PPIE peptidylprolyl isomerase E [Homo sapiens (human)] - Gene

Summary

Official Symbol: PPIEprovided by HGNC
Official Full Name: peptidylprolyl isomerase Eprovided by HGNC
Primary source: HGNC:HGNC:9258
See related: Ensembl:ENSG00000084072 MIM:602435; AllianceGenome:HGNC:9258
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: CypE; CYP33; CYP-33
Summary: The protein encoded by this gene is 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. This protein contains a highly conserved cyclophilin (CYP) domain as well as an RNA-binding domain. It was shown to possess PPIase and protein folding activities, and it also exhibits RNA-binding activity. Alternative splicing results in multiple transcript variants. A related pseudogene, which is also located on chromosome 1, has been identified. [provided by RefSeq, Aug 2010]
Expression: Ubiquitous expression in thyroid (RPKM 9.0), testis (RPKM 7.1) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 1p34.2

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	1	NC_000001.11 (39738882..39763914)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	1	NC_060925.1 (39608324..39633355)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	1	NC_000001.10 (40204554..40229586)

Chromosome 1 - NC_000001.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

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

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

RNA binding induces an allosteric switch in Cyp33 to repress MLL1-mediated transcription.
Title: RNA binding induces an allosteric switch in Cyp33 to repress MLL1-mediated transcription.
Cyp33 binds AU-rich RNA motifs via an extended interface that competitively disrupts the gene repressive Cyp33-MLL1 interaction in vitro.
Title: Cyp33 binds AU-rich RNA motifs via an extended interface that competitively disrupts the gene repressive Cyp33-MLL1 interaction in vitro.
Study of datasets analyzing the gene expression profiles and DNA methylation data of gestational Diabetes Mellitus (GDM) and confirmed through real time PCR in placenta tissue of three GDM samples and three normal samples identified Oas1, Ppie, Polr2g as possible pathogenic target genes of GDM by combining protein-protein interaction analysis.
Title: Comprehensive Analysis of Gene Expression Profiles and DNA Methylome reveals Oas1, Ppie, Polr2g as Pathogenic Target Genes of Gestational Diabetes Mellitus.
CypE is a host restriction factor that inhibits the functions of nucleoprotein, as well as viral replication and transcription, by impairing the formation of the viral ribonucleoprotein complex.
Title: Cyclophilin E functions as a negative regulator to influenza virus replication by impairing the formation of the viral ribonucleoprotein complex.
Observational study and genome-wide association study of gene-disease association. (HuGE Navigator)
Title: Use of genome-wide expression data to mine the "Gray Zone" of GWA studies leads to novel candidate obesity genes.
binding of H3K4me3 to PHD3 domain of MLL and binding of the CYP33 RRM domain to PHD3 are mutually inhibitory, implying that PHD3 is a molecular switch for the transition between activation and repression of target genes
Title: The PHD3 domain of MLL acts as a CYP33-regulated switch between MLL-mediated activation and repression .
PPIase domain of CyP33 regulates the conformation of MLL1 through proline isomerization within the PHD3-Bromo linker, thereby disrupting the PHD3-Bromo interface and facilitating binding of the MLL1-PHD3 domain to the CyP33-RRM domain.
Title: Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression.
Data provide insight into the multiple functions of Cyp33 RRM and suggest a Cyp33-dependent mechanism for regulating the transcriptional activity of MLL.
Title: Molecular mechanism of MLL PHD3 and RNA recognition by the Cyp33 RRM domain.
The results show that hCyP33 binds specifically to mRNA, namely poly(A)(+)RNA, and that binding stimulates the PPIase activity of hCyP33.
Title: Human CyP33 binds specifically to mRNA and binding stimulates PPIase activity of hCyP33.

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Phenotypes

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Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
capsid	gag	The interaction of HIV-1 CA with human cellular peptidylprolyl isomerase E protein (PPIE, cyclophilin E) is identified by yeast two-hybrid screen	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D1S3422 (e-PCR)
- UniSTS:63836

