Q99459Q76N46Q99974CDC5L_HUMANCell division cycle 5-like proteinCdc5-like proteinPombe cdc5-related proteinCDC5LKIAA0432PCDC5RPHomo sapiensHumanEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomoPombe Cdc5-related protein. A putative human transcription factor implicated in mitogen-activated signaling.NUCLEOTIDE SEQUENCE [MRNA]TISSUE SPECIFICITYSUBCELLULAR LOCATIONPHOSPHORYLATIONFUNCTIONRearrangement of the human CDC5L gene by a t(6;19)(p21;q13.1) in a patient with multicystic renal dysplasia.NUCLEOTIDE SEQUENCE [MRNA]CHROMOSOMAL TRANSLOCATION WITH USF2TISSUE SPECIFICITYSUBCELLULAR LOCATIONMyb-related Schizosaccharomyces pombe cdc5p is structurally and functionally conserved in eukaryotes.NUCLEOTIDE SEQUENCE [MRNA]TISSUE SPECIFICITYFUNCTIONPrediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro.NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.SEQUENCE REVISIONNUCLEOTIDE SEQUENCE [GENOMIC DNA]The DNA sequence and analysis of human chromosome 6.NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]A cdc5+ homolog of a higher plant, Arabidopsis thaliana.NUCLEOTIDE SEQUENCE [MRNA] OF 8-162NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a regulator of pre-mRNA splicing and mitotic entry.NUCLEOTIDE SEQUENCE [MRNA] OF 259-614INTERACTION WITH PPP1R8SUBCELLULAR LOCATIONPHOSPHORYLATIONA mammalian homolog of fission yeast Cdc5 regulates G2 progression and mitotic entry.FUNCTIONMass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex.IDENTIFICATION BY MASS SPECTROMETRY AS PART OF THE SPLICEOSOMEEvidence that Myb-related CDC5 proteins are required for pre-mRNA splicing.FUNCTIONSUBCELLULAR LOCATIONFunctional analysis of the human CDC5L complex and identification of its components by mass spectrometry.RNA-BINDINGFUNCTIONHuman Cdc5, a regulator of mitotic entry, can act as a site-specific DNA binding protein.DNA-BINDINGSUBUNITMUTAGENESIS OF TRP-31; TRP-53 AND TRP-82FUNCTIONA direct interaction between the carboxyl-terminal region of CDC5L and the WD40 domain of PLRG1 is essential for pre-mRNA splicing.FUNCTIONINTERACTION WITH PLRG1SUBCELLULAR LOCATIONPurification and characterization of native spliceosomes suitable for three-dimensional structural analysis.IDENTIFICATION BY MASS SPECTROMETRYIDENTIFICATION IN THE SPLICEOSOMAL C COMPLEXhLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing.FUNCTIONINTERACTION WITH TTF2IDENTIFICATION BY MASS SPECTROMETRYGlobal, in vivo, and site-specific phosphorylation dynamics in signaling networks.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Cell cycle-dependent phosphorylation of human CDC5 regulates RNA processing.SUBUNITSUBCELLULAR LOCATIONFUNCTIONPHOSPHORYLATION AT THR-227; SER-303; SER-358; THR-385; THR-404; THR-411; SER-417; THR-424 AND THR-438IDENTIFICATION BY MASS SPECTROMETRYMUTAGENESIS OF THR-411 AND THR-438Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385 AND THR-396IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Interaction between antibody-diversification enzyme AID and spliceosome-associated factor CTNNBL1.IDENTIFICATION BY MASS SPECTROMETRYINTERACTION WITH CTNNBL1A quantitative atlas of mitotic phosphorylation.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227; THR-377; THR-385; THR-396; THR-415; THR-424; THR-430; SER-437; THR-438 AND THR-442IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385 AND THR-396IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Molecular architecture of the human Prp19/CDC5L complex.IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L SPLICING COMPLEXIDENTIFICATION BY MASS SPECTROMETRYINTERACTION WITH CTNNBL1; PRPF19 AND BCAS2Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; THR-377 AND THR-396IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Initial characterization of the human central proteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]CTNNBL1 is a novel nuclear localization sequence-binding protein that recognizes RNA-splicing factors CDC5L and Prp31.INTERACTION WITH CTNNBL1System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-377; THR-385 AND THR-396IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Mpn1, mutated in poikiloderma with neutropenia protein 1, is a conserved 3'-to-5' RNA exonuclease processing U6 small nuclear RNA.INTERACTION WITH USB1Toward a comprehensive characterization of a human cancer cell phosphoproteome.