GenomeNet

Database: UniProt
Entry: Q96DI7
LinkDB: Q96DI7
Original site: Q96DI7 
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   29-SEP-2021, entry version 189.
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};
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   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   SMR; Q96DI7; -.
DR   BioGRID; 114805; 124.
DR   CORUM; Q96DI7; -.
DR   IntAct; Q96DI7; 68.
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; 130 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   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; CENYGVL; -.
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; 613 hits in 1034 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:sno(s)RNA-containing 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; 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:6ID0"
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:6ICZ"
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:6ZYM"
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
//
DBGET integrated database retrieval system