ID CDC5L_HUMAN Reviewed; 802 AA. AC Q99459; Q76N46; Q99974; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2005, sequence version 2. DT 27-MAR-2024, entry version 218. DE RecName: Full=Cell division cycle 5-like protein; DE Short=Cdc5-like protein; DE AltName: Full=Pombe cdc5-related protein; GN Name=CDC5L; Synonyms=KIAA0432, PCDC5RP; 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, SUBCELLULAR LOCATION, RP PHOSPHORYLATION, AND FUNCTION. RC TISSUE=Epithelium; RX PubMed=9038199; DOI=10.1074/jbc.272.9.5833; RA Bernstein H.S., Coughlin S.R.; RT "Pombe Cdc5-related protein. A putative human transcription factor RT implicated in mitogen-activated signaling."; RL J. Biol. Chem. 272:5833-5837(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION WITH USF2, TISSUE RP SPECIFICITY, AND SUBCELLULAR LOCATION. RC TISSUE=Fetal kidney; RX PubMed=9598309; DOI=10.1006/geno.1998.5254; RA Groenen P.M.A., Vanderlinden G., Devriendt K., Fryns J.-P., RA Van de Ven W.J.M.; RT "Rearrangement of the human CDC5L gene by a t(6;19)(p21;q13.1) in a patient RT with multicystic renal dysplasia."; RL Genomics 49:218-229(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION. RC TISSUE=Vascular endothelial cell; RX PubMed=9632794; DOI=10.1128/mcb.18.7.4097; RA Ohi R., Feoktistova A., McCann S., Valentine V., Look A.T., Lipsick J.S., RA Gould K.L.; RT "Myb-related Schizosaccharomyces pombe cdc5p is structurally and RT functionally conserved in eukaryotes."; RL Mol. Cell. Biol. 18:4097-4108(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=9455477; DOI=10.1093/dnares/4.5.307; RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. VIII. 78 RT new cDNA clones from brain which code for large proteins in vitro."; RL DNA Res. 4:307-313(1997). RN [5] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [8] 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 [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-162. RX PubMed=8917598; DOI=10.1073/pnas.93.23.13371; RA Hirayama T., Shinozaki K.; RT "A cdc5+ homolog of a higher plant, Arabidopsis thaliana."; RL Proc. Natl. Acad. Sci. U.S.A. 93:13371-13376(1996). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 259-614, INTERACTION WITH PPP1R8, SUBCELLULAR RP LOCATION, AND PHOSPHORYLATION. RC TISSUE=Epithelium; RX PubMed=10827081; DOI=10.1074/jbc.m001676200; RA Boudrez A., Beullens M., Groenen P.M.A., Van Eynde A., Vulsteke V., RA Jagiello I., Murray M., Krainer A.R., Stalmans W., Bollen M.; RT "NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a RT regulator of pre-mRNA splicing and mitotic entry."; RL J. Biol. Chem. 275:25411-25417(2000). RN [11] RP FUNCTION. RX PubMed=9468527; DOI=10.1074/jbc.273.8.4666; RA Bernstein H.S., Coughlin S.R.; RT "A mammalian homolog of fission yeast Cdc5 regulates G2 progression and RT mitotic entry."; RL J. Biol. Chem. 273:4666-4671(1998). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY AS PART OF THE SPLICEOSOME. 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 [13] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10570151; DOI=10.1073/pnas.96.24.13789; RA Burns C.G., Ohi R., Krainer A.R., Gould K.L.; RT "Evidence that Myb-related CDC5 proteins are required for pre-mRNA RT splicing."; RL Proc. Natl. Acad. Sci. U.S.A. 96:13789-13794(1999). RN [14] RP RNA-BINDING, AND FUNCTION. RX PubMed=11101529; DOI=10.1093/emboj/19.23.6569; RA Ajuh P., Kuster B., Panov K., Zomerdijk J.C.B.M., Mann M., Lamond A.I.; RT "Functional analysis of the human CDC5L complex and identification of its RT components by mass spectrometry."; RL EMBO J. 19:6569-6581(2000). RN [15] RP DNA-BINDING, SUBUNIT, MUTAGENESIS OF TRP-31; TRP-53 AND TRP-82, AND RP FUNCTION. RX PubMed=11082045; DOI=10.1242/jcs.113.24.4523; RA Lei X.-H., Shen X., Xu X.-Q., Bernstein H.S.; RT "Human Cdc5, a regulator of mitotic entry, can act as a site-specific DNA RT binding protein."; RL J. Cell Sci. 113:4523-4531(2000). RN [16] RP FUNCTION, INTERACTION WITH PLRG1, AND SUBCELLULAR LOCATION. RX PubMed=11544257; DOI=10.1074/jbc.m105453200; RA Ajuh P., Sleeman J., Chusainow J., Lamond A.I.; RT "A direct interaction between the carboxyl-terminal region of CDC5L and the RT WD40 domain of PLRG1 is essential for pre-mRNA splicing."; RL J. Biol. Chem. 276:42370-42381(2001). RN [17] 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 [18] RP FUNCTION, INTERACTION WITH TTF2, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12927788; DOI=10.1016/s0006-291x(03)01486-4; RA Leonard D., Ajuh P., Lamond A.I., Legerski R.J.; RT "hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA RT splicing."; RL Biochem. Biophys. Res. Commun. 308:793-801(2003). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND IDENTIFICATION BY RP 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 [20] RP SUBUNIT, SUBCELLULAR LOCATION, FUNCTION, PHOSPHORYLATION AT THR-227; RP SER-303; SER-358; THR-385; THR-404; THR-411; SER-417; THR-424 AND THR-438, RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF THR-411 AND RP THR-438. RX PubMed=18583928; DOI=10.4161/cc.7.12.6017; RA Graub R., Lancero H., Pedersen A., Chu M., Padmanabhan K., Xu X.Q., RA Spitz P., Chalkley R., Burlingame A.L., Stokoe D., Bernstein H.S.; RT "Cell cycle-dependent phosphorylation of human CDC5 regulates RNA RT processing."; RL Cell Cycle 7:1795-1803(2008). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385 AND THR-396, AND RP IDENTIFICATION BY 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 [22] RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH CTNNBL1. RX PubMed=18722174; DOI=10.1016/j.molcel.2008.07.009; RA Conticello S.G., Ganesh K., Xue K., Lu M., Rada C., Neuberger M.S.; RT "Interaction between antibody-diversification enzyme AID and spliceosome- RT associated factor CTNNBL1."; RL Mol. Cell 31:474-484(2008). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227; THR-377; THR-385; RP THR-396; THR-415; THR-424; THR-430; SER-437; THR-438 AND THR-442, 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 [24] 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 [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385 AND THR-396, 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 [26] RP IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L SPLICING COMPLEX, RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH CTNNBL1; PRPF19 RP AND BCAS2. RX PubMed=20176811; DOI=10.1128/mcb.01505-09; RA Grote M., Wolf E., Will C.L., Lemm I., Agafonov D.E., Schomburg A., RA Fischle W., Urlaub H., Luhrmann R.; RT "Molecular architecture of the human Prp19/CDC5L complex."; RL Mol. Cell. Biol. 30:2105-2119(2010). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; THR-377 AND THR-396, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [28] 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 [29] RP INTERACTION WITH CTNNBL1. RX PubMed=21385873; DOI=10.1074/jbc.m110.208769; RA Ganesh K., Adam S., Taylor B., Simpson P., Rada C., Neuberger M.; RT "CTNNBL1 is a novel nuclear localization sequence-binding protein that RT recognizes RNA-splicing factors CDC5L and Prp31."; RL J. Biol. Chem. 286:17091-17102(2011). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-377; THR-385 AND THR-396, AND RP IDENTIFICATION BY 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 [31] RP INTERACTION WITH USB1. RX PubMed=23022480; DOI=10.1016/j.celrep.2012.08.031; RA Shchepachev V., Wischnewski H., Missiaglia E., Soneson C., Azzalin C.M.; RT "Mpn1, mutated in poikiloderma with neutropenia protein 1, is a conserved RT 3'-to-5' RNA exonuclease processing U6 small nuclear RNA."; RL Cell Rep. 2:855-865(2012). