Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person UniProt:Q9Y2Q0 ATP8A1
| Class:Id | ReferenceGeneProduct:49342 |
|---|---|
| _chainChangeLog | chain:1-1164 added on Fri February 6 2015 |
| _displayName | UniProt:Q9Y2Q0 ATP8A1 |
| _timestamp | 2026-02-20 22:19:04 |
| chain | chain:1-1164 |
| checksum | CE1EAF0206CD36F7 |
| comment | FUNCTION Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids (PubMed:31416931). Phospholipid translocation also seems to be implicated in vesicle formation and in uptake of lipid signaling molecules. In vitro, its ATPase activity is selectively and stereospecifically stimulated by phosphatidylserine (PS) (PubMed:31416931). The flippase complex ATP8A1:TMEM30A seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the cell membrane (By similarity). Acts as aminophospholipid translocase at the cell membrane in neuronal cells (By similarity).CATALYTIC ACTIVITY ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.CATALYTIC ACTIVITY a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + phosphate + H(+)COFACTOR ATPase activity is stimulated by phosphatidylserine (PS) and minimally by phosphatidylethanolamine (PE). ATPase activity is inhibited by beryllium fluoride and aluminum trifluoride (PubMed:31416931).BIOPHYSICOCHEMICAL PROPERTIES Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit (PubMed:31416931). Interacts with TMEM30A to form a flippase complex; this complex forms an intermediate phosphoenzyme (PubMed:20947505, PubMed:20961850, PubMed:21914794, PubMed:31416931). Interacts with TMEM30B; this interaction is reported conflictingly (PubMed:20961850).SUBCELLULAR LOCATION Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B (PubMed:20947505). In the presence of TMEM30A, predominantly located in cytoplasmic punctate structures and localizes to the cell membrane (PubMed:20947505). Localizes to plasma membranes of red blood cells (By similarity).ALTERNATIVE PRODUCTS Found in most adult tissues except liver, testis and placenta. Most abundant in heart, brain and skeletal muscle. Also detected in fetal tissues. Isoform 1 is only detected in brain, skeletal muscle and heart and is the most abundant form in skeletal muscle. Highly expressed in platelets (PubMed:30674456).PTM Cleaved by calpain in a caspase- and calcium influx-dependent manner during platelet apoptosis leading to a 100 kDa polypeptide.SIMILARITY Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.SEQUENCE CAUTION Truncated N-terminus.SEQUENCE CAUTION Truncated N-terminus. |
| description | recommendedName: fullName evidence="14"Phospholipid-transporting ATPase IA ecNumber evidence="4"7.6.2.1 alternativeName: ATPase class I type 8A member 1 alternativeName: Chromaffin granule ATPase II alternativeName: P4-ATPase flippase complex alpha subunit ATP8A1 |
| geneName | ATP8A1 ATPIA |
| identifier | Q9Y2Q0 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Alternative splicing ATP-binding Cell membrane Cytoplasmic vesicle Endoplasmic reticulum Golgi apparatus Lipid transport Magnesium Membrane Metal-binding Nucleotide-binding Phosphoprotein Proteomics identification Reference proteome Translocase Transmembrane Transmembrane helix Transport |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9841277] Weiser, Joel [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9948485] Weiser, Joel, 2025-05-21 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | ATP8A1 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8989978] ENSEMBL:ENSG00000124406 ATP8A1 [Homo sapiens] |
| secondaryIdentifier | AT8A1_HUMAN Q32M35 Q32M36 Q4W5J7 Q4W5P2 |
| sequenceLength | 1164 |
| species | [Species:48887] Homo sapiens |
| (isoformParent) | [ReferenceIsoform:143670] UniProt:Q9Y2Q0-2 ATP8A1 [Homo sapiens] [ReferenceIsoform:415964] UniProt:Q9Y2Q0-1 ATP8A1 [Homo sapiens] [ReferenceIsoform:8966894] UniProt:Q9Y2Q0-3 ATP8A1 [Homo sapiens] |
| (referenceEntity) | [EntityWithAccessionedSequence:939739] ATP8A1 [plasma membrane] [Homo sapiens] [EntityWithAccessionedSequence:6799530] ATP8A1 [specific granule membrane] [Homo sapiens] [EntityWithAccessionedSequence:6801000] ATP8A1 [azurophil granule membrane] [Homo sapiens] |
| [Change default viewing format] | |
No pathways have been reviewed or authored by UniProt:Q9Y2Q0 ATP8A1 (49342)
