U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    PPIL3 peptidylprolyl isomerase like 3 [ Homo sapiens (human) ]

    Gene ID: 53938, updated on 10-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    PPIL3provided by HGNC
    Official Full Name
    peptidylprolyl isomerase like 3provided by HGNC
    Primary source
    HGNC:HGNC:9262
    See related
    Ensembl:ENSG00000240344 MIM:615811; AllianceGenome:HGNC:9262
    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
    CYPJ
    Summary
    This gene encodes a member of the cyclophilin family. Cyclophilins catalyze the cis-trans isomerization of peptidylprolyl imide bonds in oligopeptides. They have been proposed to act either as catalysts or as molecular chaperones in protein-folding events. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2008]
    Expression
    Ubiquitous expression in lymph node (RPKM 8.6), ovary (RPKM 7.0) and 25 other tissues See more
    Orthologs
    mouse all
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    See PPIL3 in Genome Data Viewer
    Location:
    2q33.1
    Exon count:
    11
    Annotation release Status Assembly Chr Location
    RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 2 NC_000002.12 (200870907..200889291, complement)
    RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 2 NC_060926.1 (201354357..201372783, complement)
    RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 2 NC_000002.11 (201735630..201753800, complement)

    Chromosome 2 - NC_000002.12Genomic Context describing neighboring genes Neighboring gene Sharpr-MPRA regulatory region 5577 Neighboring gene RNA, 5S ribosomal pseudogene 115 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 16963 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 16964 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 16965 Neighboring gene CDC like kinase 1 Neighboring gene BRD4-independent group 4 enhancer GRCh37_chr2:201753436-201754635 Neighboring gene RNA, U6 small nuclear 312, pseudogene Neighboring gene ATAC-STARR-seq lymphoblastoid active region 16968 Neighboring gene NGG1 interacting factor 3 like 1 Neighboring gene RNA, U6 small nuclear 762, pseudogene Neighboring gene origin recognition complex subunit 2 Neighboring gene OCT4 hESC enhancer GRCh37_chr2:201799831-201800332 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 16969 Neighboring gene uncharacterized LOC105373835

    Genomic regions, transcripts, and products

    Go to the top of the page Help

    Go to nucleotide: Graphics FASTA GenBank

    Expression

    Go to the top of the page Help
    • Project title: Tissue-specific circular RNA induction during human fetal development
    • Description: 35 human fetal samples from 6 tissues (3 - 7 replicates per tissue) collected between 10 and 20 weeks gestational time were sequenced using Illumina TruSeq Stranded Total RNA
    • BioProject: PRJNA270632
    • Publication: PMID 26076956
    • Analysis date: Mon Apr 2 22:54:59 2018

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Molecular cloning and characterization of a novel peptidylprolyl isomerase (cyclophilin)-like gene (PPIL3) from human fetal brain. Zhou Z, et al. Cytogenet Cell Genet, 2001. PMID 11435694
    2. Structure of recombinant human cyclophilin J, a novel member of the cyclophilin family. Huang LL, et al. Acta Crystallogr D Biol Crystallogr, 2005 Mar. PMID 15735342
    3. cDNA microarray in isolation of novel differentially expressed genes related to human glioma and clone of a novel full-length gene. Qi ZY, et al. Chin Med J (Engl), 2005 May 20. PMID 15989758
    4. Crystallization and preliminary X-ray crystallographic studies of human cyclophilin J. Hu H, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2005 Feb 1. PMID 16510998, Free PMC Article
    5. Cyclophilin J is a novel peptidyl-prolyl isomerase and target for repressing the growth of hepatocellular carcinoma. Chen J, et al. PLoS One, 2015. PMID 26020957, Free PMC Article

    See all (54) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Cyclophilin J expression was up-regulated in gastric carcinoma compared to normal gastric tissues.
      Title: Expression and Significance of Cyclophilin J in Primary Gastric Adenocarcinoma.
    2. CYPJ structurally resembles CYPA. It is sensitive to inhibition by CsA and plays a role in regulating cell growth, proliferation, and apoptosis.
      Title: Biochemical Features of Recombinant Human Cyclophilin J.
    3. Suppression of CYPJ could repress the growth of HCC, which makes CYPJ a potential target for the development of new strategies to treat this malignancy.
      Title: Cyclophilin J is a novel peptidyl-prolyl isomerase and target for repressing the growth of hepatocellular carcinoma.
    4. Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)
      Title: Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
    5. Human peptidyl-prolyl isomerase-like 3 (Ppil3) is one of the Apoptin-associated proteins.
      Title: Interaction with Ppil3 leads to the cytoplasmic localization of Apoptin in tumor cells.
    6. The novel full-length gene of human PPIL3 may be correlated with the formation of human glioma.
      Title: cDNA microarray in isolation of novel differentially expressed genes related to human glioma and clone of a novel full-length gene.
    7. Human cyclophilin J, a new member of the cyclophilin family, has been expressed and crystallized.
      Title: Crystallization and preliminary X-ray crystallographic studies of human cyclophilin J.
    Submit: New GeneRIF Correction

