ID SNR40_HUMAN Reviewed; 357 AA. AC Q96DI7; B4DQJ1; O75938; O95320; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 12-AUG-2020, entry version 183. DE RecName: Full=U5 small nuclear ribonucleoprotein 40 kDa protein; DE Short=U5 snRNP 40 kDa protein; DE Short=U5-40K; DE AltName: Full=38 kDa-splicing factor; DE AltName: Full=Prp8-binding protein; DE Short=hPRP8BP; DE AltName: Full=U5 snRNP-specific 40 kDa protein; DE AltName: Full=WD repeat-containing protein 57; GN Name=SNRNP40; Synonyms=PRP8BP, SFP38, WDR57; 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] (ISOFORM 1), FUNCTION, IDENTIFICATION IN U5 SNRP RP COMPLEX, AND INTERACTION WITH PRPF8. RX PubMed=9774689; DOI=10.1128/mcb.18.11.6756; RA Achsel T., Ahrens K., Brahms H., Teigelkamp S., Luehrmann R.; RT "The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with RT several U5-specific proteins, including an RNA unwindase, a homologue of RT ribosomal elongation factor EF-2, and a novel WD-40 protein."; RL Mol. Cell. Biol. 18:6756-6766(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 60-357 (ISOFORM 1), IDENTIFICATION BY MASS RP SPECTROMETRY, SUBCELLULAR LOCATION, AND IDENTIFICATION IN SPLICEOSOMAL RP COMPLEX. RX PubMed=9731529; DOI=10.1038/1700; RA Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P., RA Sleeman J., Lamond A.I., Mann M.; RT "Mass spectrometry and EST-database searching allows characterization of RT the multi-protein spliceosome complex."; RL Nat. Genet. 20:46-50(1998). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOME 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 [7] RP SUBUNIT. RX PubMed=16723661; DOI=10.1261/rna.55406; RA Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.; RT "The network of protein-protein interactions within the human U4/U6.U5 tri- RT snRNP."; RL RNA 12:1418-1430(2006). RN [8] 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 [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [10] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-270, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [11] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-18 AND LYS-270, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [12] {ECO:0000244|PDB:3JCR} RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), IDENTIFICATION BY MASS RP SPECTROMETRY, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=26912367; DOI=10.1126/science.aad2085; RA Agafonov D.E., Kastner B., Dybkov O., Hofele R.V., Liu W.T., Urlaub H., RA Luhrmann R., Stark H.; RT "Molecular architecture of the human U4/U6.U5 tri-snRNP."; RL Science 351:1416-1420(2016). RN [13] {ECO:0000244|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 [14] {ECO:0000244|PDB:5O9Z} RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011; RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N., RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.; RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for RT Activation."; RL Cell 170:701-713(2017). RN [15] {ECO:0000244|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 [16] {ECO:0000244|PDB:6AH0, ECO:0000244|PDB:6AHD} RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=30315277; DOI=10.1038/s41422-018-0094-7; RA Zhan X., Yan C., Zhang X., Lei J., Shi Y.; RT "Structures of the human pre-catalytic spliceosome and its precursor RT spliceosome."; RL Cell Res. 0:0-0(2018). RN [17] {ECO:0000244|PDB:5Z56, ECO:0000244|PDB:5Z57, ECO:0000244|PDB:5Z58} RP STRUCTURE BY ELECTRON MICROSCOPY (4.90 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 [18] {ECO:0000244|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 [19] {ECO:0000244|PDB:6QDV} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 51-357, 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:11991638, PubMed:28502770, PubMed:28781166, CC PubMed:28076346, PubMed:30315277, PubMed:29360106, PubMed:29301961, CC PubMed:30705154). Component of the U5 small nuclear ribonucleoprotein CC (snRNP) complex and the U4/U6-U5 tri-snRNP complex, building blocks of CC the spliceosome (PubMed:9774689, PubMed:16723661, PubMed:26912367). CC {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:16723661, CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346, CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166, CC ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, CC ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:30705154, CC ECO:0000269|PubMed:9774689}. CC -!