Human Gene PPIA (uc003tlw.3)
  Description: Homo sapiens peptidylprolyl isomerase A (cyclophilin A) (PPIA), mRNA.
RefSeq Summary (NM_021130): This gene encodes a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. The encoded protein is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. The protein can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported. [provided by RefSeq, Jul 2008].
Transcript (Including UTRs)
   Position: hg19 chr7:44,836,241-44,842,716 Size: 6,476 Total Exon Count: 5 Strand: +
Coding Region
   Position: hg19 chr7:44,836,324-44,841,021 Size: 4,698 Coding Exon Count: 5 

Page IndexSequence and LinksUniProtKB CommentsGenetic AssociationsMalaCardsCTD
Gene AllelesRNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther Species
GO AnnotationsmRNA DescriptionsPathwaysOther NamesModel InformationMethods
Data last updated at UCSC: 2013-06-14

-  Sequence and Links to Tools and Databases
Genomic Sequence (chr7:44,836,241-44,842,716)mRNA (may differ from genome)Protein (165 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
BioGPSCGAPEnsemblEntrez GeneExonPrimerGeneCards

-  Comments and Description Text from UniProtKB
DESCRIPTION: RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; EC=; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-binding protein; AltName: Full=Rotamase A;
FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0).
ENZYME REGULATION: Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.
SUBUNIT: Interacts with HIV-1 Capsid protein.
INTERACTION: Q72497:gag (xeno); NbExp=6; IntAct=EBI-437708, EBI-1036263; Q16849:PTPRN; NbExp=3; IntAct=EBI-437708, EBI-728153; O00267:SUPT5H; NbExp=2; IntAct=EBI-437708, EBI-710464;
SUBCELLULAR LOCATION: Cytoplasm. Secreted. Note=Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that involves actin remodeling and myosin II activation, and mediates ERK1/2 activation.
PTM: 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.
SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A subfamily.
SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
WEB RESOURCE: Name=Wikipedia; Note=Cyclophilin entry; URL="";

-  Genetic Association Studies of Complex Diseases and Disorders
  Genetic Association Database (archive): PPIA
CDC HuGE Published Literature: PPIA

-  MalaCards Disease Associations
  MalaCards Gene Search: PPIA
Diseases sorted by gene-association score: diffuse intrinsic pontine glioma (8), wolfram syndrome 2 (8), retinitis pigmentosa 14 (6), nodular nonsuppurative panniculitis (6), in situ carcinoma (6), hiv-1 (4), hepatitis c virus (3)

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 304.40 RPKM in Cells - EBV-transformed lymphocytes
Total median expression: 6121.31 RPKM

View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -25.1283-0.303 Picture PostScript Text
3' UTR -615.401695-0.363 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR002130 - Cyclophilin-like_PPIase_dom
IPR024936 - Cyclophilin-type_PPIase
IPR020892 - Cyclophilin-type_PPIase_CS