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; THR-377; THR-385; RP THR-396; SER-417; THR-424; THR-430 AND THR-438, 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 [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-396, AND IDENTIFICATION BY RP 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 [34] RP FUNCTION. RX PubMed=24332808; DOI=10.1016/j.molcel.2013.11.002; RA Marechal A., Li J.M., Ji X.Y., Wu C.S., Yazinski S.A., Nguyen H.D., Liu S., RA Jimenez A.E., Jin J., Zou L.; RT "PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives RT ATR activation via a ubiquitin-mediated circuitry."; RL Mol. Cell 53:235-246(2014). RN [35] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219, AND IDENTIFICATION BY MASS RP 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 [36] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219, 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 [37] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-219 AND LYS-487, 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 [38] RP INTERACTION WITH CTNNBL1. RX PubMed=32484799; DOI=10.1172/jci131297; RA Kuhny M., Forbes L.R., Cakan E., Vega-Loza A., Kostiuk V., Dinesh R.K., RA Glauzy S., Stray-Pedersen A., Pezzi A.E., Hanson I.C., Vargas-Hernandez A., RA Xu M.L., Coban-Akdemir Z.H., Jhangiani S.N., Muzny D.M., Gibbs R.A., RA Lupski J.R., Chinn I.K., Schatz D.G., Orange J.S., Meffre E.; RT "Disease-associated CTNNBL1 mutation impairs somatic hypermutation by RT decreasing nuclear AID."; RL J. Clin. Invest. 130:4411-4422(2020). RN [39] RP STRUCTURE BY NMR OF 7-112. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the MYB DNA-binding domain of human cell division RT cycle 5-like protein."; RL Submitted (APR-2007) to the PDB data bank. RN [40] {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 [41] {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 [42] {ECO:0007744|PDB:6FF4, ECO:0007744|PDB:6FF7} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=29361316; DOI=10.1016/j.cell.2018.01.010; RA Haselbach D., Komarov I., Agafonov D.E., Hartmuth K., Graf B., Dybkov O., RA Urlaub H., Kastner B., Luhrmann R., Stark H.; RT "Structure and Conformational Dynamics of the Human Spliceosomal Bact RT Complex."; RL Cell 172:454-464(2018). RN [43] {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 [44] {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 [45] {ECO:0007744|PDB:6ICZ, ECO:0007744|PDB:6ID0, ECO:0007744|PDB:6ID1} RP STRUCTURE BY ELECTRON MICROSCOPY (2.86 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=30728453; DOI=10.1038/s41422-019-0143-x; RA Zhang X., Zhan X., Yan C., Zhang W., Liu D., Lei J., Shi Y.; RT "Structures of the human spliceosomes before and after release of the RT ligated exon."; RL Cell Res. 29:274-285(2019). RN [46] {ECO:0007744|PDB:6QDV} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), FUNCTION, SUBCELLULAR RP 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). RN [47] {ECO:0007744|PDB:7DVQ} RP STRUCTURE BY ELECTRON MICROSCOPY (2.89 ANGSTROMS), FUNCTION, AND SUBUNIT. RX PubMed=33509932; DOI=10.1126/science.abg0879; RA Bai R., Wan R., Wang L., Xu K., Zhang Q., Lei J., Shi Y.; RT "Structure of the activated human minor spliceosome."; RL Science 371:0-0(2021). CC -!- FUNCTION: DNA-binding protein involved in cell cycle control. May act CC as a transcription activator. Plays a role in pre-mRNA splicing as core CC component of precatalytic, catalytic and postcatalytic spliceosomal CC complexes (PubMed:11991638, PubMed:20176811, PubMed:28502770, CC PubMed:28076346, PubMed:29361316, PubMed:29360106, PubMed:29301961, CC PubMed:30728453, PubMed:30705154). Component of the PRP19-CDC5L complex CC that forms an integral part of the spliceosome and is required for CC activating pre-mRNA splicing. The PRP19-CDC5L complex may also play a CC role in the response to DNA damage (DDR) (PubMed:20176811). As a CC component of the minor spliceosome, involved in the splicing of U12- CC type introns in pre-mRNAs (Probable). {ECO:0000269|PubMed:10570151, CC ECO:0000269|PubMed:11082045, ECO:0000269|PubMed:11101529, CC ECO:0000269|PubMed:11544257, ECO:0000269|PubMed:11991638, CC ECO:0000269|PubMed:12927788, ECO:0000269|PubMed:18583928, CC ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:24332808, CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, CC ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, CC ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30705154, CC ECO:0000269|PubMed:30728453, ECO:0000269|PubMed:9038199, CC ECO:0000269|PubMed:9468527, ECO:0000269|PubMed:9632794, CC ECO:0000305|PubMed:33509932}. CC -!