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; THR-377; THR-385; THR-396; SER-417; THR-424; THR-430 AND THR-438IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-396IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry.FUNCTIONSUMO-2 orchestrates chromatin modifiers in response to DNA damage.SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-219 AND LYS-487IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Disease-associated CTNNBL1 mutation impairs somatic hypermutation by decreasing nuclear AID.INTERACTION WITH CTNNBL1Solution structure of the MYB DNA-binding domain of human cell division cycle 5-like protein.STRUCTURE BY NMR OF 7-112An Atomic Structure of the Human Spliceosome.STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS)FUNCTIONSUBCELLULAR LOCATIONSUBUNITCryo-EM structure of a human spliceosome activated for step 2 of splicing.STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS)FUNCTIONSUBCELLULAR LOCATIONSUBUNITStructure and Conformational Dynamics of the Human Spliceosomal Bact Complex.STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS)FUNCTIONSUBCELLULAR LOCATIONSUBUNITStructure of the human activated spliceosome in three conformational states.STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS)FUNCTIONSUBCELLULAR LOCATIONSUBUNITStructure of a human catalytic step I spliceosome.STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS)FUNCTIONSUBCELLULAR LOCATIONSUBUNITStructures of the human spliceosomes before and after release of the ligated exon.STRUCTURE BY ELECTRON MICROSCOPY (2.86 ANGSTROMS)FUNCTIONSUBCELLULAR LOCATIONSUBUNITA human postcatalytic spliceosome structure reveals essential roles of metazoan factors for exon ligation.STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS)FUNCTIONSUBCELLULAR LOCATIONSUBUNITStructure of the activated human minor spliceosome.STRUCTURE BY ELECTRON MICROSCOPY (2.89 ANGSTROMS)FUNCTIONSUBUNITDNA-binding protein involved in cell cycle control. May act as a transcription activator. Plays a role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes (PubMed:11991638, PubMed:20176811, PubMed:28502770, PubMed:28076346, PubMed:29361316, PubMed:29360106, PubMed:29301961, PubMed:30728453, PubMed:30705154). Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR) (PubMed:20176811). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable).Homodimer. Interacts with DAPK3 (By similarity). Component of the precatalytic, catalytic and postcatalytic spliceosome complexes (PubMed:11991638, PubMed:28502770, PubMed:28076346, PubMed:29361316, PubMed:29360106, PubMed:29301961, PubMed:30728453, PubMed:30705154). Part of a spliceosomal 'core' complex consisting of CDC5L, PLRG1, SPF27, CCAP1, CCAP3 and CCAP6. Interacts with PLRG1, Lodestar/TTF2, and NIPP1/PPP1R8. Component of the minor spliceosome, which splices U12-type introns. Within this complex, interacts with SCNM1 (PubMed:33509932). Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. The interaction with CTNNBL1 is direct (PubMed:18722174, PubMed:20176811, PubMed:21385873, PubMed:32484799). Interacts (via its C-terminus) directly in the complex with PRPF19 and BCAS2. Interacts (via its C-terminus) directly with PRGL1 (via its WD40 repeat domain); the interaction is required for mRNA splicing but not for spliceosome assembly. Interacts with PRPF19 (via N-terminus) (By similarity). Interacts with USB1 (PubMed:23022480).Q99459Q13535false3Q99459O75934false13Q99459Q99459false2Q99459Q8WYA6false7Q99459Q08379false6Q99459Q0D2H9false3Q99459Q08AF8false3Q99459P07910false2Q99459P52272false7Q99459Q9UJC3false5Q99459P42858false3Q99459Q63ZY3false3Q99459Q7Z3B3false3Q99459O60341false3Q99459O95751false3Q99459Q5JR59-3false3Q99459Q13416false2Q99459O43660false8Q99459P62136false2Q99459Q96KQ4false5Q99459Q9UMS4false11Q99459Q15428false2Q99459Q01082false3Q99459Q8N3V7false5Q99459Q05BL1false3Q99459Q9UNY4false5Q99459P40222false3Q99459Q8N6Y0false3Q99459Q8N1B4false3Q99459Q9UGI0false3NucleusNucleus speckleCytoplasmMay shuttle between cytoplasm and nucleus.Ubiquitously expressed in both fetal and adult tissues.Phosphorylated on serine and threonine residues. Phosphorylation on Thr-411 and Thr-438 is required for CDC5L-mediated mRNA splicing. Has no effect on subcellular location nor on homodimerization. Phosphorylated in vitro by CDK2. Phosphorylation enhances interaction with PPP1R8.A chromosomal aberration involving CDC5L is found in multicystic renal dysplasia. Translocation t(6;19)(p21;q13.1) with USF2.Belongs to the CEF1 family.Extended N-terminus.3D-structureActivatorCell cycleChromosomal rearrangementCoiled coilCytoplasmDNA damageDNA repairDNA-bindingIsopeptide bondmRNA processingmRNA splicingNucleusPhosphoproteinReference proteomeRepeatRNA-bindingSpliceosomeTranscriptionTranscription regulationUbl conjugationYCWGWGWGTASASATATASATATARKMPRIMIKGGVWRNTEDEILKAAVMKYGKNQWSRIASLLHRKSAKQCKARWYEWLDPSIKKTEWSREEEEKLLHLAKLMPTQWRTIAPIIGRTAAQCLEHYEFLLDKAAQRDNEEETTDDPRKLKPGEIDPNPETKPARPDPIDMDEDELEMLSEARARLANTQGKKAKRKAREKQLEEARRLAALQKRRELRAAGIEIQKKRKRKRGVDYNAEIPFEKKPALGFYDTSEENYQALDADFRKLRQQDLDGELRSEKEGRDRKKDKQHLKRKKESDLPSAILQTSGVSEFTKKRSKLVLPAPQISDAELQEVVKVGQASEIARQTAEESGITNSASSTLLSEYNVTNNSVALRTPRTPASQDRILQEAQNLMALTNVDTPLKGGLNTPLHESDFSGVTPQRQVVQTPNTVLSTPFRTPSNGAEGLTPRSGTTPKPVINSTPGRTPLRDKLNINPEDGMADYSDPSYVKQMERESREHLRLGLLGLPAPKNDFEIVLPENAEKELEEREIDDTYIEDAADVDARKQAIRDAERVKEMKRMHKAVQKDLPRPSEVNETILRPLNVEPPLTDLQKSEELIKKEMITMLHYDLLHHPYEPSGNKKGKTVGFGTNNSEHITYLEHNPYEKFSKEELKKAQDVLVQEMEVVKQGMSHGELSSEAYNQVWEECYSQVLYLPGQSRYTRANLASKKDRIESLEKRLEINRGHMTTEAKRAAKMEKKMKILLGGYQSRAMGLMKQLNDLWDQIEQAHLELRTFEELKKHEDSAIPRRLECLKEDVQRQQEREKELQHRYADLLLEKETLKSKF
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms Distributed under the Creative Commons Attribution (CC BY 4.0) License