G38154 (e-PCR)
- UniSTS:53341

D1S168 (e-PCR)
- UniSTS:147043

G62039 (e-PCR)
- UniSTS:139132

PPIE_9112 (e-PCR)
- UniSTS:468110

BMP8B_2501 (e-PCR)
- UniSTS:280465

RH93165 (e-PCR)
- UniSTS:90081

D15S1390 (e-PCR)
- UniSTS:474340

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables RNA binding	HDA more info	PubMed
enables RNA binding	TAS Traceable Author Statement more info	PubMed
enables RNA polymerase II CTD heptapeptide repeat P3 isomerase activity	IEA Inferred from Electronic Annotation more info
enables RNA polymerase II CTD heptapeptide repeat P6 isomerase activity	IEA Inferred from Electronic Annotation more info
enables cyclosporin A binding	IBA Inferred from Biological aspect of Ancestor more info
enables mRNA binding	IDA Inferred from Direct Assay more info	PubMed
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	TAS Traceable Author Statement more info	PubMed
enables poly(A) binding	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in mRNA splicing, via spliceosome	IC Inferred by Curator more info	PubMed
involved_in mRNA splicing, via spliceosome	IDA Inferred from Direct Assay 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 regulation of DNA-templated transcription	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of transcription by RNA polymerase II	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of U2-type catalytic step 2 spliceosome	IDA Inferred from Direct Assay more info	PubMed
part_of catalytic step 2 spliceosome	IBA Inferred from Biological aspect of Ancestor more info
part_of catalytic step 2 spliceosome	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info
located_in extracellular region	TAS Traceable Author Statement more info
located_in ficolin-1-rich granule lumen	TAS Traceable Author Statement more info
is_active_in intracellular membrane-bounded organelle	IBA Inferred from Biological aspect of Ancestor more info
located_in nuclear speck	IDA Inferred from Direct Assay more info
located_in nucleoplasm	TAS Traceable Author Statement more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in secretory granule lumen	TAS Traceable Author Statement more info

General protein information

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Preferred Names: peptidyl-prolyl cis-trans isomerase E

Names: PPIase E; cyclophilin-33; peptidylprolyl isomerase E (cyclophilin E); rotamase E

NP_001181936.1

EC 5.2.1.8

NP_001306222.1

EC 5.2.1.8

NP_006103.1

EC 5.2.1.8

NP_982281.1

EC 5.2.1.8

XP_006710353.1

EC 5.2.1.8

XP_016855540.1

EC 5.2.1.8

XP_047286017.1

EC 5.2.1.8

XP_047286054.1

EC 5.2.1.8

XP_047286094.1

EC 5.2.1.8

XP_047286120.1

EC 5.2.1.8

XP_047286159.1

EC 5.2.1.8

XP_054189805.1

EC 5.2.1.8

XP_054189806.1

EC 5.2.1.8

XP_054189807.1

EC 5.2.1.8

XP_054189808.1

EC 5.2.1.8

XP_054189809.1

EC 5.2.1.8

XP_054189810.1

EC 5.2.1.8

NCBI Reference Sequences (RefSeq)

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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_044984.2 RefSeqGene

Range

51701..76733

Download

GenBank, FASTA, Sequence Viewer (Graphics), LRG_1053

mRNA and Protein(s)

NM_001195007.2 → NP_001181936.1 peptidyl-prolyl cis-trans isomerase E isoform 4

See identical proteins and their annotated locations for NP_001181936.1

Status: REVIEWED

Description

Transcript Variant: This variant (4) differs in the 3' coding region and 3' UTR, compared to variant 1. The resulting isoform (4) has a distinct C-terminus and is longer than isoform 1.

Source sequence(s)

AL049824, BU689929, DA079924, DQ160195

Consensus CDS

CCDS53299.1

UniProtKB/TrEMBL

A8KAM9

Related

ENSP00000361918.1, ENST00000372830.5

Conserved Domains (3) summary

COG0724
Location:5 → 84

RRM; RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis]

cd01926
Location:140 → 279

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 ...

cd12347
Location:8 → 80

RRM_PPIE; RNA recognition motif in cyclophilin-33 (Cyp33) and similar proteins
NM_001319293.2 → NP_001306222.1 peptidyl-prolyl cis-trans isomerase E isoform 5

Status: REVIEWED

Description

Transcript Variant: This variant (6) uses an alternate in-frame splice junction and differs in the 3' UTR and coding sequence compared to variant 1. The resulting isoform (5) lacks an alternate internal segment and has a shorter and distinct C-terminus compared to isoform 1.

Source sequence(s)

CA445146, CT002466, DA079924

UniProtKB/TrEMBL

A8KAM9

Conserved Domains (3) summary

COG0724
Location:5 → 84

RRM; RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis]

cd01926
Location:129 → 268

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 ...

cd12347
Location:8 → 80

RRM_PPIE; RNA recognition motif in cyclophilin-33 (Cyp33) and similar proteins
NM_006112.4 → NP_006103.1 peptidyl-prolyl cis-trans isomerase E isoform 1

See identical proteins and their annotated locations for NP_006103.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the longest transcript and encodes isoform 1.

