Details for: PPIA

Gene ID: 5478

Symbol: PPIA

Ensembl ID: ENSG00000196262

Description: peptidylprolyl isomerase A

Associated with

Cells (max top 100)

(Marker Scores and respective Thresholds are 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: 5,863
  • Cell Name: thyroid follicular cell (CL0002258)
    Fold Change: 5.61
    Marker Score: 4,390
  • Cell Name: malignant cell (CL0001064)
    Fold Change: 5
    Marker Score: 67,128
  • Cell Name: mesenchymal stem cell (CL0000134)
    Fold Change: 4.92
    Marker Score: 7,578
  • Cell Name: mature T cell (CL0002419)
    Fold Change: 4.91
    Marker Score: 48,638
  • Cell Name: mature gamma-delta T cell (CL0000800)
    Fold Change: 4.68
    Marker Score: 14,782
  • Cell Name: radial glial cell (CL0000681)
    Fold Change: 4.47
    Marker Score: 1,647
  • Cell Name: CD38-negative naive B cell (CL0002102)
    Fold Change: 4.41
    Marker Score: 9,249
  • Cell Name: mature alpha-beta T cell (CL0000791)
    Fold Change: 4.4
    Marker Score: 232,873
  • Cell Name: NKp46-positive innate lymphoid cell, human (CL0001076)
    Fold Change: 4.39
    Marker Score: 12,814
  • Cell Name: naive thymus-derived CD4-positive, alpha-beta T cell (CL0000895)
    Fold Change: 4.3
    Marker Score: 7,380
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: 4.26
    Marker Score: 145,007
  • Cell Name: kidney loop of Henle thick ascending limb epithelial cell (CL1001106)
    Fold Change: 4.22
    Marker Score: 11,319
  • Cell Name: mesodermal cell (CL0000222)
    Fold Change: 4.22
    Marker Score: 55,645
  • Cell Name: blood cell (CL0000081)
    Fold Change: 4.14
    Marker Score: 48,133
  • Cell Name: naive B cell (CL0000788)
    Fold Change: 4.1
    Marker Score: 3,663
  • Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
    Fold Change: 4.09
    Marker Score: 228,832
  • Cell Name: epithelial cell of proximal tubule (CL0002306)
    Fold Change: 4.05
    Marker Score: 14,383
  • Cell Name: alveolar capillary type 1 endothelial cell (CL4028002)
    Fold Change: 4
    Marker Score: 10,162
  • Cell Name: epithelial cell of lung (CL0000082)
    Fold Change: 3.98
    Marker Score: 20,908
  • Cell Name: double negative T regulatory cell (CL0011024)
    Fold Change: 3.93
    Marker Score: 3,802
  • Cell Name: T-helper 22 cell (CL0001042)
    Fold Change: 3.93
    Marker Score: 16,857
  • Cell Name: skeletal muscle satellite stem cell (CL0008011)
    Fold Change: 3.92
    Marker Score: 4,181
  • Cell Name: erythroid progenitor cell (CL0000038)
    Fold Change: 3.91
    Marker Score: 4,084
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: 3.91
    Marker Score: 9,557
  • Cell Name: kidney collecting duct principal cell (CL1001431)
    Fold Change: 3.85
    Marker Score: 9,717
  • Cell Name: chondrocyte (CL0000138)
    Fold Change: 3.84
    Marker Score: 1,728
  • Cell Name: embryonic stem cell (CL0002322)
    Fold Change: 3.81
    Marker Score: 1,219
  • Cell Name: CD8-positive, alpha-beta memory T cell, CD45RO-positive (CL0001203)
    Fold Change: 3.79
    Marker Score: 10,631
  • Cell Name: type I NK T cell (CL0000921)
    Fold Change: 3.79
    Marker Score: 2,974
  • Cell Name: effector memory CD8-positive, alpha-beta T cell, terminally differentiated (CL0001062)
    Fold Change: 3.78
    Marker Score: 5,565
  • Cell Name: CD4-positive, alpha-beta cytotoxic T cell (CL0000934)
    Fold Change: 3.77
    Marker Score: 3,308
  • Cell Name: decidual natural killer cell, human (CL0002343)
    Fold Change: 3.75
    Marker Score: 10,368
  • Cell Name: kidney interstitial cell (CL1000500)
    Fold Change: 3.75
    Marker Score: 2,667
  • Cell Name: naive thymus-derived CD8-positive, alpha-beta T cell (CL0000900)
    Fold Change: 3.75
    Marker Score: 6,694
  • Cell Name: germinal center B cell (CL0000844)
    Fold Change: 3.75
    Marker Score: 2,279
  • Cell Name: renal intercalated cell (CL0005010)
    Fold Change: 3.73
    Marker Score: 1,992
  • Cell Name: basal cell of epithelium of trachea (CL1000348)
    Fold Change: 3.73
    Marker Score: 27,765
  • Cell Name: central memory CD8-positive, alpha-beta T cell (CL0000907)
    Fold Change: 3.73
    Marker Score: 9,092
  • Cell Name: type I pneumocyte (CL0002062)
    Fold Change: 3.71
    Marker Score: 4,472
  • Cell Name: class switched memory B cell (CL0000972)
    Fold Change: 3.71
    Marker Score: 3,490
  • Cell Name: interstitial cell of ovary (CL0002094)
    Fold Change: 3.68
    Marker Score: 23,931
  • Cell Name: CD4-positive, alpha-beta memory T cell (CL0000897)
    Fold Change: 3.62
    Marker Score: 2,121
  • 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: 3,406
  • Cell Name: type II pneumocyte (CL0002063)
    Fold Change: 3.6
    Marker Score: 23,461
  • Cell Name: glycinergic neuron (CL1001509)
    Fold Change: 3.59
    Marker Score: 4,331
  • Cell Name: medullary thymic epithelial cell (CL0002365)
    Fold Change: 3.57
    Marker Score: 5,848
  • Cell Name: IgG-negative class switched memory B cell (CL0002117)
    Fold Change: 3.57
    Marker Score: 3,512
  • Cell Name: mucosal invariant T cell (CL0000940)
