PRP17_HUMAN
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 03-AUG-2022, entry version 189.
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]
RP INVOLVEMENT IN PCH15, VARIANT PCH15 CYS-502, CHARACTERIZATION OF VARIANT
RP PCH15 CYS-502, FUNCTION, INTERACTION WITH PPIL1, AND MUTAGENESIS OF PRO-95.
RX PubMed=33220177; DOI=10.1016/j.neuron.2020.10.035;
RA Chai G., Webb A., Li C., Antaki D., Lee S., Breuss M.W., Lang N.,
RA Stanley V., Anzenberg P., Yang X., Marshall T., Gaffney P., Wierenga K.J.,
RA Chung B.H., Tsang M.H., Pais L.S., Lovgren A.K., VanNoy G.E., Rehm H.L.,
RA Mirzaa G., Leon E., Diaz J., Neumann A., Kalverda A.P., Manfield I.W.,
RA Parry D.A., Logan C.V., Johnson C.A., Bonthron D.T., Valleley E.M.A.,
RA Issa M.Y., Abdel-Ghafar S.F., Abdel-Hamid M.S., Jennings P., Zaki M.S.,
RA Sheridan E., Gleeson J.G.;
RT "Mutations in Spliceosomal Genes PPIL1 and PRP17 Cause Neurodegenerative
RT Pontocerebellar Hypoplasia with Microcephaly.";
RL Neuron 109:241-256(2021).
RN [16] {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 [17] {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 [18] {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 [19] {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 [20] {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 [21] {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 (PubMed:33220177). Plays an important role in embryonic
CC brain development; this function does not require proline isomerization
CC (PubMed:33220177). {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, ECO:0000269|PubMed:33220177,
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). Interacts with
CC PPIL1; this interaction leads to CDC40 isomerization (PubMed:33220177).
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, ECO:0000269|PubMed:33220177}.
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 -!- PTM: Undergoes isomerization of the peptide bond between Gly-94 and
CC Pro-95. The reaction is catalyzed by PPIL1.
CC {ECO:0000269|PubMed:33220177}.
CC -!- DISEASE: Pontocerebellar hypoplasia 15 (PCH15) [MIM:619302]: A form of
CC pontocerebellar hypoplasia, a disorder characterized by structural
CC defects of the pons and cerebellum, evident upon brain imaging. PCH15
CC is a severe autosomal recessive form characterized by progressive
CC microcephaly, and poor or absent psychomotor development with severely
CC impaired intellectual development apparent from birth. Other features
CC may include spastic quadriplegia, early-onset seizures, and chronic
CC anemia and thrombocytopenia. {ECO:0000269|PubMed:33220177}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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 AlphaFoldDB; O60508; -.
DR SMR; O60508; -.
DR BioGRID; 119497; 112.
DR CORUM; O60508; -.
DR IntAct; O60508; 33.
DR MINT; O60508; -.
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; 151 antibodies from 27 providers.
DR DNASU; 51362; -.
DR Ensembl; ENST00000307731.2; ENSP00000304370.1; ENSG00000168438.15.
DR Ensembl; ENST00000368932.5; ENSP00000357928.1; ENSG00000168438.15.
DR GeneID; 51362; -.
DR KEGG; hsa:51362; -.
DR MANE-Select; ENST00000307731.2; ENSP00000304370.1; NM_015891.3; NP_056975.1.
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 MIM; 619302; phenotype.
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; HKIQAGG; -.
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; 550 hits in 1087 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 middle temporal gyrus and 210 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:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:1990403; P:embryonic brain development; IMP: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; Disease variant; Intellectual disability; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW 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 VARIANT 502
FT /note="F -> C (in PCH15; in knockdown cells, unable to
FT rescue higher intron retention levels and to restore normal
FT cell viability, contrary to wild-type; reduced protein
FT levels in homozygous patient's fibroblasts compared to
FT heterozygous or wild-type cells; dbSNP:rs779945821)"
FT /evidence="ECO:0000269|PubMed:33220177"
FT /id="VAR_085515"
FT MUTAGEN 95
FT /note="P->A: Loss of isomerization. Can rescue splicing
FT defects when transfected in knockout cells."
FT /evidence="ECO:0000269|PubMed:33220177"
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
