Gene PPIA - ENSG00000196262 | NCBI Gene ID: 5478

Details for: PPIA

Gene ID: 5478

Symbol: PPIA

Ensembl ID: ENSG00000196262

Description: peptidylprolyl isomerase A

Associated with

Adaptive immune system
(R-HSA-1280218)
Apobec3g mediated resistance to hiv-1 infection
(R-HSA-180689)
Assembly of the hiv virion
(R-HSA-175474)
Basigin interactions
(R-HSA-210991)
Binding and entry of hiv virion
(R-HSA-173107)
Budding and maturation of hiv virion
(R-HSA-162588)
Calcineurin activates nfat
(R-HSA-2025928)
Cell surface interactions at the vascular wall
(R-HSA-202733)
Cytokine signaling in immune system
(R-HSA-1280215)
Disease
(R-HSA-1643685)
Downstream signaling events of b cell receptor (bcr)
(R-HSA-1168372)
Early phase of hiv life cycle
(R-HSA-162594)
Gene and protein expression by jak-stat signaling after interleukin-12 stimulation
(R-HSA-8950505)
Hemostasis
(R-HSA-109582)
Hiv infection
(R-HSA-162906)
Hiv life cycle
(R-HSA-162587)
Host interactions of hiv factors
(R-HSA-162909)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Innate immune system
(R-HSA-168249)
Integration of provirus
(R-HSA-162592)
Interleukin-12 family signaling
(R-HSA-447115)
Interleukin-12 signaling
(R-HSA-9020591)
Late phase of hiv life cycle
(R-HSA-162599)
Minus-strand dna synthesis
(R-HSA-164516)
Neutrophil degranulation
(R-HSA-6798695)
Platelet activation, signaling and aggregation
(R-HSA-76002)
Platelet degranulation
(R-HSA-114608)
Plus-strand dna synthesis
(R-HSA-164525)
Response to elevated platelet cytosolic ca2+
(R-HSA-76005)
Reverse transcription of hiv rna
(R-HSA-162589)
Sars-cov-1 activates/modulates innate immune responses
(R-HSA-9692916)
Sars-cov-1 infection
(R-HSA-9678108)
Sars-cov-1-host interactions
(R-HSA-9692914)
Sars-cov infections
(R-HSA-9679506)
Signaling by interleukins
(R-HSA-449147)
Signaling by the b cell receptor (bcr)
(R-HSA-983705)
Uncoating of the hiv virion
(R-HSA-162585)
Viral infection pathways
(R-HSA-9824446)
Activation of protein kinase b activity
(GO:0032148)
Apoptotic process
(GO:0006915)
Cell adhesion molecule production
(GO:0060352)
Cellular response to oxidative stress
(GO:0034599)
Cyclosporin a binding
(GO:0016018)
Cytoplasm
(GO:0005737)
Cytosol
(GO:0005829)
Endothelial cell activation
(GO:0042118)
Extracellular exosome
(GO:0070062)
Extracellular region
(GO:0005576)
Extracellular space
(GO:0005615)
Ficolin-1-rich granule lumen
(GO:1904813)
Focal adhesion
(GO:0005925)
Heparan sulfate binding
(GO:1904399)
Integrin binding
(GO:0005178)
Leukocyte chemotaxis
(GO:0030595)
Lipid droplet organization
(GO:0034389)
Membrane
(GO:0016020)
Negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
(GO:1902176)
Negative regulation of protein k48-linked ubiquitination
(GO:0061944)
Negative regulation of protein kinase activity
(GO:0006469)
Negative regulation of protein phosphorylation
(GO:0001933)
Negative regulation of stress-activated mapk cascade
(GO:0032873)
Negative regulation of viral life cycle
(GO:1903901)
Neuron differentiation
(GO:0030182)
Neutrophil chemotaxis
(GO:0030593)
Nucleus
(GO:0005634)
Peptidyl-prolyl cis-trans isomerase activity
(GO:0003755)
Platelet activation
(GO:0030168)
Platelet aggregation
(GO:0070527)
Positive regulation of mapk cascade
(GO:0043410)
Positive regulation of nf-kappab transcription factor activity
(GO:0051092)
Positive regulation of protein dephosphorylation
(GO:0035307)
Positive regulation of protein phosphorylation
(GO:0001934)
Positive regulation of protein secretion
(GO:0050714)
Positive regulation of viral genome replication
(GO:0045070)
Protein-containing complex
(GO:0032991)
Protein binding
(GO:0005515)
Protein folding
(GO:0006457)
Protein peptidyl-prolyl isomerization
(GO:0000413)
Regulation of apoptotic signaling pathway
(GO:2001233)
Regulation of viral genome replication
(GO:0045069)
Rna binding
(GO:0003723)
Secretory granule lumen
(GO:0034774)
Unfolded protein binding
(GO:0051082)
Vesicle
(GO:0031982)
Viral release from host cell
(GO:0019076)
Virion binding
(GO:0046790)

