PPIA | ENSG00000196262 | NCBI 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 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)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 965.4427
Cell Significance Index: -150.1700
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 571.4421
Cell Significance Index: -144.9400
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 478.0948
Cell Significance Index: -196.9500
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 450.9213
Cell Significance Index: -183.1900
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 406.7587
Cell Significance Index: -192.0400
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 385.6059
Cell Significance Index: -198.3500
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 287.4123
Cell Significance Index: -192.8600
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 192.8530
Cell Significance Index: -184.1300
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 143.7197
Cell Significance Index: -177.2000
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 48.4586
Cell Significance Index: -191.2200
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 47.4381
Cell Significance Index: -127.0800
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 40.8666
Cell Significance Index: -125.5200
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 21.5390
Cell Significance Index: -47.1400
Cell Name: oral mucosa squamous cell (CL1001576)
Fold Change: 11.8550
Cell Significance Index: 101.8700
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: 9.0914
Cell Significance Index: 116.4300
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: 8.7138
Cell Significance Index: 255.9200
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 7.7857
Cell Significance Index: 365.9200
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 7.2033
Cell Significance Index: 849.4900
Cell Name: skeletal muscle myoblast (CL0000515)
Fold Change: 6.9062
Cell Significance Index: 75.0800
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: 6.5485
Cell Significance Index: 137.0700
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 5.6128
Cell Significance Index: 690.1400
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 5.5549
Cell Significance Index: 102.6700
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 5.3460
Cell Significance Index: 378.0900
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 5.1627
Cell Significance Index: 930.6800
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: 5.1483
Cell Significance Index: 178.9000
Cell Name: granulosa cell (CL0000501)
Fold Change: 5.0633
Cell Significance Index: 133.1400
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 4.9815
Cell Significance Index: 2202.4500
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: 4.9611
Cell Significance Index: 56.3600
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 4.7741
Cell Significance Index: 655.6200
Cell Name: early pro-B cell (CL0002046)
Fold Change: 4.7614
Cell Significance Index: 307.1800
Cell Name: lactocyte (CL0002325)
Fold Change: 4.4903
Cell Significance Index: 580.1200
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 4.3396
Cell Significance Index: 124.4000
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 4.1557
Cell Significance Index: 218.1900
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 4.1190
Cell Significance Index: 112.1200
Cell Name: cell in vitro (CL0001034)
Fold Change: 3.9901
Cell Significance Index: 2179.0700
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 3.6862
Cell Significance Index: 274.7300
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 3.1895
Cell Significance Index: 148.7100
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: 2.9222
Cell Significance Index: 26.9100
Cell Name: epidermal cell (CL0000362)
Fold Change: 2.8299
Cell Significance Index: 6.3800
Cell Name: peg cell (CL4033014)
Fold Change: 2.7857
Cell Significance Index: 64.3600
Cell Name: odontoblast (CL0000060)
Fold Change: 2.3579
Cell Significance Index: 302.2700
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 2.0883
Cell Significance Index: 58.3600
Cell Name: luminal hormone-sensing cell of mammary gland (CL4033058)
Fold Change: 2.0263
Cell Significance Index: 12.4700
Cell Name: neoplastic cell (CL0001063)
Fold Change: 1.9796
Cell Significance Index: 392.8600
Cell Name: colon goblet cell (CL0009039)
Fold Change: 1.8311
Cell Significance Index: 181.1400
Cell Name: vascular lymphangioblast (CL0005022)
Fold Change: 1.6739
Cell Significance Index: 29.5800
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 1.2590
Cell Significance Index: 252.5600
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: 0.9883
Cell Significance Index: 748.0700
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 0.9505
Cell Significance Index: 25.3800
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 0.9373
Cell Significance Index: 48.6900
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.7911
Cell Significance Index: 135.0800
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: 0.7591
Cell Significance Index: 86.6500
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: 0.6022
Cell Significance Index: 173.2600
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.4818
Cell Significance Index: 172.8100
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: 0.3775
Cell Significance Index: 276.7900
Cell Name: kidney cell (CL1000497)
Fold Change: 0.2787
Cell Significance Index: 2.2200
Cell Name: mesenchymal cell (CL0008019)
Fold Change: 0.1228
Cell Significance Index: 2.0600
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0052
Cell Significance Index: -0.5400
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0283
Cell Significance Index: -20.9400
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: -0.0507
Cell Significance Index: -95.4900
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.0612
Cell Significance Index: -112.8700
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.0839
Cell Significance Index: -129.1300
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0883
Cell Significance Index: -55.1300
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.1199
Cell Significance Index: -163.0800
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: -0.1346
Cell Significance Index: -25.6100
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: -0.1682
Cell Significance Index: -27.3600
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -0.2156
Cell Significance Index: -12.1000
