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PPIA peptidylprolyl isomerase A [ Homo sapiens (human) ]

Gene ID: 5478, updated on 15-Apr-2019

Summary

Official Symbol
PPIAprovided by HGNC
Official Full Name
peptidylprolyl isomerase Aprovided by HGNC
Primary source
HGNC:HGNC:9253
See related
Ensembl:ENSG00000196262 MIM:123840
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
CYPA; CYPH; HEL-S-69p
Summary
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]
Expression
Ubiquitous expression in lymph node (RPKM 161.2), colon (RPKM 155.9) and 25 other tissues See more
Orthologs

Genomic context

See PPIA in Genome Data Viewer
Location:
7p13
Exon count:
5
Annotation release Status Assembly Chr Location
109 current GRCh38.p12 (GCF_000001405.38) 7 NC_000007.14 (44795960..44803123)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 7 NC_000007.13 (44836241..44842716)

Chromosome 7 - NC_000007.14Genomic Context describing neighboring genes Neighboring gene oxoglutarate dehydrogenase Neighboring gene OGDH intron CAGE-defined high expression enhancer Neighboring gene zinc finger MIZ-type containing 2 Neighboring gene uncharacterized LOC105375259 Neighboring gene uncharacterized LOC105375260 Neighboring gene H2A histone family member V

Genomic regions, transcripts, and products

Expression

  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

HIV-1 interactions

Replication interactions

Interaction Pubs
HIV-1 replication requires PPIA (CypA) as shown through cyclosporine (CsA) treatment and siRNA mediated knockdown PubMed