- SUBUNIT: Homodimer. Interacts with DAPK3 (By similarity). Component of CC the precatalytic, catalytic and postcatalytic spliceosome complexes CC (PubMed:11991638, PubMed:28502770, PubMed:28076346, PubMed:29361316, CC PubMed:29360106, PubMed:29301961, PubMed:30728453, PubMed:30705154). CC Part of a spliceosomal 'core' complex consisting of CDC5L, PLRG1, CC SPF27, CCAP1, CCAP3 and CCAP6. Interacts with PLRG1, Lodestar/TTF2, and CC NIPP1/PPP1R8. Component of the minor spliceosome, which splices U12- CC type introns. Within this complex, interacts with SCNM1 CC (PubMed:33509932). Component of the PRP19-CDC5L splicing complex CC composed of a core complex comprising a homotetramer of PRPF19, CDC5L, CC PLRG1 and BCAS2, and at least three less stably associated proteins CC CTNNBL1, CWC15 and HSPA8. The interaction with CTNNBL1 is direct CC (PubMed:18722174, PubMed:20176811, PubMed:21385873, PubMed:32484799). CC Interacts (via its C-terminus) directly in the complex with PRPF19 and CC BCAS2. Interacts (via its C-terminus) directly with PRGL1 (via its WD40 CC repeat domain); the interaction is required for mRNA splicing but not CC for spliceosome assembly. Interacts with PRPF19 (via N-terminus) (By CC similarity). Interacts with USB1 (PubMed:23022480). CC {ECO:0000250|UniProtKB:O08837, ECO:0000269|PubMed:10827081, CC ECO:0000269|PubMed:11082045, ECO:0000269|PubMed:11544257, CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12927788, CC ECO:0000269|PubMed:18583928, ECO:0000269|PubMed:18722174, CC ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:21385873, CC ECO:0000269|PubMed:23022480, ECO:0000269|PubMed:28076346, CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961, CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, CC ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:30728453, CC ECO:0000269|PubMed:32484799, ECO:0000269|PubMed:33509932}. CC -!- INTERACTION: CC Q99459; Q13535: ATR; NbExp=3; IntAct=EBI-374880, EBI-968983; CC Q99459; O75934: BCAS2; NbExp=13; IntAct=EBI-374880, EBI-1050106; CC Q99459; Q99459: CDC5L; NbExp=2; IntAct=EBI-374880, EBI-374880; CC Q99459; Q8WYA6: CTNNBL1; NbExp=7; IntAct=EBI-374880, EBI-748128; CC Q99459; Q08379: GOLGA2; NbExp=6; IntAct=EBI-374880, EBI-618309; CC Q99459; Q0D2H9: GOLGA8DP; NbExp=3; IntAct=EBI-374880, EBI-10181276; CC Q99459; Q08AF8: GOLGA8G; NbExp=3; IntAct=EBI-374880, EBI-10181260; CC Q99459; P07910: HNRNPC; NbExp=2; IntAct=EBI-374880, EBI-357966; CC Q99459; P52272: HNRNPM; NbExp=7; IntAct=EBI-374880, EBI-486809; CC Q99459; Q9UJC3: HOOK1; NbExp=5; IntAct=EBI-374880, EBI-746704; CC Q99459; P42858: HTT; NbExp=3; IntAct=EBI-374880, EBI-466029; CC Q99459; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-374880, EBI-2556193; CC Q99459; Q7Z3B3: KANSL1; NbExp=3; IntAct=EBI-374880, EBI-740244; CC Q99459; O60341: KDM1A; NbExp=3; IntAct=EBI-374880, EBI-710124; CC Q99459; O95751: LDOC1; NbExp=3; IntAct=EBI-374880, EBI-740738; CC Q99459; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-374880, EBI-11522433; CC Q99459; Q13416: ORC2; NbExp=2; IntAct=EBI-374880, EBI-374957; CC Q99459; O43660: PLRG1; NbExp=8; IntAct=EBI-374880, EBI-1051504; CC Q99459; P62136: PPP1CA; NbExp=2; IntAct=EBI-374880, EBI-357253; CC Q99459; Q96KQ4: PPP1R13B; NbExp=5; IntAct=EBI-374880, EBI-1105153; CC Q99459; Q9UMS4: PRPF19; NbExp=11; IntAct=EBI-374880, EBI-395746; CC Q99459; Q15428: SF3A2; NbExp=2; IntAct=EBI-374880, EBI-2462271; CC