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Q9Y3C6 (PPIL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase-like 1

Short name=PPIase
EC=5.2.1.8
Alternative name(s):
Rotamase PPIL1
Gene names
Name:PPIL1
Synonyms:CYPL1
ORF Names:CGI-124, UNQ2425/PRO4984
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length166 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Catalytic activity

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

Enzyme regulation

Inhibited by Cyclosporin A. Ref.7

Subunit structure

Identified in the spliceosome C complex. Interacts with SNW1. Ref.7 Ref.8 Ref.10

Tissue specificity

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

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIL1 subfamily.

Contains 1 PPIase cyclophilin-type domain.

Biophysicochemical properties

Kinetic parameters:

KM=230 µM for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide Ref.7

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentSpliceosome
   Coding sequence diversityPolymorphism
   Molecular functionIsomerase
Rotamase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmRNA splicing, via spliceosome

Inferred by curator Ref.8. Source: UniProtKB

protein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.7Ref.10PubMed 22365833. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 166166Peptidyl-prolyl cis-trans isomerase-like 1
PRO_0000064164

Regions

Domain10 – 164155PPIase cyclophilin-type
Region54 – 6512Cyclosporin A binding
Region70 – 712Cyclosporin A binding
Region99 – 1046Cyclosporin A binding
Region109 – 1135Cyclosporin A binding

Sites

Binding site1191Cyclosporin A
Binding site1251Cyclosporin A

Natural variations

Natural variant361C → S.
Corresponds to variant rs12194408 [ dbSNP | Ensembl ].
VAR_051772

Secondary structure

................................... 166
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y3C6 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 2872DC3336CD05E4

FASTA16618,237
        10         20         30         40         50         60 
MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF 

        70         80         90        100        110        120 
MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ 

       130        140        150        160 
WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSG 

« Hide

References

« Hide 'large scale' references
[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]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4826.1.
RefSeqNP_057143.1. NM_016059.4.
UniGeneHs.27693.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XWNNMR-A1-166[»]
2K7NNMR-A1-166[»]
2X7KX-ray1.15A1-166[»]
ProteinModelPortalQ9Y3C6.
SMRQ9Y3C6. Positions 1-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119654. 22 interactions.
IntActQ9Y3C6. 15 interactions.
MINTMINT-4654404.
STRING9606.ENSP00000362803.

PTM databases

PhosphoSiteQ9Y3C6.

Polymorphism databases

DMDM20177874.

Proteomic databases

MaxQBQ9Y3C6.
PaxDbQ9Y3C6.
PeptideAtlasQ9Y3C6.
PRIDEQ9Y3C6.

Protocols and materials databases

DNASU51645.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373699; ENSP00000362803; ENSG00000137168.
GeneID51645.
KEGGhsa:51645.
UCSCuc003omu.2. human.

Organism-specific databases

CTD51645.
GeneCardsGC06M036869.
HGNCHGNC:9260. PPIL1.
MIM601301. gene.
neXtProtNX_Q9Y3C6.
PharmGKBPA33587.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000065981.
HOVERGENHBG001065.
InParanoidQ9Y3C6.
KOK12733.
OMAITIELYW.
OrthoDBEOG7NW6BK.
PhylomeDBQ9Y3C6.
TreeFamTF300200.

Gene expression databases

BgeeQ9Y3C6.
CleanExHS_PPIL1.
GenevestigatorQ9Y3C6.

Family and domain databases

Gene3D2.40.100.10. 1 hit.
InterProIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. SSF50891. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPIL1. human.
EvolutionaryTraceQ9Y3C6.
GeneWikiPPIL1.
GenomeRNAi51645.
NextBio55588.
PROQ9Y3C6.
SOURCESearch...

Entry information

Entry namePPIL1_HUMAN
AccessionPrimary (citable) accession number: Q9Y3C6
Secondary accession number(s): O15001, Q5TDC9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM