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Protein

Peptidyl-prolyl cis-trans isomerase-like 1

Gene

PPIL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing.1 Publication

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Inhibited by Cyclosporin A.1 Publication

Kineticsi

  1. KM=230 µM for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei119 – 1191Cyclosporin A
    Binding sitei125 – 1251Cyclosporin A

    GO - Molecular functioni

    GO - Biological processi

    • mRNA splicing, via spliceosome Source: UniProtKB
    • protein folding Source: InterPro
    • protein peptidyl-prolyl isomerization Source: GO_Central
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Enzyme and pathway databases

    BRENDAi5.2.1.8. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase-like 1 (EC:5.2.1.8)
    Short name:
    PPIase
    Alternative name(s):
    Rotamase PPIL1
    Gene namesi
    Name:PPIL1
    Synonyms:CYPL1
    ORF Names:CGI-124, UNQ2425/PRO4984
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:9260. PPIL1.

    Subcellular locationi

    GO - Cellular componenti

    • catalytic step 2 spliceosome Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33587.

    Polymorphism and mutation databases

    BioMutaiPPIL1.
    DMDMi20177874.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 166166Peptidyl-prolyl cis-trans isomerase-like 1PRO_0000064164Add
    BLAST

    Proteomic databases

    MaxQBiQ9Y3C6.
    PaxDbiQ9Y3C6.
    PeptideAtlasiQ9Y3C6.
    PRIDEiQ9Y3C6.

    PTM databases

    PhosphoSiteiQ9Y3C6.

    Expressioni

    Tissue specificityi

    Ubiquitous, with the most abundant expression in heart and skeletal muscle.

    Gene expression databases

    BgeeiQ9Y3C6.
    CleanExiHS_PPIL1.
    ExpressionAtlasiQ9Y3C6. baseline and differential.
    GenevisibleiQ9Y3C6. HS.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex. Interacts with SNW1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CPSF6Q166303EBI-2557649,EBI-358410
    RIMBP3Q9UFD93EBI-2557649,EBI-10182375
    SNW1Q135739EBI-2557649,EBI-632715
    TCF4P158843EBI-2557649,EBI-533224
    WDR83Q9BRX92EBI-2557649,EBI-7705033

    Protein-protein interaction databases

    BioGridi119654. 28 interactions.
    IntActiQ9Y3C6. 18 interactions.
    MINTiMINT-4654404.
    STRINGi9606.ENSP00000362803.

    Structurei

    Secondary structure

    1
    166
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 187Combined sources
    Beta strandi21 – 277Combined sources
    Turni29 – 313Combined sources
    Helixi33 – 4513Combined sources
    Turni46 – 505Combined sources
    Beta strandi55 – 573Combined sources
    Turni58 – 603Combined sources
    Beta strandi61 – 644Combined sources
    Beta strandi69 – 724Combined sources
    Beta strandi97 – 1004Combined sources
    Beta strandi102 – 1043Combined sources
    Beta strandi112 – 1176Combined sources
    Helixi120 – 1223Combined sources
    Turni123 – 1253Combined sources
    Beta strandi128 – 1347Combined sources
    Helixi136 – 1427Combined sources
    Beta strandi149 – 1513Combined sources
    Beta strandi153 – 1553Combined sources
    Beta strandi158 – 1647Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XWNNMR-A1-166[»]
    2K7NNMR-A1-166[»]
    2X7KX-ray1.15A1-166[»]
    ProteinModelPortaliQ9Y3C6.
    SMRiQ9Y3C6. Positions 1-166.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y3C6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 164155PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni54 – 6512Cyclosporin A bindingAdd
    BLAST
    Regioni70 – 712Cyclosporin A binding
    Regioni99 – 1046Cyclosporin A binding
    Regioni109 – 1135Cyclosporin A binding

    Sequence similaritiesi

    Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0652.
    GeneTreeiENSGT00760000119072.
    HOGENOMiHOG000065981.
    HOVERGENiHBG001065.
    InParanoidiQ9Y3C6.
    KOiK12733.
    OMAiIELYWNH.
    OrthoDBiEOG7NW6BK.
    PhylomeDBiQ9Y3C6.
    TreeFamiTF300200.

    Family and domain databases

    Gene3Di2.40.100.10. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view]
    PANTHERiPTHR11071. PTHR11071. 1 hit.
    PfamiPF00160. Pro_isomerase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSiPR00153. CSAPPISMRASE.
    SUPFAMiSSF50891. SSF50891. 1 hit.
    PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y3C6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG
    60 70 80 90 100
    TKFHRIIKDF MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM
    110 120 130 140 150
    ANAGPDTNGS QFFVTLAPTQ WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ
    160
    DRPVDDVKII KAYPSG
    Length:166
    Mass (Da):18,237
    Last modified:November 1, 1999 - v1
    Checksum:i2872DC3336CD05E4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361C → S.
    Corresponds to variant rs12194408 [ dbSNP | Ensembl ].
    VAR_051772

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF151882 mRNA. Translation: AAD34119.1.
    AY359032 mRNA. Translation: AAQ89391.1.
    Z85996, AL122034 Genomic DNA. Translation: CAI20894.1.
    AL122034, Z85996 Genomic DNA. Translation: CAI23296.1.
    CH471081 Genomic DNA. Translation: EAX03916.1.
    BC003048 mRNA. Translation: AAH03048.1.
    CCDSiCCDS4826.1.
    RefSeqiNP_057143.1. NM_016059.4.
    UniGeneiHs.27693.