Q99459; Q01082: SPTBN1; NbExp=3; IntAct=EBI-374880, EBI-351561; CC Q99459; Q8N3V7: SYNPO; NbExp=5; IntAct=EBI-374880, EBI-352936; CC Q99459; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-374880, EBI-11952721; CC Q99459; Q9UNY4: TTF2; NbExp=5; IntAct=EBI-374880, EBI-2322921; CC Q99459; P40222: TXLNA; NbExp=3; IntAct=EBI-374880, EBI-359793; CC Q99459; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-374880, EBI-739895; CC Q99459; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-374880, EBI-2799833; CC Q99459; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-374880, EBI-527853; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10570151, CC ECO:0000269|PubMed:11544257, ECO:0000269|PubMed:18583928, CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, CC ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, CC ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30705154, CC ECO:0000269|PubMed:30728453, ECO:0000269|PubMed:9038199, CC ECO:0000269|PubMed:9598309}. Nucleus speckle CC {ECO:0000269|PubMed:10570151, ECO:0000269|PubMed:10827081, CC ECO:0000269|PubMed:11544257}. Cytoplasm {ECO:0000269|PubMed:9038199}. CC Note=May shuttle between cytoplasm and nucleus. CC {ECO:0000269|PubMed:9038199}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in both fetal and adult CC tissues. {ECO:0000269|PubMed:9038199, ECO:0000269|PubMed:9598309, CC ECO:0000269|PubMed:9632794}. CC -!- PTM: Phosphorylated on serine and threonine residues. Phosphorylation CC on Thr-411 and Thr-438 is required for CDC5L-mediated mRNA splicing. CC Has no effect on subcellular location nor on homodimerization. CC Phosphorylated in vitro by CDK2. Phosphorylation enhances interaction CC with PPP1R8. {ECO:0000269|PubMed:10827081, ECO:0000269|PubMed:18583928, CC ECO:0000269|PubMed:9038199}. CC -!- DISEASE: Note=A chromosomal aberration involving CDC5L is found in CC multicystic renal dysplasia. Translocation t(6;19)(p21;q13.1) with CC USF2. CC -!- SIMILARITY: Belongs to the CEF1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA24862.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/cdc5l/"; 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; U86753; AAB61210.1; -; mRNA. DR EMBL; AB007892; BAA24862.2; ALT_INIT; mRNA. DR EMBL; AY518540; AAR89913.1; -; Genomic_DNA. DR EMBL; AL133262; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL353588; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001568; AAH01568.1; -; mRNA. DR EMBL; D85423; BAA20885.1; -; mRNA. DR CCDS; CCDS4912.1; -. DR RefSeq; NP_001244.1; NM_001253.3. DR PDB; 2DIM; NMR; -; A=7-63. DR PDB; 2DIN; NMR; -; A=59-111. DR PDB; 5MQF; EM; 5.90 A; L=1-802. DR PDB; 5XJC; EM; 3.60 A; L=1-802. DR PDB; 5YZG; EM; 4.10 A; L=1-802. DR PDB; 5Z56; EM; 5.10 A; L=1-802. DR PDB; 5Z57; EM; 6.50 A; L=1-802. DR PDB; 5Z58; EM; 4.90 A; L=1-802. DR PDB; 6FF4; EM; 16.00 A; L=1-802. DR PDB; 6FF7; EM; 4.50 A; L=1-802. DR PDB; 6ICZ; EM; 3.00 A; L=1-802. DR PDB; 6ID0; EM; 2.90 A; L=1-802. DR PDB; 6ID1; EM; 2.86 A; L=1-802. DR PDB; 6QDV; EM; 3.30 A; O=1-802. DR PDB; 6ZYM; EM; 3.40 A; L=1-802. DR PDB; 7A5P; EM; 5.00 A; L=1-802. DR PDB; 7AAV; EM; 4.20 A; L=1-802. DR PDB; 7ABG; EM; 7.80 A; L=1-802. DR PDB; 7ABH; EM; 4.50 A; L=1-802. DR PDB; 7ABI; EM; 8.00 A; L=1-802. DR PDB; 7DVQ; EM; 2.89 A; L=1-802. DR PDB; 7QTT; EM; 3.10 A; P=1-802. DR PDB; 7W59; EM; 3.60 A; L=1-802. DR PDB; 7W5A; EM; 3.60 A; L=1-802. DR PDB; 7W5B; EM; 4.30 A; L=1-802. DR PDB; 8C6J; EM; 2.80 A; O=1-802. DR PDB; 8CH6; EM; 5.90 A; P=1-802. DR PDBsum; 2DIM; -. DR PDBsum; 2DIN; -. DR PDBsum; 5MQF; -. DR PDBsum; 5XJC; -. DR PDBsum; 5YZG; -. DR PDBsum; 5Z56; -. DR PDBsum; 5Z57; -. DR PDBsum; 5Z58; -. DR PDBsum; 6FF4; -. DR PDBsum; 6FF7; -. DR PDBsum; 6ICZ; -. DR PDBsum; 6ID0; -. DR PDBsum; 6ID1; -. DR PDBsum; 6QDV; -. DR PDBsum; 6ZYM; -. DR PDBsum; 7A5P; -. DR PDBsum; 7AAV; -. DR PDBsum; 7ABG; -. DR PDBsum; 7ABH; -. DR PDBsum; 7ABI; -. DR PDBsum; 7DVQ; -. DR