Pfam Domains:
PF00160 - Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD

SCOP Domains:
50891 - Cyclophilin-like

Protein Data Bank (PDB) 3-D Structure
MuPIT help

- X-ray

- X-ray MuPIT

- X-ray MuPIT
To conserve bandwidth, only the images from the first 3 structures are shown.
1AWS - X-ray MuPIT 1AWT - X-ray MuPIT 1AWU - X-ray MuPIT
1AWV - X-ray MuPIT 1BCK - X-ray MuPIT 1CWA - X-ray MuPIT
1CWB - X-ray MuPIT 1CWC - X-ray MuPIT 1CWF - X-ray MuPIT
1CWH - X-ray MuPIT 1CWI - X-ray MuPIT 1CWJ - X-ray MuPIT
1CWK - X-ray MuPIT 1CWL - X-ray MuPIT 1CWM - X-ray MuPIT
1CWO - X-ray MuPIT 1FGL - X-ray 1M63 - X-ray MuPIT
1M9C - X-ray MuPIT 1M9D - X-ray MuPIT 1M9E - X-ray MuPIT
1M9F - X-ray MuPIT 1M9X - X-ray MuPIT 1M9Y - X-ray MuPIT
1MF8 - X-ray MuPIT 1MIK - X-ray MuPIT 1NMK - X-ray MuPIT
1OCA - NMR MuPIT 1RMH - X-ray MuPIT 1VBS - X-ray
1VBT - X-ray 1W8L - X-ray MuPIT 1W8M - X-ray MuPIT
1W8V - X-ray MuPIT 1YND - X-ray MuPIT 1ZKF - X-ray MuPIT
2ALF - X-ray MuPIT 2CPL - X-ray MuPIT 2CYH - X-ray
2RMA - X-ray MuPIT 2RMB - X-ray MuPIT 2X25 - X-ray
2X2A - X-ray 2X2C - X-ray MuPIT 2X2D - X-ray MuPIT
2XGY - X-ray MuPIT 3CYH - X-ray 3CYS - NMR
3K0M - X-ray MuPIT 3K0N - X-ray MuPIT 3K0O - X-ray MuPIT
3K0P - X-ray MuPIT 3K0Q - X-ray MuPIT 3K0R - X-ray MuPIT
3ODI - X-ray MuPIT 3ODL - X-ray MuPIT 3RDD - X-ray MuPIT
4CYH - X-ray MuPIT 5CYH - X-ray MuPIT

ModBase Predicted Comparative 3D Structure on P62937
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologGenome BrowserNo orthologNo orthologGenome BrowserNo ortholog
Gene DetailsGene Details  Gene Details 
Gene SorterGene Sorter  Gene Sorter 
 RGD  WormBase 
 Protein Sequence  Protein Sequence 
 Alignment  Alignment 

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0003723 RNA binding
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005515 protein binding
GO:0016018 cyclosporin A binding
GO:0016853 isomerase activity
GO:0046790 virion binding
GO:0051082 unfolded protein binding

Biological Process:
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006278 RNA-dependent DNA biosynthetic process
GO:0006457 protein folding
GO:0016032 viral process
GO:0019058 viral life cycle
GO:0019061 uncoating of virus
GO:0019064 fusion of virus membrane with host plasma membrane
GO:0019068 virion assembly
GO:0019076 viral release from host cell
GO:0030260 entry into host cell
GO:0034389 lipid particle organization
GO:0035722 interleukin-12-mediated signaling pathway
GO:0043312 neutrophil degranulation
GO:0045069 regulation of viral genome replication
GO:0045070 positive regulation of viral genome replication
GO:0050714 positive regulation of protein secretion
GO:0050900 leukocyte migration
GO:0075713 establishment of integrated proviral latency

Cellular Component:
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005925 focal adhesion
GO:0016020 membrane
GO:0031982 vesicle
GO:0032991 macromolecular complex
GO:0034774 secretory granule lumen
GO:0070062 extracellular exosome
GO:1904813 ficolin-1-rich granule lumen

