SNUT1_HUMAN
ID SNUT1_HUMAN Reviewed; 800 AA.
AC O43290; A6NDN1; Q53GB5;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=U4/U6.U5 tri-snRNP-associated protein 1;
DE AltName: Full=SNU66 homolog;
DE Short=hSnu66;
DE AltName: Full=Squamous cell carcinoma antigen recognized by T-cells 1;
DE Short=SART-1;
DE Short=hSART-1;
DE AltName: Full=U4/U6.U5 tri-snRNP-associated 110 kDa protein;
DE AltName: Allergen=Hom s 1;
GN Name=SART1;
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], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=9449708; DOI=10.1084/jem.187.3.277;
RA Shichijo S., Nakao M., Imai Y., Takasu H., Kawamoto M., Niiya F., Yang D.,
RA Toh Y., Yamana H., Itoh K.;
RT "A gene encoding antigenic peptides of human squamous cell carcinoma
RT recognized cytotoxic T lymphocytes.";
RL J. Exp. Med. 187:277-288(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, FUNCTION, AND SUBUNIT.
RX PubMed=11350945; DOI=10.1093/emboj/20.10.2553;
RA Makarova O.V., Makarov E.M., Luehrmann R.;
RT "The 65 and 110 kDa SR-related proteins of the U4/U6*U5 tri-snRNP are
RT essential for the assembly of mature spliceosomes.";
RL EMBO J. 20:2553-2563(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-485.
RC TISSUE=Small intestine;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 639-732.
RX PubMed=11410364; DOI=10.1016/s0378-1119(01)00504-2;
RA Bolland D.J., Hewitt J.E.;
RT "Intron loss in the SART1 genes of Fugu rubripes and Tetraodon
RT nigroviridis.";
RL Gene 271:43-49(2001).
RN [8]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RX PubMed=9856836; DOI=10.1046/j.1523-1747.1998.00413.x;
RA Valenta R., Natter S., Seiberler S., Wichlas S., Maurer D., Hess M.,
RA Pavelka M., Grote M., Ferreira F., Szepfalusi Z., Valent P., Stingl G.;
RT "Molecular characterization of an autoallergen, Hom s 1, identified by
RT serum IgE from atopic dermatitis patients.";
RL J. Invest. Dermatol. 111:1178-1183(1998).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448 AND SER-591, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-430 AND THR-695, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-392; SER-448 AND SER-486, AND
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-430; SER-448 AND THR-764, AND
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-521; SER-591;
RP SER-596 AND SER-598, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION BY
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-348; THR-392;
RP THR-430; SER-448; SER-761 AND SER-789, AND IDENTIFICATION BY MASS
RP 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474 AND SER-621, AND
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 [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-141; LYS-147 AND LYS-188, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-141, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-141; LYS-147 AND LYS-188, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-141; LYS-147 AND LYS-188, AND
RP IDENTIFICATION BY MASS 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 [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-125; LYS-133; LYS-141; LYS-147;
RP LYS-188; LYS-277; LYS-329; LYS-336; LYS-400; LYS-414; LYS-548; LYS-648;
RP LYS-657; LYS-684; LYS-699; LYS-709; LYS-723; LYS-749; LYS-758; LYS-775;
RP LYS-780 AND LYS-791, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
CC -!- FUNCTION: Plays a role in mRNA splicing as a component of the U4/U6-U5
CC tri-snRNP, one of the building blocks of the spliceosome. May also bind
CC to DNA. {ECO:0000269|PubMed:11350945}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Component of the
CC U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at
CC least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40,
CC DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39.
CC {ECO:0000269|PubMed:11350945, ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:16723661}.
CC -!- INTERACTION:
CC O43290; O75031: HSF2BP; NbExp=6; IntAct=EBI-607761, EBI-7116203;
CC O43290; O43395: PRPF3; NbExp=4; IntAct=EBI-607761, EBI-744322;
CC O43290; O94906: PRPF6; NbExp=4; IntAct=EBI-607761, EBI-536755;
CC O43290; O75643: SNRNP200; NbExp=5; IntAct=EBI-607761, EBI-1045395;
CC O43290; Q13573: SNW1; NbExp=3; IntAct=EBI-607761, EBI-632715;
CC O43290; P63165: SUMO1; NbExp=2; IntAct=EBI-607761, EBI-80140;
CC O43290; P55854: SUMO3; NbExp=2; IntAct=EBI-607761, EBI-474067;
CC O43290; Q9BZL1: UBL5; NbExp=4; IntAct=EBI-607761, EBI-607755;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11350945,
CC ECO:0000269|PubMed:9449708}. Note=Found in the nucleus of mitogen-
CC activated peripheral blood mononuclear cells (PBMCs), tumor cells, or
CC normal cell lines, but not in normal tissues except testis and fetal
CC liver or in unstimulated PBMCs, suggesting preferential expression in
CC proliferating cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms may be produced.;
CC Name=1; Synonyms=125 kDa;
CC IsoId=O43290-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:9449708}.