Protein interactions

Protein Gene Interaction Pubs
Envelope surface glycoprotein gp120 env The interaction between exposed cyclophilin A (CypA) and cell surface heparans represents the initial step of HIV-1 attachment and is a necessary step for HIV-1 gp120 binding to CD4 PubMed
env Macrophage- and T-cell-tropic V3 loop peptides of HIV-1 gp120 bind specifically to the active site of the immunophilins FK506-binding protein (FKBP12), and cyclophilins A and B, and inhibit their peptidyl-prolyl cis-trans isomerase (PPIase) activities PubMed
Nef nef HIV-1 Nef downregulates the expression of cyclophilin A protein in Nef-transfected SupT1 cells PubMed
nef Cyclophilin A has been demonstrated to bind to HIV-1 Nef using a biochemical binding assay, however the biological significance of this interaction is currently not known PubMed
Pr55(Gag) gag Treatment of cells with cyclosporine A blocks the interaction of HIV-1 Gag with eEF2, indicating that cyclophilin A (CypA) stabilizes the Gag-eEF2 association PubMed
gag Targeting of the catalytic HECT domain (residues 598-952) of NEDD4-2s to HIV-1 Gag via CypA is sufficient to rescue HIV-1 budding defects PubMed
gag H219Q and H219P substitutions in the viral CypA binding loop of HIV-1 Gag reduces CypA incorporation into HIV-1 and potentiates viral replication in CypA-rich MT-2 and H9 cells PubMed
gag A fusion protein CypA-Nef consisting of cyclophilin A (CypA) linked to the amino terminus of Nef enhances the infectivity of Nef-defective HIV-1 particles and is incorporated into virions via association with Gag during particle assembly PubMed
gag Binding of HIV-1 Gag to cyclophilin A requires a region within the nucleocapsid domain of Gag which is important for Gag self-association PubMed
gag Cyclophilin A modulates processing of HIV-1 Gag by the viral protease PubMed
Vif vif Vif has been demonstrated to bind to cyclophilin A using a biochemical binding assay PubMed
Vpr vpr The complete C-terminal peptide Vpr75-90, comprising the 16 residues 75GCRHSRIGVTRQRRAR90, is required for maintaining the strong interaction with CypA in a 1:1 binding model. Replacement of R80 with alanine significantly reduces the binding affinity PubMed
vpr Cyclophilin A catalyzes the prolyl cis/trans interconversion of proline residues at positions 5, 10, 14, and 35 in HIV-1 Vpr PubMed
vpr Cyclophilin A interacts directly with HIV-1 Vpr to mediate the cis/trans-proline isomerization of Vpr, which is important for Vpr synthesis and function PubMed
capsid gag HIV-1 HXB2 CA binds PPIA (CypA) and increasing amounts of PPIA can destabilize CA assembly PubMed
gag HIV-1 CA binds PPIA (CypA); the crystal structure has been solved PubMed
gag HIV-1 CA binds PPIA; binding is dependent upon residues W23, A77, and L189 in CA PubMed
gag HIV-1 CA binds PPIA PubMed
gag Binding of HIV-1 Capsid to cyclophilin A requires HIV-1 Gag dimerization PubMed
gag The interaction of HIV-1 Capsid to cyclophilin A can be inhibited by cyclosporin A leading to inhibition of virus replication PubMed
gag HIV-1 Capsid and Gag proteins bind to cyclophilin A, resulting in the incorporation of cyclophilin A into virions, which is important for the completion of early steps in HIV-1 replication following entry of the virus into cells PubMed
gag Viral particles containing the CA mutations, H87Q, A88P and I91V (located in the PPIA- binding site), encapsidate 30% less PPIA (CypA) into virions relative to viral particles conatining wild type CA PubMed
gag CA mutations (H87Q, A88P and I91V) in the PPIA (CypA) binding site reduce PPIA (CypA) affinity for CA BUT do not prevent PPIA (CypA) from binding to CA in a CA/NC biochemical based assay PubMed
gag HIV-1 N74D CA mutant has less binding affinity to CypA and less HIV-1 infectivity than wild type PubMed
gag V86M capsid mutant, a single amino acid change in the cyclophilin-binding loop of the HIV-1 capsid protein, can replicate in cells expressing TRIM5alpha(rh). This involves decreased binding to TRIM5alpha(rh) and retention of binding to cyclophilin A PubMed
gag Substitution of Thr for Ala at position 105 of CA (A105T) rescues the impaired single-cycle infectivity of T54A and A92E mutants, indicating that CA determinants outside the CypA-binding loop can modulate the dependence of HIV-1 infection on CypA PubMed
gag The enhancement of infection of A92E and G94D HIV-1 Capsid mutants by CypA is a result of enhanced reverse transcription in HeLa-P4 cells PubMed
gag Proline-90 and Glycine-89 of HIV-1 Capsid are required for the binding of cyclophilin A to Capsid PubMed
gag HIV-1 CA mutants N74D and P90A fail to bind to CPSF6 and cyclophilins (Nup358 and CypA), respectively, and trigger innate sensors, leading to nuclear translocation of NFkappaB and IRF3, production of type 1 IFN and induction of an antiviral state PubMed
gag Cyclophilin A inhibits HIV-1 nuclear entry by promoting HIV-1 CA core stability PubMed