-  Descriptions from all associated GenBank mRNAs
  BC137057 - Homo sapiens peptidylprolyl isomerase A (cyclophilin A), mRNA (cDNA clone MGC:168677 IMAGE:9021054), complete cds.
BC137058 - Homo sapiens peptidylprolyl isomerase A (cyclophilin A), mRNA (cDNA clone MGC:168678 IMAGE:9021055), complete cds.
BC005982 - Homo sapiens peptidylprolyl isomerase A (cyclophilin A), mRNA (cDNA clone MGC:14681 IMAGE:4109260), complete cds.
AK290851 - Homo sapiens cDNA FLJ78589 complete cds, highly similar to Homo sapiens peptidylprolyl isomerase A (cyclophilin A) (PPIA), transcript variant 1, mRNA.
BC007104 - Homo sapiens peptidylprolyl isomerase A (cyclophilin A), mRNA (cDNA clone MGC:14747 IMAGE:4281376), complete cds.
BC013915 - Homo sapiens peptidylprolyl isomerase A (cyclophilin A), mRNA (cDNA clone MGC:22814 IMAGE:3684721), complete cds.
AK293003 - Homo sapiens cDNA FLJ75025 complete cds, highly similar to Homo sapiens peptidylprolyl isomerase A (cyclophilin A) (PPIA), transcript variant 2, mRNA.
AK130101 - Homo sapiens cDNA FLJ26591 fis, clone LNF08046, highly similar to Peptidyl-prolyl cis-trans isomerase A (EC
AK316564 - Homo sapiens cDNA, FLJ92934, highly similar to Homo sapiens peptidylprolyl isomerase A (cyclophilin A) (PPIA),mRNA.
AK026569 - Homo sapiens cDNA: FLJ22916 fis, clone KAT06406, highly similar to HSCYCR Human mRNA for T-cell cyclophilin.
BC093076 - Homo sapiens peptidylprolyl isomerase A (cyclophilin A), mRNA (cDNA clone MGC:111221 IMAGE:30414589), complete cds.
AK297340 - Homo sapiens cDNA FLJ53060 complete cds, moderately similar to Peptidyl-prolyl cis-trans isomerase A (EC
D28351 - Homo sapiens mRNA for cyclophilin, 5'UTR region.
BC005320 - Homo sapiens peptidylprolyl isomerase A (cyclophilin A), mRNA (cDNA clone MGC:12404 IMAGE:3935025), complete cds.
AK290085 - Homo sapiens cDNA FLJ78336 complete cds, highly similar to Homo sapiens peptidylprolyl isomerase A (cyclophilin A) (PPIA), transcript variant 1, mRNA.
BC106030 - Homo sapiens peptidylprolyl isomerase A (cyclophilin A), mRNA (cDNA clone MGC:117158 IMAGE:2986147), complete cds.
EU794650 - Homo sapiens epididymis secretory sperm binding protein Li 69p (HEL-S-69p) mRNA, complete cds.
BC073992 - Homo sapiens peptidylprolyl isomerase A (cyclophilin A), mRNA (cDNA clone MGC:87929 IMAGE:6161389), complete cds.
BC069050 - Homo sapiens cDNA clone IMAGE:6671081, **** WARNING: chimeric clone ****.
BC003026 - Homo sapiens peptidylprolyl isomerase A (cyclophilin A), mRNA (cDNA clone MGC:4203 IMAGE:2823490), complete cds.
BC000689 - Homo sapiens peptidylprolyl isomerase A (cyclophilin A), mRNA (cDNA clone MGC:2351 IMAGE:3349335), complete cds.
