Details for: CDC5L

Gene ID: 988

Symbol: CDC5L

Ensembl ID: ENSG00000096401

Description: cell division cycle 5 like

Associated with

Other Information

Genular Protein ID: 4214608898

Symbol: CDC5L_HUMAN

Name: Cell division cycle 5-like protein

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 9038199

Title: Pombe Cdc5-related protein. A putative human transcription factor implicated in mitogen-activated signaling.

PubMed ID: 9038199

DOI: 10.1074/jbc.272.9.5833

PubMed ID: 9598309

Title: Rearrangement of the human CDC5L gene by a t(6;19)(p21;q13.1) in a patient with multicystic renal dysplasia.

PubMed ID: 9598309

DOI: 10.1006/geno.1998.5254

PubMed ID: 9632794

Title: Myb-related Schizosaccharomyces pombe cdc5p is structurally and functionally conserved in eukaryotes.

PubMed ID: 9632794

DOI: 10.1128/mcb.18.7.4097

PubMed ID: 9455477

Title: Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro.

PubMed ID: 9455477

DOI: 10.1093/dnares/4.5.307

PubMed ID: 12168954

Title: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.

PubMed ID: 12168954

DOI: 10.1093/dnares/9.3.99

PubMed ID: 14574404

Title: The DNA sequence and analysis of human chromosome 6.

PubMed ID: 14574404

DOI: 10.1038/nature02055

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8917598

Title: A cdc5+ homolog of a higher plant, Arabidopsis thaliana.

PubMed ID: 8917598

DOI: 10.1073/pnas.93.23.13371

PubMed ID: 10827081

Title: NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a regulator of pre-mRNA splicing and mitotic entry.

PubMed ID: 10827081

DOI: 10.1074/jbc.m001676200

PubMed ID: 9468527

Title: A mammalian homolog of fission yeast Cdc5 regulates G2 progression and mitotic entry.

PubMed ID: 9468527

DOI: 10.1074/jbc.273.8.4666

PubMed ID: 9731529

Title: Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex.

PubMed ID: 9731529

DOI: 10.1038/1700

PubMed ID: 10570151

Title: Evidence that Myb-related CDC5 proteins are required for pre-mRNA splicing.

PubMed ID: 10570151

DOI: 10.1073/pnas.96.24.13789

PubMed ID: 11101529

Title: Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry.

PubMed ID: 11101529

DOI: 10.1093/emboj/19.23.6569

PubMed ID: 11082045

Title: Human Cdc5, a regulator of mitotic entry, can act as a site-specific DNA binding protein.

PubMed ID: 11082045

DOI: 10.1242/jcs.113.24.4523

PubMed ID: 11544257

Title: A direct interaction between the carboxyl-terminal region of CDC5L and the WD40 domain of PLRG1 is essential for pre-mRNA splicing.

PubMed ID: 11544257

DOI: 10.1074/jbc.m105453200

PubMed ID: 11991638

Title: Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.

PubMed ID: 11991638

DOI: 10.1017/s1355838202021088

PubMed ID: 12927788

Title: hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing.

PubMed ID: 12927788

DOI: 10.1016/s0006-291x(03)01486-4

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 18583928

Title: Cell cycle-dependent phosphorylation of human CDC5 regulates RNA processing.

PubMed ID: 18583928

DOI: 10.4161/cc.7.12.6017

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18722174

Title: Interaction between antibody-diversification enzyme AID and spliceosome-associated factor CTNNBL1.

PubMed ID: 18722174

DOI: 10.1016/j.molcel.2008.07.009

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20176811

Title: Molecular architecture of the human Prp19/CDC5L complex.

PubMed ID: 20176811

DOI: 10.1128/mcb.01505-09

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21385873

Title: CTNNBL1 is a novel nuclear localization sequence-binding protein that recognizes RNA-splicing factors CDC5L and Prp31.

PubMed ID: 21385873

DOI: 10.1074/jbc.m110.208769

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23022480

Title: Mpn1, mutated in poikiloderma with neutropenia protein 1, is a conserved 3'-to-5' RNA exonuclease processing U6 small nuclear RNA.

PubMed ID: 23022480

DOI: 10.1016/j.celrep.2012.08.031

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24332808

Title: PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry.

PubMed ID: 24332808

DOI: 10.1016/j.molcel.2013.11.002

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: 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.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 32484799

Title: Disease-associated CTNNBL1 mutation impairs somatic hypermutation by decreasing nuclear AID.

PubMed ID: 32484799

DOI: 10.1172/jci131297

PubMed ID: 28502770

Title: An Atomic Structure of the Human Spliceosome.

PubMed ID: 28502770

DOI: 10.1016/j.cell.2017.04.033

PubMed ID: 28076346

Title: Cryo-EM structure of a human spliceosome activated for step 2 of splicing.

PubMed ID: 28076346

DOI: 10.1038/nature21079

PubMed ID: 29361316

Title: Structure and Conformational Dynamics of the Human Spliceosomal Bact Complex.

PubMed ID: 29361316

DOI: 10.1016/j.cell.2018.01.010

PubMed ID: 29360106

Title: Structure of the human activated spliceosome in three conformational states.

PubMed ID: 29360106

DOI: 10.1038/cr.2018.14

PubMed ID: 29301961

Title: Structure of a human catalytic step I spliceosome.

PubMed ID: 29301961

DOI: 10.1126/science.aar6401

PubMed ID: 30728453

Title: Structures of the human spliceosomes before and after release of the ligated exon.

PubMed ID: 30728453

DOI: 10.1038/s41422-019-0143-x

PubMed ID: 30705154

Title: A human postcatalytic spliceosome structure reveals essential roles of metazoan factors for exon ligation.

PubMed ID: 30705154

DOI: 10.1126/science.aaw5569

PubMed ID: 33509932

Title: Structure of the activated human minor spliceosome.

PubMed ID: 33509932

DOI: 10.1126/science.abg0879

Sequence Information:

  • Length: 802
  • Mass: 92251
  • Checksum: 3390F91EE7E79DA6
  • Sequence:
  • 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

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.