gag The effect of inhibition of CA-CypA interaction by TRIM5alpha is virus isolate-dependent, which can result in inhibition, no change, or an increase in viral infectivity PubMed
gag Cyclophilin A stabilizes the HIV-1 CA and antagonizes TNPO3 acceleration of uncoating in vitro PubMed
gag Inhibition of the HIV-1 CA-CypA interaction rescues the infectivity of CA-N121K HIV-1. The N121K mutant is inhibited by CypA in HIV-1 infected cells PubMed
gag Cyclophilin A mutants, R55K, R55A, F113W, and H126A, exhibit the most pronounced decrease in PPIase activity compared to wild type. These mutants bind to HIV-1 CA with low affinity PubMed
gag A small molecule HIV-1 inhibitor PF74 destabilizes the viral capsid in vitro and its antiviral activity is promoted by binding of the host protein cyclophilin A to the HIV-1 capsid PubMed
gag Cyclophilin A decreases the stability of the in vitro-assembled HIV-1 CA-NC complexes in the presence of cellular cytosolic extracts PubMed
gag Delaying reverse transcription leads to a time-dependent loss in viral infectivity that is increased by inhibiting capsid-cyclophilin A interactions, but does not result in increased viral sensitivity to hTRIM5alpha PubMed
gag CypA-CA interactions dictate the use of a NUP358/NUP153 dependent nuclear entry pathway PubMed
gag Cyclophilin A is acetylated at amino acid residue Lys125 in human cells. Acetylated cyclophilin A inhibits its catalysis, inhibits cyclosporine binding, and alters HIV-1 capsid interaction PubMed
gag TRIM5 alpha-mediated resistance to HIV-1 in Old World monkey cells is modulated by the HIV-1 Capsid and cyclophilin A interaction PubMed
gag The interaction between cyclophilin A and HIV-1 CA is required for the enhanced restriction of HIV-1 due to rhTRIM5alpha in non-dividing cells PubMed
gag Alignment of primate lentiviral capsid protein sequences demonstrates that they have conserved the proline rich cyclophilin A binding loop on their outer surface PubMed
gag Reducing the binding of CypA to the A92E mutant capsid, either by cyclosporine treatment or by an additional P90A change in the CA protein, increases the amount of particulate capsids and viral infectivity in HeLa cells PubMed
gag H219Q and H219P substitutions in the cyclophilin A binding loop of HIV-1 CA enhance HIV-1 replication by reducing viral cyclophilin A content in resulting virions as produced in cyclophilin A-rich cells PubMed
gag HIV-1 CA R264K mutant is impaired in generating late reverse transcription products, is inhibited by the presence of normal levels of cyclophilin A, and is rescued with the development of a rare secondary mutation S173A PubMed
gag Increasing CypA levels in permissive TE671 cells restrict HIV-1 CA mutants A92E and G94D in a CypA-dependent way PubMed
gag Cyclophilin A binding to HIV-1 Capsid modulates the sensitivity of HIV-1 to host restriction factors PubMed
gag Cyclophilin A decreases the degree of capsid protein processing by the HIV-1 protease PubMed
gag The HIV-1 p2 peptide (spacer peptide in the HIV-1 Gag polyprotein between Capsid and Nucleocapsid; SP1) is involved in the interaction between HIV-1 Capsid and cyclophilin A PubMed
gag Cyclophilin A catalyzes efficiently the cis/trans isomerization of the Gly-89-Pro-90 peptide bond of HIV-1 Capsid PubMed
gag Cyclophilin A has a higher affinity for HIV-1 Gag than for the mature HIV-1 Capsid protein, as a result of additional interactions with the 12 C-terminal amino acids of HIV-1 Matrix PubMed
gag The active site hydrophobic binding pocket of cyclophilin A (amino acids 54-126) binds to the N-Terminal and central portion of HIV-1 Capsid, most importantly to Capsid amino acids 85-93 PubMed
integrase gag-pol Compared to the HIV-1 IN wild type, two IN mutants (DeltaIN and C130S) have reduced levels of the cytoplasmic CA, suggesting accelerated uncoating. Virus derived from the IN mutants incorporates decreased levels of cyclophilin A (CypA) PubMed
matrix gag The 12 carboxy-terminal amino acids of HIV-1 Matrix (p17; amino acids 121-132) are important for optimal binding of cyclophilin to HIV-1 Gag and Capsid (p24) PubMed
gag Cyclophilin A binds to HIV-1 Matrix PubMed
nucleocapsid gag Cyclophilin A decreases the stability of the in vitro-assembled HIV-1 CA-NC complexes in the presence of cellular cytosolic extracts PubMed
gag Binding of HIV-1 Gag to cyclophilin A requires a region within the nucleocapsid domain of Gag which is important for Gag self-association PubMed
p6 gag HIV-1 p6 binds to cyclophilin A, particularly, through the p6 proline residues, located at positions 5, 7, 10, 11, 24, 30, 37 and 49 PubMed
retropepsin gag-pol Positional proteomics analysis identifies the cleavage of human peptidylprolyl isomerase A (PPIA; cyclophilin A) at amino acid residues 6-9 and 23-24 by the HIV-1 protease PubMed
reverse transcriptase gag-pol The enhancement of infection of A92E and G94D HIV-1 Capsid mutants by CypA is a result of enhanced reverse transcription in HeLa-P4 cells PubMed

