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Database: UniProt
Entry: Q99459
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Original site: Q99459 
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   29-SEP-2021, entry version 206.
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;
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   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   [32]
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   [33]
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   [34]
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   [35]
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   [36]
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   [37]
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   [38] {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   [39] {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   [40] {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   [41] {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   [42] {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   [43] {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   [44] {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).
CC   -!- FUNCTION: DNA-binding protein involved in cell cycle control. May act
CC       as a transcription activator. Plays 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).
CC       {ECO:0000269|PubMed:10570151, ECO:0000269|PubMed:11082045,
CC       ECO:0000269|PubMed:11101529, ECO:0000269|PubMed:11544257,
CC       ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12927788,
CC       ECO:0000269|PubMed:18583928, ECO:0000269|PubMed:20176811,
CC       ECO:0000269|PubMed:24332808, 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:9038199, ECO:0000269|PubMed:9468527,
CC       ECO:0000269|PubMed:9632794}.
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 PRP19-CDC5L splicing complex composed of
CC       a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and
CC       BCAS2, and at least three less stably associated proteins CTNNBL1,
CC       CWC15 and HSPA8. Interacts (via its C-terminus) directly in the complex
CC       with PRPF19 and BCAS2. Interacts (via its C-terminus) directly with
CC       PRGL1 (via its WD40 repeat domain); the interaction is required for
CC       mRNA splicing but not for spliceosome assembly. Also interacts with
CC       CTNNBL1. Interacts with PRPF19 (via N-terminus) (By similarity).
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: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}.
CC   -!- INTERACTION:
CC       Q99459; Q13535: ATR; NbExp=3; IntAct=EBI-374880, EBI-968983;
CC       Q99459; O75934: BCAS2; NbExp=3; IntAct=EBI-374880, EBI-1050106;
CC       Q99459; Q8WYA6: CTNNBL1; NbExp=2; 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; 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=3; 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/";
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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   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   BMRB; Q99459; -.
DR   SMR; Q99459; -.
DR   BioGRID; 107424; 743.
DR   ComplexPortal; CPX-5824; PRP19-CDC5L complex.
DR   CORUM; Q99459; -.
DR   DIP; DIP-31731N; -.
DR   IntAct; Q99459; 662.
DR   MINT; Q99459; -.
DR   STRING; 9606.ENSP00000360532; -.
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; Q99459; -.
DR   PeptideAtlas; Q99459; -.
DR   PRIDE; Q99459; -.
DR   ProteomicsDB; 78277; -.
DR   Antibodypedia; 1422; 314 antibodies.
DR   DNASU; 988; -.
DR   Ensembl; ENST00000371477; ENSP00000360532; ENSG00000096401.
DR   GeneID; 988; -.
DR   KEGG; hsa:988; -.
DR   UCSC; uc003oxl.4; human.
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; PFRTQRE; -.
DR   OrthoDB; 975557at2759; -.
DR   PhylomeDB; Q99459; -.
DR   TreeFam; TF101061; -.
DR   PathwayCommons; Q99459; -.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   SIGNOR; Q99459; -.
DR   BioGRID-ORCS; 988; 803 hits in 1042 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 amniotic fluid and 247 other tissues.
DR   Genevisible; Q99459; HS.
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:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
DR   GO; GO:0000974; C:Prp19 complex; IDA:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
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:0043522; F:leucine zipper domain binding; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IEA:Ensembl.
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:0001222; F:transcription corepressor binding; IEA:Ensembl.
DR   GO; GO:0071987; F:WD40-repeat domain binding; IDA:UniProtKB.
DR   GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0071352; P:cellular response to interleukin-2; IEA:Ensembl.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
DR   GO; GO:1990646; P:cellular response to prolactin; IEA:Ensembl.
DR   GO; GO:1904568; P:cellular response to wortmannin; IEA:Ensembl.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
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   InterPro; IPR021786; Cdc5p/Cef1_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   Pfam; PF11831; Myb_Cef; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS51294; HTH_MYB; 2.
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 G-
FT                   53 and G-82."
FT                   /evidence="ECO:0000269|PubMed:11082045"
FT   MUTAGEN         53
FT                   /note="W->G: Abolishes DNA-binding; when associated with G-
FT                   31 and G-82."
FT                   /evidence="ECO:0000269|PubMed:11082045"
FT   MUTAGEN         82
FT                   /note="W->G: Abolishes DNA-binding; when associated with G-
FT                   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; A-
FT                   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; A-
FT                   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   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:6ICZ"
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
//
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