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Protein CASC3 (Cancer susceptibility candidate gene 3 protein) (Metastatic lymph node gene 51 protein) (MLN 51) (Protein barentsz) (Btz)

 CASC3_HUMAN             Reviewed;         703 AA.
O15234; A8K8R0;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
14-AUG-2001, sequence version 2.
22-NOV-2017, entry version 168.
RecName: Full=Protein CASC3;
AltName: Full=Cancer susceptibility candidate gene 3 protein;
AltName: Full=Metastatic lymph node gene 51 protein;
Short=MLN 51;
AltName: Full=Protein barentsz;
Short=Btz;
Name=CASC3; Synonyms=MLN51;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary carcinoma;
PubMed=7490069; DOI=10.1006/geno.1995.1163;
Tomasetto C.L., Regnier C.H., Moog-Lutz C., Mattei M.-G.,
Chenard M.-P., Lidereau R., Basset P., Rio M.-C.;
"Identification of four novel human genes amplified and overexpressed
in breast carcinoma and localized to the q11-q21.3 region of
chromosome 17.";
Genomics 28:367-376(1995).
[2]
SEQUENCE REVISION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
PHOSPHORYLATION.
TISSUE=Mammary carcinoma;
PubMed=12080473; DOI=10.1038/sj.onc.1205611;
Degot S.F., Regnier C.H., Wendling C., Chenard M.-P., Rio M.-C.,
Tomasetto C.L.;
"Metastatic lymph node 51, a novel nucleo-cytoplasmic protein
overexpressed in breast cancer.";
Oncogene 21:4422-4434(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Duodenum, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
OVEREXPRESSION IN GASTRIC CANCERS.
PubMed=11980659;
Varis A., Wolf M., Monni O., Vakkari M.-L., Kokkola A., Moskaluk C.,
Frierson H.F. Jr., Powell S.M., Knuutila S., Kallioniemi A.,
El-Rifai W.;
"Targets of gene amplification and overexpression at 17q in gastric
cancer.";
Cancer Res. 62:2625-2629(2002).
[7]
INTERACTION WITH MAGOH; NXF1 AND RBM8A, RNA-BINDING, AND SUBCELLULAR
LOCATION.
PubMed=15166247; DOI=10.1074/jbc.M402754200;
Degot S., Le Hir H., Alpy F., Kedinger V., Stoll I., Wendling C.,
Seraphin B., Rio M.-C., Tomasetto C.;
"Association of the breast cancer protein MLN51 with the exon junction
complex via its speckle localizer and RNA binding module.";
J. Biol. Chem. 279:33702-33715(2004).
[8]
IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, INTERACTION WITH
EIF4A3, MUTAGENESIS OF TYR-181; 184-ARG-LYS-185; PHE-188; TRP-218;
220-HIS-ASP-221 AND 240-TYR-GLY-241, SUBCELLULAR LOCATION, AND
RNA-BINDING.
PubMed=16170325; DOI=10.1038/nsmb990;
Ballut L., Marchadier B., Baguet A., Tomasetto C., Seraphin B.,
Le Hir H.;
"The exon junction core complex is locked onto RNA by inhibition of
eIF4AIII ATPase activity.";
Nat. Struct. Mol. Biol. 12:861-869(2005).
[9]
IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, IDENTIFICATION IN A
MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=16314458; DOI=10.1261/rna.2155905;
Tange T.O., Shibuya T., Jurica M.S., Moore M.J.;
"Biochemical analysis of the EJC reveals two new factors and a stable
tetrameric protein core.";
RNA 11:1869-1883(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363 AND SER-373, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
FUNCTION IN STRESS RESPONSE, AND SUBCELLULAR LOCATION.
PubMed=17652158; DOI=10.1242/jcs.009225;
Baguet A., Degot S., Cougot N., Bertrand E., Chenard M.P.,
Wendling C., Kessler P., Le Hir H., Rio M.C., Tomasetto C.;
"The exon-junction-complex-component metastatic lymph node 51
functions in stress-granule assembly.";
J. Cell Sci. 120:2774-2784(2007).
[12]
FUNCTION IN EIF4A3 ATPASE AND RNA-HELICASE ACTIVITY.