Go to the HIV-1, Human Interaction Database

Pathways from BioSystems

  • APOBEC3G mediated resistance to HIV-1 infection, organism-specific biosystem (from REACTOME)
    APOBEC3G mediated resistance to HIV-1 infection, organism-specific biosystemRepresentatives of the apolipoprotein B mRNA editing enzyme catalytic polypeptide 3 (APOBEC3) family provide innate resistance to exogeneous and endogenous retroviruses (see Cullen 2006 for a recent ...
  • Assembly Of The HIV Virion, organism-specific biosystem (from REACTOME)
    Assembly Of The HIV Virion, organism-specific biosystemVirion assembly packages all the components required for infectivity. These steps include two copies of the positive sense genomic viral RNA, cellular tRNALys, the viral envelope (Env) protein, the G...
  • Basigin interactions, organism-specific biosystem (from REACTOME)
    Basigin interactions, organism-specific biosystemBasigin is a widely expressed transmembrane glycoprotein that belongs to the Ig superfamily and is highly enriched on the surface of epithelial cells. Basigin is involved in intercellular interaction...
  • Binding and entry of HIV virion, organism-specific biosystem (from REACTOME)
    Binding and entry of HIV virion, organism-specific biosystemHIV enters cells by fusion at the cell surface, that results in a productive infection. The envelope (Env) protein of HIV mediates entry. Env is composed of a surface subunit, gp120, and a transmemb...
  • Budding and maturation of HIV virion, organism-specific biosystem (from REACTOME)
    Budding and maturation of HIV virion, organism-specific biosystemWith the virus components precariously assembled on the inner leaflet of the plasma membrane, the host cell machinery is required for viral budding. The virus takes advantage of the host ESCRT pathwa...
  • Cell surface interactions at the vascular wall, organism-specific biosystem (from REACTOME)
    Cell surface interactions at the vascular wall, organism-specific biosystemLeukocyte extravasation is a rigorously controlled process that guides white cell movement from the vascular lumen to sites of tissue inflammation. The powerful adhesive interactions that are require...
  • Disease, organism-specific biosystem (from REACTOME)
    Disease, organism-specific biosystemBiological processes are captured in Reactome by identifying the molecules (DNA, RNA, protein, small molecules) involved in them and describing the details of their interactions. From this molecular ...
  • Early Phase of HIV Life Cycle, organism-specific biosystem (from REACTOME)
    Early Phase of HIV Life Cycle, organism-specific biosystemIn the early phase of HIV lifecycle, an active virion binds and enters a target cell mainly by specific interactions of the viral envelope proteins with host cell surface receptors. The virion core...
  • HIV Infection, organism-specific biosystem (from REACTOME)
    HIV Infection, organism-specific biosystemThe global pandemic of Human Immunodeficiency Virus (HIV) infection has resulted in tens of millions of people infected by the virus and millions more affected. UNAIDS estimates around 40 million ...
  • HIV Life Cycle, organism-specific biosystem (from REACTOME)
    HIV Life Cycle, organism-specific biosystemThe life cycle of HIV-1 is divided into early and late phases, shown schematically in the figure. In the early phase, an HIV-1 virion binds to receptors and co-receptors on the human host cell surfac...
  • Hemostasis, organism-specific biosystem (from REACTOME)
    Hemostasis, organism-specific biosystemHemostasis is a physiological response that culminates in the arrest of bleeding from an injured vessel. Under normal conditions the vascular endothelium supports vasodilation, inhibits platelet adhe...
  • Host Interactions of HIV factors, organism-specific biosystem (from REACTOME)
    Host Interactions of HIV factors, organism-specific biosystemLike all viruses, HIV-1 must co-opt the host cell macromolecular transport and processing machinery. HIV-1 Vpr and Rev proteins play key roles in this co-optation. Efficient HIV-1 replication likewis...
  • Immune System, organism-specific biosystem (from REACTOME)
