SNR40_HUMAN
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 03-AUG-2022, entry version 192.
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:0007744|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: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 [14] {ECO:0007744|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: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 [16] {ECO:0007744|PDB:6AH0, ECO:0007744|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. 28:1129-1140(2018).
RN [17] {ECO:0007744|PDB:5Z56, ECO:0007744|PDB:5Z57, ECO:0007744|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: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 [19] {ECO:0007744|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; P54253: ATXN1; NbExp=3; IntAct=EBI-538492, EBI-930964;
CC Q96DI7; Q9BUQ8: DDX23; NbExp=2; IntAct=EBI-538492, EBI-540096;
CC Q96DI7; Q15029: EFTUD2; NbExp=2; IntAct=EBI-538492, EBI-357897;
CC Q96DI7; P14136: GFAP; NbExp=3; IntAct=EBI-538492, EBI-744302;
CC Q96DI7; P28799: GRN; NbExp=3; IntAct=EBI-538492, EBI-747754;
CC Q96DI7; D3DTS7: PMP22; NbExp=3; IntAct=EBI-538492, EBI-25882629;
CC Q96DI7; O60260-5: PRKN; NbExp=3; IntAct=EBI-538492, EBI-21251460;
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};
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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 PDB; 6ZYM; EM; 3.40 A; F=1-357.
DR PDB; 7ABG; EM; 7.80 A; D=1-357.
DR PDB; 7ABI; EM; 8.00 A; D=1-357.
DR PDB; 7DVQ; EM; 2.89 A; E=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 PDBsum; 6ZYM; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABI; -.
DR PDBsum; 7DVQ; -.
DR AlphaFoldDB; Q96DI7; -.
DR SMR; Q96DI7; -.
DR BioGRID; 114805; 146.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; Q96DI7; -.
DR IntAct; Q96DI7; 72.
DR MINT; Q96DI7; -.
DR STRING; 9606.ENSP00000263694; -.
DR GlyGen; Q96DI7; 1 site, 1 O-linked glycan (1 site).
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; 131 antibodies from 17 providers.
DR DNASU; 9410; -.
DR Ensembl; ENST00000263694.9; ENSP00000263694.4; ENSG00000060688.13. [Q96DI7-1]
DR GeneID; 9410; -.
DR KEGG; hsa:9410; -.
DR MANE-Select; ENST00000263694.9; ENSP00000263694.4; NM_004814.3; NP_004805.2.
DR UCSC; uc001bso.4; human. [Q96DI7-1]
DR CTD; 9410; -.
DR DisGeNET; 9410; -.
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 VEuPathDB; HostDB:ENSG00000060688; -.
DR eggNOG; KOG0265; Eukaryota.
DR GeneTree; ENSGT00940000155058; -.
DR HOGENOM; CLU_000288_57_2_1; -.
DR InParanoid; Q96DI7; -.
DR OMA; WDLRKNA; -.
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; 619 hits in 1090 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 ganglionic eminence and 175 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:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; NAS:UniProtKB.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IPI:ComplexPortal.
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; IC:UniProtKB.
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; 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:0007744|PubMed:28112733"
FT CROSSLNK 270
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|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:0007829|PDB:6ID0"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6ID0"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 337..346
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 349..355
FT /evidence="ECO:0007829|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