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: cord blood hematopoietic stem cell (CL2000095)
Fold Change: 7.77
Marker Score: 5863
Cell Name: thyroid follicular cell (CL0002258)
Fold Change: 5.61
Marker Score: 4390
Cell Name: malignant cell (CL0001064)
Fold Change: 5
Marker Score: 67128
Cell Name: mesenchymal stem cell (CL0000134)
Fold Change: 4.92
Marker Score: 7578
Cell Name: mature T cell (CL0002419)
Fold Change: 4.91
Marker Score: 48638
Cell Name: mature gamma-delta T cell (CL0000800)
Fold Change: 4.68
Marker Score: 14782
Cell Name: radial glial cell (CL0000681)
Fold Change: 4.47
Marker Score: 1647
Cell Name: CD38-negative naive B cell (CL0002102)
Fold Change: 4.41
Marker Score: 9249
Cell Name: mature alpha-beta T cell (CL0000791)
Fold Change: 4.4
Marker Score: 232873
Cell Name: NKp46-positive innate lymphoid cell, human (CL0001076)
Fold Change: 4.39
Marker Score: 12814
Cell Name: naive thymus-derived CD4-positive, alpha-beta T cell (CL0000895)
Fold Change: 4.3
Marker Score: 7380
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 4.26
Marker Score: 145007
Cell Name: kidney loop of Henle thick ascending limb epithelial cell (CL1001106)
Fold Change: 4.22
Marker Score: 11319
Cell Name: mesodermal cell (CL0000222)
Fold Change: 4.22
Marker Score: 55645
Cell Name: blood cell (CL0000081)
Fold Change: 4.14
Marker Score: 48133
Cell Name: naive B cell (CL0000788)
Fold Change: 4.1
Marker Score: 3663
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 4.09
Marker Score: 228832
Cell Name: epithelial cell of proximal tubule (CL0002306)
Fold Change: 4.05
Marker Score: 14383
Cell Name: alveolar capillary type 1 endothelial cell (CL4028002)
Fold Change: 4
Marker Score: 10162
Cell Name: epithelial cell of lung (CL0000082)
Fold Change: 3.98
Marker Score: 20908
Cell Name: double negative T regulatory cell (CL0011024)
Fold Change: 3.93
Marker Score: 3802
Cell Name: T-helper 22 cell (CL0001042)
Fold Change: 3.93
Marker Score: 16856.5
Cell Name: skeletal muscle satellite stem cell (CL0008011)
Fold Change: 3.92
Marker Score: 4181
Cell Name: erythroid progenitor cell (CL0000038)
Fold Change: 3.91
Marker Score: 4084
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 3.91
Marker Score: 9557
Cell Name: kidney collecting duct principal cell (CL1001431)
Fold Change: 3.85
Marker Score: 9716.5
Cell Name: chondrocyte (CL0000138)
Fold Change: 3.84
Marker Score: 1728
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 3.81
Marker Score: 1218.5
Cell Name: CD8-positive, alpha-beta memory T cell, CD45RO-positive (CL0001203)
Fold Change: 3.79
Marker Score: 10630.5
Cell Name: type I NK T cell (CL0000921)
Fold Change: 3.79
Marker Score: 2973.5
Cell Name: effector memory CD8-positive, alpha-beta T cell, terminally differentiated (CL0001062)
Fold Change: 3.78
Marker Score: 5565
Cell Name: CD4-positive, alpha-beta cytotoxic T cell (CL0000934)
Fold Change: 3.77
Marker Score: 3308
Cell Name: decidual natural killer cell, human (CL0002343)
Fold Change: 3.75
Marker Score: 10367.5
Cell Name: kidney interstitial cell (CL1000500)
Fold Change: 3.75
Marker Score: 2667
Cell Name: naive thymus-derived CD8-positive, alpha-beta T cell (CL0000900)
Fold Change: 3.75
Marker Score: 6693.5
Cell Name: germinal center B cell (CL0000844)
Fold Change: 3.75
Marker Score: 2279
Cell Name: renal intercalated cell (CL0005010)
Fold Change: 3.73
Marker Score: 1991.5
Cell Name: basal cell of epithelium of trachea (CL1000348)
Fold Change: 3.73
Marker Score: 27765
Cell Name: central memory CD8-positive, alpha-beta T cell (CL0000907)
Fold Change: 3.73
Marker Score: 9092
Cell Name: type I pneumocyte (CL0002062)
Fold Change: 3.71
Marker Score: 4472
Cell Name: class switched memory B cell (CL0000972)
Fold Change: 3.71
Marker Score: 3490
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: 3.68
Marker Score: 23930.5
Cell Name: CD4-positive, alpha-beta memory T cell (CL0000897)
Fold Change: 3.62
Marker Score: 2121
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 3.62
Marker Score: 864
Cell Name: glycinergic amacrine cell (CL4030028)
Fold Change: 3.61
Marker Score: 3405.5
Cell Name: type II pneumocyte (CL0002063)
Fold Change: 3.6
Marker Score: 23461
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 3.59
Marker Score: 4331
Cell Name: medullary thymic epithelial cell (CL0002365)
Fold Change: 3.57
Marker Score: 5848
Cell Name: IgG-negative class switched memory B cell (CL0002117)
Fold Change: 3.57
Marker Score: 3512
Cell Name: mucosal invariant T cell (CL0000940)