PDBsum; 7QTT; -. DR PDBsum; 7W59; -. DR PDBsum; 7W5A; -. DR PDBsum; 7W5B; -. DR PDBsum; 8C6J; -. DR PDBsum; 8CH6; -. DR AlphaFoldDB; Q99459; -. DR BMRB; Q99459; -. DR EMDB; EMD-11569; -. DR EMDB; EMD-11693; -. DR EMDB; EMD-11695; -. DR EMDB; EMD-11696; -. DR EMDB; EMD-11697; -. DR EMDB; EMD-14146; -. DR EMDB; EMD-16452; -. DR EMDB; EMD-16658; -. DR EMDB; EMD-30875; -. DR EMDB; EMD-32317; -. DR EMDB; EMD-32319; -. DR EMDB; EMD-32321; -. DR EMDB; EMD-3545; -. DR EMDB; EMD-4255; -. DR EMDB; EMD-4525; -. DR EMDB; EMD-6721; -. DR EMDB; EMD-6864; -. DR EMDB; EMD-6889; -. DR EMDB; EMD-6890; -. DR EMDB; EMD-6891; -. DR EMDB; EMD-9645; -. DR EMDB; EMD-9646; -. DR EMDB; EMD-9647; -. DR SMR; Q99459; -. DR BioGRID; 107424; 843. DR ComplexPortal; CPX-5824; PRP19-CDC5L complex. DR CORUM; Q99459; -. DR DIP; DIP-31731N; -. DR IntAct; Q99459; 681. DR MINT; Q99459; -. DR STRING; 9606.ENSP00000360532; -. DR GlyCosmos; Q99459; 1 site, 1 glycan. DR GlyGen; Q99459; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q99459; -. DR MetOSite; Q99459; -. DR PhosphoSitePlus; Q99459; -. DR SwissPalm; Q99459; -. DR BioMuta; CDC5L; -. DR DMDM; 73619933; -. DR EPD; Q99459; -. DR jPOST; Q99459; -. DR MassIVE; Q99459; -. DR MaxQB; Q99459; -. DR PaxDb; 9606-ENSP00000360532; -. DR PeptideAtlas; Q99459; -. DR ProteomicsDB; 78277; -. DR Pumba; Q99459; -. DR Antibodypedia; 1422; 357 antibodies from 34 providers. DR DNASU; 988; -. DR Ensembl; ENST00000371477.4; ENSP00000360532.3; ENSG00000096401.8. DR GeneID; 988; -. DR KEGG; hsa:988; -. DR MANE-Select; ENST00000371477.4; ENSP00000360532.3; NM_001253.4; NP_001244.1. DR UCSC; uc003oxl.4; human. DR AGR; HGNC:1743; -. DR CTD; 988; -. DR DisGeNET; 988; -. DR GeneCards; CDC5L; -. DR HGNC; HGNC:1743; CDC5L. DR HPA; ENSG00000096401; Low tissue specificity. DR MIM; 602868; gene. DR neXtProt; NX_Q99459; -. DR OpenTargets; ENSG00000096401; -. DR PharmGKB; PA26270; -. DR VEuPathDB; HostDB:ENSG00000096401; -. DR eggNOG; KOG0050; Eukaryota. DR GeneTree; ENSGT00550000074922; -. DR HOGENOM; CLU_009082_0_0_1; -. DR InParanoid; Q99459; -. DR OMA; KMGMAGE; -. DR OrthoDB; 131128at2759; -. DR PhylomeDB; Q99459; -. DR TreeFam; TF101061; -. DR PathwayCommons; Q99459; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; Q99459; -. DR SIGNOR; Q99459; -. DR BioGRID-ORCS; 988; 844 hits in 1184 CRISPR screens. DR ChiTaRS; CDC5L; human. DR EvolutionaryTrace; Q99459; -. DR GeneWiki; CDC5L; -. DR GenomeRNAi; 988; -. DR Pharos; Q99459; Tbio. DR PRO; PR:Q99459; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q99459; Protein. DR Bgee; ENSG00000096401; Expressed in buccal mucosa cell and 213 other cell types or tissues. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:CACAO. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000974; C:Prp19 complex; IDA:UniProtKB. DR GO; GO:0005681; C:spliceosomal complex; IPI:ComplexPortal. DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0071987; F:WD40-repeat domain binding; IDA:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:UniProtKB. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd00167; SANT; 1. DR CDD; cd11659; SANT_CDC5_II; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 2. DR InterPro; IPR047242; CDC5L/Cef1. DR InterPro; IPR021786; Cdc5p/Cef1_C. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR017930; Myb_dom. DR InterPro; IPR001005; SANT/Myb. DR InterPro; IPR047240; SANT_CDC5L_II. DR PANTHER; PTHR45885; CELL DIVISION CYCLE 5-LIKE PROTEIN; 1. DR PANTHER; PTHR45885:SF1; CELL DIVISION CYCLE 5-LIKE PROTEIN; 1. DR Pfam; PF11831; Myb_Cef; 1. DR Pfam; PF13921; Myb_DNA-bind_6; 1. DR SMART; SM00717; SANT; 2. DR SUPFAM; SSF46689; Homeodomain-like; 1. DR PROSITE; PS51294; HTH_MYB; 2. DR Genevisible; Q99459; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Cell cycle; Chromosomal rearrangement; KW Coiled coil; Cytoplasm; DNA damage; DNA