CC -!- PTM: Sumoylated with SUMO2.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE from
CC atopic dermatitis (AD) patients. Identified as an IgE autoantigen in
CC atopic dermatitis (AD) patients with severe skin manifestations.
CC {ECO:0000269|PubMed:9856836}.
CC -!- SIMILARITY: Belongs to the SNU66/SART1 family. {ECO:0000305}.
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DR EMBL; AB006198; BAA24056.1; -; mRNA.
DR EMBL; AF353625; AAK49523.1; -; mRNA.
DR EMBL; BT006637; AAP35283.1; -; mRNA.
DR EMBL; AK223016; BAD96736.1; -; mRNA.
DR EMBL; AP006287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001058; AAH01058.1; -; mRNA.
DR EMBL; AF109680; AAD20223.1; -; Genomic_DNA.
DR CCDS; CCDS31611.1; -. [O43290-1]
DR PIR; T00034; T00034.
DR RefSeq; NP_005137.1; NM_005146.4. [O43290-1]
DR PDB; 4PYU; X-ray; 2.00 A; C/D/H/L/P/T=117-135.
DR PDB; 5O9Z; EM; 4.50 A; P=1-800.
DR PDB; 6AHD; EM; 3.80 A; 9=1-800.
DR PDB; 6QW6; EM; 2.92 A; S=1-800.
DR PDB; 6QX9; EM; 3.28 A; S=1-800.
DR PDBsum; 4PYU; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR AlphaFoldDB; O43290; -.
DR SMR; O43290; -.
DR BioGRID; 114546; 247.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; O43290; -.
DR DIP; DIP-33360N; -.
DR IntAct; O43290; 67.
DR MINT; O43290; -.
DR STRING; 9606.ENSP00000310448; -.
DR Allergome; 3322; Hom s 1.0101.
DR Allergome; 411; Hom s 1.
DR GlyGen; O43290; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43290; -.
DR MetOSite; O43290; -.
DR PhosphoSitePlus; O43290; -.
DR BioMuta; SART1; -.
DR EPD; O43290; -.
DR jPOST; O43290; -.
DR MassIVE; O43290; -.
DR MaxQB; O43290; -.
DR PaxDb; O43290; -.
DR PeptideAtlas; O43290; -.
DR PRIDE; O43290; -.
DR ProteomicsDB; 48858; -. [O43290-1]
DR Antibodypedia; 30019; 219 antibodies from 36 providers.
DR DNASU; 9092; -.
DR Ensembl; ENST00000312397.10; ENSP00000310448.5; ENSG00000175467.15. [O43290-1]
DR GeneID; 9092; -.
DR KEGG; hsa:9092; -.
DR MANE-Select; ENST00000312397.10; ENSP00000310448.5; NM_005146.5; NP_005137.1.
DR UCSC; uc001ogl.4; human. [O43290-1]
DR CTD; 9092; -.
DR DisGeNET; 9092; -.
DR GeneCards; SART1; -.
DR HGNC; HGNC:10538; SART1.
DR HPA; ENSG00000175467; Low tissue specificity.
DR MIM; 605941; gene.
DR neXtProt; NX_O43290; -.
DR OpenTargets; ENSG00000175467; -.
DR PharmGKB; PA34947; -.
DR VEuPathDB; HostDB:ENSG00000175467; -.
DR eggNOG; KOG2217; Eukaryota.
DR GeneTree; ENSGT00390000007071; -.
DR HOGENOM; CLU_009379_3_0_1; -.
DR InParanoid; O43290; -.
DR OMA; EYARWEN; -.
DR OrthoDB; 1068640at2759; -.
DR PhylomeDB; O43290; -.