Fold Change: 3.55
Marker Score: 3160
Cell Name: kidney loop of Henle thin ascending limb epithelial cell (CL1001107)
Fold Change: 3.55
Marker Score: 3599
Cell Name: myofibroblast cell (CL0000186)
Fold Change: 3.53
Marker Score: 4362
Cell Name: alveolar capillary type 2 endothelial cell (CL4028003)
Fold Change: 3.5
Marker Score: 5070
Cell Name: effector CD8-positive, alpha-beta T cell (CL0001050)
Fold Change: 3.49
Marker Score: 2935
Cell Name: lung macrophage (CL1001603)
Fold Change: 3.48
Marker Score: 3986
Cell Name: memory B cell (CL0000787)
Fold Change: 3.47
Marker Score: 2627
Cell Name: naive T cell (CL0000898)
Fold Change: 3.47
Marker Score: 2235
Cell Name: Sertoli cell (CL0000216)
Fold Change: 3.45
Marker Score: 20442.5
Cell Name: CD16-negative, CD56-bright natural killer cell, human (CL0000938)
Fold Change: 3.43
Marker Score: 2806
Cell Name: activated CD4-positive, alpha-beta T cell, human (CL0001043)
Fold Change: 3.42
Marker Score: 1553
Cell Name: capillary endothelial cell (CL0002144)
Fold Change: 3.42
Marker Score: 3674
Cell Name: kidney collecting duct intercalated cell (CL1001432)
Fold Change: 3.41
Marker Score: 5656
Cell Name: late pro-B cell (CL0002048)
Fold Change: 3.4
Marker Score: 4008
Cell Name: immature B cell (CL0000816)
Fold Change: 3.4
Marker Score: 2249.5
Cell Name: stratified epithelial cell (CL0000079)
Fold Change: 3.39
Marker Score: 26498
Cell Name: T follicular helper cell (CL0002038)
Fold Change: 3.39
Marker Score: 2818
Cell Name: foveolar cell of stomach (CL0002179)
Fold Change: 3.39
Marker Score: 21636
Cell Name: professional antigen presenting cell (CL0000145)
Fold Change: 3.39
Marker Score: 1748
Cell Name: unswitched memory B cell (CL0000970)
Fold Change: 3.38
Marker Score: 1981
Cell Name: CD4-positive helper T cell (CL0000492)
Fold Change: 3.38
Marker Score: 3677
Cell Name: epithelial cell (CL0000066)
Fold Change: 3.34
Marker Score: 5313
Cell Name: centroblast (CL0009112)
Fold Change: 3.33
Marker Score: 1638.5
Cell Name: CD8-positive, alpha-beta memory T cell (CL0000909)
Fold Change: 3.33
Marker Score: 2823
Cell Name: myoepithelial cell of mammary gland (CL0002324)
Fold Change: 3.32
Marker Score: 16302
Cell Name: activated CD8-positive, alpha-beta T cell (CL0000906)
Fold Change: 3.32
Marker Score: 2405
Cell Name: activated CD4-positive, alpha-beta T cell (CL0000896)
Fold Change: 3.31
Marker Score: 2395
Cell Name: CD8-alpha-alpha-positive, alpha-beta intraepithelial T cell (CL0000915)
Fold Change: 3.3
Marker Score: 4664.5
Cell Name: endothelial cell (CL0000115)
Fold Change: 3.29
Marker Score: 2947
Cell Name: smooth muscle cell (CL0000192)
Fold Change: 3.27
Marker Score: 2152
Cell Name: CD14-positive, CD16-positive monocyte (CL0002397)
Fold Change: 3.25
Marker Score: 6332
Cell Name: Kupffer cell (CL0000091)
Fold Change: 3.24
Marker Score: 3245.5
Cell Name: natural T-regulatory cell (CL0000903)
Fold Change: 3.24
Marker Score: 1663.5
Cell Name: colon epithelial cell (CL0011108)
Fold Change: 3.24
Marker Score: 10163
Cell Name: kidney distal convoluted tubule epithelial cell (CL1000849)
Fold Change: 3.23
Marker Score: 3422
Cell Name: epithelial cell of urethra (CL1000296)
Fold Change: 3.23
Marker Score: 2542
Cell Name: effector CD4-positive, alpha-beta T cell (CL0001044)
Fold Change: 3.23
Marker Score: 3018.5
Cell Name: hematopoietic cell (CL0000988)
Fold Change: 3.22
Marker Score: 2142
Cell Name: secretory cell (CL0000151)
Fold Change: 3.22
Marker Score: 5877
Cell Name: CD8-positive, alpha-beta thymocyte (CL0000811)
Fold Change: 3.21
Marker Score: 1774
Cell Name: DN3 thymocyte (CL0000807)
Fold Change: 3.21
Marker Score: 1603
Cell Name: neuroblast (sensu Vertebrata) (CL0000031)
Fold Change: 3.2
Marker Score: 2012
Cell Name: bronchial epithelial cell (CL0002328)
Fold Change: 3.2
Marker Score: 847
Cell Name: supporting cell (CL0000630)
Fold Change: 3.19
Marker Score: 5990
Cell Name: CD8-positive, alpha-beta cytotoxic T cell (CL0000794)
Fold Change: 3.19
Marker Score: 2810
Cell Name: pulmonary artery endothelial cell (CL1001568)
Fold Change: 3.18
Marker Score: 2740
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 3.17
Marker Score: 9413.5
Cell Name: regulatory T cell (CL0000815)
Fold Change: 3.17
Marker Score: 3508
Cell Name: gamma-delta T cell (CL0000798)
Fold Change: 3.17
Marker Score: 2131
Cell Name: cell in vitro (CL0001034)
Fold Change: 3.15
Marker Score: 109247
Cell Name: memory regulatory T cell (CL0002678)
Fold Change: 3.13
Marker Score: 1091

