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:P62937 PPIA

Class:Id	ReferenceGeneProduct:53304
_chainChangeLog	initiator methionine:1 added on Fri February 6 2015;chain:1-165 added on Fri February 6 2015;chain:2-165 added on Fri February 6 2015;initiator methionine:1 for 53304 removed on Fri Nov 03 2023;initiator methionine: for 53304 added on Fri Nov 03 2023;initiator methionine: for 53304 removed on Fri Aug 15 2025;initiator methionine:1 for 53304 added on Fri Aug 15 2025
_displayName	UniProt:P62937 PPIA
_timestamp	2026-02-20 22:02:52
chain	chain:1-165 initiator methionine:1 chain:2-165
checksum	9B2E637A555E4434
comment	FUNCTION Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:2001362, PubMed:20676357, PubMed:21245143, PubMed:21593166, PubMed:25678563). Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (PubMed:11943775, PubMed:21245143). Activates endothelial cells (ECs) in a pro-inflammatory manner by stimulating activation of NF-kappa-B and ERK, JNK and p38 MAP-kinases and by inducing expression of adhesion molecules including SELE and VCAM1 (PubMed:15130913). Induces apoptosis in ECs by promoting the FOXO1-dependent expression of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815). In response to oxidative stress, initiates proapoptotic and antiapoptotic signaling in ECs via activation of NF-kappa-B and AKT1 and up-regulation of antiapoptotic protein BCL2 (PubMed:23180369). Negatively regulates MAP3K5/ASK1 kinase activity, autophosphorylation and oxidative stress-induced apoptosis mediated by MAP3K5/ASK1 (PubMed:26095851). Necessary for the assembly of TARDBP in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and regulates TARDBP binding to RNA UG repeats and TARDBP-dependent expression of HDAC6, ATG7 and VCP which are involved in clearance of protein aggregates (PubMed:25678563). Plays an important role in platelet activation and aggregation (By similarity). Regulates calcium mobilization and integrin ITGA2B:ITGB3 bidirectional signaling via increased ROS production as well as by facilitating the interaction between integrin and the cell cytoskeleton (By similarity). Binds heparan sulfate glycosaminoglycans (PubMed:11943775). Inhibits replication of influenza A virus (IAV) (PubMed:19207730). Inhibits ITCH/AIP4-mediated ubiquitination of matrix protein 1 (M1) of IAV by impairing the interaction of ITCH/AIP4 with M1, followed by the suppression of the nuclear export of M1, and finally reduction of the replication of IAV (PubMed:22347431, PubMed:30328013).FUNCTION (Microbial infection) May act as a mediator between human SARS coronavirus nucleoprotein and BSG/CD147 in the process of invasion of host cells by the virus (PubMed:15688292).FUNCTION (Microbial infection) Stimulates RNA-binding ability of HCV NS5A in a peptidyl-prolyl cis-trans isomerase activity-dependent manner.FUNCTION (Microbial infection) May act as a receptor for M.genitalium adhesin protein P140 (also called MgPa) (PubMed:29551599, PubMed:33013867).CATALYTIC ACTIVITY [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)ACTIVITY REGULATION Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.SUBUNIT Interacts with protein phosphatase PPP3CA/calcineurin A (PubMed:12218175, PubMed:12357034). Interacts with PRPF19 isoform 2 (via N-terminus) (By similarity). Interacts with isoform 2 of BSG/CD147 (PubMed:11353871, PubMed:11943775, PubMed:15688292, PubMed:21245143). Interacts with FOXO1; the interaction promotes FOXO1 dephosphorylation, nuclear accumulation and transcriptional activity (PubMed:31063815). Interacts with integrin ITGA2B:ITGB3; the interaction is ROS and peptidyl-prolyl cis-trans isomerase (PPIase) activity-dependent and is increased in the presence of thrombin (By similarity). Interacts with MAP3K5 (PubMed:26095851). Interacts with TARDBP; the interaction is dependent on the RNA-binding activity of TARDBP and the PPIase activity of PPIA/CYPA and the acetylation of PPIA/CYPA at Lys-125 favors the interaction (PubMed:25678563). Interacts with HNRNPA1, HNRNPA2B1, HNRNPC, RBMX, HNRNPK and HNRNPM (PubMed:25678563).SUBUNIT (Microbial infection) Interacts with HIV-1 capsid protein (PubMed:20364129, PubMed:8513493).SUBUNIT (Microbial infection) Interacts with human SARS coronavirus nucleoprotein.SUBUNIT (Microbial infection) Interacts with measles virus nucleoprotein.SUBUNIT (Microbial infection) Interacts with influenza A virus matrix protein 1.SUBUNIT (Microbial infection) Interacts with M.genitalium adhesin P140 protein (also called MgPa).SUBUNIT (Microbial infection) Interacts with HCV NS5A; the interaction stimulates RNA-binding ability of NS5A and is dependent on the peptidyl-prolyl cis-trans isomerase activity of PPIA/CYPA.INTERACTION Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that includes Rho GTPase signaling, actin remodeling, and myosin II activation.SUBCELLULAR LOCATION (Microbial infection) Increased amounts of protein are secreted after treatment with M.genitalium P140 adhesin (MgPa).ALTERNATIVE PRODUCTS Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization and stabilizes cis rather than trans forms of the HIV-1 capsid. PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition (PubMed:20364129, Ref.12). Acetylation at Lys-125 favors its interaction with TARDBP (PubMed:25678563).SIMILARITY Belongs to the cyclophilin-type PPIase family. PPIase A subfamily.ONLINE INFORMATION Cyclophilin entry
description	recommendedName: Peptidyl-prolyl cis-trans isomerase A shortName: PPIase A ecNumber evidence="13 16 17 18 22 35 36"5.2.1.8 alternativeName: Cyclophilin A alternativeName: Cyclosporin A-binding protein alternativeName: Rotamase A component recommendedName: Peptidyl-prolyl cis-trans isomerase A, N-terminally processed /component
geneName	PPIA CYPA
identifier	P62937
isSequenceChanged	FALSE
keyword	3D-structure Acetylation Alternative splicing Apoptosis Cell membrane Cytoplasm Direct protein sequencing Glycoprotein Host-virus interaction Isomerase Isopeptide bond Membrane Nucleus Phosphoprotein Proteomics identification Reference proteome Rotamase 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	PPIA
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:8950492] ENSEMBL:ENSG00000196262 PPIA [Homo sapiens]
secondaryIdentifier	PPIA_HUMAN A8K220 P05092 Q3KQW3 Q567Q0 Q6IBU5 Q96IX3 Q9BRU4 Q9BTY9 Q9UC61
sequenceLength	165
species	[Species:48887] Homo sapiens
(isoformParent)	[ReferenceIsoform:8970687] UniProt:P62937-1 PPIA [Homo sapiens] [ReferenceIsoform:8970688] UniProt:P62937-2 PPIA [Homo sapiens]
(referenceEntity)	[EntityWithAccessionedSequence:173123] PPIA [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:173646] PPIA [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:6801391] PPIA [ficolin-1-rich granule lumen] [Homo sapiens] [EntityWithAccessionedSequence:6801400] PPIA [secretory granule lumen] [Homo sapiens] [EntityWithAccessionedSequence:6801538] PPIA [extracellular exosome] [Homo sapiens]
[Change default viewing format]

No pathways have been reviewed or authored by UniProt:P62937 PPIA (53304)