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Database: UniProt
Entry: Q9UNP9
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Original site: Q9UNP9 
ID   PPIE_HUMAN              Reviewed;         301 AA.
AC   Q9UNP9; B2R971; O43634; O43635; Q32Q72; Q3S611; Q5TGA0; Q5TGA2; Q5TGA3;
AC   Q9UIZ5;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   29-SEP-2021, entry version 205.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase E;
DE            Short=PPIase E;
DE            EC=5.2.1.8 {ECO:0000269|PubMed:18258190, ECO:0000269|PubMed:20541251, ECO:0000269|PubMed:20677832, ECO:0000269|PubMed:8977107};
DE   AltName: Full=Cyclophilin E;
DE   AltName: Full=Cyclophilin-33 {ECO:0000303|PubMed:8977107};
DE   AltName: Full=Rotamase E;
GN   Name=PPIE; Synonyms=CYP33 {ECO:0000303|PubMed:8977107};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RX   PubMed=9747881; DOI=10.1038/sj.onc.1202006;
RA   Kim J.-O., Nau M.M., Allikian K.A., Makela T.P., Alitalo K., Johnson B.E.,
RA   Kelley M.J.;
RT   "Co-amplification of a novel cyclophilin-like gene (PPIE) with L-myc in
RT   small cell lung cancer cell lines.";
RL   Oncogene 17:1019-1026(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RA   Slater C., Thill G., Obar R.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA   Zhou G., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA   Tang Z., Huang B., Lin L., Yang S.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   TISSUE=Bone marrow, Colon, and Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, RNA-BINDING, SUBCELLULAR LOCATION, AND
RP   ACTIVITY REGULATION.
RX   PubMed=8977107; DOI=10.1016/s0014-5793(96)01248-3;
RA   Mi H., Kops O., Zimmermann E., Jaeschke A., Tropschug M.;
RT   "A nuclear RNA-binding cyclophilin in human T cells.";
RL   FEBS Lett. 398:201-205(1996).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C
RP   COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=11991638; DOI=10.1017/s1355838202021088;
RA   Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT   "Purification and characterization of native spliceosomes suitable for
RT   three-dimensional structural analysis.";
RL   RNA 8:426-439(2002).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, RNA-BINDING, AND ACTIVITY REGULATION.
RX   PubMed=18258190; DOI=10.1016/j.febslet.2008.01.055;
RA   Wang Y., Han R., Zhang W., Yuan Y., Zhang X., Long Y., Mi H.;
RT   "Human CyP33 binds specifically to mRNA and binding stimulates PPIase
RT   activity of hCyP33.";
RL   FEBS Lett. 582:835-839(2008).
RN   [11]
RP   IDENTIFICATION AS PART OF THE XAB2 COMPLEX.
RX   PubMed=17981804; DOI=10.1074/jbc.m706647200;
RA   Kuraoka I., Ito S., Wada T., Hayashida M., Lee L., Saijo M., Nakatsu Y.,
RA   Matsumoto M., Matsunaga T., Handa H., Qin J., Nakatani Y., Tanaka K.;
RT   "Isolation of XAB2 complex involved in pre-mRNA splicing, transcription,
RT   and transcription-coupled repair.";
RL   J. Biol. Chem. 283:940-950(2008).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND SER-97, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE IB COMPLEX,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=25599396; DOI=10.1038/nsmb.2951;
RA   De I., Bessonov S., Hofele R., dos Santos K., Will C.L., Urlaub H.,
RA   Luhrmann R., Pena V.;
RT   "The RNA helicase Aquarius exhibits structural adaptations mediating its
RT   recruitment to spliceosomes.";
RL   Nat. Struct. Mol. Biol. 22:138-144(2015).
RN   [16]
RP   STRUCTURE BY NMR OF 1-89.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the RNA recognition motif in peptidyl-prolyl cis-
RT   trans isomerase E.";
RL   Submitted (NOV-2005) to the PDB data bank.
RN   [17] {ECO:0007744|PDB:1ZMF}
RP   X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 137-301.