    Phenotypes

    Go to the top of the page Help

    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)

    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

    Homology

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    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 peptidyl-prolyl cis-trans isomerase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    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 protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in regulation of transcription by RNA polymerase II IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    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 
    located_in nucleoplasm TAS
    Traceable Author Statement
    more info
    		  

    General protein information

    Go to the top of the page Help
    Preferred Names
    peptidyl-prolyl cis-trans isomerase-like 3
    Names
    PPIase
    PPIase-like protein 3
    cyclophilin J
    cyclophilin-like protein 3
    cyclophilin-like protein PPIL3
    peptidylprolyl cis-trans isomerase-like protein 3
    peptidylprolyl isomerase (cyclophilin)-like 3
    rotamase PPIL3
    NP_115861.1
    NP_570981.1
    XP_005246708.1
    XP_005246709.1
    XP_011509660.1
    XP_016859841.1
    XP_016859842.1
    XP_016859843.1
    XP_016859844.1
    XP_016859845.1
    XP_054198563.1
    XP_054198564.1
    XP_054198565.1
    XP_054198566.1
    XP_054198567.1
    XP_054198568.1
    XP_054198569.1
    XP_054198570.1

    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.

    mRNA and Protein(s)

    1. NM_032472.4 → NP_115861.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform PPIL3a

      See identical proteins and their annotated locations for NP_115861.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (PPIL3a) encodes the longer isoform (PPIL3a).
      Source sequence(s)
      AC005037, AF251049, AF271652
      Consensus CDS
      CCDS2332.1
      UniProtKB/TrEMBL
      A0A0S2Z5A8, B8ZZ77
      Related
      ENSP00000286175.8, ENST00000286175.12
      Conserved Domains (1) summary
      cl00197
      Location:1 → 158
      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_130906.3 → NP_570981.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform PPIL3b

      See identical proteins and their annotated locations for NP_570981.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (PPIL3b) includes an alternate in-frame segment, compared to variant PPIL3a, resulting in a shorter protein (isoform PPIL3b), compared to isoform PPIL3a. Variants PPIL3b and PPIL3c encode the same protein.
      Source sequence(s)
      AC005037, AF271652, CB961908
      Consensus CDS
      CCDS2333.1
      UniProtKB/Swiss-Prot
      Q86WF9, Q96IA9, Q9BXZ1, Q9H2H8
      UniProtKB/TrEMBL
      A0A024R3V4, A0A0S2Z5G0, H7BZ14
      Related
      ENSP00000376107.4, ENST00000392283.9
      Conserved Domains (1) summary
      cd01928
      Location:1 → 154
      Cyclophilin_PPIL3_like; Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans isomerase (PPIL3). Members of this family lack a key residue important for cyclosporin binding: the tryptophan residue corresponding to W121 in human hCyP-18a; most members have a ...

    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

    1. NC_000002.12 Reference GRCh38.p14 Primary Assembly

      Range
      200870907..200889291 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_005246652.6 → XP_005246709.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X2

      See identical proteins and their annotated locations for XP_005246709.1

      UniProtKB/Swiss-Prot
      Q86WF9, Q96IA9, Q9BXZ1, Q9H2H8
      UniProtKB/TrEMBL
      A0A024R3V4, A0A0S2Z5G0, H7BZ14
      Conserved Domains (1) summary
      cd01928
      Location:1 → 154
      Cyclophilin_PPIL3_like; Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans isomerase (PPIL3). Members of this family lack a key residue important for cyclosporin binding: the tryptophan residue corresponding to W121 in human hCyP-18a; most members have a ...

    2. XM_005246651.4 → XP_005246708.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X1

      See identical proteins and their annotated locations for XP_005246708.1

      UniProtKB/TrEMBL
      A0A0S2Z5A8, B8ZZ77
      Related
      ENSP00000387012.1, ENST00000409449.5
      Conserved Domains (1) summary
      cl00197
      Location:1 → 158
      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 ...

    3. XM_011511358.3 → XP_011509660.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X2

      See identical proteins and their annotated locations for XP_011509660.1

      UniProtKB/Swiss-Prot
      Q86WF9, Q96IA9, Q9BXZ1, Q9H2H8
      UniProtKB/TrEMBL
      A0A024R3V4, A0A0S2Z5G0, H7BZ14
      Related
      ENST00000465823.5
      Conserved Domains (1) summary
      cd01928
      Location:1 → 154
      Cyclophilin_PPIL3_like; Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans isomerase (PPIL3). Members of this family lack a key residue important for cyclosporin binding: the tryptophan residue corresponding to W121 in human hCyP-18a; most members have a ...