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**Key characteristics:** * PPIA is a transmembrane protein with a conserved catalytic domain responsible for isomerizing proline residues in various cytokines and chemokines. * It acts as a regulator of inflammation and immune responses by controlling the production of inflammatory cytokines and promoting immune tolerance. * PPIA is involved in the regulation of the adaptive immune response, including the development of tolerance and the generation of immune responses. **Pathways and functions:** * PPIA is involved in the regulation of inflammation through the production of anti-inflammatory cytokines such as IL-10 and TGF-beta. * It promotes immune tolerance by inhibiting the production of inflammatory cytokines and promoting the production of regulatory cytokines. * PPIA also regulates cell surface interactions and signaling pathways, including the B cell receptor (bcr) pathway. * It is involved in the regulation of platelet activation and aggregation, potentially influencing immune responses. **Clinical significance:** * PPIA mutations have been linked to several autoimmune disorders, including rheumatoid arthritis, psoriasis, and inflammatory bowel disease. * PPIA inhibitors are being investigated as potential therapeutic agents for these diseases, as they could help to regulate inflammation and promote immune tolerance. * Understanding the role of PPIA in the immune system could provide new insights for the development of novel therapeutic strategies for autoimmune diseases. **Additional notes:** * PPIA is a highly conserved protein with homologs in other species. * It is a key regulator of the immune response and is essential for the development of tolerance. * PPIA is a promising target for the development of novel therapeutic strategies for autoimmune diseases.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Peptidyl-prolyl cis-trans isomerase A

