ANXA1
entrez
301
canonical
uniprot
P04083
canonical
ensembl
ENSG00000135046
resolver
ensp
ENSP00000257497
resolver
ensp
ENSP00000366109
resolver
ensp
ENSP00000527848
resolver
ensp
ENSP00000527849
resolver
ensp
ENSP00000527850
resolver
ensp
ENSP00000527851
resolver
ensp
ENSP00000527853
resolver
ensp
ENSP00000527855
resolver
ensp
ENSP00000527856
resolver
ensp
ENSP00000624854
resolver
ensp
ENSP00000624855
resolver
ensp
ENSP00000624857
resolver
ensp
ENSP00000624860
resolver
ensp
ENSP00000624861
resolver
ensp
ENSP00000624862
resolver
ensp
ENSP00000624864
resolver
ensp
ENSP00000624865
resolver
enst
ENST00000257497
resolver
enst
ENST00000376911
resolver
enst
ENST00000857789
resolver
enst
ENST00000857790
resolver
enst
ENST00000857791
resolver
enst
ENST00000857792
resolver
enst
ENST00000857794
resolver
enst
ENST00000857796
resolver
enst
ENST00000857797
resolver
enst
ENST00000954795
resolver
enst
ENST00000954796
resolver
enst
ENST00000954798
resolver
enst
ENST00000954801
resolver
enst
ENST00000954802
resolver
enst
ENST00000954803
resolver
enst
ENST00000954805
resolver
enst
ENST00000954806
resolver
genesymbol
ANXA1
resolver
genesymbol_syn
ANX1
resolver
genesymbol_syn
LPC1
resolver
hgnc
HGNC:533
resolver
uniprot
B5BU38
resolver
uniprot
Q5TZZ9
resolver
uniprot_entry
ANXA1_HUMAN
resolver
uniprot_entry
Q5TZZ9_HUMAN
resolver
uniprot_sec
B5BU38
resolver
amino_acid_sequence
MAMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN
uniprot
proteins
function
FUNCTION: 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). 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 (PubMed:17008549). Promotes the differentiation of T cells into Th1 cells and negatively regulates differentiation into Th2 cells (PubMed:17008549). Has no effect on unstimulated T cells (PubMed:17008549). Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (PubMed:19625660). 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:2532504, PubMed:8557678). 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). In the context of antitumor immunity, interacts with FPR1 on dendritic cells allowing for tumor-associated antigens uptake and cross-presentation to T cells to mount an antitumor specific T cell response. {ECO:0000250|UniProtKB:P10107, ECO:0000250|UniProtKB:P19619, ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:19625660, ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:2936963, ECO:0000269|PubMed:8425544, ECO:0000269|PubMed:8557678}.; FUNCTION: [Annexin Ac2-26]: Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades (PubMed:15187149, PubMed:22879591, PubMed:25664854). Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors (PubMed:15187149). Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration (PubMed:15187149). Promotes resolution of inflammation and wound healing (PubMed:25664854). Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (PubMed:22879591). {ECO:0000269|PubMed:15187149, ECO:0000269|PubMed:22879591, ECO:0000269|PubMed:25664854}.
uniprot
proteins
mass_dalton
38714
uniprot
proteins
mutagenesis
MUTAGEN 27; /note="S->A: Abolishes secretion and modulation of exocytosis."; /evidence="ECO:0000269|PubMed:19625660"; MUTAGEN 34; /note="S->A: No effect on secretion and modulation of exocytosis."; /evidence="ECO:0000269|PubMed:19625660"; MUTAGEN 45; /note="S->A: Abolishes secretion and nearly abolishes modulation of exocytosis."; /evidence="ECO:0000269|PubMed:19625660
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by protein kinase C, EGFR and TRPM7 (PubMed:15485879, PubMed:2457390). Phosphorylated in response to EGF treatment (PubMed:2532504). {ECO:0000269|PubMed:15485879, ECO:0000269|PubMed:2457390, ECO:0000269|PubMed:2532504}.; PTM: Sumoylated. {ECO:0000250|UniProtKB:P10107}.; PTM: Proteolytically cleaved by cathepsin CTSG to release the active N-terminal peptide Ac2-26. {ECO:0000269|PubMed:22879591}.
uniprot
proteins
protein_family
Annexin family
uniprot
proteins
pubmed
10673436
uniprot
proteins
pubmed
10772777
uniprot
proteins
pubmed
15187149
uniprot
proteins
pubmed
15485879
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17008549
uniprot
proteins
pubmed
1832554
uniprot
proteins
pubmed
18641677
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19625660
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22879591
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2457390
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
2532504
uniprot
proteins
pubmed
25664854
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
2936963
uniprot
proteins
pubmed
32272059
uniprot
proteins
pubmed
3303336
uniprot
proteins
pubmed
8425544
uniprot
proteins
pubmed
8453382
uniprot
proteins
pubmed
8557678
uniprot
proteins
pubmed
9915835
uniprot
proteins
sequence_length
346
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:19625660}. Cytoplasm {ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:19625660}. Cell projection, cilium {ECO:0000250|UniProtKB:P46193}. Cell membrane {ECO:0000269|PubMed:10772777}. Membrane {ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:8557678}; Peripheral membrane protein {ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:8557678}. Endosome membrane {ECO:0000250|UniProtKB:P07150}; Peripheral membrane protein {ECO:0000250|UniProtKB:P07150}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51662}. Apical cell membrane {ECO:0000250|UniProtKB:P10107}. Lateral cell membrane {ECO:0000250|UniProtKB:P10107}. Secreted {ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:19625660, ECO:0000269|PubMed:25664854}. Secreted, extracellular space {ECO:0000269|PubMed:25664854}. Cell membrane {ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:19625660, ECO:0000269|PubMed:25664854}; Peripheral membrane protein {ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:19625660, ECO:0000269|PubMed:25664854}; Extracellular side {ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:19625660, ECO:0000269|PubMed:25664854}. Secreted, extracellular exosome {ECO:0000269|PubMed:25664854}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000269|PubMed:10772777}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:P10107}. Early endosome {ECO:0000250|UniProtKB:P19619}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P19619}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19619}. Note=Secreted, at least in part via exosomes and other secretory vesicles. Detected in exosomes and other extracellular vesicles (PubMed:25664854). Alternatively, the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in the protein translocation from the cytoplasm into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059). Detected in gelatinase granules in resting neutrophils (PubMed:10772777). Secretion is increased in response to wounding and inflammation (PubMed:25664854). Secretion is increased upon T-cell activation (PubMed:17008549). Neutrophil adhesion to endothelial cells stimulates secretion via gelatinase granules, but foreign particle phagocytosis has no effect (PubMed:10772777). Colocalizes with actin fibers at phagocytic cups (By similarity). Displays calcium-dependent binding to phospholipid membranes (PubMed:2532504, PubMed:8557678). {ECO:0000250|UniProtKB:P10107, ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:25664854, ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:8557678}.
uniprot
proteins