PPIE_HUMAN
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 03-AUG-2022, entry version 208.
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 PDB; 7ZEV; NMR; -; A=1-114.
DR PDB; 7ZEW; NMR; -; A=1-114.
DR PDB; 7ZEY; NMR; -; A=1-114.
DR PDB; 7ZEZ; NMR; -; A=1-90.
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 PDBsum; 7ZEV; -.
DR PDBsum; 7ZEW; -.
DR PDBsum; 7ZEY; -.
DR PDBsum; 7ZEZ; -.
DR AlphaFoldDB; Q9UNP9; -.
DR BMRB; Q9UNP9; -.
DR SMR; Q9UNP9; -.
DR BioGRID; 115714; 268.
DR CORUM; Q9UNP9; -.
DR DIP; DIP-34757N; -.
DR IntAct; Q9UNP9; 66.
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 MaxQB; 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 from 30 providers.
DR DNASU; 10450; -.
DR Ensembl; ENST00000324379.10; ENSP00000312769.5; ENSG00000084072.17. [Q9UNP9-1]
DR Ensembl; ENST00000356511.6; ENSP00000348904.2; ENSG00000084072.17. [Q9UNP9-2]
DR Ensembl; ENST00000372830.5; ENSP00000361918.1; ENSG00000084072.17. [Q9UNP9-3]
DR GeneID; 10450; -.
DR KEGG; hsa:10450; -.
DR MANE-Select; ENST00000324379.10; ENSP00000312769.5; NM_006112.4; NP_006103.1.
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 SignaLink; Q9UNP9; -.
DR BioGRID-ORCS; 10450; 492 hits in 1082 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 left testis and 204 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