PubMed=17375189; DOI=10.1371/journal.pone.0000303;
Noble C.G., Song H.;
"MLN51 stimulates the RNA-helicase activity of eIF4AIII.";
PLoS ONE 2:E303-E303(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-477, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
ADP-RIBOSYLATION, AND UBIQUITINATION.
PubMed=21478859; DOI=10.1038/ncb2222;
Zhang Y., Liu S., Mickanin C., Feng Y., Charlat O., Michaud G.A.,
Schirle M., Shi X., Hild M., Bauer A., Myer V.E., Finan P.M.,
Porter J.A., Huang S.M., Cong F.;
"RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin
degradation and Wnt signalling.";
Nat. Cell Biol. 13:623-629(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-148; SER-265;
SER-363 AND SER-373, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-148; SER-265
AND SER-363, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-148 AND
THR-357, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 137-286 IN THE EJC COMPLEX
WITH EIF4A3; MAGOH; RBM8A AND AMP-PNP.
PubMed=16923391; DOI=10.1016/j.cell.2006.08.006;
Bono F., Ebert J., Lorentzen E., Conti E.;
"The crystal structure of the exon junction complex reveals how it
maintains a stable grip on mRNA.";
Cell 126:713-725(2006).
[23]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 170-246 IN THE EJC COMPLEX
WITH EIF4A3; MAGOH; RBM8A AND ADP-NP.
PubMed=16931718; DOI=10.1126/science.1131981;
Andersen C.B., Ballut L., Johansen J.S., Chamieh H., Nielsen K.H.,
Oliveira C.L., Pedersen J.S., Seraphin B., Le Hir H., Andersen G.R.;
"Structure of the exon junction core complex with a trapped DEAD-box
ATPase bound to RNA.";
Science 313:1968-1972(2006).
[24]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 138-283 IN THE EJC COMPLEX
WITH EIF4A3; MAGOH; RBM8A AND TRANSITION STATE ANALOG ADP-ALF3.
PubMed=19033377; DOI=10.1261/rna.1283109;
Nielsen K.H., Chamieh H., Andersen C.B., Fredslund F., Hamborg K.,
Le Hir H., Andersen G.R.;
"Mechanism of ATP turnover inhibition in the EJC.";
RNA 15:67-75(2009).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:17375189, ECO:0000269|PubMed:17652158}.
-!- SUBUNIT: Part of the mRNA splicing-dependent exon junction complex
(EJC) complex; the core complex contains CASC3, EIF4A3, MAGOH and
RBM8A. Forms homooligomers. Interacts with STAU in an RNA-
dependent manner. Interacts with EIF4A3, MAGOH, NXF1 and RBM8A.
{ECO:0000269|PubMed:15166247, ECO:0000269|PubMed:16170325,
ECO:0000269|PubMed:16314458}.
-!- INTERACTION:
P38919:EIF4A3; NbExp=29; IntAct=EBI-299118, EBI-299104;
P61326:MAGOH; NbExp=22; IntAct=EBI-299118, EBI-299134;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus.
Nucleus speckle. Note=Predominantly found in the perinuclear
region (By similarity). Shuttles between the nucleus and the
cytoplasm in a CRM1-dependent manner. Travels to the cytoplasm as
part of the exon junction complex (EJC) bound to mRNA. Shuttles
between the cytoplasm and the stress granules. More specifically
found in nuclear intrachromatin granules clusters (IGC), also
called nuclear speckles, which are storage compartments for
nuclear proteins involved in mRNA processing. Colocalizes in
nuclear speckles with MAGOH. Under stress condition, colocalizes
with FMR1 and TIA1, but not MAGOH and RBM8A EJC core factors, in
cytoplasmic stress granules, which contain stored mRNAs whose
translation is stopped in response to stress. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed. Overexpressed in breast
cancers and metastasis, as well as in gastric cancers.
{ECO:0000269|PubMed:12080473}.
-!- DOMAIN: The coiled coil domain may be involved in oligomerization.
-!- 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}.