Y00052 - Human mRNA for T-cell cyclophilin.
AB464007 - Synthetic construct DNA, clone: pF1KB8197, Homo sapiens PPIA gene for peptidylprolyl isomerase A, without stop codon, in Flexi system.
DQ895865 - Synthetic construct Homo sapiens clone IMAGE:100010325; FLH188415.01L; RZPDo839C0263D peptidylprolyl isomerase A (cyclophilin A) (PPIA) gene, encodes complete protein.
DQ892625 - Synthetic construct clone IMAGE:100005255; FLH188419.01X; RZPDo839C0273D peptidylprolyl isomerase A (cyclophilin A) (PPIA) gene, encodes complete protein.
KJ905864 - Synthetic construct Homo sapiens clone ccsbBroadEn_15534 PPIA gene, encodes complete protein.
CU674338 - Synthetic construct Homo sapiens gateway clone IMAGE:100017949 5' read PPIA mRNA.
KJ891858 - Synthetic construct Homo sapiens clone ccsbBroadEn_01252 PPIA gene, encodes complete protein.
KJ897362 - Synthetic construct Homo sapiens clone ccsbBroadEn_06756 PPIA gene, encodes complete protein.
AB451438 - Homo sapiens PPIA mRNA for peptidylprolyl isomerase A, partial cds, clone: FLJ08164AAAF.
AB451307 - Homo sapiens PPIA mRNA for peptidylprolyl isomerase A, complete cds, clone: FLJ08164AAAN.
CR456707 - Homo sapiens full open reading frame cDNA clone RZPDo834F113D for gene PPIA, peptidylprolyl isomerase A (cyclophilin A); complete cds, incl. stopcodon.
BC037419 - Homo sapiens peptidylprolyl isomerase A (cyclophilin A), mRNA (cDNA clone IMAGE:5498059), with apparent retained intron.
JD273789 - Sequence 254813 from Patent EP1572962.
LF351480 - JP 2014500723-A/158983: Polycomb-Associated Non-Coding RNAs.
LF362864 - JP 2014500723-A/170367: Polycomb-Associated Non-Coding RNAs.
LF356323 - JP 2014500723-A/163826: Polycomb-Associated Non-Coding RNAs.
JD025110 - Sequence 6134 from Patent EP1572962.
JD029578 - Sequence 10602 from Patent EP1572962.
LF369431 - JP 2014500723-A/176934: Polycomb-Associated Non-Coding RNAs.
LF351482 - JP 2014500723-A/158985: Polycomb-Associated Non-Coding RNAs.
JD390451 - Sequence 371475 from Patent EP1572962.
JD151746 - Sequence 132770 from Patent EP1572962.
JD500334 - Sequence 481358 from Patent EP1572962.
JD297753 - Sequence 278777 from Patent EP1572962.
JD472286 - Sequence 453310 from Patent EP1572962.
MA587057 - JP 2018138019-A/158983: Polycomb-Associated Non-Coding RNAs.
MA598441 - JP 2018138019-A/170367: Polycomb-Associated Non-Coding RNAs.
MA605008 - JP 2018138019-A/176934: Polycomb-Associated Non-Coding RNAs.
MA587059 - JP 2018138019-A/158985: Polycomb-Associated Non-Coding RNAs.
MA591900 - JP 2018138019-A/163826: Polycomb-Associated Non-Coding RNAs.

