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3.A.18.1.1
The nuclear mRNA Export Complex (mRNA-E also called TREX) (including the exon junction complex) [TAP+p15 interact as a complex with the nuclear pore to facilitate mRNA transport to the cytoplasm] (Nojimma et al. 2007; Cheng et al., 2006)

Accession Number:O15234
Protein Name:Protein CASC3 aka MLN51
Length:703
Molecular Weight:76278.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Cytoplasm1
Substrate mRNA

Cross database links:

Genevestigator: O15234
eggNOG: prNOG08646
HEGENOM: HBG715340
RefSeq: NP_031385.2   
Entrez Gene ID: 22794   
Pfam: PF09405   
OMIM: 606504  gene
KEGG: hsa:22794   

Gene Ontology

GO:0016607 C:nuclear speck
GO:0048471 C:perinuclear region of cytoplasm
GO:0042802 F:identical protein binding
GO:0003723 F:RNA binding
GO:0006397 P:mRNA processing
GO:0051028 P:mRNA transport
GO:0000184 P:nuclear-transcribed mRNA catabolic process,...
GO:0006417 P:regulation of translation
GO:0006950 P:response to stress
GO:0008380 P:RNA splicing

References (18)

[1] “Identification of four novel human genes amplified and overexpressed in breast carcinoma and localized to the q11-q21.3 region of chromosome 17.”  Tomasetto C.L.et.al.   7490069
[2] “Metastatic lymph node 51, a novel nucleo-cytoplasmic protein overexpressed in breast cancer.”  Degot S.F.et.al.   12080473
[3] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[4] “DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.”  Zody M.C.et.al.   16625196
[5] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[6] “Targets of gene amplification and overexpression at 17q in gastric cancer.”  Varis A.et.al.   11980659
[7] “Association of the breast cancer protein MLN51 with the exon junction complex via its speckle localizer and RNA binding module.”  Degot S.et.al.   15166247
[8] “The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity.”  Ballut L.et.al.   16170325
[9] “Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core.”  Tange T.O.et.al.   16314458
[10] “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.”  Olsen J.V.et.al.   17081983
[11] “The exon-junction-complex-component metastatic lymph node 51 functions in stress-granule assembly.”  Baguet A.et.al.   17652158
[12] “MLN51 stimulates the RNA-helicase activity of eIF4AIII.”  Noble C.G.et.al.   17375189
[13] “A quantitative atlas of mitotic phosphorylation.”  Dephoure N.et.al.   18669648
[14] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[15] “Large-scale proteomics analysis of the human kinome.”  Oppermann F.S.et.al.   19369195
[16] “The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA.”  Bono F.et.al.   16923391
[17] “Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA.”  Andersen C.B.et.al.   16931718
[18] “Mechanism of ATP turnover inhibition in the EJC.”  Nielsen K.H.et.al.   19033377
Structure:
2HYI   2J0Q   2J0S   2J0U   3EX7   2XB2     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MADRRRQRAS QDTEDEESGA SGSDSGGSPL RGGGSCSGSA GGGGSGSLPS QRGGRTGALH 
61:	LRRVESGGAK SAEESECESE DGIEGDAVLS DYESAEDSEG EEGEYSEEEN SKVELKSEAN 
121:	DAVNSSTKEE KGEEKPDTKS TVTGERQSGD GQESTEPVEN KVGKKGPKHL DDDEDRKNPA 
181:	YIPRKGLFFE HDLRGQTQEE EVRPKGRQRK LWKDEGRWEH DKFREDEQAP KSRQELIALY 
241:	GYDIRSAHNP DDIKPRRIRK PRYGSPPQRD PNWNGERLNK SHRHQGLGGT LPPRTFINRN 
301:	AAGTGRMSAP RNYSRSGGFK EGRAGFRPVE AGGQHGGRSG ETVKHEISYR SRRLEQTSVR 
361:	DPSPEADAPV LGSPEKEEAA SEPPAAAPDA APPPPDRPIE KKSYSRARRT RTKVGDAVKL 
421:	AEEVPPPPEG LIPAPPVPET TPTPPTKTGT WEAPVDSSTS GLEQDVAQLN IAEQNWSPGQ 
481:	PSFLQPRELR GMPNHIHMGA GPPPQFNRME EMGVQGGRAK RYSSQRQRPV PEPPAPPVHI 
541:	SIMEGHYYDP LQFQGPIYTH GDSPAPLPPQ GMLVQPGMNL PHPGLHPHQT PAPLPNPGLY 
601:	PPPVSMSPGQ PPPQQLLAPT YFSAPGVMNF GNPSYPYAPG ALPPPPPPHL YPNTQAPSQV 
661:	YGGVTYYNPA QQQVQPKPSP PRRTPQPVTI KPPPPEVVSR GSS