U520_MOUSE
ID U520_MOUSE Reviewed; 2136 AA.
AC Q6P4T2; Q69ZZ3;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=U5 small nuclear ribonucleoprotein 200 kDa helicase;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:O75643};
DE AltName: Full=BRR2 homolog;
DE AltName: Full=U5 snRNP-specific 200 kDa protein;
DE Short=U5-200KD;
GN Name=Snrnp200; Synonyms=Kiaa0788;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 228-2136.
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1765, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; THR-2131; SER-2133 AND
RP SER-2135, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays role in pre-mRNA splicing as core component of
CC precatalytic, catalytic and postcatalytic spliceosomal complexes.
CC Involved in spliceosome assembly, activation and disassembly. Mediates
CC changes in the dynamic network of RNA-RNA interactions in the
CC spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA
CC duplices, an essential step in the assembly of a catalytically active
CC spliceosome. {ECO:0000250|UniProtKB:O75643}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:O75643};
CC -!- SUBUNIT: Component of a core complex containing at least PRPF8,
CC SNRNP200, EFTUD2 and SNRNP40. Component of the U5 snRNP and U4/U6-U5
CC tri-snRNP complexes, building blocks of the spliceosome. Component of
CC the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and
CC at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40,
CC DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39. Component of
CC precatalytic, catalytic and postcatalytic spliceosomal complexes.
CC {ECO:0000250|UniProtKB:O75643}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75643}.
CC -!- DOMAIN: Contains two helicase domains. The N-terminal helicase domain
CC has catalytic activity by itself, contrary to C-terminal helicase
CC domain that may have a regulatory role and enhance the activity of the
CC first helicase domain. {ECO:0000250|UniProtKB:O75643}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AL845368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063261; AAH63261.1; -; mRNA.
DR EMBL; AK173025; BAD32303.1; -; mRNA.
DR CCDS; CCDS16695.1; -.
DR RefSeq; NP_796188.2; NM_177214.4.
DR AlphaFoldDB; Q6P4T2; -.
DR SMR; Q6P4T2; -.
DR BioGRID; 236173; 66.
DR IntAct; Q6P4T2; 8.
DR MINT; Q6P4T2; -.
DR STRING; 10090.ENSMUSP00000099509; -.
DR iPTMnet; Q6P4T2; -.
DR PhosphoSitePlus; Q6P4T2; -.
DR SwissPalm; Q6P4T2; -.
DR EPD; Q6P4T2; -.
DR jPOST; Q6P4T2; -.
DR MaxQB; Q6P4T2; -.
DR PaxDb; Q6P4T2; -.
DR PeptideAtlas; Q6P4T2; -.
DR PRIDE; Q6P4T2; -.
DR ProteomicsDB; 298056; -.
DR Antibodypedia; 32425; 83 antibodies from 20 providers.
DR DNASU; 320632; -.
DR Ensembl; ENSMUST00000103220; ENSMUSP00000099509; ENSMUSG00000003660.
DR GeneID; 320632; -.
DR KEGG; mmu:320632; -.
DR UCSC; uc008mez.1; mouse.
DR CTD; 23020; -.
DR MGI; MGI:2444401; Snrnp200.
DR VEuPathDB; HostDB:ENSMUSG00000003660; -.
DR eggNOG; KOG0951; Eukaryota.
DR GeneTree; ENSGT00940000154966; -.
DR HOGENOM; CLU_000335_2_1_1; -.
DR InParanoid; Q6P4T2; -.
DR OMA; ESFWIIV; -.
DR OrthoDB; 154891at2759; -.
DR PhylomeDB; Q6P4T2; -.
DR TreeFam; TF300056; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR BioGRID-ORCS; 320632; 27 hits in 71 CRISPR screens.
DR ChiTaRS; Snrnp200; mouse.
DR PRO; PR:Q6P4T2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q6P4T2; protein.
DR Bgee; ENSMUSG00000003660; Expressed in manus and 220 other tissues.
DR Genevisible; Q6P4T2; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; ISS:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISO:MGI.
DR GO; GO:0005682; C:U5 snRNP; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000388; P:spliceosome conformational change to release U4 (or U4atac) and U1 (or U11); IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.40.50.300; -; 4.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
DR SUPFAM; SSF52540; SSF52540; 4.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 2.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Coiled coil; Helicase; Hydrolase;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW Spliceosome; Ubl conjugation.
