276
272	Phosphorylation	TTIVKCATSTPAFFA HHHHHHCCCCHHHHH	42.47	20139300
283	Phosphorylation	AFFAEKLYEAMKGAG HHHHHHHHHHHCCCC	16.83	125943533
312	Acetylation	EIDMNEIKVFYQKKY CCCHHHHHHHHHHHH	21.80	23806337
318	Acetylation	IKVFYQKKYGISLCQ HHHHHHHHHCHHHHH	32.93	22826441
324	Glutathionylation	KKYGISLCQAILDET HHHCHHHHHHHHHCC	1.73	24333276
332	Acetylation	QAILDETKGDYEKIL HHHHHCCCCCHHHHH	47.97	23236377

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	TRPM7	Q923J1	Uniprot
27	S	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ANXA1_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 ANXA1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
DYSF_MOUSE	Dysf	physical	14506282

Drug and Disease Associations

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

Regulatory Network of ANXA1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-21, AND MASSSPECTROMETRY.	19131326 [Abstract]