Genular Protein ID: 2426384294

Symbol: PPIA_HUMAN

Name: Peptidyl-prolyl cis-trans isomerase A

UniProtKB Accession Codes:

P62937 A8K220 P05092 Q3KQW3 Q567Q0 Q6IBU5 Q96IX3 Q9BRU4 Q9BTY9 Q9UC61

Database IDs:

Citations:

PubMed ID: 3297675

Title: Complementary DNA for human T-cell cyclophilin.

PubMed ID: 3297675

DOI: 10.1002/j.1460-2075.1987.tb04843.x

PubMed ID: 2197089

Title: Characterization of the human cyclophilin gene and of related processed pseudogenes.

PubMed ID: 2197089

DOI: 10.1111/j.1432-1033.1990.tb15598.x

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 19054851

Title: Human protein factory for converting the transcriptome into an in vitro-expressed proteome.

PubMed ID: 19054851

DOI: 10.1038/nmeth.1273

PubMed ID: 12853948

Title: The DNA sequence of human chromosome 7.

PubMed ID: 12853948

DOI: 10.1038/nature01782

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 7657784

Title: Identification of cyclophilin A from human decidual and placental tissue in the first trimester of pregnancy.

PubMed ID: 7657784

DOI: 10.1093/oxfordjournals.humrep.a136138

PubMed ID: 12665801

Title: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.

PubMed ID: 12665801

DOI: 10.1038/nbt810

PubMed ID: 2001362

Title: Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue.

PubMed ID: 2001362

DOI: 10.1021/bi00223a003

PubMed ID: 8513493

Title: Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B.

PubMed ID: 8513493

DOI: 10.1016/0092-8674(93)90637-6

PubMed ID: 11353871

Title: CD147 facilitates HIV-1 infection by interacting with virus-associated cyclophilin A.

PubMed ID: 11353871

DOI: 10.1073/pnas.111583198

PubMed ID: 11943775

Title: Active site residues of cyclophilin A are crucial for its signaling activity via CD147.

PubMed ID: 11943775

DOI: 10.1074/jbc.m201593200

PubMed ID: 14654843

Title: Proteomic characterization of the human centrosome by protein correlation profiling.

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 15130913

Title: Cyclophilin A is a proinflammatory cytokine that activates endothelial cells.

PubMed ID: 15130913

DOI: 10.1161/01.atv.0000130664.51010.28

PubMed ID: 15688292

Title: Function of HAb18G/CD147 in invasion of host cells by severe acute respiratory syndrome coronavirus.

PubMed ID: 15688292

DOI: 10.1086/427811

PubMed ID: 16527992

Title: Cyclophilin A is secreted by a vesicular pathway in vascular smooth muscle cells.

PubMed ID: 16527992

DOI: 10.1161/01.res.0000216405.85080.a6

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19207730

Title: Cyclophilin A interacts with influenza A virus M1 protein and impairs the early stage of the viral replication.

