CDC5L
entrez
988
canonical
uniprot
Q99459
canonical
ensembl
ENSG00000096401
resolver
ensp
ENSP00000360532
resolver
enst
ENST00000371477
resolver
genesymbol
CDC5L
resolver
genesymbol_syn
KIAA0432
resolver
genesymbol_syn
PCDC5RP
resolver
hgnc
HGNC:1743
resolver
uniprot
Q76N46
resolver
uniprot
Q99974
resolver
uniprot_entry
CDC5L_HUMAN
resolver
uniprot_sec
Q76N46
resolver
uniprot_sec
Q99974
resolver
amino_acid_sequence
MPRIMIKGGVWRNTEDEILKAAVMKYGKNQWSRIASLLHRKSAKQCKARWYEWLDPSIKKTEWSREEEEKLLHLAKLMPTQWRTIAPIIGRTAAQCLEHYEFLLDKAAQRDNEEETTDDPRKLKPGEIDPNPETKPARPDPIDMDEDELEMLSEARARLANTQGKKAKRKAREKQLEEARRLAALQKRRELRAAGIEIQKKRKRKRGVDYNAEIPFEKKPALGFYDTSEENYQALDADFRKLRQQDLDGELRSEKEGRDRKKDKQHLKRKKESDLPSAILQTSGVSEFTKKRSKLVLPAPQISDAELQEVVKVGQASEIARQTAEESGITNSASSTLLSEYNVTNNSVALRTPRTPASQDRILQEAQNLMALTNVDTPLKGGLNTPLHESDFSGVTPQRQVVQTPNTVLSTPFRTPSNGAEGLTPRSGTTPKPVINSTPGRTPLRDKLNINPEDGMADYSDPSYVKQMERESREHLRLGLLGLPAPKNDFEIVLPENAEKELEEREIDDTYIEDAADVDARKQAIRDAERVKEMKRMHKAVQKDLPRPSEVNETILRPLNVEPPLTDLQKSEELIKKEMITMLHYDLLHHPYEPSGNKKGKTVGFGTNNSEHITYLEHNPYEKFSKEELKKAQDVLVQEMEVVKQGMSHGELSSEAYNQVWEECYSQVLYLPGQSRYTRANLASKKDRIESLEKRLEINRGHMTTEAKRAAKMEKKMKILLGGYQSRAMGLMKQLNDLWDQIEQAHLELRTFEELKKHEDSAIPRRLECLKEDVQRQQEREKELQHRYADLLLEKETLKSKF
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving CDC5L is found in multicystic renal dysplasia. Translocation t(6;19)(p21;q13.1) with USF2.
uniprot
proteins
function
FUNCTION: DNA-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:28076346, PubMed:28502770, PubMed:29301961, PubMed:29360106, PubMed:29361316, PubMed:30705154, PubMed:30728453). 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). {ECO:0000269|PubMed:10570151, ECO:0000269|PubMed:11082045, ECO:0000269|PubMed:11101529, ECO:0000269|PubMed:11544257, ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12927788, ECO:0000269|PubMed:18583928, ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:30728453, ECO:0000269|PubMed:9038199, ECO:0000269|PubMed:9468527, ECO:0000269|PubMed:9632794, ECO:0000305|PubMed:33509932}.
uniprot
proteins
mass_dalton
92251
uniprot
proteins
mutagenesis
MUTAGEN 31; /note="W->G: Abolishes DNA-binding; when associated with G-53 and G-82."; /evidence="ECO:0000269|PubMed:11082045"; MUTAGEN 53; /note="W->G: Abolishes DNA-binding; when associated with G-31 and G-82."; /evidence="ECO:0000269|PubMed:11082045"; MUTAGEN 82; /note="W->G: Abolishes DNA-binding; when associated with G-31 and G-53."; /evidence="ECO:0000269|PubMed:11082045"; MUTAGEN 227; /note="T->A: Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-303; A-358; A-385; A-404; A-411; A-417; A-424 and A-438."; MUTAGEN 303; /note="S->A: Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-358; A-385; A-404; A-411; A-417; A-424 and A-438."; MUTAGEN 358; /note="S->A: Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-385; A-404; A-411; A-417; A-424 and A-438."; MUTAGEN 404; /note="T->A: Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-358; A-385; A-411; A-417; A-424 and A-438."; MUTAGEN 411; /note="T->A: Abolishes phosphorylation. Markedly diminished pre-mRNA splicing activity; when associated with A-438. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-358; A-385; A-404; A-417; A-424 and A-438."; /evidence="ECO:0000269|PubMed:18583928"; MUTAGEN 417; /note="S->A: Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-358; A-385; A-404; A-411; A-424 and A-438."; MUTAGEN 424; /note="T->A: Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-358; A-385; A-404; A-411; A-417 and A-438."; MUTAGEN 438; /note="T->A: Abolishes phosphorylation. Markedly diminished pre-mRNA splicing activity; when associated with A-411. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-358; A-385; A-404; A-411; A-417 and A-424."; /evidence="ECO:0000269|PubMed:18583928
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:10827081, ECO:0000269|PubMed:18583928, ECO:0000269|PubMed:9038199}.
uniprot
proteins
protein_family
CEF1 family
uniprot
proteins
pubmed
10570151
uniprot
proteins
pubmed
10827081
uniprot
proteins
pubmed
11082045
uniprot
proteins
pubmed
11101529
uniprot
proteins
pubmed
11544257
uniprot
proteins
pubmed
11991638
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
12927788
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18583928
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18722174
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20176811
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21385873
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23022480
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24332808
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
28076346
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28502770
uniprot
proteins
pubmed
29301961
uniprot
proteins
pubmed
29360106
uniprot
proteins
pubmed
29361316
uniprot
proteins
pubmed
30705154
uniprot
proteins
pubmed
30728453
uniprot
proteins
pubmed
32484799
uniprot
proteins
pubmed
33509932
uniprot
proteins
pubmed
36229594
uniprot
proteins
pubmed
8917598
uniprot
proteins
pubmed
9038199
uniprot
proteins
pubmed
9455477
uniprot
proteins
pubmed
9468527
uniprot
proteins
pubmed
9598309
uniprot
proteins
pubmed
9632794
uniprot
proteins
pubmed
9731529
uniprot
proteins
sequence_length
802
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10570151, ECO:0000269|PubMed:11544257, ECO:0000269|PubMed:18583928, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:30728453, ECO:0000269|PubMed:9038199, ECO:0000269|PubMed:9598309}. Nucleus speckle {ECO:0000269|PubMed:10570151, ECO:0000269|PubMed:10827081, ECO:0000269|PubMed:11544257}. Cytoplasm {ECO:0000269|PubMed:9038199}. Note=May shuttle between cytoplasm and nucleus. {ECO:0000269|PubMed:9038199}.
uniprot
proteins