dbPTM

CASC3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CASC3_HUMAN
UniProt AC	O15234
Protein Name	Protein CASC3
Gene Name	CASC3
Organism	Homo sapiens (Human).
Sequence Length	703
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..
Protein Sequence	MADRRRQRASQDTEDEESGASGSDSGGSPLRGGGSCSGSAGGGGSGSLPSQRGGRTGALHLRRVESGGAKSAEESECESEDGIEGDAVLSDYESAEDSEGEEGEYSEEENSKVELKSEANDAVNSSTKEEKGEEKPDTKSTVTGERQSGDGQESTEPVENKVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYDIRSAHNPDDIKPRRIRKPRYGSPPQRDPNWNGERLNKSHRHQGLGGTLPPRTFINRNAAGTGRMSAPRNYSRSGGFKEGRAGFRPVEAGGQHGGRSGETVKHEISYRSRRLEQTSVRDPSPEADAPVLGSPEKEEAASEPPAAAPDAAPPPPDRPIEKKSYSRARRTRTKVGDAVKLAEEVPPPPEGLIPAPPVPETTPTPPTKTGTWEAPVDSSTSGLEQDVAQLNIAEQNWSPGQPSFLQPRELRGMPNHIHMGAGPPPQFNRMEEMGVQGGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTHGDSPAPLPPQGMLVQPGMNLPHPGLHPHQTPAPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPSYPYAPGALPPPPPPHLYPNTQAPSQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVTIKPPPPEVVSRGSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	DRRRQRASQDTEDEE HHHHHHHHCCCCCHH	30.67	20873877
13	Phosphorylation	RQRASQDTEDEESGA HHHHHCCCCCHHHCC	37.39	28985074
18	Phosphorylation	QDTEDEESGASGSDS CCCCCHHHCCCCCCC	37.30	29888752
21	Phosphorylation	EDEESGASGSDSGGS CCHHHCCCCCCCCCC	42.21	20873877
23	Phosphorylation	EESGASGSDSGGSPL HHHCCCCCCCCCCCC	26.55	20873877
25	Phosphorylation	SGASGSDSGGSPLRG HCCCCCCCCCCCCCC	46.91	20873877
28	Phosphorylation	SGSDSGGSPLRGGGS CCCCCCCCCCCCCCC	25.04	25849741
35	Phosphorylation	SPLRGGGSCSGSAGG CCCCCCCCCCCCCCC	14.37	29255136
37	Phosphorylation	LRGGGSCSGSAGGGG CCCCCCCCCCCCCCC	37.16	29255136
39	Phosphorylation	GGGSCSGSAGGGGSG CCCCCCCCCCCCCCC	13.88	29255136
45	Phosphorylation	GSAGGGGSGSLPSQR CCCCCCCCCCCCCCC	28.60	23401153
47	Phosphorylation	AGGGGSGSLPSQRGG CCCCCCCCCCCCCCC	38.51	29255136
50	Phosphorylation	GGSGSLPSQRGGRTG CCCCCCCCCCCCCCC	37.49	29255136
52	Methylation	SGSLPSQRGGRTGAL CCCCCCCCCCCCCCE	54.60	-
55	Methylation	LPSQRGGRTGALHLR CCCCCCCCCCCEEEE	32.58	-
66	Phosphorylation	LHLRRVESGGAKSAE EEEEEHHCCCCCCHH	39.40	25884760
116	Ubiquitination	ENSKVELKSEANDAV HHCCEEEHHHHHHHH	32.51	33845483
117	Phosphorylation	NSKVELKSEANDAVN HCCEEEHHHHHHHHH	55.34	29255136
125	Phosphorylation	EANDAVNSSTKEEKG HHHHHHHCCCCCCCC	32.55	23401153
126	Phosphorylation	ANDAVNSSTKEEKGE HHHHHHCCCCCCCCC	37.99	29255136
127	Phosphorylation	NDAVNSSTKEEKGEE HHHHHCCCCCCCCCC	42.15	29255136
128	Ubiquitination	DAVNSSTKEEKGEEK HHHHCCCCCCCCCCC	66.86	21906983
131	Ubiquitination	NSSTKEEKGEEKPDT HCCCCCCCCCCCCCC	73.11	22817900
138	Phosphorylation	KGEEKPDTKSTVTGE CCCCCCCCCCEECCC	35.11	30108239
139	Ubiquitination	GEEKPDTKSTVTGER CCCCCCCCCEECCCC	52.05	32015554
140	Phosphorylation	EEKPDTKSTVTGERQ CCCCCCCCEECCCCC	30.15	23927012
141	Phosphorylation	EKPDTKSTVTGERQS CCCCCCCEECCCCCC	24.52	23927012
143	Phosphorylation	PDTKSTVTGERQSGD CCCCCEECCCCCCCC	33.15	20201521
148	Phosphorylation	TVTGERQSGDGQEST EECCCCCCCCCCCCC	45.10	29255136
154	Phosphorylation	QSGDGQESTEPVENK CCCCCCCCCCCCCCC	30.13	23927012
155	Phosphorylation	SGDGQESTEPVENKV CCCCCCCCCCCCCCC	43.48	23927012
161	Ubiquitination	STEPVENKVGKKGPK CCCCCCCCCCCCCCC	38.57	21906983
164	Ubiquitination	PVENKVGKKGPKHLD CCCCCCCCCCCCCCC	58.50	22817900
165	Ubiquitination	VENKVGKKGPKHLDD CCCCCCCCCCCCCCC	74.62	22817900
168	Ubiquitination	KVGKKGPKHLDDDED CCCCCCCCCCCCCHH	66.52	29967540
177	Ubiquitination	LDDDEDRKNPAYIPR CCCCHHCCCCCCCCC	78.56	33845483
