ANXA1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ANXA1_RAT
• UniProt AC: P07150
• Protein Name: Annexin A1
• Gene Name: Anxa1
• Organism: Rattus norvegicus (Rat).
• 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 . Endosome membrane ; Peripheral membrane prote
• 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. Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response. Promotes resolution of inflammation and wound healing (By similarity). Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades. Promotes chemotaxis of granulocytes and monocytes via activation ofthe formyl peptide receptors (By similarity). Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T-cells. Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (By similarity). Has no effect on unstimulated T-cells. Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration. Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (By similarity). Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)-dependent binding to phospholipid membranes. [PubMed: 3020049 Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (By similarity]
• Protein Sequence: MAMVSEFLKQACYIEKQEQEYVQAVKSYKGGPGSAVSPYPSFNPSSDVAALHKAIMVKGVDEATIIDILTKRTNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLAMLKTPAQFDADELRAAMKGLGTDEDTLIEILTTRSNQQIREITRVYREELKRDLAKDITSDTSGDFRNALLALAKGDRCEDMSVNQDLADTDARALYEAGERRKGTDVNVFNTILTTRSYPHLRKVFQNYRKYSQHDMNKALDLELKGDIEKCLTTIVKCATSTPAFFAEKLYEAMKGAGTRHKTLIRIMVSRSEIDMNEIKVFYQKKYGIPLCQAILDETKGDYEKILVALCGGN

Overview of Protein Modification Sites with Functional and Structural Information

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	---MAMVSEFLKQAC ---CCHHHHHHHHHH	15.00	29895
16	Acetylation	KQACYIEKQEQEYVQ HHHHHHHHHHHHHHH	49.96	25786129
21	Phosphorylation	IEKQEQEYVQAVKSY HHHHHHHHHHHHHHC	9.50	1832554
26	Acetylation	QEYVQAVKSYKGGPG HHHHHHHHHCCCCCC	51.59	26302492
27	Phosphorylation	EYVQAVKSYKGGPGS HHHHHHHHCCCCCCC	26.02	-
34	Phosphorylation	SYKGGPGSAVSPYPS HCCCCCCCCCCCCCC	28.73	23984901
37	Phosphorylation	GGPGSAVSPYPSFNP CCCCCCCCCCCCCCC	20.59	23298284
39	Phosphorylation	PGSAVSPYPSFNPSS CCCCCCCCCCCCCCH	12.19	23984901
41	Phosphorylation	SAVSPYPSFNPSSDV CCCCCCCCCCCCHHH	31.63	23984901
58	Acetylation	LHKAIMVKGVDEATI HHHHHHCCCCCHHHH	35.52	-
71	Acetylation	TIIDILTKRTNAQRQ HHHHHHHHCCHHHHH	54.50	22902405
90	Acetylation	AYLQETGKPLDETLK HHHHHHCCCHHHHHH	50.23	22902405
97	Acetylation	KPLDETLKKALTGHL CCHHHHHHHHHCCCH	43.34	22902405
128	Acetylation	DELRAAMKGLGTDED HHHHHHHHCCCCCHH	46.38	22902405
136	Phosphorylation	GLGTDEDTLIEILTT CCCCCHHHHHHHHHC	27.82	-
161	Acetylation	RVYREELKRDLAKDI HHHHHHHHHHHHHHC	47.33	22902405
166	Acetylation	ELKRDLAKDITSDTS HHHHHHHHHCCCCCC	57.89	22902405
172	Phosphorylation	AKDITSDTSGDFRNA HHHCCCCCCHHHHHH	34.08	22673903
173	Phosphorylation	KDITSDTSGDFRNAL HHCCCCCCHHHHHHH	41.16	22673903
185	Acetylation	NALLALAKGDRCEDM HHHHHHHCCCCCCCC	63.29	22902405
193	Phosphorylation	GDRCEDMSVNQDLAD CCCCCCCCCCCHHHH	30.18	22108457
216	Phosphorylation	AGERRKGTDVNVFNT HHHHCCCCCCEECCH	39.55	11317
242	Acetylation	KVFQNYRKYSQHDMN HHHHHHHHHCHHHHH	38.60	22902405
257	Acetylation	KALDLELKGDIEKCL HHHCHHHHHCHHHHH	45.20	22902405
265	Phosphorylation	GDIEKCLTTIVKCAT HCHHHHHHHHHHHCC	24.77	56059029
266	Phosphorylation	DIEKCLTTIVKCATS CHHHHHHHHHHHCCC	15.72	56059035
304	Phosphorylation	IRIMVSRSEIDMNEI HHHEEECCCCCHHHH	31.25	26022182
312	Acetylation	EIDMNEIKVFYQKKY CCCHHHHHHHHHHHH	21.80	25786129
317	Acetylation	EIKVFYQKKYGIPLC HHHHHHHHHHCCCHH	36.26	22902405
318	Acetylation	IKVFYQKKYGIPLCQ HHHHHHHHHCCCHHH	32.93	26302492

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	Q925B3	Uniprot
21	Y	Phosphorylation	Kinase	INSR	P15127	PSP
21	Y	Phosphorylation	Kinase	EGFR	-	Uniprot
27	S	Phosphorylation	Kinase	PKC	-	Uniprot
216	T	Phosphorylation	Kinase	PRKACA	P00517	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ANXA1_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ANXA1_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of ANXA1_RAT !!

Drug and Disease Associations

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