RX   PubMed=15963461; DOI=10.1016/j.bbrc.2005.06.006;
RA   Wang T., Yun C.H., Gu S.Y., Chang W.R., Liang D.C.;
RT   "1.88 A crystal structure of the C domain of hCyP33: a novel domain of
RT   peptidyl-prolyl cis-trans isomerase.";
RL   Biochem. Biophys. Res. Commun. 333:845-849(2005).
RN   [18] {ECO:0007744|PDB:2KYX}
RP   STRUCTURE BY NMR OF 3-83, CATALYTIC ACTIVITY, INTERACTION WITH KMT2A AND
RP   RNA, FUNCTION, DOMAIN, AND MUTAGENESIS OF LEU-39; LYS-45; ARG-47; PHE-49;
RP   PHE-51; ARG-191 AND PHE-196.
RX   PubMed=20677832; DOI=10.1021/bi1009387;
RA   Park S., Osmers U., Raman G., Schwantes R.H., Diaz M.O., Bushweller J.H.;
RT   "The PHD3 domain of MLL acts as a CYP33-regulated switch between MLL-
RT   mediated activation and repression.";
RL   Biochemistry 49:6576-6586(2010).
RN   [19] {ECO:0007744|PDB:2KU7, ECO:0007744|PDB:3LPY}
RP   STRUCTURE BY NMR OF 2-82 IN COMPLEX WITH KMT2A, CATALYTIC ACTIVITY,
RP   FUNCTION, INTERACTION WITH KMT2A, AND MUTAGENESIS OF PHE-51 AND
RP   196-PHE-MET-197.
RX   PubMed=20541251; DOI=10.1016/j.cell.2010.05.016;
RA   Wang Z., Song J., Milne T.A., Wang G.G., Li H., Allis C.D., Patel D.J.;
RT   "Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to
RT   CyP33 and HDAC-mediated repression.";
RL   Cell 141:1183-1194(2010).
RN   [20] {ECO:0007744|PDB:3MDF}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-83, FUNCTION, INTERACTION WITH
RP   KMT2A AND RNA, DOMAIN, AND MUTAGENESIS OF TYR-9; LEU-39; 40-ASP--LYS-45;
RP   GLU-42; ARG-47; PHE-49 AND PHE-51.
RX   PubMed=20460131; DOI=10.1016/j.jmb.2010.04.067;
RA   Hom R.A., Chang P.Y., Roy S., Musselman C.A., Glass K.C., Selezneva A.I.,
RA   Gozani O., Ismagilov R.F., Cleary M.L., Kutateladze T.G.;
RT   "Molecular mechanism of MLL PHD3 and RNA recognition by the Cyp33 RRM
RT   domain.";
RL   J. Mol. Biol. 400:145-154(2010).
RN   [21] {ECO:0007744|PDB:5MQF}
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=28076346; DOI=10.1038/nature21079;
RA   Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA   Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT   "Cryo-EM structure of a human spliceosome activated for step 2 of
RT   splicing.";
RL   Nature 542:318-323(2017).
CC   -!- FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome
CC       (PubMed:11991638, PubMed:28076346). Combines RNA-binding and PPIase
CC       activities (PubMed:8977107, PubMed:18258190, PubMed:20677832,
CC       PubMed:20460131). Binds mRNA and has a preference for single-stranded
CC       RNA molecules with poly-A and poly-U stretches, suggesting it binds to
CC       the poly(A)-region in the 3'-UTR of mRNA molecules (PubMed:8977107,
CC       PubMed:18258190, PubMed:20460131). Catalyzes the cis-trans
CC       isomerization of proline imidic peptide bonds in proteins
CC       (PubMed:8977107, PubMed:18258190, PubMed:20677832, PubMed:20541251).
CC       Inhibits KMT2A activity; this requires proline isomerase activity
CC       (PubMed:20677832, PubMed:20541251, PubMed:20460131).
