CDC5L_HUMAN
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 03-AUG-2022, entry version 209.
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 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 [39] {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 [40] {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 [41] {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 [42] {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 [43] {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 [44] {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 [45] {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 Interacts with USB1 (PubMed:23022480). {ECO:0000250|UniProtKB:O08837,
CC ECO:0000269|PubMed:10827081, ECO:0000269|PubMed:11082045,
CC ECO:0000269|PubMed:11544257, ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:12927788, ECO:0000269|PubMed:18583928,
CC ECO:0000269|PubMed:18722174, ECO:0000269|PubMed:20176811,
CC ECO:0000269|PubMed:21385873, ECO:0000269|PubMed:23022480,
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=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/";
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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 AlphaFoldDB; Q99459; -.
DR BMRB; Q99459; -.
DR SMR; Q99459; -.
DR BioGRID; 107424; 789.
DR ComplexPortal; CPX-5824; PRP19-CDC5L complex.
DR CORUM; Q99459; -.
DR DIP; DIP-31731N; -.
DR IntAct; Q99459; 675.
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; 324 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 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 SignaLink; Q99459; -.
DR SIGNOR; Q99459; -.
DR BioGRID-ORCS; 988; 811 hits in 1106 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 211 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: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 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: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