repair; DNA-binding; KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; RNA-binding; Spliceosome; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..802 FT /note="Cell division cycle 5-like protein" FT /id="PRO_0000197091" FT DOMAIN 1..56 FT /note="HTH myb-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625" FT DOMAIN 57..108 FT /note="HTH myb-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625" FT DNA_BIND 31..54 FT /note="H-T-H motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625" FT DNA_BIND 82..104 FT /note="H-T-H motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625" FT REGION 108..143 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 200..206 FT /note="Required for interaction with CTNNBL1" FT /evidence="ECO:0000269|PubMed:21385873" FT REGION 247..278 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 260..606 FT /note="Interaction with PPP1R8" FT /evidence="ECO:0000269|PubMed:10827081" FT REGION 408..443 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 501..659 FT /note="Interaction with DAPK3" FT /evidence="ECO:0000250|UniProtKB:O08837" FT REGION 706..800 FT /note="Interaction with PLRG1" FT /evidence="ECO:0000269|PubMed:11544257" FT COILED 142..245 FT /evidence="ECO:0000255" FT COILED 676..701 FT /evidence="ECO:0000255" FT COILED 764..802 FT /evidence="ECO:0000255" FT MOTIF 165..271 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 108..142 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 247..261 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 408..437 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 414 FT /note="Breakpoint for translocation" FT MOD_RES 227 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18583928, FT ECO:0007744|PubMed:18669648" FT MOD_RES 303 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18583928, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 358 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18583928" FT MOD_RES 377 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 385 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18583928, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 396 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 404 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18583928" FT MOD_RES 411 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18583928" FT MOD_RES 415 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 417 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18583928, FT ECO:0007744|PubMed:23186163" FT MOD_RES 424 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18583928, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 430 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 437 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 438 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18583928, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 442 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT CROSSLNK 135 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 219 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 487 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 459 FT /note="Y -> C (in dbSNP:rs11572006)" FT /id="VAR_050181" FT MUTAGEN 31 FT /note="W->G: Abolishes DNA-binding; when associated with FT G-53 and G-82." FT /evidence="ECO:0000269|PubMed:11082045" FT MUTAGEN 53 FT /note="W->G: Abolishes DNA-binding; when associated with FT G-31 and G-82." FT /evidence="ECO:0000269|PubMed:11082045" FT MUTAGEN 82 FT /note="W->G: Abolishes DNA-binding; when associated with FT G-31 and G-53." FT /evidence="ECO:0000269|PubMed:11082045" FT MUTAGEN 227 FT /note="T->A: Abolishes phosphorylation. No effect on FT homodimerization nor on nuclear localization; when FT associated with A-303; A-358; A-385; A-404; A-411; A-417; FT A-424 and A-438." FT MUTAGEN 303 FT /note="S->A: Abolishes phosphorylation. No effect on FT homodimerization nor on nuclear localization; when FT associated with A-227; A-358; A-385; A-404; A-411; A-417; FT