UniProt ID | CASC3_MOUSE | |
---|---|---|
UniProt AC | Q8K3W3 | |
Protein Name | Protein CASC3 | |
Gene Name | Casc3 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 698 | |
Subcellular Localization | Cytoplasm . Cytoplasm, perinuclear region . Nucleus . Nucleus speckle . Cytoplasm, Stress granule . Cytoplasm, Cytoplasmic ribonucleoprotein granule . Cell projection, dendrite . Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent | |
Protein Description | 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 homopolymer (By similarity).. | |
Protein Sequence | MADRRRQRASQDTEDEESGASGSDSGSPARGGGSCSGSVGGGGSGSLPSQRGGRGGGLHLRRVESGGAKSAEESECESEDGMEGDAVLSDYESAEDSEGEEDYSEEENSKVELKSEANDAADSSAKEKGEEKPESKGTVTGERQSGDGQESTEPVENKVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYDIRSAHNPDDIKPRRIRKPRFGSSPQRDPNWIGDRSSKSHRHQGPGGNLPPRTFINRNTAGTGRMSASRNYSRSGGFKDGRTSFRPVEVAGQHGGRSAETLKHEASYRSRRLEQTPVRDPSPEPDAPLLGSPEKEEVASETPAAVPDITPPAPDRPIEKKSYSRARRTRTKVGDAVKAAEEVPPPSEGLASTATVPETTPAAKTGNWEAPVDSTTGGLEQDVAQLNIAEQSWSPSQPSFLQPRELRGVPNHIHMGAGPPPQFNRMEEMGVQSGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTHGDSPAPLPPQGMIVQPEMHLPHPGLHPHQSPGPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPNYPYAPGALPPPPPPHLYPNTQAPPQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVSIKPPPPEVVSRGSS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
10 | Phosphorylation | DRRRQRASQDTEDEE HHHHHHHHCCCCCHH | 30.67 | 27087446 | |
13 | Phosphorylation | RQRASQDTEDEESGA HHHHHCCCCCHHHCC | 37.39 | 27087446 | |
18 | Phosphorylation | QDTEDEESGASGSDS CCCCCHHHCCCCCCC | 37.30 | 30635358 | |
25 | Phosphorylation | SGASGSDSGSPARGG HCCCCCCCCCCCCCC | 42.75 | 25195567 | |
27 | Phosphorylation | ASGSDSGSPARGGGS CCCCCCCCCCCCCCC | 21.24 | 25195567 | |
34 | Phosphorylation | SPARGGGSCSGSVGG CCCCCCCCCCCCCCC | 14.37 | 25521595 | |
36 | Phosphorylation | ARGGGSCSGSVGGGG CCCCCCCCCCCCCCC | 35.48 | 25619855 | |
38 | Phosphorylation | GGGSCSGSVGGGGSG CCCCCCCCCCCCCCC | 10.99 | 25619855 | |
44 | Phosphorylation | GSVGGGGSGSLPSQR CCCCCCCCCCCCCCC | 28.60 | 28973931 | |
46 | Phosphorylation | VGGGGSGSLPSQRGG CCCCCCCCCCCCCCC | 38.51 | 25619855 | |
49 | Phosphorylation | GGSGSLPSQRGGRGG CCCCCCCCCCCCCCC | 37.49 | 25619855 | |
51 | Methylation | SGSLPSQRGGRGGGL CCCCCCCCCCCCCCE | 54.60 | - | |
65 | Phosphorylation | LHLRRVESGGAKSAE EEEEEECCCCCCCHH | 39.40 | 27087446 | |
114 | Ubiquitination | ENSKVELKSEANDAA HHCCCCHHHHHHHHH | 32.51 | 22790023 | |
115 | Phosphorylation | NSKVELKSEANDAAD HCCCCHHHHHHHHHH | 55.34 | 25521595 | |
123 | Phosphorylation | EANDAADSSAKEKGE HHHHHHHHHHHHHCC | 27.71 | 25266776 | |
124 | Phosphorylation | ANDAADSSAKEKGEE HHHHHHHHHHHHCCC | 43.86 | 25777480 | |
135 | Phosphorylation | KGEEKPESKGTVTGE HCCCCCCCCCEECEE | 44.93 | 25777480 | |