-  Biochemical and Signaling Pathways
  BioCarta from NCI Cancer Genome Anatomy Project
h_il2rbPathway - IL-2 Receptor Beta Chain in T cell Activation

Reactome (by CSHL, EBI, and GO)

Protein P62937 (Reactome details) participates in the following event(s):

R-HSA-3149454 Packaging of HIV virion on the host cell plasma membrane
R-HSA-173115 Formation of Pre-Integration Complex (PIC)
R-HSA-204485 Basigin binds CyPA
R-HSA-173771 Formation of RTC (Reverse Transcription Complex)
R-HSA-173111 Disassembly of viral capsid
R-HSA-164524 Fusion of viral membrane with host cell membrane
R-HSA-164513 3' PPT-primed initiation of plus-strand DNA synthesis
R-HSA-182795 RNase H-mediated degradation of the template strand
R-HSA-164503 First strand transfer mediated by Repeated (R) sequence
R-HSA-182859 RNase H-mediated degradation of the RNA strand of the -sssDNA:RNA duplex
R-HSA-164519 RNase H-mediated cleavage of the RNA strand of the -sssDNA:RNA duplex
R-HSA-180634 Association of APOBEC3G with single-stranded region of forming HIV-1 minus strand
R-HSA-164504 Synthesis of minus strand strong stop DNA (-sssDNA)
R-HSA-164520 Minus strand DNA synthesis resumes
R-HSA-164528 RNase H-mediated cleavage of the template strand
R-HSA-164505 Synthesis of full-length duplex viral DNA with a discontinuous plus strand
R-HSA-164512 Second strand transfer by annealing complementary PBS sequences
R-HSA-164527 Annealing of 3'-end of unwound transfer RNA primer with genomic RNA
R-HSA-173769 RNase H-mediated digestion of tRNA, 3'PPT and cPPT RNA primers
R-HSA-8951690 Formation of RTC with integration competent viral DNA:BANF1:HMGA1:PSIP1
R-HSA-182876 Removal of plus-strand flap and gap closure complete synthesis of linear duplex viral DNA
R-HSA-482775 Release of (inferred) platelet cytosolic components
R-HSA-164521 Insertion of gp41 fusion peptide into the target membrane
R-HSA-164515 Fusogenic activation of gp41
R-HSA-164507 CD4:gp120 binds to chemokine co-receptor CCR5/CXCR4
R-HSA-164510 Conformational change in gp120 of Env oligomer
R-HSA-164508 N and C terminal heptad repeat helices of gp41 form six-helix bundle
R-HSA-164509 Binding of gp120 of ENV oligomer to the host CD4
R-HSA-164500 Conformational changes in gp120 exposes gp41
R-HSA-3139027 Maturation of HIV Virion
R-HSA-6800434 Exocytosis of ficolin-rich granule lumen proteins
R-HSA-6798748 Exocytosis of secretory granule lumen proteins
R-HSA-180632 Deamination of C residues during synthesis of HIV-1 reverse transcript minus-strand
R-HSA-175474 Assembly Of The HIV Virion
R-HSA-162592 Integration of provirus
R-HSA-210991 Basigin interactions
R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation
R-HSA-162594 Early Phase of HIV Life Cycle
R-HSA-162585 Uncoating of the HIV Virion
R-HSA-173107 Binding and entry of HIV virion
R-HSA-164525 Plus-strand DNA synthesis
R-HSA-164516 Minus-strand DNA synthesis
R-HSA-180689 APOBEC3G mediated resistance to HIV-1 infection
R-HSA-162588 Budding and maturation of HIV virion
R-HSA-114608 Platelet degranulation
R-HSA-162599 Late Phase of HIV Life Cycle
R-HSA-6798695 Neutrophil degranulation
R-HSA-202733 Cell surface interactions at the vascular wall
R-HSA-9020591 Interleukin-12 signaling
R-HSA-162587 HIV Life Cycle
R-HSA-162589 Reverse Transcription of HIV RNA
R-HSA-162909 Host Interactions of HIV factors
R-HSA-76005 Response to elevated platelet cytosolic Ca2+
R-HSA-168249 Innate Immune System
R-HSA-109582 Hemostasis
R-HSA-447115 Interleukin-12 family signaling
R-HSA-162906 HIV Infection
R-HSA-76002 Platelet activation, signaling and aggregation
R-HSA-168256 Immune System
R-HSA-449147 Signaling by Interleukins
R-HSA-5663205 Infectious disease
R-HSA-1280215 Cytokine Signaling in Immune system
R-HSA-1643685 Disease

-  Other Names for This Gene
  Alternate Gene Symbols: A8K220, CYPA, NM_021130, NP_066953, P05092, P62937, PPIA_HUMAN, Q3KQW3, Q6IBU5, Q96IX3, Q9BRU4, Q9BTY9, Q9UC61
UCSC ID: uc003tlw.3
RefSeq Accession: NM_021130
Protein: P62937 (aka PPIA_HUMAN)
CCDS: CCDS5494.1

-  Gene Model Information
category: coding nonsense-mediated-decay: no RNA accession: NM_021130.3
exon count: 5CDS single in 3' UTR: no RNA size: 2276
ORF size: 498CDS single in intron: no Alignment % ID: 100.00
txCdsPredict score: 1196.00frame shift in genome: no % Coverage: 100.00
has start codon: yes stop codon in genome: no # of Alignments: 1
has end codon: yes retained intron: no # AT/AC introns 0
selenocysteine: no end bleed into intron: 0# strange splices: 0
Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.