    Immune System, organism-specific biosystemHumans are exposed to millions of potential pathogens daily, through contact, ingestion, and inhalation. Our ability to avoid infection depends on the adaptive immune system and during the first crit...
  • Infectious disease, organism-specific biosystem (from REACTOME)
    Infectious disease, organism-specific biosystem
    Infectious disease
  • Innate Immune System, organism-specific biosystem (from REACTOME)
    Innate Immune System, organism-specific biosystemInnate immunity encompases the nonspecific part of immunity tha are part of an individual's natural biologic makeup
  • Integration of provirus, organism-specific biosystem (from REACTOME)
    Integration of provirus, organism-specific biosystemFor retroviral DNA to direct production of progeny virions it must become covalently integrated into the host cell chromosome (reviewed in Coffin et al. 1997; Hansen et al. 1998). Analyses of mutants...
  • Late Phase of HIV Life Cycle, organism-specific biosystem (from REACTOME)
    Late Phase of HIV Life Cycle, organism-specific biosystemThe late phase of the HIV-1 life cycle includes the regulated expression of the HIV gene products and the assembly of viral particles. The assembly of viral particles will be covered in a later relea...
  • Minus-strand DNA synthesis, organism-specific biosystem (from REACTOME)
    Minus-strand DNA synthesis, organism-specific biosystemIn the first part of reverse transcription, minus-strand synthesis, a DNA strand complementary to the HIV genomic RNA is synthesized, using the viral RNA as a template and a host cell lysine tRNA mol...
  • Neutrophil degranulation, organism-specific biosystem (from REACTOME)
    Neutrophil degranulation, organism-specific biosystemNeutrophils are the most abundant leukocytes (white blood cells), indispensable in defending the body against invading microorganisms. In response to infection, neutrophils leave the circulation and ...
  • Platelet activation, signaling and aggregation, organism-specific biosystem (from REACTOME)
    Platelet activation, signaling and aggregation, organism-specific biosystemPlatelet activation begins with the initial binding of adhesive ligands and of the excitatory platelet agonists (released or generated at the sites of vascular trauma) to cognate receptors on the pla...
  • Platelet degranulation, organism-specific biosystem (from REACTOME)
    Platelet degranulation, organism-specific biosystemPlatelets function as exocytotic cells, secreting a plethora of effector molecules at sites of vascular injury. Platelets contain a number of distinguishable storage granules including alpha granules...
  • Plus-strand DNA synthesis, organism-specific biosystem (from REACTOME)
    Plus-strand DNA synthesis, organism-specific biosystemTwo specific polypurine tracts (PPT sequences) in the viral RNA, one within the pol gene (central or cPPT) and one immediately preceding the U3 sequence (3' PPT), are spared from degradation during m...
  • Prolactin Signaling Pathway, organism-specific biosystem (from WikiPathways)
    Prolactin Signaling Pathway, organism-specific biosystemProlactin (PRL), a pleiotropic polypeptide hormone, mostly secreted by the lactotrophic cells of anterior pituitary gland and to a lesser extent expressed in numerous extra pituitary tissues such as ...
  • Response to elevated platelet cytosolic Ca2+, organism-specific biosystem (from REACTOME)
    Response to elevated platelet cytosolic Ca2+, organism-specific biosystemActivation of phospholipase C enzymes results in the generation of second messengers of the phosphatidylinositol pathway. The events resulting from this pathway are a rise in intracellular calcium an...
  • Reverse Transcription of HIV RNA, organism-specific biosystem (from REACTOME)
    Reverse Transcription of HIV RNA, organism-specific biosystemThe RNA genome of HIV-1, like that of other retroviruses, is reverse-transcribed (Baltimore 1970; Temin and Mizutani 1970) into double-stranded DNA, which is then integrated into a host cell chromoso...
  • Uncoating of the HIV Virion, organism-specific biosystem (from REACTOME)
    Uncoating of the HIV Virion, organism-specific biosystemHIV-1 uncoating is a poorly understood process. It likely involves a progressive and partial dissembly of matrix and capsid layers. While viral proteins like MA and Nef are thought to be involved, t...