138 | Phosphorylation | EKPESKGTVTGERQS CCCCCCCEECEEEEC | 20.73 | 27742792 | |
140 | Phosphorylation | PESKGTVTGERQSGD CCCCCEECEEEECCC | 32.91 | 27742792 | |
145 | Phosphorylation | TVTGERQSGDGQEST EECEEEECCCCCCCC | 45.10 | 27087446 | |
151 | Phosphorylation | QSGDGQESTEPVENK ECCCCCCCCCCCCCC | 30.13 | 27742792 | |
152 | Phosphorylation | SGDGQESTEPVENKV CCCCCCCCCCCCCCC | 43.48 | 27087446 | |
174 | Ubiquitination | LDDDEDRKNPAYIPR CCCCHHCCCCCCCCC | 78.56 | 22790023 | |
182 | Ubiquitination | NPAYIPRKGLFFEHD CCCCCCCCCCCCCCC | 55.39 | 22790023 | |
202 | Ubiquitination | QEEEVRPKGRQRKLW CCEECCCCCHHCCHH | 57.04 | 27667366 | |
243 | Phosphorylation | LYGYDIRSAHNPDDI HHCCCHHHCCCCCCC | 33.93 | 23737553 | |
262 | Phosphorylation | IRKPRFGSSPQRDPN CCCCCCCCCCCCCCC | 35.81 | 27742792 | |
263 | Phosphorylation | RKPRFGSSPQRDPNW CCCCCCCCCCCCCCC | 25.98 | 27087446 | |
275 | Phosphorylation | PNWIGDRSSKSHRHQ CCCCCCCCCCCCCCC | 47.02 | 23984901 | |
276 | Phosphorylation | NWIGDRSSKSHRHQG CCCCCCCCCCCCCCC | 38.79 | 23984901 | |
307 | Phosphorylation | GTGRMSASRNYSRSG CCCCCCCCCCCCCCC | 17.47 | - | |
321 | Phosphorylation | GGFKDGRTSFRPVEV CCCCCCCCCCEEEEE | 37.43 | 28725479 | |
322 | Phosphorylation | GFKDGRTSFRPVEVA CCCCCCCCCEEEEEC | 20.21 | 29176673 | |
345 | Phosphorylation | ETLKHEASYRSRRLE HHHHHHHHHHHHCCC | 20.35 | 27149854 | |
346 | Phosphorylation | TLKHEASYRSRRLEQ HHHHHHHHHHHCCCC | 21.47 | - | |
354 | Phosphorylation | RSRRLEQTPVRDPSP HHHCCCCCCCCCCCC | 17.86 | 22324799 | |
360 | Phosphorylation | QTPVRDPSPEPDAPL CCCCCCCCCCCCCCC | 46.30 | 25521595 | |
370 | Phosphorylation | PDAPLLGSPEKEEVA CCCCCCCCCCHHHHH | 29.83 | 25521595 | |
378 | Phosphorylation | PEKEEVASETPAAVP CCHHHHHCCCCCCCC | 47.37 | 19060867 | |
380 | Phosphorylation | KEEVASETPAAVPDI HHHHHCCCCCCCCCC | 18.74 | 25293948 | |
388 | Phosphorylation | PAAVPDITPPAPDRP CCCCCCCCCCCCCCC | 30.51 | 25293948 | |
470 | Phosphorylation | QLNIAEQSWSPSQPS HHHHHHHCCCCCCCC | 22.49 | 26643407 | |
472 | Phosphorylation | NIAEQSWSPSQPSFL HHHHHCCCCCCCCCC | 21.66 | 23649490 | |
474 | Phosphorylation | AEQSWSPSQPSFLQP HHHCCCCCCCCCCCH | 49.56 | 26643407 | |
684 | Phosphorylation | RRTPQPVSIKPPPPE CCCCCCCCCCCCCHH | 31.42 | 28285833 | |
694 | Phosphorylation | PPPPEVVSRGSS--- CCCHHHHCCCCC--- | 35.78 | 23684622 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of CASC3_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CASC3_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CASC3_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
STAU1_MOUSE | Stau1 | physical | 12843282 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, AND MASSSPECTROMETRY. | |
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND MASSSPECTROMETRY. | |
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASSSPECTROMETRY. |