    Fold Change: 3.55
    Marker Score: 3,160
  • Cell Name: kidney loop of Henle thin ascending limb epithelial cell (CL1001107)
    Fold Change: 3.55
    Marker Score: 3,599
  • Cell Name: myofibroblast cell (CL0000186)
    Fold Change: 3.53
    Marker Score: 4,362
  • Cell Name: alveolar capillary type 2 endothelial cell (CL4028003)
    Fold Change: 3.5
    Marker Score: 5,070
  • Cell Name: effector CD8-positive, alpha-beta T cell (CL0001050)
    Fold Change: 3.49
    Marker Score: 2,935
  • Cell Name: lung macrophage (CL1001603)
    Fold Change: 3.48
    Marker Score: 3,986
  • Cell Name: memory B cell (CL0000787)
    Fold Change: 3.47
    Marker Score: 2,627
  • Cell Name: naive T cell (CL0000898)
    Fold Change: 3.47
    Marker Score: 2,235
  • Cell Name: Sertoli cell (CL0000216)
    Fold Change: 3.45
    Marker Score: 20,443
  • Cell Name: CD16-negative, CD56-bright natural killer cell, human (CL0000938)
    Fold Change: 3.43
    Marker Score: 2,806
  • Cell Name: activated CD4-positive, alpha-beta T cell, human (CL0001043)
    Fold Change: 3.42
    Marker Score: 1,553
  • Cell Name: capillary endothelial cell (CL0002144)
    Fold Change: 3.42
    Marker Score: 3,674
  • Cell Name: kidney collecting duct intercalated cell (CL1001432)
    Fold Change: 3.41
    Marker Score: 5,656
  • Cell Name: late pro-B cell (CL0002048)
    Fold Change: 3.4
    Marker Score: 4,008
  • Cell Name: immature B cell (CL0000816)
    Fold Change: 3.4
    Marker Score: 2,250
  • Cell Name: stratified epithelial cell (CL0000079)
    Fold Change: 3.39
    Marker Score: 26,498
  • Cell Name: T follicular helper cell (CL0002038)
    Fold Change: 3.39
    Marker Score: 2,818
  • Cell Name: foveolar cell of stomach (CL0002179)
    Fold Change: 3.39
    Marker Score: 21,636
  • Cell Name: professional antigen presenting cell (CL0000145)
    Fold Change: 3.39
    Marker Score: 1,748
  • Cell Name: unswitched memory B cell (CL0000970)
    Fold Change: 3.38
    Marker Score: 1,981
  • Cell Name: CD4-positive helper T cell (CL0000492)
    Fold Change: 3.38
    Marker Score: 3,677
  • Cell Name: epithelial cell (CL0000066)
    Fold Change: 3.34
    Marker Score: 5,313
  • Cell Name: centroblast (CL0009112)
    Fold Change: 3.33
    Marker Score: 1,639
  • Cell Name: CD8-positive, alpha-beta memory T cell (CL0000909)
    Fold Change: 3.33
    Marker Score: 2,823
  • Cell Name: myoepithelial cell of mammary gland (CL0002324)
    Fold Change: 3.32
    Marker Score: 16,302
  • Cell Name: activated CD8-positive, alpha-beta T cell (CL0000906)
    Fold Change: 3.32
    Marker Score: 2,405
  • Cell Name: activated CD4-positive, alpha-beta T cell (CL0000896)
    Fold Change: 3.31
    Marker Score: 2,395
  • Cell Name: CD8-alpha-alpha-positive, alpha-beta intraepithelial T cell (CL0000915)
    Fold Change: 3.3
    Marker Score: 4,665
  • Cell Name: endothelial cell (CL0000115)
    Fold Change: 3.29
    Marker Score: 2,947
  • Cell Name: smooth muscle cell (CL0000192)
    Fold Change: 3.27
    Marker Score: 2,152
  • Cell Name: CD14-positive, CD16-positive monocyte (CL0002397)
    Fold Change: 3.25
    Marker Score: 6,332
  • Cell Name: Kupffer cell (CL0000091)
    Fold Change: 3.24
    Marker Score: 3,246
  • Cell Name: natural T-regulatory cell (CL0000903)
    Fold Change: 3.24
    Marker Score: 1,664
  • Cell Name: colon epithelial cell (CL0011108)
    Fold Change: 3.24
    Marker Score: 10,163
  • Cell Name: kidney distal convoluted tubule epithelial cell (CL1000849)
    Fold Change: 3.23
    Marker Score: 3,422
  • Cell Name: epithelial cell of urethra (CL1000296)
    Fold Change: 3.23
    Marker Score: 2,542
  • Cell Name: effector CD4-positive, alpha-beta T cell (CL0001044)
    Fold Change: 3.23
    Marker Score: 3,019
  • Cell Name: hematopoietic cell (CL0000988)
    Fold Change: 3.22
    Marker Score: 2,142
  • Cell Name: secretory cell (CL0000151)
    Fold Change: 3.22
    Marker Score: 5,877
  • Cell Name: CD8-positive, alpha-beta thymocyte (CL0000811)
    Fold Change: 3.21
    Marker Score: 1,774
  • Cell Name: DN3 thymocyte (CL0000807)
    Fold Change: 3.21
    Marker Score: 1,603
  • Cell Name: neuroblast (sensu Vertebrata) (CL0000031)
    Fold Change: 3.2
    Marker Score: 2,012
  • Cell Name: bronchial epithelial cell (CL0002328)
    Fold Change: 3.2
    Marker Score: 847
  • Cell Name: supporting cell (CL0000630)
    Fold Change: 3.19
    Marker Score: 5,990
  • Cell Name: CD8-positive, alpha-beta cytotoxic T cell (CL0000794)
    Fold Change: 3.19
    Marker Score: 2,810
  • Cell Name: pulmonary artery endothelial cell (CL1001568)
    Fold Change: 3.18
    Marker Score: 2,740
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: 3.17
    Marker Score: 9,414
  • Cell Name: regulatory T cell (CL0000815)
    Fold Change: 3.17
    Marker Score: 3,508
  • Cell Name: gamma-delta T cell (CL0000798)
    Fold Change: 3.17
    Marker Score: 2,131
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 3.15
    Marker Score: 109,247
  • Cell Name: memory regulatory T cell (CL0002678)
    Fold Change: 3.13
    Marker Score: 1,091

