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Database: UniProt
Entry: O60508
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Original site: O60508 
ID   PRP17_HUMAN             Reviewed;         579 AA.
AC   O60508; B2RBC5; O75471; Q5SRN0; Q9UPG1;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   29-SEP-2021, entry version 186.
DE   RecName: Full=Pre-mRNA-processing factor 17;
DE   AltName: Full=Cell division cycle 40 homolog;
DE   AltName: Full=EH-binding protein 3;
DE            Short=Ehb3;
DE   AltName: Full=PRP17 homolog;
DE            Short=hPRP17;
GN   Name=CDC40; Synonyms=EHB3, PRP17, PRPF17;
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].
RC   TISSUE=Colon epithelium;
RX   PubMed=9524131; DOI=10.1093/emboj/17.7.2095;
RA   Zhou Z., Reed R.;
RT   "Human homologs of yeast prp16 and prp17 reveal conservation of the
RT   mechanism for catalytic step II of pre-mRNA splicing.";
RL   EMBO J. 17:2095-2106(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=9830021; DOI=10.1074/jbc.273.49.32771;
RA   Lindsey L.A., Garcia-Blanco M.A.;
RT   "Functional conservation of the human homolog of the yeast pre-mRNA
RT   splicing factor Prp17p.";
RL   J. Biol. Chem. 273:32771-32775(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Trachea;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-579.
RX   PubMed=9769104; DOI=10.1017/s1355838298980712;
RA   Ben-Yehuda S., Dix I., Russell C.S., Levy S., Beggs J.D., Kupiec M.;
RT   "Identification and functional analysis of hPRP17, the human homologue of
RT   the PRP17/CDC40 yeast gene involved in splicing and cell cycle control.";
RL   RNA 4:1304-1312(1998).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-173.
RX   PubMed=9303539; DOI=10.1101/gad.11.17.2239;
RA   Salcini A.E., Confalonieri S., Doria M., Santolini E., Tassi E.,
RA   Minenkova O., Cesareni G., Pelicci P.G., Di Fiore P.P.;
RT   "Binding specificity and in vivo targets of the EH domain, a novel protein-
RT   protein interaction module.";
RL   Genes Dev. 11:2239-2249(1997).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP   C COMPLEX.
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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY
RP   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   IDENTIFICATION BY 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] {ECO:0007744|PDB:5XJC}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RX   PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA   Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT   "An Atomic Structure of the Human Spliceosome.";
RL   Cell 169:918-929(2017).
RN   [16] {ECO:0007744|PDB:5MQF}
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
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).
RN   [17] {ECO:0007744|PDB:6FF4}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RX   PubMed=29361316; DOI=10.1016/j.cell.2018.01.010;
RA   Haselbach D., Komarov I., Agafonov D.E., Hartmuth K., Graf B., Dybkov O.,
RA   Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT   "Structure and Conformational Dynamics of the Human Spliceosomal Bact
RT   Complex.";
RL   Cell 172:454-464(2018).
RN   [18] {ECO:0007744|PDB:5Z56, ECO:0007744|PDB:5Z57}
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.10 ANGSTROMS), FUNCTION, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RX   PubMed=29360106; DOI=10.1038/cr.2018.14;
RA   Zhang X., Yan C., Zhan X., Li L., Lei J., Shi Y.;
RT   "Structure of the human activated spliceosome in three conformational
RT   states.";
RL   Cell Res. 28:307-322(2018).
RN   [19] {ECO:0007744|PDB:5YZG}
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS), FUNCTION, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RX   PubMed=29301961; DOI=10.1126/science.aar6401;
RA   Zhan X., Yan C., Zhang X., Lei J., Shi Y.;
RT   "Structure of a human catalytic step I spliceosome.";
RL   Science 359:537-545(2018).
RN   [20] {ECO:0007744|PDB:6QDV}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 67-579, FUNCTION,
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=30705154; DOI=10.1126/science.aaw5569;
RA   Fica S.M., Oubridge C., Wilkinson M.E., Newman A.J., Nagai K.;
RT   "A human postcatalytic spliceosome structure reveals essential roles of
RT   metazoan factors for exon ligation.";
RL   Science 363:710-714(2019).
CC   -!- FUNCTION: Required for pre-mRNA splicing as component of the activated
CC       spliceosome. {ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC       ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106,
CC       ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30705154,
CC       ECO:0000269|PubMed:9830021}.
CC   -!- SUBUNIT: Component of the pre-catalytic and catalytic spliceosome
CC       complexes (PubMed:11991638, PubMed:28502770, PubMed:28076346,
CC       PubMed:29361316, PubMed:29360106, PubMed:29301961). Component of the
CC       postcatalytic spliceosome P complex (PubMed:30705154).
