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Details on Person UniProt:P04083 ANXA1

Class:Id	ReferenceGeneProduct:50042
_chainChangeLog	initiator methionine:1 added on Fri February 6 2015;chain:2-346 added on Fri February 6 2015;peptide:2-26 for 50042 added on Wed May 4 2022;initiator methionine:1 for 50042 removed on Fri Nov 03 2023;initiator methionine: for 50042 added on Fri Nov 03 2023;initiator methionine: for 50042 removed on Fri Aug 15 2025;initiator methionine:1 for 50042 added on Fri Aug 15 2025
_displayName	UniProt:P04083 ANXA1
_timestamp	2026-02-20 22:06:39
chain	initiator methionine:1 chain:2-346 peptide:2-26
checksum	14B42E1FA4178EC0
comment	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.FUNCTION 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).SUBUNIT Homodimer; non-covalently linked (By similarity). Homodimer; linked by transglutamylation (PubMed:2532504). Homodimers linked by transglutamylation are observed in placenta, but not in other tissues (PubMed:2532504). Interacts with S100A11 (PubMed:10673436, PubMed:8557678). Heterotetramer, formed by two molecules each of S100A11 and ANXA1 (PubMed:10673436). Interacts with DYSF (By similarity). Interacts with EGFR (By similarity).INTERACTION 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).TISSUE SPECIFICITY Detected in resting neutrophils (PubMed:10772777). Detected in peripheral blood T cells (PubMed:17008549). Detected in extracellular vesicles in blood serum from patients with inflammatory bowel disease, but not in serum from healthy donors (PubMed:25664854). Detected in placenta (at protein level) (PubMed:2532504). Detected in liver.DOMAIN The full-length protein can bind eight Ca(2+) ions via the annexin repeats. Calcium binding causes a major conformation change that modifies dimer contacts and leads to surface exposure of the N-terminal phosphorylation sites; in the absence of Ca(2+), these sites are buried in the interior of the protein core. The N-terminal region becomes disordered in response to calcium-binding.PTM Phosphorylated by protein kinase C, EGFR and TRPM7 (PubMed:15485879, PubMed:2457390). Phosphorylated in response to EGF treatment (PubMed:2532504).PTM Sumoylated.PTM Proteolytically cleaved by cathepsin CTSG to release the active N-terminal peptide Ac2-26.PHARMACEUTICAL Peptides based on the N-terminal sequence might be used for the treatment of inflammation, e.g. in chronic bowel diseases and in rheumatoid arthritis.MISCELLANEOUS Was originally identified as calcium and phospholipid binding protein that displays Ca(2+)-dependent binding to phospholipid membranes and can promote membrane aggregation in vitro. Was initially identified as inhibitor of phospholipase A2 activity (in vitro) (PubMed:2936963, PubMed:8425544). Inhibition of phospholipase activity is mediated via its phospholipid binding activity that limits the access of phospholipase to its substrates.SIMILARITY Belongs to the annexin family.
description	recommendedName: Annexin A1 alternativeName: Annexin I alternativeName: Annexin-1 alternativeName: Calpactin II alternativeName: Calpactin-2 alternativeName: Chromobindin-9 alternativeName: fullName evidence="22"Lipocortin I alternativeName: Phospholipase A2 inhibitory protein alternativeName: p35 component recommendedName: fullName evidence="23"Annexin Ac2-26 /component
geneName	ANXA1 ANX1 LPC1
identifier	P04083
isSequenceChanged	FALSE
keyword	3D-structure Acetylation Adaptive immunity Annexin Calcium Calcium/phospholipid-binding Cell membrane Cell projection Cilium Cytoplasm Cytoplasmic vesicle Direct protein sequencing Disulfide bond Endosome Immunity Inflammatory response Innate immunity Isopeptide bond Membrane Metal-binding Nucleus Pharmaceutical Phospholipase A2 inhibitor Phosphoprotein Proteomics identification Reference proteome Repeat Secreted Ubl conjugation
modified	[InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20
name	ANXA1
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:6789497] ENSEMBL:ENSG00000135046 ANXA1 [Homo sapiens]
secondaryIdentifier	ANXA1_HUMAN B5BU38
sequenceLength	346
species	[Species:48887] Homo sapiens
(referenceEntity)	[EntityWithAccessionedSequence:444539] ANXA1 [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:5263630] ANXA1 [cytosol] [Homo sapiens]
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No pathways have been reviewed or authored by UniProt:P04083 ANXA1 (50042)