PubMed ID: 19207730

DOI: 10.1111/j.1462-5822.2009.01286.x

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20147391

Title: CD147/EMMPRIN acts as a functional entry receptor for measles virus on epithelial cells.

PubMed ID: 20147391

DOI: 10.1128/jvi.02168-09

PubMed ID: 20676357

Title: Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases.

PubMed ID: 20676357

DOI: 10.1371/journal.pbio.1000439

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21245143

Title: Cyclophilin A (CyPA) induces chemotaxis independent of its peptidylprolyl cis-trans isomerase activity: direct binding between CyPA and the ectodomain of CD147.

PubMed ID: 21245143

DOI: 10.1074/jbc.c110.181347

PubMed ID: 21593166

Title: Cyclophilin A interacts with domain II of hepatitis C virus NS5A and stimulates RNA binding in an isomerase-dependent manner.

PubMed ID: 21593166

DOI: 10.1128/jvi.00393-11

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 22347431

Title: Cyclophilin A restricts influenza A virus replication through degradation of the M1 protein.

PubMed ID: 22347431

DOI: 10.1371/journal.pone.0031063

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23180369

Title: Antiapoptotic and proapoptotic signaling of cyclophilin A in endothelial cells.

PubMed ID: 23180369

DOI: 10.1007/s10753-012-9578-7

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 26095851

Title: Cyclophilin A regulates JNK/p38-MAPK signaling through its physical interaction with ASK1.

PubMed ID: 26095851

DOI: 10.1016/j.bbrc.2015.06.078

PubMed ID: 25678563

Title: Peptidylprolyl isomerase A governs TARDBP function and assembly in heterogeneous nuclear ribonucleoprotein complexes.

PubMed ID: 25678563

DOI: 10.1093/brain/awv005

PubMed ID: 25489052

Title: Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-acetylation defects.

PubMed ID: 25489052

DOI: 10.1093/hmg/ddu611

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 30328013

Title: CypA Regulates AIP4-Mediated M1 Ubiquitination of Influenza A Virus.

PubMed ID: 30328013

DOI: 10.1007/s12250-018-0058-6

PubMed ID: 31063815

Title: Cyclophilin A-FoxO1 signaling pathway in endothelial cell apoptosis.

PubMed ID: 31063815

DOI: 10.1016/j.cellsig.2019.04.014

PubMed ID: 1896075

Title: Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy.

PubMed ID: 1896075

DOI: 10.1038/353276a0

PubMed ID: 1946361

Title: Crystal structure of recombinant human T-cell cyclophilin A at 2.5-A resolution.

PubMed ID: 1946361

DOI: 10.1073/pnas.88.21.9483

PubMed ID: 8421501

Title: X-ray structure of a decameric cyclophilin-cyclosporin crystal complex.

PubMed ID: 8421501

DOI: 10.1038/361091a0

PubMed ID: 8263916

Title: X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1-A resolution.

PubMed ID: 8263916

DOI: 10.1006/jmbi.1993.1664

PubMed ID: 8652511

Title: Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization.

PubMed ID: 8652511

DOI: 10.1021/bi9602775

PubMed ID: 9385632

Title: Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein.

PubMed ID: 9385632

DOI: 10.1002/pro.5560061103

PubMed ID: 9769216

Title: X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A.

PubMed ID: 9769216

DOI: 10.1006/jmbi.1998.2108

PubMed ID: 12218175

Title: Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes.

PubMed ID: 12218175

DOI: 10.1073/pnas.192206699

PubMed ID: 12357034

Title: Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin.

PubMed ID: 12357034

DOI: 10.1073/pnas.212504399

PubMed ID: 8421500

Title: Solution structure of the cyclosporin A/cyclophilin complex by NMR.

PubMed ID: 8421500

DOI: 10.1038/361088a0

PubMed ID: 9299338

Title: The NMR solution conformation of unligated human cyclophilin A.

PubMed ID: 9299338

DOI: 10.1006/jmbi.1997.1220

PubMed ID: 20364129

Title: Acetylation regulates cyclophilin A catalysis, immunosuppression and HIV isomerization.