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Clone Names

  • MGC12404, MGC23397, MGC117158

Gene Ontology Provided by GOA

Function Evidence Code Pubs
RNA binding HDA PubMed 
cyclosporin A binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
cyclosporin A binding IDA
Inferred from Direct Assay
more info
PubMed 
peptidyl-prolyl cis-trans isomerase activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
peptidyl-prolyl cis-trans isomerase activity IDA
Inferred from Direct Assay
more info
PubMed 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
unfolded protein binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
unfolded protein binding TAS
Traceable Author Statement
more info
PubMed 
virion binding NAS
Non-traceable Author Statement
more info
PubMed 
Process Evidence Code Pubs
RNA-dependent DNA biosynthetic process TAS
Traceable Author Statement
more info
 
entry into host cell TAS
Traceable Author Statement
more info
 
establishment of integrated proviral latency TAS
Traceable Author Statement
more info
 
fusion of virus membrane with host plasma membrane TAS
Traceable Author Statement
more info
 
interleukin-12-mediated signaling pathway TAS
Traceable Author Statement
more info
 
leukocyte migration TAS
Traceable Author Statement
more info
 
lipid droplet organization IMP
Inferred from Mutant Phenotype
more info
PubMed 
neutrophil degranulation TAS
Traceable Author Statement
more info
 
positive regulation of protein secretion IMP
Inferred from Mutant Phenotype
more info
PubMed 
positive regulation of viral genome replication IMP
Inferred from Mutant Phenotype
more info
PubMed 
protein folding TAS
Traceable Author Statement
more info
PubMed 
protein peptidyl-prolyl isomerization IDA
Inferred from Direct Assay
more info
PubMed 
protein refolding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
regulation of viral genome replication IMP
Inferred from Mutant Phenotype
more info
PubMed 
regulation of viral genome replication TAS
Traceable Author Statement
more info
PubMed 
uncoating of virus TAS
Traceable Author Statement
more info
 
viral life cycle TAS
Traceable Author Statement
more info
 
viral release from host cell TAS
Traceable Author Statement
more info
PubMed 
virion assembly TAS
Traceable Author Statement
more info
 

General protein information

Preferred Names
peptidyl-prolyl cis-trans isomerase A
Names
PPIase A
T cell cyclophilin
cyclosporin A-binding protein
epididymis secretory sperm binding protein Li 69p
peptidylprolyl isomerase A (cyclophilin A)
rotamase A
NP_001287910.1
NP_066953.1
XP_024302576.1
XP_024302577.1

NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

  1. NG_029697.1 RefSeqGene

    Range
    4995..11482
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001300981.1NP_001287910.1  peptidyl-prolyl cis-trans isomerase A isoform 2

    See identical proteins and their annotated locations for NP_001287910.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) differs in its 5' UTR and uses a downstream start codon, compared to variant 1. The encoded isoform (2) has a shorter N-terminus, compared to isoform 1.
    Source sequence(s)
    AC013436, AK293003, BC137057
    Consensus CDS
    CCDS75592.1
    UniProtKB/Swiss-Prot
    P62937
    Related
    ENSP00000427976.1, ENST00000489459.5
    Conserved Domains (1) summary
    cl00197
    Location:1102
    cyclophilin; cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the ...
  2. NM_021130.5NP_066953.1  peptidyl-prolyl cis-trans isomerase A isoform 1

    See identical proteins and their annotated locations for NP_066953.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) represents the shorter transcript but encodes the longer isoform (1).
    Source sequence(s)
    AC013436, BC137057
    Consensus CDS
    CCDS5494.1
    UniProtKB/Swiss-Prot
    P62937
    UniProtKB/TrEMBL
    V9HWF5
    Related
    ENSP00000419425.1, ENST00000468812.6
    Conserved Domains (1) summary
    cd01926
    Location:4162
    cyclophilin_ABH_like; cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which ...

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 109

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p12 Primary Assembly

Genomic

  1. NC_000007.14 Reference GRCh38.p12 Primary Assembly

    Range
    44795960..44803123
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_024446809.1XP_024302577.1  peptidyl-prolyl cis-trans isomerase A isoform X2

    Related
    ENSP00000430817.1, ENST00000355968.10
    Conserved Domains (1) summary
    cl00197
    Location:1102
    cyclophilin; cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the ...
  2. XM_024446808.1XP_024302576.1  peptidyl-prolyl cis-trans isomerase A isoform X1

RNA

  1. XR_002956460.1 RNA Sequence

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

  1. NM_203430.1: Suppressed sequence

    Description
    NM_203430.1: This RefSeq was permanently suppressed because it uses an internal initiation methionine, which when corrected results in a nonsense-mediated mRNA decay (NMD) candidate.
  2. NM_203431.1: Suppressed sequence

    Description
    NM_203431.1: This RefSeq was permanently suppressed because it uses an internal initiation methionine, which when corrected results in a nonsense-mediated mRNA decay (NMD) candidate.
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