PPIA peptidylprolyl isomerase A [Homo sapiens (human)] - Gene

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; AllianceGenome:HGNC:9253
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: mouse all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: 7p13

Exon count:: 7

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	7	NC_000007.14 (44796681..44803117)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	7	NC_060931.1 (44957232..44963670)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	7	NC_000007.13 (44836280..44842716)

Chromosome 7 - NC_000007.14 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help

See details

Project title: HPA RNA-seq normal tissues 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

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Peptidylprolyl isomerase A guides SENP5/GAU1 DNA-lncRNA triplex generation for driving tumorigenesis.
Title: Peptidylprolyl isomerase A guides SENP5/GAU1 DNA-lncRNA triplex generation for driving tumorigenesis.
PPIA dictates NRF2 stability to promote lung cancer progression.
Title: PPIA dictates NRF2 stability to promote lung cancer progression.
Secreted cyclophilin A is non-genotoxic but acts as a tumor promoter.
Title: Secreted cyclophilin A is non-genotoxic but acts as a tumor promoter.
Emerging role of cyclophilin A in HIV-1 infection: from producer cell to the target cell nucleus.
Title: Emerging role of cyclophilin A in HIV-1 infection: from producer cell to the target cell nucleus.
Bioinformatics analysis and experimental validation of tumorigenic role of PPIA in gastric cancer.
Title: Bioinformatics analysis and experimental validation of tumorigenic role of PPIA in gastric cancer.
New Insights into Dyskerin-CypA Interaction: Implications for X-Linked Dyskeratosis Congenita and Beyond.
Title: New Insights into Dyskerin-CypA Interaction: Implications for X-Linked Dyskeratosis Congenita and Beyond.
TRIM5alpha restricts poxviruses and is antagonized by CypA and the viral protein C6.
Title: TRIM5α restricts poxviruses and is antagonized by CypA and the viral protein C6.
A Tripartite Complex HIV-1 Tat-Cyclophilin A-Capsid Protein Enables Tat Encapsidation That Is Required for HIV-1 Infectivity.
Title: A Tripartite Complex HIV-1 Tat-Cyclophilin A-Capsid Protein Enables Tat Encapsidation That Is Required for HIV-1 Infectivity.
Cyclophilin A accelerates SiO2-induced macrophage foaming.
Title: Cyclophilin A accelerates SiO(2)-induced macrophage foaming.
Cyclophilin A associates with and regulates the activity of ZAP70 in TCR/CD3-stimulated T cells.
Title: Cyclophilin A associates with and regulates the activity of ZAP70 in TCR/CD3-stimulated T cells.

Submit: New GeneRIF Correction See all GeneRIFs (212)

Phenotypes

Go to the top of the page Help

Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

Go to the top of the page Help

See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

Go to the top of the page Help

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

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Markers

SHGC-56052 (e-PCR)
- UniSTS:24938

Ppi-rs (e-PCR), detects polymorphism
- UniSTS:144251

PMC112625P1 (e-PCR)
- UniSTS:270235

PPIA (e-PCR)
- UniSTS:70044

G20876 (e-PCR)
- UniSTS:56252

A006J31 (e-PCR)
- UniSTS:56253

PMC262691P6 (e-PCR)
- UniSTS:272328

PMC307696P1 (e-PCR)
- UniSTS:272588

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables RNA binding	HDA more info	PubMed
enables cyclosporin A binding	IBA Inferred from Biological aspect of Ancestor more info
enables heparan sulfate binding	IDA Inferred from Direct Assay more info	PubMed
enables integrin binding	ISS Inferred from Sequence or Structural Similarity more info
enables peptidyl-prolyl cis-trans isomerase activity	IBA Inferred from Biological aspect of Ancestor more info
enables peptidyl-prolyl cis-trans isomerase activity	IDA Inferred from Direct Assay more info	PubMed
enables peptidyl-prolyl cis-trans isomerase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables unfolded protein binding	TAS Traceable Author Statement more info	PubMed
enables virion binding	NAS Non-traceable Author Statement more info	PubMed

