Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

  1. peptidyl-prolyl cis-trans isomerase activity Source: GO_Central

GO - Biological processi

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

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: UniProtKB
Complete GO annotation...

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.
ExpressionAtlasiQ9Y3C6. baseline and differential.
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. 28 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 – 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]
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.

Polymorphism databases

DMDMi20177874.

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. 15 interactions.
MINTiMINT-4654404.
STRINGi9606.ENSP00000362803.

Chemistry

BindingDBiQ9Y3C6.

PTM databases

PhosphoSiteiQ9Y3C6.

Polymorphism databases

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.

Miscellaneous databases

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

Gene expression databases

BgeeiQ9Y3C6.
CleanExiHS_PPIL1.
ExpressionAtlasiQ9Y3C6. baseline and differential.
GenevestigatoriQ9Y3C6.

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]
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: February 4, 2015
This is version 137 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.