    Genome annotation databases

    EnsembliENST00000373699; ENSP00000362803; ENSG00000137168.
    GeneIDi51645.
    KEGGihsa:51645.
    UCSCiuc003omu.2. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF151882 mRNA. Translation: AAD34119.1.
    AY359032 mRNA. Translation: AAQ89391.1.
    Z85996, AL122034 Genomic DNA. Translation: CAI20894.1.
    AL122034, Z85996 Genomic DNA. Translation: CAI23296.1.
    CH471081 Genomic DNA. Translation: EAX03916.1.
    BC003048 mRNA. Translation: AAH03048.1.
    CCDSiCCDS4826.1.
    RefSeqiNP_057143.1. NM_016059.4.
    UniGeneiHs.27693.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XWNNMR-A1-166[»]
    2K7NNMR-A1-166[»]
    2X7KX-ray1.15A1-166[»]
    ProteinModelPortaliQ9Y3C6.
    SMRiQ9Y3C6. Positions 1-166.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi119654. 28 interactions.
    IntActiQ9Y3C6. 18 interactions.
    MINTiMINT-4654404.
    STRINGi9606.ENSP00000362803.

    Chemistry

    BindingDBiQ9Y3C6.

    PTM databases

    PhosphoSiteiQ9Y3C6.

    Polymorphism and mutation databases

    BioMutaiPPIL1.
    DMDMi20177874.

    Proteomic databases

    MaxQBiQ9Y3C6.
    PaxDbiQ9Y3C6.
    PeptideAtlasiQ9Y3C6.
    PRIDEiQ9Y3C6.

    Protocols and materials databases

    DNASUi51645.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000373699; ENSP00000362803; ENSG00000137168.
    GeneIDi51645.
    KEGGihsa:51645.
    UCSCiuc003omu.2. human.

    Organism-specific databases

    CTDi51645.
    GeneCardsiGC06M036869.
    HGNCiHGNC:9260. PPIL1.
    MIMi601301. gene.
    neXtProtiNX_Q9Y3C6.
    PharmGKBiPA33587.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0652.
    GeneTreeiENSGT00760000119072.
    HOGENOMiHOG000065981.
    HOVERGENiHBG001065.
    InParanoidiQ9Y3C6.
    KOiK12733.
    OMAiIELYWNH.
    OrthoDBiEOG7NW6BK.
    PhylomeDBiQ9Y3C6.
    TreeFamiTF300200.

    Enzyme and pathway databases

    BRENDAi5.2.1.8. 2681.

    Miscellaneous databases

    ChiTaRSiPPIL1. human.
    EvolutionaryTraceiQ9Y3C6.
    GeneWikiiPPIL1.
    GenomeRNAii51645.
    NextBioi55588.
    PROiQ9Y3C6.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9Y3C6.
    CleanExiHS_PPIL1.
    ExpressionAtlasiQ9Y3C6. baseline and differential.
    GenevisibleiQ9Y3C6. HS.

    Family and domain databases

    Gene3Di2.40.100.10. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view]
    PANTHERiPTHR11071. PTHR11071. 1 hit.
    PfamiPF00160. Pro_isomerase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSiPR00153. CSAPPISMRASE.
    SUPFAMiSSF50891. SSF50891. 1 hit.
    PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning, expression and chromosomal mapping of a novel cyclophilin-related gene (PPIL1) from human fetal brain."
      Ozaki K., Fujiwara T., Kawai A., Shimizu F., Takami S., Okuno S., Takeda S., Shimada Y., Nagata M., Watanabe T., Takaichi A., Takahashi E., Nakamura Y., Shin S.
      Cytogenet. Cell Genet. 72:242-245(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal brain.
    2. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lymph.
    7. "Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP."
      Xu C., Zhang J., Huang X., Sun J., Xu Y., Tang Y., Wu J., Shi Y., Huang Q., Zhang Q.
      J. Biol. Chem. 281:15900-15908(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, KINETIC PARAMETERS, ENZYME REGULATION, CYCLOSPORIN A BINDING, INTERACTION WITH SNW1, STRUCTURE BY NMR.
    8. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
      Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
      RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "The crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode for a linear epitope of the SKIP protein."
      Stegmann C.M., Luhrmann R., Wahl M.C.
      PLoS ONE 5:E10013-E10013(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), INTERACTION WITH SNW1.

    Entry informationi

    Entry nameiPPIL1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y3C6
    Secondary accession number(s): O15001, Q5TDC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2002
    Last sequence update: November 1, 1999
    Last modified: June 24, 2015
    This is version 141 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.