CC       {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:18258190,
CC       ECO:0000269|PubMed:20460131, ECO:0000269|PubMed:20541251,
CC       ECO:0000269|PubMed:20677832, ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:8977107}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:11991638,
CC         ECO:0000269|PubMed:18258190, ECO:0000269|PubMed:20541251,
CC         ECO:0000269|PubMed:20677832, ECO:0000269|PubMed:28076346,
CC         ECO:0000269|PubMed:8977107};
CC   -!- ACTIVITY REGULATION: Enzyme activity is inhibited by cyclosporin A.
CC       {ECO:0000269|PubMed:18258190, ECO:0000269|PubMed:8977107}.
CC   -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:11991638,
CC       PubMed:28076346). Component of the XAB2 complex, a multimeric protein
CC       complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE
CC       (PubMed:17981804). Identified in a pentameric intron-binding (IB)
CC       complex composed of AQR, XAB2, ISY1, ZNF830 and PPIE that is
CC       incorporated into the spliceosome as a preassembled complex
CC       (PubMed:25599396). The IB complex does not contain PRPF19
CC       (PubMed:25599396). Interacts (via RNA-binding domain) with KMT2A (via
CC       the third PHD-type zinc-finger) (PubMed:20677832, PubMed:20541251,
CC       PubMed:20460131). {ECO:0000269|PubMed:11991638,
CC       ECO:0000269|PubMed:17981804, ECO:0000269|PubMed:20460131,
CC       ECO:0000269|PubMed:20541251, ECO:0000269|PubMed:20677832,
CC       ECO:0000269|PubMed:25599396, ECO:0000269|PubMed:28076346}.
CC   -!- INTERACTION:
CC       Q9UNP9; O60306: AQR; NbExp=9; IntAct=EBI-591818, EBI-2512328;
CC       Q9UNP9; P22607: FGFR3; NbExp=3; IntAct=EBI-591818, EBI-348399;
CC       Q9UNP9; P06396: GSN; NbExp=3; IntAct=EBI-591818, EBI-351506;
CC       Q9UNP9; Q03164: KMT2A; NbExp=4; IntAct=EBI-591818, EBI-591370;
CC       Q9UNP9; Q9HCS7: XAB2; NbExp=12; IntAct=EBI-591818, EBI-295232;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11991638,
CC       ECO:0000269|PubMed:25599396, ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:8977107}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=A;
CC         IsoId=Q9UNP9-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q9UNP9-2; Sequence=VSP_005181;
CC       Name=3; Synonyms=Cyclophilin-33B;
CC         IsoId=Q9UNP9-3; Sequence=VSP_046370;
CC   -!- TISSUE SPECIFICITY: Found in all the examined tissues including heart,
CC       brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.
CC   -!- DOMAIN: The RRM domain mediates both interaction with RNA and with
CC       KMT2A (via the third PHD-type zinc-finger), but has much higher
CC       affinity for the KMT2A PHD-type zinc-finger.
CC       {ECO:0000269|PubMed:20460131, ECO:0000269|PubMed:20677832}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase E
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF104012; AAD19906.1; -; mRNA.
DR   EMBL; AF104013; AAD19907.1; -; mRNA.
DR   EMBL; AF042385; AAC00006.1; -; mRNA.
DR   EMBL; AF042386; AAC00007.1; -; mRNA.
DR   EMBL; DQ160195; AAZ93379.1; -; mRNA.
DR   EMBL; AK313666; BAG36418.1; -; mRNA.
DR   EMBL; AL049824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL033527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL035404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX07255.1; -; Genomic_DNA.
DR   EMBL; BC004898; AAH04898.1; -; mRNA.
DR   EMBL; BC008451; AAH08451.1; -; mRNA.
DR   EMBL; BC107736; AAI07737.1; -; mRNA.
DR   CCDS; CCDS442.1; -. [Q9UNP9-2]
DR   CCDS; CCDS443.1; -. [Q9UNP9-1]
DR   CCDS; CCDS53299.1; -. [Q9UNP9-3]
DR   PIR; S66681; S66681.