CC       {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961,
CC       ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316,
CC       ECO:0000269|PubMed:30705154}.
CC   -!- INTERACTION:
CC       O60508; Q9UMS4: PRPF19; NbExp=3; IntAct=EBI-2557812, EBI-395746;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961,
CC       ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316,
CC       ECO:0000269|PubMed:30705154}. Nucleus speckle
CC       {ECO:0000269|PubMed:9830021}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC25166.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF038392; AAC39730.1; -; mRNA.
DR   EMBL; AL671518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK314601; BAG37172.1; -; mRNA.
DR   EMBL; BC117145; AAI17146.1; -; mRNA.
DR   EMBL; BC126114; AAI26115.1; -; mRNA.
DR   EMBL; AF061241; AAC25166.1; ALT_INIT; mRNA.
DR   EMBL; AF015044; AAD01552.1; -; mRNA.
DR   CCDS; CCDS5081.1; -.
DR   RefSeq; NP_056975.1; NM_015891.2.
DR   PDB; 5MQF; EM; 5.90 A; E=1-579.
DR   PDB; 5XJC; EM; 3.60 A; W=1-579.
DR   PDB; 5YZG; EM; 4.10 A; W=1-579.
DR   PDB; 5Z56; EM; 5.10 A; W=1-579.
DR   PDB; 5Z57; EM; 6.50 A; W=1-579.
DR   PDB; 6FF4; EM; 16.00 A; E=1-579.
DR   PDB; 6FF7; EM; 4.50 A; E=1-579.
DR   PDB; 6ICZ; EM; 3.00 A; W=1-579.
DR   PDB; 6ID0; EM; 2.90 A; W=1-579.
DR   PDB; 6ID1; EM; 2.86 A; W=1-579.
DR   PDB; 6QDV; EM; 3.30 A; o=67-579.
DR   PDB; 6ZYM; EM; 3.40 A; E=1-579.
DR   PDB; 7A5P; EM; 5.00 A; E=1-579.
DR   PDB; 7AAV; EM; 4.20 A; 8=1-579.
DR   PDB; 7ABI; EM; 8.00 A; 8=1-579.
DR   PDBsum; 5MQF; -.
DR   PDBsum; 5XJC; -.
DR   PDBsum; 5YZG; -.
DR   PDBsum; 5Z56; -.
DR   PDBsum; 5Z57; -.
DR   PDBsum; 6FF4; -.
DR   PDBsum; 6FF7; -.
DR   PDBsum; 6ICZ; -.
DR   PDBsum; 6ID0; -.
DR   PDBsum; 6ID1; -.
DR   PDBsum; 6QDV; -.
DR   PDBsum; 6ZYM; -.
DR   PDBsum; 7A5P; -.
DR   PDBsum; 7AAV; -.
DR   PDBsum; 7ABI; -.
DR   SMR; O60508; -.
DR   BioGRID; 119497; 79.
DR   CORUM; O60508; -.
DR   IntAct; O60508; 32.
DR   STRING; 9606.ENSP00000357928; -.
DR   iPTMnet; O60508; -.
DR   PhosphoSitePlus; O60508; -.
DR   SwissPalm; O60508; -.
DR   BioMuta; CDC40; -.
DR   EPD; O60508; -.
DR   jPOST; O60508; -.
DR   MassIVE; O60508; -.
DR   MaxQB; O60508; -.
DR   PaxDb; O60508; -.
DR   PeptideAtlas; O60508; -.
DR   PRIDE; O60508; -.
DR   ProteomicsDB; 49450; -.
DR   Antibodypedia; 32306; 144 antibodies.
DR   DNASU; 51362; -.
DR   Ensembl; ENST00000307731; ENSP00000304370; ENSG00000168438.
DR   Ensembl; ENST00000368932; ENSP00000357928; ENSG00000168438.
DR   GeneID; 51362; -.
DR   KEGG; hsa:51362; -.
DR   UCSC; uc003pua.4; human.
DR   CTD; 51362; -.
DR   DisGeNET; 51362; -.
DR   GeneCards; CDC40; -.
DR   HGNC; HGNC:17350; CDC40.
DR   HPA; ENSG00000168438; Low tissue specificity.
DR   MIM; 605585; gene.
DR   neXtProt; NX_O60508; -.
DR   OpenTargets; ENSG00000168438; -.
DR   PharmGKB; PA134891332; -.
DR   VEuPathDB; HostDB:ENSG00000168438; -.
DR   eggNOG; KOG0282; Eukaryota.
DR   GeneTree; ENSGT00530000063583; -.
DR   HOGENOM; CLU_022571_2_1_1; -.
DR   InParanoid; O60508; -.