A-424 and A-438." FT MUTAGEN 358 FT /note="S->A: Abolishes phosphorylation. No effect on FT homodimerization nor on nuclear localization; when FT associated with A-227; A-303; A-385; A-404; A-411; A-417; FT A-424 and A-438." FT MUTAGEN 404 FT /note="T->A: Abolishes phosphorylation. No effect on FT homodimerization nor on nuclear localization; when FT associated with A-227; A-303; A-358; A-385; A-411; A-417; FT A-424 and A-438." FT MUTAGEN 411 FT /note="T->A: Abolishes phosphorylation. Markedly diminished FT pre-mRNA splicing activity; when associated with A-438. No FT effect on homodimerization nor on nuclear localization; FT when associated with A-227; A-303; A-358; A-385; A-404; FT A-417; A-424 and A-438." FT /evidence="ECO:0000269|PubMed:18583928" FT MUTAGEN 417 FT /note="S->A: Abolishes phosphorylation. No effect on FT homodimerization nor on nuclear localization; when FT associated with A-227; A-303; A-358; A-385; A-404; A-411; FT A-424 and A-438." FT MUTAGEN 424 FT /note="T->A: Abolishes phosphorylation. No effect on FT homodimerization nor on nuclear localization; when FT associated with A-227; A-303; A-358; A-385; A-404; A-411; FT A-417 and A-438." FT MUTAGEN 438 FT /note="T->A: Abolishes phosphorylation. Markedly diminished FT pre-mRNA splicing activity; when associated with A-411. No FT effect on homodimerization nor on nuclear localization; FT when associated with A-227; A-303; A-358; A-385; A-404; FT A-411; A-417 and A-424." FT /evidence="ECO:0000269|PubMed:18583928" FT CONFLICT 12 FT /note="R -> K (in Ref. 9; BAA20885)" FT /evidence="ECO:0000305" FT HELIX 13..26 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 27..29 FT /evidence="ECO:0007829|PDB:7QTT" FT HELIX 31..34 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 43..53 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:2DIM" FT HELIX 65..77 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:6FF4" FT HELIX 82..89 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 93..111 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 146..160 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 165..194 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 208..211 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 239..241 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 244..248 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 252..269 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 505..507 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 508..525 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 529..533 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 546..551 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 557..570 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 594..607 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 615..628 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 691..789 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 791..794 FT /evidence="ECO:0007829|PDB:6ID1" SQ SEQUENCE 802 AA; 92251 MW; 3390F91EE7E79DA6 CRC64; MPRIMIKGGV WRNTEDEILK AAVMKYGKNQ WSRIASLLHR KSAKQCKARW YEWLDPSIKK TEWSREEEEK LLHLAKLMPT QWRTIAPIIG RTAAQCLEHY EFLLDKAAQR DNEEETTDDP RKLKPGEIDP NPETKPARPD PIDMDEDELE MLSEARARLA NTQGKKAKRK AREKQLEEAR RLAALQKRRE LRAAGIEIQK KRKRKRGVDY NAEIPFEKKP ALGFYDTSEE NYQALDADFR KLRQQDLDGE LRSEKEGRDR KKDKQHLKRK KESDLPSAIL QTSGVSEFTK KRSKLVLPAP QISDAELQEV VKVGQASEIA RQTAEESGIT NSASSTLLSE YNVTNNSVAL RTPRTPASQD RILQEAQNLM ALTNVDTPLK GGLNTPLHES DFSGVTPQRQ VVQTPNTVLS TPFRTPSNGA EGLTPRSGTT PKPVINSTPG RTPLRDKLNI NPEDGMADYS DPSYVKQMER ESREHLRLGL LGLPAPKNDF EIVLPENAEK ELEEREIDDT YIEDAADVDA RKQAIRDAER VKEMKRMHKA VQKDLPRPSE VNETILRPLN VEPPLTDLQK SEELIKKEMI TMLHYDLLHH PYEPSGNKKG KTVGFGTNNS EHITYLEHNP YEKFSKEELK KAQDVLVQEM EVVKQGMSHG ELSSEAYNQV WEECYSQVLY LPGQSRYTRA NLASKKDRIE SLEKRLEINR GHMTTEAKRA AKMEKKMKIL LGGYQSRAMG LMKQLNDLWD QIEQAHLELR TFEELKKHED SAIPRRLECL KEDVQRQQER EKELQHRYAD LLLEKETLKS KF //