Source sequence(s)

AL049824, BC004898, CK300365, DA079924

Consensus CDS

CCDS443.1

UniProtKB/Swiss-Prot

B2R971, O43634, O43635, Q32Q72, Q3S611, Q5TGA0, Q5TGA2, Q5TGA3, Q9UIZ5, Q9UNP9

UniProtKB/TrEMBL

A8KAM9

Related

ENSP00000312769.5, ENST00000324379.10

Conserved Domains (2) summary

cd01926
Location:140 → 298

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 ...

cd12347
Location:8 → 82

RRM_PPIE; RNA recognition motif (RRM) found in cyclophilin-33 (Cyp33) and similar proteins
NM_203456.3 → NP_982281.1 peptidyl-prolyl cis-trans isomerase E isoform 2

See identical proteins and their annotated locations for NP_982281.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) uses an alternate 3' exon and thereby differs in the 3' coding region and 3' UTR, compared to variant 1. The resulting isoform (2) has a distinct and shorter C-terminus, compared to isoform 1.

Source sequence(s)

AF042386, BU689929, DA079924

Consensus CDS

CCDS442.1

UniProtKB/TrEMBL

A8KAM9

Related

ENSP00000348904.2, ENST00000356511.6

Conserved Domains (2) summary

cd01926
Location:140 → 281

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 ...

cd12347
Location:8 → 82

RRM_PPIE; RNA recognition motif (RRM) found in cyclophilin-33 (Cyp33) and similar proteins

RNA

NR_036543.2 RNA Sequence

Status: REVIEWED

Description

Transcript Variant: This variant (3) uses an alternate splice site in the 5'-most exon, compared to variant 1. This variant is represented as non-coding because the use of the supported translational start codon, as used in variant 1, renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).

Source sequence(s)

AL049824, BU160972, CK300365, DA079924
NR_036544.2 RNA Sequence

Status: REVIEWED

Description

Transcript Variant: This variant (5) uses alternate splice sites in the 5'-most exon and in an internal exon, compared to variant 1. This variant is represented as non-coding because the use of the supported translational start codon, as used in variant 1, renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).

Source sequence(s)

AK304694, AL049824, CK300365, DA079924

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_000001.11 Reference GRCh38.p14 Primary Assembly

Range

39738882..39763914

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_047430138.1 → XP_047286094.1 peptidyl-prolyl cis-trans isomerase E isoform X4

Related

ENSP00000433475.1, ENST00000497370.5
XM_017000051.3 → XP_016855540.1 peptidyl-prolyl cis-trans isomerase E isoform X1

UniProtKB/TrEMBL

A8KAM9

Conserved Domains (3) summary

COG0724
Location:5 → 84

RRM; RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis]

cd01926
Location:140 → 279

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 ...

cd12347
Location:8 → 80

RRM_PPIE; RNA recognition motif in cyclophilin-33 (Cyp33) and similar proteins
XM_047430061.1 → XP_047286017.1 peptidyl-prolyl cis-trans isomerase E isoform X1
XM_047430098.1 → XP_047286054.1 peptidyl-prolyl cis-trans isomerase E isoform X2
XM_006710290.5 → XP_006710353.1 peptidyl-prolyl cis-trans isomerase E isoform X3

See identical proteins and their annotated locations for XP_006710353.1

UniProtKB/TrEMBL

A8KAM9

Conserved Domains (2) summary

cd01926
Location:129 → 285

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 ...

cd12347
Location:8 → 80

RRM_PPIE; RNA recognition motif in cyclophilin-33 (Cyp33) and similar proteins
XM_047430203.1 → XP_047286159.1 peptidyl-prolyl cis-trans isomerase E isoform X6

UniProtKB/TrEMBL

E9PK21

Related

ENSP00000431714.1, ENST00000470213.5
XM_047430164.1 → XP_047286120.1 peptidyl-prolyl cis-trans isomerase E isoform X5

Alternate T2T-CHM13v2.0

Genomic

NC_060925.1 Alternate T2T-CHM13v2.0

Range

39608324..39633355

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_054333831.1 → XP_054189806.1 peptidyl-prolyl cis-trans isomerase E isoform X1
XM_054333830.1 → XP_054189805.1 peptidyl-prolyl cis-trans isomerase E isoform X1
XM_054333832.1 → XP_054189807.1 peptidyl-prolyl cis-trans isomerase E isoform X2
XM_054333833.1 → XP_054189808.1 peptidyl-prolyl cis-trans isomerase E isoform X3
XM_054333835.1 → XP_054189810.1 peptidyl-prolyl cis-trans isomerase E isoform X6

UniProtKB/TrEMBL

E9PK21
XM_054333834.1 → XP_054189809.1 peptidyl-prolyl cis-trans isomerase E isoform X5

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

NM_203457.1: Suppressed sequence

Description

NM_203457.1: This RefSeq was permanently suppressed because it is a nonsense-mediated mRNA decay (NMD) candidate.