DR   OMA; SGGYVCF; -.
DR   OrthoDB; 967109at2759; -.
DR   PhylomeDB; O60508; -.
DR   TreeFam; TF101064; -.
DR   PathwayCommons; O60508; -.
DR   Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-HSA-72187; mRNA 3'-end processing.
DR   Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR   SignaLink; O60508; -.
DR   BioGRID-ORCS; 51362; 543 hits in 1024 CRISPR screens.
DR   ChiTaRS; CDC40; human.
DR   GeneWiki; CDC40; -.
DR   GenomeRNAi; 51362; -.
DR   Pharos; O60508; Tbio.
DR   PRO; PR:O60508; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; O60508; protein.
DR   Bgee; ENSG00000168438; Expressed in frontal cortex and 246 other tissues.
DR   ExpressionAtlas; O60508; baseline and differential.
DR   Genevisible; O60508; HS.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR032847; PRPF17.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR43979; PTHR43979; 1.
DR   Pfam; PF00400; WD40; 5.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Spliceosome; WD repeat.
FT   CHAIN           1..579
FT                   /note="Pre-mRNA-processing factor 17"
FT                   /id="PRO_0000051142"
FT   REPEAT          286..326
FT                   /note="WD 1"
FT   REPEAT          330..369
FT                   /note="WD 2"
FT   REPEAT          371..413
FT                   /note="WD 3"
FT   REPEAT          416..455
FT                   /note="WD 4"
FT   REPEAT          459..498
FT                   /note="WD 5"
FT   REPEAT          504..545
FT                   /note="WD 6"
FT   REPEAT          548..578
FT                   /note="WD 7"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CONFLICT        7
FT                   /note="A -> V (in Ref. 7; AAD01552)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        31
FT                   /note="L -> P (in Ref. 6; AAC25166)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        210
FT                   /note="E -> R (in Ref. 6; AAC25166)"
FT                   /evidence="ECO:0000305"
FT   TURN            86..88
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           102..105
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          109..112
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          114..116
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           122..134
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          136..139
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          143..149
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          152..155
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           156..161
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   TURN            162..164
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:6ICZ"
FT   TURN            189..191
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:6ICZ"
FT   STRAND          199..202
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           212..224
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          239..241
FT                   /evidence="ECO:0007829|PDB:6ICZ"
FT   TURN            249..251
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          254..256
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          261..263
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          291..295
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          298..302
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          304..308
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          311..316
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          318..320
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          326..329
FT                   /evidence="ECO:0007829|PDB:6ICZ"
FT   STRAND          335..340
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          342..351
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          356..360
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   TURN            361..363
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          366..370
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          376..381
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          388..398
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          400..404
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   TURN            405..407
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          410..414
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          421..428
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   TURN            429..431
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          432..440
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          442..446
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          453..456
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          465..469
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          475..480
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   TURN            481..483
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          484..489
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          491..493
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          496..502
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          514..516
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   HELIX           518..520
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          522..525
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          533..536
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   TURN            537..540
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          541..545
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          553..558
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          566..570
FT                   /evidence="ECO:0007829|PDB:6ID0"
SQ   SEQUENCE   579 AA;  65521 MW;  1DE2BAA6F03FF16D CRC64;
     MSAAIAALAA SYGSGSGSES DSDSESSRCP LPAADSLMHL TKSPSSKPSL AVAVDSAPEV
     AVKEDLETGV HLDPAVKEVQ YNPTYETMFA PEFGPENPFR TQQMAAPRNM LSGYAEPAHI
     NDFMFEQQRR TFATYGYALD PSLDNHQVSA KYIGSVEEAE KNQGLTVFET GQKKTEKRKK
     FKENDASNID GFLGPWAKYV DEKDVAKPSE EEQKELDEIT AKRQKKGKQE EEKPGEEKTI
     LHVKEMYDYQ GRSYLHIPQD VGVNLRSTMP PEKCYLPKKQ IHVWSGHTKG VSAVRLFPLS
     GHLLLSCSMD CKIKLWEVYG ERRCLRTFIG HSKAVRDICF NTAGTQFLSA AYDRYLKLWD
     TETGQCISRF TNRKVPYCVK FNPDEDKQNL FVAGMSDKKI VQWDIRSGEI VQEYDRHLGA
     VNTIVFVDEN RRFVSTSDDK SLRVWEWDIP VDFKYIAEPS MHSMPAVTLS PNGKWLACQS
     MDNQILIFGA QNRFRLNKKK IFKGHMVAGY ACQVDFSPDM SYVISGDGNG KLNIWDWKTT
     KLYSRFKAHD KVCIGAVWHP HETSKVITCG WDGLIKLWD
//
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