DR   RefSeq; NP_001181936.1; NM_001195007.1. [Q9UNP9-3]
DR   RefSeq; NP_006103.1; NM_006112.3. [Q9UNP9-1]
DR   RefSeq; NP_982281.1; NM_203456.2. [Q9UNP9-2]
DR   RefSeq; XP_016855540.1; XM_017000051.1. [Q9UNP9-3]
DR   PDB; 1ZMF; X-ray; 1.88 A; A=137-301.
DR   PDB; 2CQB; NMR; -; A=1-89.
DR   PDB; 2KU7; NMR; -; A=2-82.
DR   PDB; 2KYX; NMR; -; A=3-83.
DR   PDB; 2R99; X-ray; 1.61 A; A=131-301.
DR   PDB; 3LPY; X-ray; 2.00 A; A/B=5-82.
DR   PDB; 3MDF; X-ray; 1.85 A; A/B=1-83.
DR   PDB; 3UCH; X-ray; 2.50 A; A=129-301.
DR   PDB; 5MQF; EM; 5.90 A; o=1-301.
DR   PDB; 5YZG; EM; 4.10 A; 1=1-301.
DR   PDB; 5Z56; EM; 5.10 A; y=1-301.
DR   PDB; 5Z57; EM; 6.50 A; y=1-301.
DR   PDB; 6FF7; EM; 4.50 A; o=1-301.
DR   PDB; 6ICZ; EM; 3.00 A; y=1-301.
DR   PDB; 6ID0; EM; 2.90 A; y=1-301.
DR   PDB; 6ID1; EM; 2.86 A; y=1-301.
DR   PDB; 7A5P; EM; 5.00 A; o=1-301.
DR   PDB; 7ABI; EM; 8.00 A; o=1-301.
DR   PDBsum; 1ZMF; -.
DR   PDBsum; 2CQB; -.
DR   PDBsum; 2KU7; -.
DR   PDBsum; 2KYX; -.
DR   PDBsum; 2R99; -.
DR   PDBsum; 3LPY; -.
DR   PDBsum; 3MDF; -.
DR   PDBsum; 3UCH; -.
DR   PDBsum; 5MQF; -.
DR   PDBsum; 5YZG; -.
DR   PDBsum; 5Z56; -.
DR   PDBsum; 5Z57; -.
DR   PDBsum; 6FF7; -.
DR   PDBsum; 6ICZ; -.
DR   PDBsum; 6ID0; -.
DR   PDBsum; 6ID1; -.
DR   PDBsum; 7A5P; -.
DR   PDBsum; 7ABI; -.
DR   BMRB; Q9UNP9; -.
DR   SMR; Q9UNP9; -.
DR   BioGRID; 115714; 238.
DR   CORUM; Q9UNP9; -.
DR   DIP; DIP-34757N; -.
DR   IntAct; Q9UNP9; 63.
DR   MINT; Q9UNP9; -.
DR   STRING; 9606.ENSP00000361918; -.
DR   GlyGen; Q9UNP9; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9UNP9; -.
DR   MetOSite; Q9UNP9; -.
DR   PhosphoSitePlus; Q9UNP9; -.
DR   BioMuta; PPIE; -.
DR   DMDM; 13124097; -.
DR   EPD; Q9UNP9; -.
DR   jPOST; Q9UNP9; -.
DR   MassIVE; Q9UNP9; -.
DR   PeptideAtlas; Q9UNP9; -.
DR   PRIDE; Q9UNP9; -.
DR   ProteomicsDB; 65110; -.
DR   ProteomicsDB; 85321; -. [Q9UNP9-1]
DR   ProteomicsDB; 85322; -. [Q9UNP9-2]
DR   TopDownProteomics; Q9UNP9-1; -. [Q9UNP9-1]
DR   TopDownProteomics; Q9UNP9-2; -. [Q9UNP9-2]
DR   Antibodypedia; 17854; 275 antibodies.
DR   DNASU; 10450; -.
DR   Ensembl; ENST00000324379; ENSP00000312769; ENSG00000084072. [Q9UNP9-1]
DR   Ensembl; ENST00000356511; ENSP00000348904; ENSG00000084072. [Q9UNP9-2]
DR   Ensembl; ENST00000372830; ENSP00000361918; ENSG00000084072. [Q9UNP9-3]
DR   GeneID; 10450; -.
