CASC3_MOUSE - dbPTM
CASC3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
10PhosphorylationDRRRQRASQDTEDEE
HHHHHHHHCCCCCHH
30.6727087446
13PhosphorylationRQRASQDTEDEESGA
HHHHHCCCCCHHHCC
37.3927087446
18PhosphorylationQDTEDEESGASGSDS
CCCCCHHHCCCCCCC
37.3030635358
25PhosphorylationSGASGSDSGSPARGG
HCCCCCCCCCCCCCC
42.7525195567
27PhosphorylationASGSDSGSPARGGGS
CCCCCCCCCCCCCCC
21.2425195567
34PhosphorylationSPARGGGSCSGSVGG
CCCCCCCCCCCCCCC
14.3725521595
36PhosphorylationARGGGSCSGSVGGGG
CCCCCCCCCCCCCCC
35.4825619855
38PhosphorylationGGGSCSGSVGGGGSG
CCCCCCCCCCCCCCC
10.9925619855
44PhosphorylationGSVGGGGSGSLPSQR
CCCCCCCCCCCCCCC
28.6028973931
46PhosphorylationVGGGGSGSLPSQRGG
CCCCCCCCCCCCCCC
38.5125619855
49PhosphorylationGGSGSLPSQRGGRGG
CCCCCCCCCCCCCCC
37.4925619855
51MethylationSGSLPSQRGGRGGGL
CCCCCCCCCCCCCCE
54.60-
65PhosphorylationLHLRRVESGGAKSAE
EEEEEECCCCCCCHH
39.4027087446
114UbiquitinationENSKVELKSEANDAA
HHCCCCHHHHHHHHH
32.5122790023
115PhosphorylationNSKVELKSEANDAAD
HCCCCHHHHHHHHHH
55.3425521595
123PhosphorylationEANDAADSSAKEKGE
HHHHHHHHHHHHHCC
27.7125266776
124PhosphorylationANDAADSSAKEKGEE
HHHHHHHHHHHHCCC
43.8625777480
135PhosphorylationKGEEKPESKGTVTGE
HCCCCCCCCCEECEE
44.9325777480
138PhosphorylationEKPESKGTVTGERQS
CCCCCCCEECEEEEC
20.7327742792
140PhosphorylationPESKGTVTGERQSGD
CCCCCEECEEEECCC
32.9127742792
145PhosphorylationTVTGERQSGDGQEST
EECEEEECCCCCCCC
45.1027087446
151PhosphorylationQSGDGQESTEPVENK
ECCCCCCCCCCCCCC
30.1327742792
152PhosphorylationSGDGQESTEPVENKV
CCCCCCCCCCCCCCC
43.4827087446
174UbiquitinationLDDDEDRKNPAYIPR
CCCCHHCCCCCCCCC
78.5622790023
182UbiquitinationNPAYIPRKGLFFEHD
CCCCCCCCCCCCCCC
55.3922790023
202UbiquitinationQEEEVRPKGRQRKLW
CCEECCCCCHHCCHH
57.0427667366
243PhosphorylationLYGYDIRSAHNPDDI
HHCCCHHHCCCCCCC
33.9323737553
262PhosphorylationIRKPRFGSSPQRDPN
CCCCCCCCCCCCCCC
35.8127742792
263PhosphorylationRKPRFGSSPQRDPNW
CCCCCCCCCCCCCCC
25.9827087446
275PhosphorylationPNWIGDRSSKSHRHQ
CCCCCCCCCCCCCCC
47.0223984901
276PhosphorylationNWIGDRSSKSHRHQG
CCCCCCCCCCCCCCC
38.7923984901
307PhosphorylationGTGRMSASRNYSRSG
CCCCCCCCCCCCCCC
17.47-
321PhosphorylationGGFKDGRTSFRPVEV
CCCCCCCCCCEEEEE
37.4328725479
322PhosphorylationGFKDGRTSFRPVEVA
CCCCCCCCCEEEEEC
20.2129176673
345PhosphorylationETLKHEASYRSRRLE
HHHHHHHHHHHHCCC
20.3527149854
346PhosphorylationTLKHEASYRSRRLEQ
HHHHHHHHHHHCCCC
21.47-
354PhosphorylationRSRRLEQTPVRDPSP
HHHCCCCCCCCCCCC
17.8622324799
360PhosphorylationQTPVRDPSPEPDAPL
CCCCCCCCCCCCCCC
46.3025521595
370PhosphorylationPDAPLLGSPEKEEVA
CCCCCCCCCCHHHHH
29.8325521595
378PhosphorylationPEKEEVASETPAAVP
CCHHHHHCCCCCCCC
47.3719060867
380PhosphorylationKEEVASETPAAVPDI
HHHHHCCCCCCCCCC
18.7425293948
388PhosphorylationPAAVPDITPPAPDRP
CCCCCCCCCCCCCCC
30.5125293948
470PhosphorylationQLNIAEQSWSPSQPS
HHHHHHHCCCCCCCC
22.4926643407
472PhosphorylationNIAEQSWSPSQPSFL
HHHHHCCCCCCCCCC
21.6623649490
474PhosphorylationAEQSWSPSQPSFLQP
HHHCCCCCCCCCCCH
49.5626643407
684PhosphorylationRRTPQPVSIKPPPPE
CCCCCCCCCCCCCHH
31.4228285833
694PhosphorylationPPPPEVVSRGSS---
CCCHHHHCCCCC---
35.7823684622

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CASC3_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CASC3_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STAU1_MOUSEStau1physical
12843282

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CASC3_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

TOP