- SUBUNIT: Component of the pre-catalytic and catalytic spliceosome CC complexes (PubMed:9731529, PubMed:11991638, PubMed:28502770, CC PubMed:28781166, PubMed:28076346, PubMed:30315277, PubMed:29360106, CC PubMed:29301961). Component of the postcatalytic spliceosome P complex CC (PubMed:30705154). Part of the U5 snRNP complex. Interacts with PRPF8. CC Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and CC U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, CC TXNL4A, WDR57, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and CC USP39 (PubMed:16723661). {ECO:0000269|PubMed:11991638, CC ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:28076346, CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166, CC ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, CC ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:30705154, CC ECO:0000269|PubMed:9731529, ECO:0000269|PubMed:9774689}. CC -!- INTERACTION: CC Q96DI7; Q9BUQ8: DDX23; NbExp=2; IntAct=EBI-538492, EBI-540096; CC Q96DI7; Q15029: EFTUD2; NbExp=2; IntAct=EBI-538492, EBI-357897; CC Q96DI7; Q6P2Q9: PRPF8; NbExp=4; IntAct=EBI-538492, EBI-538479; CC Q96DI7; O75643: SNRNP200; NbExp=2; IntAct=EBI-538492, EBI-1045395; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26912367, CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, CC ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:29301961, CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:30315277, CC ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:9731529}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96DI7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96DI7-2; Sequence=VSP_056395; CC -!- SEQUENCE CAUTION: CC Sequence=AAC64084.1; Type=Frameshift; Note=An insertion/deletion of a short nucleotide stretch in its cDNA resulting in a frameshift.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF090988; AAC69625.1; -; mRNA. DR EMBL; AK298823; BAG60953.1; -; mRNA. DR EMBL; AC114495; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL451070; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001494; AAH01494.1; -; mRNA. DR EMBL; AF083383; AAC64084.1; ALT_SEQ; mRNA. DR CCDS; CCDS340.1; -. [Q96DI7-1] DR RefSeq; NP_004805.2; NM_004814.2. [Q96DI7-1] DR PDB; 3JCR; EM; 7.00 A; D=1-357. DR PDB; 5MQF; EM; 5.90 A; F=1-357. DR PDB; 5O9Z; EM; 4.50 A; D=1-357. DR PDB; 5XJC; EM; 3.60 A; E=1-357. DR PDB; 5YZG; EM; 4.10 A; E=1-357. DR PDB; 5Z56; EM; 5.10 A; E=1-357. DR PDB; 5Z57; EM; 6.50 A; E=1-357. DR PDB; 5Z58; EM; 4.90 A; E=1-357. DR PDB; 6AH0; EM; 5.70 A; E=1-357. DR PDB; 6AHD; EM; 3.80 A; E=1-357. DR PDB; 6FF7; EM; 4.50 A; F=1-357. DR PDB; 6ICZ; EM; 3.00 A; E=1-357. DR PDB; 6ID0; EM; 2.90 A; E=1-357. DR PDB; 6ID1; EM; 2.86 A; E=1-357. DR PDB; 6QDV; EM; 3.30 A; N=51-357. DR PDB; 6QW6; EM; 2.92 A; 5O=1-357. DR PDB; 6QX9; EM; 3.28 A; 5O=1-357. DR PDBsum; 3JCR; -. DR PDBsum; 5MQF; -. DR PDBsum; 5O9Z; -. DR PDBsum; 5XJC; -. DR PDBsum; 5YZG; -. DR PDBsum; 5Z56; -. DR PDBsum; 5Z57; -. DR PDBsum; 5Z58; -. DR PDBsum; 6AH0; -. DR PDBsum; 6AHD; -. DR PDBsum; 6FF7; -. DR PDBsum; 6ICZ; -. DR PDBsum; 6ID0; -. DR PDBsum; 6ID1; -. DR PDBsum; 6QDV; -. DR PDBsum; 6QW6; -. DR PDBsum; 6QX9; -. DR SMR; Q96DI7; -. DR BioGRID; 114805; 97. DR CORUM; Q96DI7; -. DR IntAct; Q96DI7; 58. DR MINT; Q96DI7; -. DR STRING; 9606.ENSP00000263694; -. DR iPTMnet; Q96DI7; -. DR PhosphoSitePlus; Q96DI7; -. DR SwissPalm; Q96DI7; -. DR BioMuta; SNRNP40; -. DR DMDM; 67462075; -. DR EPD; Q96DI7; -. DR jPOST; Q96DI7; -. DR MassIVE; Q96DI7; -. DR MaxQB; Q96DI7; -. DR PaxDb; Q96DI7; -. DR PeptideAtlas; Q96DI7; -. DR PRIDE; Q96DI7; -. DR ProteomicsDB; 4882; -. DR ProteomicsDB; 76291; -. [Q96DI7-1] DR TopDownProteomics; Q96DI7-1; -. [Q96DI7-1] DR Antibodypedia; 16742; 123 antibodies. DR DNASU; 9410; -. DR Ensembl; ENST00000263694; ENSP00000263694; ENSG00000060688. [Q96DI7-1] DR GeneID; 9410; -. DR KEGG; hsa:9410; -. DR UCSC; uc001bso.4; human. [Q96DI7-1] DR CTD; 9410; -. DR DisGeNET; 9410; -. DR EuPathDB; HostDB:ENSG00000060688.12; -. DR GeneCards; SNRNP40; -. DR HGNC; HGNC:30857; SNRNP40. DR HPA; ENSG00000060688; Low tissue specificity. DR MIM; 607797; gene. DR neXtProt; NX_Q96DI7; -. DR OpenTargets; ENSG00000060688; -. DR PharmGKB; PA164726132; -. DR eggNOG; KOG0265; Eukaryota. DR GeneTree; ENSGT00940000155058; -. DR HOGENOM; CLU_000288_57_2_1; -. DR InParanoid; Q96DI7; -. DR KO; K12857; -. DR OMA; NTCYPAR; -. DR OrthoDB; 606683at2759; -. DR PhylomeDB; Q96DI7; -. DR TreeFam; TF300039; -. DR PathwayCommons; Q96DI7; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway. DR SignaLink; Q96DI7; -. DR BioGRID-ORCS; 9410; 573 hits in 887 CRISPR screens. DR ChiTaRS; SNRNP40; human. DR GeneWiki; WDR57; -. DR GenomeRNAi; 9410; -. DR Pharos; Q96DI7; Tbio. DR PRO; PR:Q96DI7; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q96DI7; protein. DR Bgee; ENSG00000060688; Expressed in lung and 213 other tissues. DR ExpressionAtlas; Q96DI7; baseline and differential. DR Genevisible; Q96DI7; HS. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005732; C:small nucleolar ribonucleoprotein complex; NAS:UniProtKB. DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0005682; C:U5 snRNP; TAS:ProtInc. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome. DR GO; GO:0006396; P:RNA processing; TAS:ProtInc. DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc. DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB. DR Gene3D; 2.130.10.10; -; 1. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR001680; WD40_repeat. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR017986; WD40_repeat_dom. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR Pfam; PF00400; WD40; 7. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF50978; SSF50978; 1. DR PROSITE; PS00678; WD_REPEATS_1; 5. DR PROSITE; PS50082; WD_REPEATS_2; 7. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Isopeptide bond; Methylation; KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat; KW Spliceosome; Ubl conjugation; WD repeat. FT CHAIN 1..357 FT /note="U5 small nuclear ribonucleoprotein 40 kDa protein" FT /id="PRO_0000051417" FT REPEAT 64..103 FT /note="WD 1" FT REPEAT 107..146 FT /note="WD 2" FT REPEAT 149..189 FT /note="WD 3" FT REPEAT 191..230 FT /note="WD 4" FT REPEAT 233..272 FT /note="WD 5" FT REPEAT 283..322 FT /note="WD 6" FT REPEAT 325..357 FT /note="WD 7" FT MOD_RES 21 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:Q6PE01" FT CROSSLNK 18 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 270 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:25755297, FT ECO:0000244|PubMed:28112733" FT VAR_SEQ 343..357 FT /note="ISASSDKRLYMGEIQ -> ETGFHRIGQGGHELLTSSNPPASASQSAGITGV FT SHCAQLQTVFMWVSMSVSPLLISGESKSNAPFSS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056395" FT CONFLICT 3 FT /note="E -> D (in Ref. 1; AAC69625)" FT /evidence="ECO:0000305" FT CONFLICT 162..163 FT /note="RG -> KS (in Ref. 1; AAC69625)" FT /evidence="ECO:0000305" FT CONFLICT 187 FT /note="I -> V (in Ref. 5; AAC64084)" FT /evidence="ECO:0000305" FT CONFLICT 343 FT /note="I -> L (in Ref. 5)" FT /evidence="ECO:0000305" FT STRAND 56..62 FT /evidence="ECO:0000244|PDB:6ID0" FT STRAND 71..74 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 76..84 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 90..96 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 101..104 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 112..117 FT /evidence="ECO:0000244|PDB:6ID0" FT STRAND 119..121 FT /evidence="ECO:0000244|PDB:6ID0" FT STRAND 122..127 FT /evidence="ECO:0000244|PDB:6ID1" FT TURN 129..131 FT /evidence="ECO:0000244|PDB:6ICZ" FT STRAND 133..137 FT /evidence="ECO:0000244|PDB:6ID1" FT TURN 138..140 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 143..147 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 154..159 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 161..164 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 167..171 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 174..179 FT /evidence="ECO:0000244|PDB:6ID1" FT TURN 181..183 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 184..191 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 196..201 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 207..215 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 217..221 FT /evidence="ECO:0000244|PDB:6ID1" FT TURN 222..224 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 226..231 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 238..243 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 247..254 FT /evidence="ECO:0000244|PDB:6ID1" FT TURN 255..257 FT /evidence="ECO:0000244|PDB:6ICZ" FT STRAND 259..263 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 275..277 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 291..293 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 297..302 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 309..313 FT /evidence="ECO:0000244|PDB:6ID1" FT TURN 314..316 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 319..323 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 330..335 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 337..346 FT /evidence="ECO:0000244|PDB:6ID1" FT STRAND 349..355 FT /evidence="ECO:0000244|PDB:6ID1" SQ SEQUENCE 357 AA; 39311 MW; DE8CADEB098E560C CRC64; MIEQQKRKGP ELPLVPVKRQ RHELLLGAGS GPGAGQQQAT PGALLQAGPP RCSSLQAPIM LLSGHEGEVY CCKFHPNGST LASAGFDRLI LLWNVYGDCD NYATLKGHSG AVMELHYNTD GSMLFSASTD KTVAVWDSET GERVKRLKGH TSFVNSCYPA RRGPQLVCTG SDDGTVKLWD IRKKAAIQTF QNTYQVLAVT FNDTSDQIIS GGIDNDIKVW DLRQNKLTYT MRGHADSVTG LSLSSEGSYL LSNAMDNTVR VWDVRPFAPK ERCVKIFQGN VHNFEKNLLR CSWSPDGSKI AAGSADRFVY VWDTTSRRIL YKLPGHAGSI NEVAFHPDEP IIISASSDKR LYMGEIQ //