DR   KEGG; hsa:10450; -.
DR   UCSC; uc001cds.3; human. [Q9UNP9-1]
DR   CTD; 10450; -.
DR   DisGeNET; 10450; -.
DR   GeneCards; PPIE; -.
DR   HGNC; HGNC:9258; PPIE.
DR   HPA; ENSG00000084072; Low tissue specificity.
DR   MIM; 602435; gene.
DR   neXtProt; NX_Q9UNP9; -.
DR   OpenTargets; ENSG00000084072; -.
DR   PharmGKB; PA33583; -.
DR   VEuPathDB; HostDB:ENSG00000084072; -.
DR   eggNOG; KOG0111; Eukaryota.
DR   GeneTree; ENSGT00940000158790; -.
DR   HOGENOM; CLU_012062_27_0_1; -.
DR   InParanoid; Q9UNP9; -.
DR   OMA; KIVIYAC; -.
DR   OrthoDB; 1484092at2759; -.
DR   PhylomeDB; Q9UNP9; -.
DR   TreeFam; TF313817; -.
DR   BRENDA; 5.2.1.8; 2681.
DR   PathwayCommons; Q9UNP9; -.
DR   Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR   Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR   Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 10450; 487 hits in 1023 CRISPR screens.
DR   ChiTaRS; PPIE; human.
DR   EvolutionaryTrace; Q9UNP9; -.
DR   GeneWiki; PPIE_(gene); -.
DR   GenomeRNAi; 10450; -.
DR   Pharos; Q9UNP9; Tbio.
DR   PRO; PR:Q9UNP9; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9UNP9; protein.
DR   Bgee; ENSG00000084072; Expressed in right testis and 243 other tissues.
DR   ExpressionAtlas; Q9UNP9; baseline and differential.
DR   Genevisible; Q9UNP9; HS.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0016018; F:cyclosporin A binding; IDA:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR   GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR   GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   CDD; cd12347; RRM_PPIE; 1.
DR   Gene3D; 2.40.100.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR016304; PPIE.
DR   InterPro; IPR034168; PPIE_RRM.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF001475; PPI_cyclophilin_E; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Isomerase; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW   Rotamase; Spliceosome.
FT   CHAIN           1..301
FT                   /note="Peptidyl-prolyl cis-trans isomerase E"
FT                   /id="PRO_0000064157"
FT   DOMAIN          6..84
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          143..299
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          107..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         97
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         280..301
FT                   /note="AQGSKDGKPKQKVIIADCGEYV -> VAPDTKASKARGSRKNKDGQERNWGK
FT                   SQKVESHTI (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_046370"
FT   VAR_SEQ         280..301
FT                   /note="AQGSKDGKPKQKVIIADCGEYV -> KQEESAITSQPRSWKLT (in
FT                   isoform B)"
FT                   /evidence="ECO:0000303|PubMed:9747881, ECO:0000303|Ref.2"
FT                   /id="VSP_005181"
FT   MUTAGEN         9
FT                   /note="Y->A: Decreased affinity for RNA."
FT                   /evidence="ECO:0000269|PubMed:20460131"
FT   MUTAGEN         39
FT                   /note="L->A: Decreased affinity for KMT2A."
FT                   /evidence="ECO:0000269|PubMed:20460131,
FT                   ECO:0000269|PubMed:20677832"
FT   MUTAGEN         40..45
FT                   /note="Missing: Abolishes interaction with KMT2A."
FT                   /evidence="ECO:0000269|PubMed:20460131"
FT   MUTAGEN         42
FT                   /note="E->A: Slightly decreased affinity for KMT2A."
FT                   /evidence="ECO:0000269|PubMed:20460131"
FT   MUTAGEN         45
FT                   /note="K->A: No effect on interaction with KMT2A."
FT                   /evidence="ECO:0000269|PubMed:20677832"
FT   MUTAGEN         47
FT                   /note="R->A: No effect on interaction with KMT2A."