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 Marker Score to the Marker Score Threshold, indicating how much the gene expression has changed compared to a baseline.
Marker Score: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

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 Marker Score to the Marker Score Threshold, indicating how much the gene expression has changed compared to a baseline.
Marker Score: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

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 Marker Score to the Marker Score Threshold, indicating how much the gene expression has changed compared to a baseline.
Marker Score: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**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.

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:

ABCD 1 AGR 1 AlphaFoldDB 1 Antibodypedia 1 BMRB 1 BRENDA 1 Bgee 1 BindingDB 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 2 CDD 1 CORUM 1 CTD 1 ChEBI 2 ChEMBL 1 ChiTaRS 1 DIP 1 DMDM 1 DNASU 1 DOSAC-COBS-2DPAGE 1 DisGeNET 1 DrugBank 7 DrugCentral 1 EC 1 EMBL 21 EMDB 8 EPD 1 Ensembl 7 EvolutionaryTrace 1 ExpressionAtlas 1 GO 47 Gene3D 1 GeneCards 1 GeneTree 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyCosmos 1 GlyGen 1 GuidetoPHARMACOLOGY 1 HGNC 1 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 4 KEGG 1 MANE-Select 1 MIM 1 MINT 1 MassIVE 1 MetOSite 1 NCBI Taxonomy 1 OGP 1 OMA 1 OpenTargets 1 OrthoDB 1 PANTHER 2 PDB 100 PDBsum 100 PIR 1 PIRSF 1 PRIDE 1 PRINTS 1 PRO 1 PROSITE 2 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 1 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 2 Pumba 1 REPRODUCTION-2DPAGE 2 RNAct 1 Reactome 15 RefSeq 2 Rhea 3 SMR 1 STRING 1 SUPFAM 1 SWISS-2DPAGE 1 SignaLink 1 SwissPalm 1 TopDownProteomics 1 TreeFam 1 UCD-2DPAGE 1 UCSC 1 UniProtKB 3 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

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.