-!- SIMILARITY: Belongs to the CASC3 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MLN51ID241.html";
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EMBL; X80199; CAC27699.1; -; mRNA.
EMBL; AK292425; BAF85114.1; -; mRNA.
EMBL; AC068669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC044656; AAH44656.1; -; mRNA.
EMBL; BC050526; AAH50526.1; -; mRNA.
CCDS; CCDS11362.1; -.
RefSeq; NP_031385.2; NM_007359.4.
RefSeq; XP_005257220.1; XM_005257163.1.
UniGene; Hs.743287; -.
PDB; 2HYI; X-ray; 2.30 A; D/J=170-246.
PDB; 2J0Q; X-ray; 3.20 A; I/T=137-286.
PDB; 2J0S; X-ray; 2.21 A; T=137-286.
PDB; 2J0U; X-ray; 3.00 A; T=137-250.
PDB; 2XB2; X-ray; 3.40 A; S/T=137-286.
PDB; 3EX7; X-ray; 2.30 A; D/I=138-283.
PDB; 5XJC; EM; 3.60 A; x=1-703.
PDBsum; 2HYI; -.
PDBsum; 2J0Q; -.
PDBsum; 2J0S; -.
PDBsum; 2J0U; -.
PDBsum; 2XB2; -.
PDBsum; 3EX7; -.
PDBsum; 5XJC; -.
ProteinModelPortal; O15234; -.
SMR; O15234; -.
BioGrid; 116475; 58.
CORUM; O15234; -.
DIP; DIP-33288N; -.
ELM; O15234; -.
IntAct; O15234; 32.
STRING; 9606.ENSP00000264645; -.
TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
iPTMnet; O15234; -.
PhosphoSitePlus; O15234; -.
BioMuta; CASC3; -.
EPD; O15234; -.
MaxQB; O15234; -.
PaxDb; O15234; -.
PeptideAtlas; O15234; -.
PRIDE; O15234; -.
TopDownProteomics; O15234; -.
Ensembl; ENST00000264645; ENSP00000264645; ENSG00000108349.
GeneID; 22794; -.
KEGG; hsa:22794; -.
UCSC; uc002hue.4; human.
CTD; 22794; -.
DisGeNET; 22794; -.
EuPathDB; HostDB:ENSG00000108349.14; -.
GeneCards; CASC3; -.
HGNC; HGNC:17040; CASC3.
HPA; HPA024592; -.
HPA; HPA050262; -.
MIM; 606504; gene.
neXtProt; NX_O15234; -.
OpenTargets; ENSG00000108349; -.
PharmGKB; PA134948596; -.
eggNOG; KOG4264; Eukaryota.
eggNOG; ENOG410ZW5Y; LUCA.
GeneTree; ENSGT00390000006930; -.
HOGENOM; HOG000069997; -.
HOVERGEN; HBG050799; -.
InParanoid; O15234; -.
KO; K14323; -.
OMA; FKEGRAG; -.
OrthoDB; EOG091G0JLP; -.
PhylomeDB; O15234; -.
TreeFam; TF329663; -.
Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72187; mRNA 3'-end processing.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
ChiTaRS; CASC3; human.
EvolutionaryTrace; O15234; -.
GeneWiki; CASC3; -.
GenomeRNAi; 22794; -.
PMAP-CutDB; O15234; -.
PRO; PR:O15234; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108349; -.
CleanEx; HS_CASC3; -.
ExpressionAtlas; O15234; baseline and differential.
Genevisible; O15234; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0035145; C:exon-exon junction complex; IDA:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IEA:Ensembl.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:MGI.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0008298; P:intracellular mRNA localization; IEA:Ensembl.
GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0006405; P:RNA export from nucleus; TAS:Reactome.
GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
InterPro; IPR018545; Btz_dom.
InterPro; IPR028544; CASC3.
PANTHER; PTHR13434; PTHR13434; 1.
Pfam; PF09405; Btz; 1.
SMART; SM01044; Btz; 1.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; Coiled coil; Complete proteome;
Cytoplasm; mRNA processing; mRNA splicing; mRNA transport;
Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; Stress response;
Translation regulation; Transport; Ubl conjugation.