PubMed ID: 20364129

DOI: 10.1038/nchembio.342

Sequence Information:

Length: 165
Mass: 18012
Checksum: 9B2E637A555E4434
Sequence:

MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG SCFHRIIPGF 
MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM ANAGPNTNGS QFFICTAKTE 
WLDGKHVVFG KVKEGMNIVE AMERFGSRNG KTSKKITIAD CGQLE

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. For the full schema, download it here.

Details for: PPIA

Associated with

Cells (max top 100)

Other Information

Complementary DNA for human T-cell cyclophilin. PubMed ID: 3297675

Characterization of the human cyclophilin gene and of related processed pseudogenes. PubMed ID: 2197089

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

Human protein factory for converting the transcriptome into an in vitro-expressed proteome. PubMed ID: 19054851

The DNA sequence of human chromosome 7. PubMed ID: 12853948

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Identification of cyclophilin A from human decidual and placental tissue in the first trimester of pregnancy. PubMed ID: 7657784

Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. PubMed ID: 12665801

Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue. PubMed ID: 2001362

Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B. PubMed ID: 8513493

CD147 facilitates HIV-1 infection by interacting with virus-associated cyclophilin A. PubMed ID: 11353871

Active site residues of cyclophilin A are crucial for its signaling activity via CD147. PubMed ID: 11943775

Proteomic characterization of the human centrosome by protein correlation profiling. PubMed ID: 14654843

Cyclophilin A is a proinflammatory cytokine that activates endothelial cells. PubMed ID: 15130913

Function of HAb18G/CD147 in invasion of host cells by severe acute respiratory syndrome coronavirus. PubMed ID: 15688292

Cyclophilin A is secreted by a vesicular pathway in vascular smooth muscle cells. PubMed ID: 16527992

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Cyclophilin A interacts with influenza A virus M1 protein and impairs the early stage of the viral replication. PubMed ID: 19207730

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

CD147/EMMPRIN acts as a functional entry receptor for measles virus on epithelial cells. PubMed ID: 20147391

Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases. PubMed ID: 20676357

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

Cyclophilin A (CyPA) induces chemotaxis independent of its peptidylprolyl cis-trans isomerase activity: direct binding between CyPA and the ectodomain of CD147. PubMed ID: 21245143

Cyclophilin A interacts with domain II of hepatitis C virus NS5A and stimulates RNA binding in an isomerase-dependent manner. PubMed ID: 21593166

Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. PubMed ID: 22223895

Cyclophilin A restricts influenza A virus replication through degradation of the M1 protein. PubMed ID: 22347431

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Antiapoptotic and proapoptotic signaling of cyclophilin A in endothelial cells. PubMed ID: 23180369

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Cyclophilin A regulates JNK/p38-MAPK signaling through its physical interaction with ASK1. PubMed ID: 26095851

Peptidylprolyl isomerase A governs TARDBP function and assembly in heterogeneous nuclear ribonucleoprotein complexes. PubMed ID: 25678563

Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-acetylation defects. PubMed ID: 25489052

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

CypA Regulates AIP4-Mediated M1 Ubiquitination of Influenza A Virus. PubMed ID: 30328013

Cyclophilin A-FoxO1 signaling pathway in endothelial cell apoptosis. PubMed ID: 31063815

Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy. PubMed ID: 1896075

Crystal structure of recombinant human T-cell cyclophilin A at 2.5-A resolution. PubMed ID: 1946361

X-ray structure of a decameric cyclophilin-cyclosporin crystal complex. PubMed ID: 8421501

X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1-A resolution. PubMed ID: 8263916

Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization. PubMed ID: 8652511

Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein. PubMed ID: 9385632

X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A. PubMed ID: 9769216

Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. PubMed ID: 12218175

Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin. PubMed ID: 12357034

Solution structure of the cyclosporin A/cyclophilin complex by NMR. PubMed ID: 8421500

The NMR solution conformation of unligated human cyclophilin A. PubMed ID: 9299338

Acetylation regulates cyclophilin A catalysis, immunosuppression and HIV isomerization. PubMed ID: 20364129