Process	Evidence Code	Pubs
involved_in activation of protein kinase B activity	IDA Inferred from Direct Assay more info	PubMed
involved_in apoptotic process	IDA Inferred from Direct Assay more info	PubMed
involved_in apoptotic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cell adhesion molecule production	IDA Inferred from Direct Assay more info	PubMed
involved_in cellular response to oxidative stress	IDA Inferred from Direct Assay more info	PubMed
involved_in endothelial cell activation	IDA Inferred from Direct Assay more info	PubMed
involved_in leukocyte chemotaxis	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in lipid droplet organization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of protein K48-linked ubiquitination	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of protein kinase activity	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of protein phosphorylation	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of stress-activated MAPK cascade	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of viral life cycle	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in neuron differentiation	IEA Inferred from Electronic Annotation more info
involved_in neutrophil chemotaxis	IDA Inferred from Direct Assay more info	PubMed
involved_in platelet activation	ISS Inferred from Sequence or Structural Similarity more info
involved_in platelet aggregation	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of MAPK cascade	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of NF-kappaB transcription factor activity	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of protein phosphorylation	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of protein secretion	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of viral genome replication	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	TAS Traceable Author Statement more info	PubMed
involved_in protein peptidyl-prolyl isomerization	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of apoptotic signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of viral genome replication	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of viral genome replication	TAS Traceable Author Statement more info	PubMed
involved_in viral release from host cell	TAS Traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	HDA more info	PubMed
located_in cytosol	TAS Traceable Author Statement more info
located_in extracellular exosome	HDA more info	PubMed
located_in extracellular exosome	TAS Traceable Author Statement more info
located_in extracellular region	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular region	TAS Traceable Author Statement more info
located_in extracellular space	HDA more info	PubMed
located_in ficolin-1-rich granule lumen	TAS Traceable Author Statement more info
located_in focal adhesion	HDA more info	PubMed
located_in membrane	HDA more info	PubMed
located_in nucleus	HDA more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
part_of protein-containing complex	IDA Inferred from Direct Assay more info	PubMed
located_in secretory granule lumen	TAS Traceable Author Statement more info
located_in vesicle	HDA more info	PubMed

General protein information

Go to the top of the page Help

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

EC 5.2.1.8

NP_066953.1

EC 5.2.1.8

XP_047276492.1

EC 5.2.1.8

XP_047276493.1

EC 5.2.1.8

XP_054214491.1

EC 5.2.1.8

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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

NG_029697.1 RefSeqGene

Range

5040..11476

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001300981.2 → NP_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

Consensus CDS

CCDS75592.1

UniProtKB/Swiss-Prot

P62937

Related

ENSP00000427976.1, ENST00000489459.5

Conserved Domains (1) summary

cl00197
Location:1 → 102

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 immunosuppressive drug ...
NM_021130.5 → NP_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

A8K220, P05092, P62937, Q3KQW3, Q567Q0, Q6IBU5, Q96IX3, Q9BRU4, Q9BTY9, Q9UC61

UniProtKB/TrEMBL

A8K486, B2RE56, V9HWF5

Related

ENSP00000419425.1, ENST00000468812.6

Conserved Domains (1) summary

cd01926
Location:4 → 162

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 accelerates protein folding ...

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

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

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000007.14 Reference GRCh38.p14 Primary Assembly

Range

44796681..44803117

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_047420536.1 → XP_047276492.1 peptidyl-prolyl cis-trans isomerase A isoform X1

Related

ENSP00000504216.1, ENST00000677022.1
XM_047420537.1 → XP_047276493.1 peptidyl-prolyl cis-trans isomerase A isoform X1

Related

ENSP00000503804.1, ENST00000678789.1

Alternate T2T-CHM13v2.0

Genomic

NC_060931.1 Alternate T2T-CHM13v2.0

Range

44957232..44963670

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_054358516.1 → XP_054214491.1 peptidyl-prolyl cis-trans isomerase A isoform X1

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

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.
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.