    4. XM_017004352.2 → XP_016859841.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X1

      UniProtKB/TrEMBL
      A0A0S2Z5A8, B8ZZ77
      Related
      ENSP00000386235.1, ENST00000409361.5
      Conserved Domains (1) summary
      cl00197
      Location:1 → 158
      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 ...

    5. XM_017004354.3 → XP_016859843.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X1

      UniProtKB/TrEMBL
      A0A0S2Z5A8, B8ZZ77
      Conserved Domains (1) summary
      cl00197
      Location:1 → 158
      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 ...

    6. XM_017004356.3 → XP_016859845.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X2

      UniProtKB/Swiss-Prot
      Q86WF9, Q96IA9, Q9BXZ1, Q9H2H8
      UniProtKB/TrEMBL
      A0A024R3V4, A0A0S2Z5G0, H7BZ14
      Conserved Domains (1) summary
      cd01928
      Location:1 → 154
      Cyclophilin_PPIL3_like; Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans isomerase (PPIL3). Members of this family lack a key residue important for cyclosporin binding: the tryptophan residue corresponding to W121 in human hCyP-18a; most members have a ...

    7. XM_017004355.3 → XP_016859844.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X2

      UniProtKB/Swiss-Prot
      Q86WF9, Q96IA9, Q9BXZ1, Q9H2H8
      UniProtKB/TrEMBL
      A0A024R3V4, A0A0S2Z5G0, H7BZ14
      Conserved Domains (1) summary
      cd01928
      Location:1 → 154
      Cyclophilin_PPIL3_like; Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans isomerase (PPIL3). Members of this family lack a key residue important for cyclosporin binding: the tryptophan residue corresponding to W121 in human hCyP-18a; most members have a ...

    8. XM_017004353.2 → XP_016859842.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X1

      UniProtKB/TrEMBL
      A0A0S2Z5A8, B8ZZ77
      Conserved Domains (1) summary
      cl00197
      Location:1 → 158
      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 ...

    Alternate T2T-CHM13v2.0

    Genomic

    1. NC_060926.1 Alternate T2T-CHM13v2.0

      Range
      201354357..201372783 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_054342588.1 → XP_054198563.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X1

      UniProtKB/TrEMBL
      A0A0S2Z5A8, B8ZZ77

    2. XM_054342592.1 → XP_054198567.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X2

      UniProtKB/Swiss-Prot
      Q86WF9, Q96IA9, Q9BXZ1, Q9H2H8
      UniProtKB/TrEMBL
      A0A024R3V4, A0A0S2Z5G0, H7BZ14

    3. XM_054342590.1 → XP_054198565.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X1

      UniProtKB/TrEMBL
      A0A0S2Z5A8, B8ZZ77

    4. XM_054342593.1 → XP_054198568.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X2

      UniProtKB/Swiss-Prot
      Q86WF9, Q96IA9, Q9BXZ1, Q9H2H8
      UniProtKB/TrEMBL
      A0A024R3V4, A0A0S2Z5G0, H7BZ14

    5. XM_054342589.1 → XP_054198564.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X1

      UniProtKB/TrEMBL
      A0A0S2Z5A8, B8ZZ77

    6. XM_054342595.1 → XP_054198570.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X2

      UniProtKB/Swiss-Prot
      Q86WF9, Q96IA9, Q9BXZ1, Q9H2H8
      UniProtKB/TrEMBL
      A0A024R3V4, A0A0S2Z5G0, H7BZ14

    7. XM_054342594.1 → XP_054198569.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X2

      UniProtKB/Swiss-Prot
      Q86WF9, Q96IA9, Q9BXZ1, Q9H2H8
      UniProtKB/TrEMBL
      A0A024R3V4, A0A0S2Z5G0, H7BZ14

    8. XM_054342591.1 → XP_054198566.1  peptidyl-prolyl cis-trans isomerase-like 3 isoform X1

      UniProtKB/TrEMBL
      A0A0S2Z5A8, B8ZZ77

    Suppressed Reference Sequence(s)

    The following Reference Sequences have been suppressed. Explain

    1. NM_131916.1: Suppressed sequence

      Description
      NM_131916.1: This RefSeq was permanently suppressed because currently there is insufficient support for the transcript, which aligns with non-consensus splice sites in the 5' UTR.
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q9H2H8.1 GenPept UniProtKB/Swiss-Prot:Q9H2H8

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Chemical Information
    Molecular Biology Databases
    Research Materials
    Tools
    Miscellaneous