DR TreeFam; TF318828; -.
DR PathwayCommons; O43290; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; O43290; -.
DR BioGRID-ORCS; 9092; 592 hits in 1083 CRISPR screens.
DR ChiTaRS; SART1; human.
DR GeneWiki; SART1; -.
DR GenomeRNAi; 9092; -.
DR Pharos; O43290; Tbio.
DR PRO; PR:O43290; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O43290; protein.
DR Bgee; ENSG00000175467; Expressed in tendon of biceps brachii and 205 other tissues.
DR ExpressionAtlas; O43290; baseline and differential.
DR Genevisible; O43290; HS.
DR GO; GO:0015030; C:Cajal body; IDA:BHF-UCL.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IPI:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000481; P:maturation of 5S rRNA; IBA:GO_Central.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0045585; P:positive regulation of cytotoxic T cell differentiation; IDA:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; TAS:BHF-UCL.
DR InterPro; IPR045347; HIND.
DR InterPro; IPR005011; SNU66/SART1.
DR PANTHER; PTHR14152; PTHR14152; 1.
DR Pfam; PF19252; HIND; 1.
DR Pfam; PF03343; SART-1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Alternative splicing; Coiled coil; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome; Ubl conjugation.
FT CHAIN 1..800
FT /note="U4/U6.U5 tri-snRNP-associated protein 1"
FT /id="PRO_0000223308"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 157..231
FT /evidence="ECO:0000255"
FT COILED 490..533
FT /evidence="ECO:0000255"
FT COMPBIAS 44..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 189
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z315"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 392
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 430
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 695
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 764
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 789
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 188
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 329
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 336
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 414
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 548
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 648
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 657
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 684
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 699
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 709
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 723
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 749
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 758
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 775
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 780
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 791
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 245
FT /note="R -> C (in dbSNP:rs688862)"
FT /id="VAR_051367"
FT VARIANT 463
FT /note="S -> A (in dbSNP:rs35036096)"
FT /id="VAR_034504"
FT VARIANT 485
FT /note="G -> A (in dbSNP:rs660118)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025319"
FT CONFLICT 209
FT /note="Q -> R (in Ref. 4; BAD96736)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="Y -> H (in Ref. 4; BAD96736)"
FT /evidence="ECO:0000305"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:4PYU"
SQ SEQUENCE 800 AA; 90255 MW; B13525E80640DF9E CRC64;
MGSSKKHRGE KEAAGTTAAA GTGGATEQPP RHREHKKHKH RSGGSGGSGG ERRKRSRERG
GERGSGRRGA EAEARSSTHG RERSQAEPSE RRVKREKRDD GYEAAASSKT SSGDASSLSI
EETNKLRAKL GLKPLEVNAI KKEAGTKEEP VTADVINPMA LRQREELREK LAAAKEKRLL
NQKLGKIKTL GEDDPWLDDT AAWIERSRQL QKEKDLAEKR AKLLEEMDQE FGVSTLVEEE
FGQRRQDLYS ARDLQGLTVE HAIDSFREGE TMILTLKDKG VLQEEEDVLV NVNLVDKERA
EKNVELRKKK PDYLPYAEDE SVDDLAQQKP RSILSKYDEE LEGERPHSFR LEQGGTADGL
RERELEEIRA KLRLQAQSLS TVGPRLASEY LTPEEMVTFK KTKRRVKKIR KKEKEVVVRA
DDLLPLGDQT QDGDFGSRLR GRGRRRVSEV EEEKEPVPQP LPSDDTRVEN MDISDEEEGG
APPPGSPQVL EEDEAELELQ KQLEKGRRLR QLQQLQQLRD SGEKVVEIVK KLESRQRGWE
EDEDPERKGA IVFNATSEFC RTLGEIPTYG LAGNREEQEE LMDFERDEER SANGGSESDG
EENIGWSTVN LDEEKQQQDF SASSTTILDE EPIVNRGLAA ALLLCQNKGL LETTVQKVAR
VKAPNKSLPS AVYCIEDKMA IDDKYSRREE YRGFTQDFKE KDGYKPDVKI EYVDETGRKL
TPKEAFRQLS HRFHGKGSGK MKTERRMKKL DEEALLKKMS SSDTPLGTVA LLQEKQKAQK
TPYIVLSGSG KSMNANTITK