181	Phosphorylation	EDRKNPAYIPRKGLF HHCCCCCCCCCCCCC	16.83	-
185	Ubiquitination	NPAYIPRKGLFFEHD CCCCCCCCCCCCCCC	55.39	33845483
194	Methylation	LFFEHDLRGQTQEEE CCCCCCCCCCCCCEE	41.03	-
197	Phosphorylation	EHDLRGQTQEEEVRP CCCCCCCCCCEECCC	40.55	28555341
205	Ubiquitination	QEEEVRPKGRQRKLW CCEECCCCCHHCCHH	57.04	24816145
213	Ubiquitination	GRQRKLWKDEGRWEH CHHCCHHHCCCCCCC	57.23	29967540
240	Phosphorylation	RQELIALYGYDIRSA HHHHHHHHCCCHHHC	12.48	27642862
254	Ubiquitination	AHNPDDIKPRRIRKP CCCCCCCCCCCCCCC	39.19	24816145
263	Phosphorylation	RRIRKPRYGSPPQRD CCCCCCCCCCCCCCC	30.40	30266825
265	Phosphorylation	IRKPRYGSPPQRDPN CCCCCCCCCCCCCCC	25.19	23927012
295	Phosphorylation	GGTLPPRTFINRNAA CCCCCCCCCCCCCCC	34.34	24505115
304	Phosphorylation	INRNAAGTGRMSAPR CCCCCCCCCCCCCCC	19.52	28290473
306	Methylation	RNAAGTGRMSAPRNY CCCCCCCCCCCCCCC	18.73	-
308	Phosphorylation	AAGTGRMSAPRNYSR CCCCCCCCCCCCCCC	33.49	27251789
313	Phosphorylation	RMSAPRNYSRSGGFK CCCCCCCCCCCCCCC	13.52	29759185
320	Ubiquitination	YSRSGGFKEGRAGFR CCCCCCCCCCCCCCE	63.63	33845483
323	Methylation	SGGFKEGRAGFRPVE CCCCCCCCCCCEEEC	32.40	-
339	Phosphorylation	GGQHGGRSGETVKHE CCCCCCCCCCCCCHH	44.23	28555341
342	Phosphorylation	HGGRSGETVKHEISY CCCCCCCCCCHHHHH	38.08	29449344
344	Ubiquitination	GRSGETVKHEISYRS CCCCCCCCHHHHHHH	42.83	33845483
348	Phosphorylation	ETVKHEISYRSRRLE CCCCHHHHHHHHCCE	16.12	27251275
349	Phosphorylation	TVKHEISYRSRRLEQ CCCHHHHHHHHCCEE	20.47	25839225
357	Phosphorylation	RSRRLEQTSVRDPSP HHHCCEECCCCCCCC	21.58	23898821
358	Phosphorylation	SRRLEQTSVRDPSPE HHCCEECCCCCCCCC	18.17	19276368
363	Phosphorylation	QTSVRDPSPEADAPV ECCCCCCCCCCCCCC	39.39	19664994
373	Phosphorylation	ADAPVLGSPEKEEAA CCCCCCCCHHHHHHH	26.23	29255136
381	Phosphorylation	PEKEEAASEPPAAAP HHHHHHHCCCCCCCC	58.65	25159151
440	Phosphorylation	PAPPVPETTPTPPTK CCCCCCCCCCCCCCC	31.82	30266825
441	Phosphorylation	APPVPETTPTPPTKT CCCCCCCCCCCCCCC	24.41	30266825
443	Phosphorylation	PVPETTPTPPTKTGT CCCCCCCCCCCCCCC	39.55	30266825
446	Phosphorylation	ETTPTPPTKTGTWEA CCCCCCCCCCCCEEC	42.30	30266825
448	Phosphorylation	TPTPPTKTGTWEAPV CCCCCCCCCCEECCC	42.18	26074081
450	Phosphorylation	TPPTKTGTWEAPVDS CCCCCCCCEECCCCC	25.93	26074081
477	Phosphorylation	NIAEQNWSPGQPSFL HHHHHCCCCCCCCCC	27.05	16170325
482	Phosphorylation	NWSPGQPSFLQPREL CCCCCCCCCCCHHHH	30.60	26074081
490	Methylation	FLQPRELRGMPNHIH CCCHHHHCCCCCCCC	34.31	-
518	Methylation	EMGVQGGRAKRYSSQ HHCCCCCCHHCCCCC	43.70	-
667	Phosphorylation	VYGGVTYYNPAQQQV EECCEEEECHHHCCC	12.80	26074081
679	Phosphorylation	QQVQPKPSPPRRTPQ CCCCCCCCCCCCCCC	54.37	26074081
684	Phosphorylation	KPSPPRRTPQPVTIK CCCCCCCCCCCCEEC	27.79	20873877
689	Phosphorylation	RRTPQPVTIKPPPPE CCCCCCCEECCCCHH	29.93	26074081
699	Phosphorylation	PPPPEVVSRGSS--- CCCHHHCCCCCC---	35.78	25159151
702	Phosphorylation	PEVVSRGSS------ HHHCCCCCC------	31.59	30576142
703	Phosphorylation	EVVSRGSS------- HHCCCCCC-------	47.25	29496963

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
-	K	Ubiquitination	E3 ubiquitin ligase	RNF146	Q9NTX7	PMID:21478859

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CASC3_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
GRB2_HUMAN	GRB2	physical	21988832

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CASC3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-45 AND SER-148,AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-477, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363 AND SER-373, ANDMASS SPECTROMETRY.	17081983 [Abstract]