FT                   /evidence="ECO:0000269|PubMed:20460131,
FT                   ECO:0000269|PubMed:20677832"
FT   MUTAGEN         49
FT                   /note="F->A: Strongly decreased affinity for KMT2A.
FT                   Decreased affinity for RNA."
FT                   /evidence="ECO:0000269|PubMed:20460131,
FT                   ECO:0000269|PubMed:20677832"
FT   MUTAGEN         51
FT                   /note="F->A: Impairs protein folding."
FT                   /evidence="ECO:0000269|PubMed:20460131,
FT                   ECO:0000269|PubMed:20677832"
FT   MUTAGEN         51
FT                   /note="F->D: Abolishes interaction with KMT2A. Abolishes
FT                   inhibition of KMT2A activity."
FT                   /evidence="ECO:0000269|PubMed:20541251"
FT   MUTAGEN         191
FT                   /note="R->A: Expected to disrupt proline isomerase
FT                   activity. Abolishes inhibition of KMT2A activity; when
FT                   associated with A-196."
FT                   /evidence="ECO:0000269|PubMed:20677832"
FT   MUTAGEN         196..197
FT                   /note="FM->EE: Expected to disrupt peptidylproline binding.
FT                   Decreases interaction with KMT2A. Abolishes inhibition of
FT                   KMT2A activity."
FT                   /evidence="ECO:0000269|PubMed:20541251"
FT   MUTAGEN         196
FT                   /note="F->A: Expected to disrupt proline isomerase
FT                   activity. Abolishes inhibition of KMT2A activity; when
FT                   associated with A-191."
FT                   /evidence="ECO:0000269|PubMed:20677832"
FT   CONFLICT        151
FT                   /note="K -> R (in Ref. 3; AAZ93379)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        207
FT                   /note="N -> D (in Ref. 3; AAZ93379)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="K -> N (in Ref. 2; AAC00006)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..11
FT                   /evidence="ECO:0007829|PDB:3MDF"
FT   HELIX           19..26
FT                   /evidence="ECO:0007829|PDB:3MDF"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:3MDF"
FT   STRAND          32..36
FT                   /evidence="ECO:0007829|PDB:3MDF"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:3MDF"
FT   STRAND          48..56
FT                   /evidence="ECO:0007829|PDB:3MDF"
FT   HELIX           57..67
FT                   /evidence="ECO:0007829|PDB:3MDF"
FT   TURN            71..74
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:3MDF"
FT   STRAND          141..148
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   STRAND          151..160
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   TURN            162..164
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   HELIX           166..177
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   TURN            178..180
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   STRAND          188..193
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   TURN            194..196
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   STRAND          197..200
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   TURN            203..205
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   STRAND          206..209
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   STRAND          214..217
FT                   /evidence="ECO:0007829|PDB:3UCH"
FT   STRAND          230..236
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   STRAND          248..253
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   HELIX           256..258
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   TURN            259..261
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   STRAND          264..270
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   HELIX           272..279
FT                   /evidence="ECO:0007829|PDB:2R99"
FT   STRAND          292..299
FT                   /evidence="ECO:0007829|PDB:2R99"
SQ   SEQUENCE   301 AA;  33431 MW;  F3226149A790BA42 CRC64;
     MATTKRVLYV GGLAEEVDDK VLHAAFIPFG DITDIQIPLD YETEKHRGFA FVEFELAEDA
     AAAIDNMNES ELFGRTIRVN LAKPMRIKEG SSRPVWSDDD WLKKFSGKTL EENKEEEGSE
     PPKAETQEGE PIAKKARSNP QVYMDIKIGN KPAGRIQMLL RSDVVPMTAE NFRCLCTHEK
     GFGFKGSSFH RIIPQFMCQG GDFTNHNGTG GKSIYGKKFD DENFILKHTG PGLLSMANSG
     PNTNGSQFFL TCDKTDWLDG KHVVFGEVTE GLDVLRQIEA QGSKDGKPKQ KVIIADCGEY
     V
//
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