CASC3
entrez
22794
canonical
uniprot
O15234
canonical
ensembl
ENSG00000108349
resolver
ensp
ENSP00000264645
resolver
ensp
ENSP00000523451
resolver
ensp
ENSP00000523452
resolver
ensp
ENSP00000523455
resolver
ensp
ENSP00000523464
resolver
ensp
ENSP00000523465
resolver
ensp
ENSP00000641424
resolver
ensp
ENSP00000746122
resolver
enst
ENST00000264645
resolver
enst
ENST00000853392
resolver
enst
ENST00000853393
resolver
enst
ENST00000853396
resolver
enst
ENST00000853405
resolver
enst
ENST00000853406
resolver
enst
ENST00000971365
resolver
genesymbol
CASC3
resolver
genesymbol_syn
MLN51
resolver
hgnc
HGNC:17040
resolver
uniprot
A8K8R0
resolver
uniprot_entry
CASC3_HUMAN
resolver
uniprot_sec
A8K8R0
resolver
amino_acid_sequence
MADRRRQRASQDTEDEESGASGSDSGGSPLRGGGSCSGSAGGGGSGSLPSQRGGRTGALHLRRVESGGAKSAEESECESEDGIEGDAVLSDYESAEDSEGEEGEYSEEENSKVELKSEANDAVNSSTKEEKGEEKPDTKSTVTGERQSGDGQESTEPVENKVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYDIRSAHNPDDIKPRRIRKPRYGSPPQRDPNWNGERLNKSHRHQGLGGTLPPRTFINRNAAGTGRMSAPRNYSRSGGFKEGRAGFRPVEAGGQHGGRSGETVKHEISYRSRRLEQTSVRDPSPEADAPVLGSPEKEEAASEPPAAAPDAAPPPPDRPIEKKSYSRARRTRTKVGDAVKLAEEVPPPPEGLIPAPPVPETTPTPPTKTGTWEAPVDSSTSGLEQDVAQLNIAEQNWSPGQPSFLQPRELRGMPNHIHMGAGPPPQFNRMEEMGVQGGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTHGDSPAPLPPQGMLVQPGMNLPHPGLHPHQTPAPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPSYPYAPGALPPPPPPHLYPNTQAPSQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVTIKPPPPEVVSRGSS
uniprot
proteins
function
FUNCTION: Required for pre-mRNA splicing as component of the spliceosome (PubMed:28502770, PubMed:29301961). Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Binds poly(G) and poly(U) RNA homomer. {ECO:0000269|PubMed:17375189, ECO:0000269|PubMed:17652158, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}.
uniprot
proteins
mass_dalton
76278
uniprot
proteins
mutagenesis
MUTAGEN 181; /note="Y->A: Does not affect EJC formation."; /evidence="ECO:0000269|PubMed:16170325"; MUTAGEN 184..185; /note="RK->AA: Does not affect EJC formation."; /evidence="ECO:0000269|PubMed:16170325"; MUTAGEN 188; /note="F->A: Does not affect EJC formation."; /evidence="ECO:0000269|PubMed:16170325"; MUTAGEN 218; /note="W->A: Abolishes interaction with EIF4A3, EJC formation and localization in nucleus speckles."; /evidence="ECO:0000269|PubMed:16170325"; MUTAGEN 220..221; /note="HD->AA: Abolishes interaction with EIF4A3, EJC formation and localization in nucleus speckles."; /evidence="ECO:0000269|PubMed:16170325"; MUTAGEN 240..241; /note="YG->AA: Abolishes interaction with EIF4A3, EJC formation and localization in nucleus speckles."; /evidence="ECO:0000269|PubMed:16170325
uniprot
proteins
post_translational_modification
PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination. {ECO:0000269|PubMed:21478859}.; PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation. {ECO:0000269|PubMed:21478859}.
uniprot
proteins
protein_family
CASC3 family
uniprot
proteins
pubmed
11980659
uniprot
proteins
pubmed
12080473
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15166247
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16170325
uniprot
proteins
pubmed
16314458
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16923391
uniprot
proteins
pubmed
16931718
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17375189
uniprot
proteins
pubmed
17652158
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19033377
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20479275
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21478859
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25220460
uniprot
proteins
pubmed
28502770
uniprot
proteins
pubmed
29301961
uniprot
proteins
pubmed
7490069
uniprot
proteins
sequence_length
703
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12080473}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K3W3}. Nucleus {ECO:0000269|PubMed:12080473, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}. Nucleus speckle {ECO:0000269|PubMed:16170325}. Cytoplasm, Stress granule {ECO:0000269|PubMed:17652158}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q8K3X0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8K3X0}. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner. Transported to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (PubMed:15166247). In nuclear speckles, colocalizes with MAGOH. Under stress conditions, colocalizes with FMR1 and TIA1, but not MAGOH and RBM8A EJC core factors, in cytoplasmic stress granules (PubMed:17652158). In the dendrites of hippocampal neurons, localizes to dendritic ribonucleoprotein granules (By similarity). {ECO:0000250|UniProtKB:Q8K3X0, ECO:0000269|PubMed:15166247, ECO:0000269|PubMed:17652158}.
uniprot
proteins