CHAIN 1 703 Protein CASC3.
/FTId=PRO_0000089324.
REGION 137 283 Necessary for RNA-binding, interaction
with MAGOH and localization in nucleus
speckles. {ECO:0000269|PubMed:15166247}.
REGION 137 283 Sufficient to form the EJC.
REGION 377 703 Necessary for localization in cytoplasmic
stress granules.
COILED 95 131 {ECO:0000255}.
MOTIF 204 210 Nuclear localization signal 1.
{ECO:0000255}.
MOTIF 254 262 Nuclear localization signal 2.
{ECO:0000255}.
MOTIF 462 466 Nuclear export signal.
COMPBIAS 41 46 Poly-Gly.
COMPBIAS 392 395 Poly-Pro.
COMPBIAS 425 428 Poly-Pro.
COMPBIAS 643 648 Poly-Pro.
COMPBIAS 692 695 Poly-Pro.
MOD_RES 35 35 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K3W3}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 148 148 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 357 357 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:21406692}.
MOD_RES 477 477 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MUTAGEN 181 181 Y->A: Does not affect EJC formation.
{ECO:0000269|PubMed:16170325}.
MUTAGEN 184 185 RK->AA: Does not affect EJC formation.
{ECO:0000269|PubMed:16170325}.
MUTAGEN 188 188 F->A: Does not affect EJC formation.
{ECO:0000269|PubMed:16170325}.
MUTAGEN 218 218 W->A: Abolishes interaction with EIF4A3,
EJC formation and localization in nucleus
speckles. {ECO:0000269|PubMed:16170325}.
MUTAGEN 220 221 HD->AA: Abolishes interaction with
EIF4A3, EJC formation and localization in
nucleus speckles.
{ECO:0000269|PubMed:16170325}.
MUTAGEN 240 241 YG->AA: Abolishes interaction with
EIF4A3, EJC formation and localization in
nucleus speckles.
{ECO:0000269|PubMed:16170325}.
HELIX 172 174 {ECO:0000244|PDB:2J0S}.
HELIX 226 228 {ECO:0000244|PDB:2J0S}.
HELIX 233 240 {ECO:0000244|PDB:2HYI}.
TURN 244 246 {ECO:0000244|PDB:3EX7}.
SEQUENCE 703 AA; 76278 MW; 642A4C01C8DD3BE0 CRC64;
MADRRRQRAS QDTEDEESGA SGSDSGGSPL RGGGSCSGSA GGGGSGSLPS QRGGRTGALH
LRRVESGGAK SAEESECESE DGIEGDAVLS DYESAEDSEG EEGEYSEEEN SKVELKSEAN
DAVNSSTKEE KGEEKPDTKS TVTGERQSGD GQESTEPVEN KVGKKGPKHL DDDEDRKNPA
YIPRKGLFFE HDLRGQTQEE EVRPKGRQRK LWKDEGRWEH DKFREDEQAP KSRQELIALY
GYDIRSAHNP DDIKPRRIRK PRYGSPPQRD PNWNGERLNK SHRHQGLGGT LPPRTFINRN
AAGTGRMSAP RNYSRSGGFK EGRAGFRPVE AGGQHGGRSG ETVKHEISYR SRRLEQTSVR
DPSPEADAPV LGSPEKEEAA SEPPAAAPDA APPPPDRPIE KKSYSRARRT RTKVGDAVKL
AEEVPPPPEG LIPAPPVPET TPTPPTKTGT WEAPVDSSTS GLEQDVAQLN IAEQNWSPGQ
PSFLQPRELR GMPNHIHMGA GPPPQFNRME EMGVQGGRAK RYSSQRQRPV PEPPAPPVHI
SIMEGHYYDP LQFQGPIYTH GDSPAPLPPQ GMLVQPGMNL PHPGLHPHQT PAPLPNPGLY
PPPVSMSPGQ PPPQQLLAPT YFSAPGVMNF GNPSYPYAPG ALPPPPPPHL YPNTQAPSQV
YGGVTYYNPA QQQVQPKPSP PRRTPQPVTI KPPPPEVVSR GSS


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