FT CHAIN 1..2136
FT /note="U5 small nuclear ribonucleoprotein 200 kDa helicase"
FT /id="PRO_0000422049"
FT DOMAIN 490..673
FT /note="Helicase ATP-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 684..921
FT /note="Helicase C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 982..1286
FT /note="SEC63 1"
FT DOMAIN 1337..1512
FT /note="Helicase ATP-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1545..1753
FT /note="Helicase C-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1812..2124
FT /note="SEC63 2"
FT REGION 39..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 54..84
FT /evidence="ECO:0000255"
FT MOTIF 615..618
FT /note="DEAH box"
FT MOTIF 1454..1457
FT /note="DEAH box"
FT COMPBIAS 51..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 503..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1350..1357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 389
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT MOD_RES 709
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:F1LNJ2"
FT MOD_RES 971
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT MOD_RES 1428
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT MOD_RES 1765
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 2002
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT MOD_RES 2131
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT CROSSLNK 944
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 971
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 1071
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 1199
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 2091
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2136 AA; 244547 MW; BBDD6058CA635519 CRC64;
MADVTARSLQ YEYKANSNLV LQADRSLIDR TRRDEPTGEV LSLVGKLEGT RMGDKAQRTK
PQMQEERRAK RRKRDEDRHD MNKMKGYTLL SEGIDEMVGI IYKPKTKETR ETYEVLLSFI
QAALGDQPRD ILCGAADEVL AVLKNEKLRD KERRREIDLL LGQTDDTRYH VLVNLGKKIT
DYGGDKEIQN MDDNIDETYG VNVQFESDEE EGDEDVYGEV REEASDDDME GDEAVVRCTL
SANLVASGEL MSSKKKDLHP RDIDAFWLQR QLSRFYDDAI VSQKKADEVL EILKTASDDR
ECENQLVLLL GFNTFDFIKV LRQHRMMILY CTLLASAQSE PEKERIVGKM EADPELSKFL
YQLHETEKED LIREERSRRE RVRQSRMDTD LETMDLDQGG EALAPRQVLD LEDLVFTQGS
HFMANKRCQL PDGSFRRQRK GYEEVHVPAL KPKPFGSEEQ LLPVEKLPKY AQAGFEGFKT
LNRIQSKLYR AALETDENLL LCAPTGAGKT NVALMCMLRE IGKHINMDGT INVDDFKIIY
IAPMRSLVQE MVGSFGKRLA TYGITVAELT GDHQLCKEEI SATQIIVCTP EKWDIITRKG
GERTYTQLVR LIVLDEIHLL HDDRGPVLEA LVARAIRNIE MTQEDVRLIG LSATLPNYED
VATFLRVDPA KGLFYFDNSF RPVPLEQTYV GITEKKAIKR FQIMNEIVYE KIMEHAGKNQ
VLVFVHSRKE TGKTARAIRD MCLEKDTLGL FLREGSASTE VLRTEAEQCK NLELKDLLPY
GFAIHHAGMT RVDRTLVEDL FADKHIQVLV STATLAWGVN LPAHTVIIKG TQVYSPEKGR
WTELGALDIL QMLGRAGRPQ YDTKGEGILI TSHGELQYYL SLLNQQLPIE SQMVSKLPDM
LNAEIVLGNV QNAKDAVNWL GYAYLYIRML RSPTLYGISH DDLKGDPLLD QRRLDLVHTA
ALMLDKNNLV KYDKKTGNFQ VTELGRIASH YYITNDTVQT YNQLLKPTLS EIELFRVFSL
SSEFKNITVR EEEKLELQKL LERVPIPVKE SIEEPSAKIN VLLQAFISQL KLEGFALMAD
MVYVTQSAGR LMRAIFEIVL NRGWAQLTDK TLNLCKMIDK RMWQSMCPLR QFRKLPEEVV
KKIEKKNFPF ERLYDLNHNE IGELIRMPKM GKTIHKYVHL FPKLELSVHL QPITRSTLKV
ELTITPDFQW DEKVHGSSEA FWILVEDVDS EVILHHEYFL LKAKYAQDEH LITFFVPVFE
PLPPQYFIRV VSDRWLSCET QLPVSFRHLI LPEKYPPPTE LLDLQPLPVS ALRNSAFESL
YQDKFPFFNP IQTQVFNTVY NSDDNVFVGA PTGSGKTICA EFAILRMLLQ NSEGRCVYIT
PMEALAEQVY MDWYEKFQDR LNKKVVLLTG ETSTDLKLLG KGNIIISTPE KWDILSRRWK
QRKNVQNINL FVVDEVHLIG GENGPVLEVI CSRMRYISSQ IERPIRIVAL SSSLSNAKDV
AHWLGCSATS TFNFHPNVRP VPLELHIQGF NISHTQTRLL SMAKPVYHAI TKHSPKKPVI
VFVPSRKQTR LTAIDILTTC AADIQRQRFL HCTEKDLIPY LEKLSDSTLK ETLLNGVGYL
HEGLSPMERR LVEQLFSSGA IQVVVASRSL CWGMNVAAHL VIIMDTQYYN GKIHAYVDYP
IYDVLQMVGH ANRPLQDDEG RCVIMCQGSK KDFFKKFLYE PLPVESHLDH CMHDHFNAEI
VTKTIENKQD AVDYLTWTFL YRRMTQNPNY YNLQGISHRH LSDHLSELVE QTLSDLEQSK
CISIEDEMDV APLNLGMIAA YYYINYTTIE LFSMSLNAKT KVRGLIEIIS NAAEYENIPI
RHHEDNLLRQ LAQKVPHKLN NPKFNDPHVK TNLLLQAHLS RMQLSAELQS DTEEILSKAI
RLIQACVDVL SSNGWLSPAL AAMELAQMVT QAMWSKDSYL KQLPHFTSEH IKRCTDKGVE
SVFDIMEMED EERNALLQLT DSQIADVARF CNRYPNIELS YEVVDKDSIR SGGPVVVLVQ
LEREEEVTGP VIAPLFPQKR EEGWWVVIGD AKSNSLISIK RLTLQQKAKV KLDFVAPATG
GHNYTLYFMS DAYMGCDQEY KFSVDVKEAE TDSDSD