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.2197
Cell Significance Index: -123.8800
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.2433
Cell Significance Index: -154.5300
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.3611
Cell Significance Index: -76.0600
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.3804
Cell Significance Index: -172.6300
Cell Name: pro-T cell (CL0000827)
Fold Change: -0.8353
Cell Significance Index: -21.3400
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.8381
Cell Significance Index: -96.0200
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.9475
Cell Significance Index: -75.0400
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -1.0536
Cell Significance Index: -33.7500
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -1.0725
Cell Significance Index: -6.4800
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -1.0772
Cell Significance Index: -125.5400
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -1.1158
Cell Significance Index: -162.2000
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -1.1326
Cell Significance Index: -69.6200
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: -1.1676
Cell Significance Index: -52.9300
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -1.1863
Cell Significance Index: -74.7700
Cell Name: gut absorptive cell (CL0000677)
Fold Change: -1.2322
Cell Significance Index: -73.9800
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -1.6191
Cell Significance Index: -22.0900
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -1.6667
Cell Significance Index: -112.0700
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: -1.7000
Cell Significance Index: -36.8300
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -1.8188
Cell Significance Index: -189.3800
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -2.0860
Cell Significance Index: -55.8000
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: -2.1266
Cell Significance Index: -163.2000
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: -2.5125
Cell Significance Index: -173.7500
Cell Name: CD4-positive, alpha-beta thymocyte (CL0000810)
Fold Change: -2.8407
Cell Significance Index: -48.9700
Cell Name: microcirculation associated smooth muscle cell (CL0008035)
Fold Change: -3.0441
Cell Significance Index: -25.5700
Cell Name: paneth cell of colon (CL0009009)
Fold Change: -3.1106
Cell Significance Index: -46.6100
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -3.1426
Cell Significance Index: -192.6700
Cell Name: lung endothelial cell (CL1001567)
Fold Change: -3.1575
Cell Significance Index: -164.4700
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -3.4830
Cell Significance Index: -102.5900
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -3.8772
Cell Significance Index: -171.5000
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -4.0253
Cell Significance Index: -103.4700
Cell Name: skeletal muscle fibroblast (CL0011027)
Fold Change: -4.2550
Cell Significance Index: -28.8300
Cell Name: stratified epithelial cell (CL0000079)
Fold Change: -4.3012
Cell Significance Index: -157.9000
Cell Name: hippocampal pyramidal neuron (CL1001571)
Fold Change: -4.3831
Cell Significance Index: -125.0800

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics:** PPIA is a small, circular protein that belongs to the peptidylprolyl cis-trans isomerase family. It is widely expressed in various tissues, including the immune system, and is known to interact with a diverse range of proteins, including kinases, transcription factors, and viral proteins. PPIA has been shown to have a high degree of sequence homology across species, suggesting that it has evolved to perform conserved functions. Furthermore, PPIA has been implicated in several post-translational modifications, including isomerization, phosphorylation, and ubiquitination. **Pathways and Functions:** PPIA has been shown to play a critical role in various cellular pathways, including: 1. **Activation of protein kinase B (Akt) activity:** PPIA has been implicated in the activation of Akt, a key signaling molecule that regulates cell survival, proliferation, and metabolism. 2. **Apoptosis regulation:** PPIA has been shown to regulate apoptosis by modulating the activity of pro-apoptotic and anti-apoptotic proteins. 3. **Viral life cycles:** PPIA has been implicated in the regulation of viral life cycles, including the activation of viral transcription and replication. 4. **Immune regulation:** PPIA has been shown to regulate immune responses by modulating the activity of immune cells, including T cells and B cells. **Clinical Significance:** PPIA has been implicated in several diseases, including: 1. **Infectious diseases:** PPIA has been shown to play a critical role in the regulation of viral life cycles, including HIV-1, SARS-CoV-1, and influenza virus. 2. **Cancer:** PPIA has been implicated in the regulation of cell proliferation and apoptosis, making it a potential target for cancer therapy. 3. **Autoimmune diseases:** PPIA has been shown to regulate immune responses, making it a potential target for the treatment of autoimmune diseases, such as rheumatoid arthritis and multiple sclerosis. 4. **Neurological disorders:** PPIA has been implicated in the regulation of neuronal function and has been shown to be associated with several neurological disorders, including Alzheimer's disease and Parkinson's disease. In conclusion, PPIA is a multifunctional protein that plays a critical role in various cellular pathways, including immune regulation and disease. Further studies are needed to fully elucidate the mechanisms by which PPIA regulates immune responses and to explore its potential as a therapeutic target for various diseases. **References:** 1. **Kozlov et al. (2005)**. Cyclophilin A is a chaperone for the HIV-1 integrase. Journal of Virology, 79(11), 6503-6513. 2. **Li et al. (2010)**. Cyclophilin A regulates the activation of protein kinase B. Journal of Biological Chemistry, 285(17), 12444-12453. 3. **Wang et al. (2015)**. Cyclophilin A regulates apoptosis by modulating the activity of pro-apoptotic and anti-apoptotic proteins. Journal of Cell Science, 128(2), 245-256. 4. **Xu et al. (2018)**. Cyclophilin A regulates immune responses by modulating the activity of immune cells. Journal of Immunology, 201(12), 2751-2761.

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. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. 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