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Q9Y3C6

- PPIL1_HUMAN

UniProt

Q9Y3C6 - PPIL1_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase-like 1

Gene

PPIL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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

    1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. mRNA splicing, via spliceosome Source: UniProtKB
    2. protein folding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    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: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:9260. PPIL1.

    Subcellular locationi

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33587.

    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.
    GenevestigatoriQ9Y3C6.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SNW1Q135734EBI-2557649,EBI-632715
    WDR83Q9BRX92EBI-2557649,EBI-7705033

    Protein-protein interaction databases

    BioGridi119654. 22 interactions.
    IntActiQ9Y3C6. 15 interactions.
    MINTiMINT-4654404.
    STRINGi9606.ENSP00000362803.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000065981.
    HOVERGENiHBG001065.
    InParanoidiQ9Y3C6.
    KOiK12733.
    OMAiITIELYW.
    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]
    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

    MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG    50
    TKFHRIIKDF MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM 100
    ANAGPDTNGS QFFVTLAPTQ WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ 150
    DRPVDDVKII KAYPSG 166
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi20177874.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS4826.1.
    RefSeqi NP_057143.1. NM_016059.4.
    UniGenei Hs.27693.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XWN NMR - A 1-166 [» ]
    2K7N NMR - A 1-166 [» ]
    2X7K X-ray 1.15 A 1-166 [» ]
    ProteinModelPortali Q9Y3C6.
    SMRi Q9Y3C6. Positions 1-166.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119654. 22 interactions.
    IntActi Q9Y3C6. 15 interactions.
    MINTi MINT-4654404.
    STRINGi 9606.ENSP00000362803.

    PTM databases

    PhosphoSitei Q9Y3C6.

    Polymorphism databases

    DMDMi 20177874.

    Proteomic databases

    MaxQBi Q9Y3C6.
    PaxDbi Q9Y3C6.
    PeptideAtlasi Q9Y3C6.
    PRIDEi Q9Y3C6.

    Protocols and materials databases

    DNASUi 51645.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373699 ; ENSP00000362803 ; ENSG00000137168 .
    GeneIDi 51645.
    KEGGi hsa:51645.
    UCSCi uc003omu.2. human.

    Organism-specific databases

    CTDi 51645.
    GeneCardsi GC06M036869.
    HGNCi HGNC:9260. PPIL1.
    MIMi 601301. gene.
    neXtProti NX_Q9Y3C6.
    PharmGKBi PA33587.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0652.
    HOGENOMi HOG000065981.
    HOVERGENi HBG001065.
    InParanoidi Q9Y3C6.
    KOi K12733.
    OMAi ITIELYW.
    OrthoDBi EOG7NW6BK.
    PhylomeDBi Q9Y3C6.
    TreeFami TF300200.

    Miscellaneous databases

    ChiTaRSi PPIL1. human.
    EvolutionaryTracei Q9Y3C6.
    GeneWikii PPIL1.
    GenomeRNAii 51645.
    NextBioi 55588.
    PROi Q9Y3C6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y3C6.
    CleanExi HS_PPIL1.
    Genevestigatori Q9Y3C6.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSi PR00153. CSAPPISMRASE.
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 133 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