MGN_MOUSE - dbPTM
MGN_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MGN_MOUSE
UniProt AC P61327
Protein Name Protein mago nashi homolog
Gene Name Magoh
Organism Mus musculus (Mouse).
Sequence Length 146
Subcellular Localization Nucleus. Nucleus speckle. Cytoplasm. Detected in granule-like structures in the dendroplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus
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). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms; the function is different from the established EJC assembly (By similarity)..
Protein Sequence MESDFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKNDVMIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYYLVQDLKCLVFSLIGLHFKIKPI
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
1Acetylation-------MESDFYLR
-------CCCCEEEE
11.39-
16AcetylationYYVGHKGKFGHEFLE
EECCCCCCCCCEEEE
53.6423806337
38PhosphorylationKLRYANNSNYKNDVM
CEEECCCCCCCCCEE
41.1525367039
40PhosphorylationRYANNSNYKNDVMIR
EECCCCCCCCCEEEE
15.8125367039
41UbiquitinationYANNSNYKNDVMIRK
ECCCCCCCCCEEEEH
51.4222790023
41AcetylationYANNSNYKNDVMIRK
ECCCCCCCCCEEEEH
51.4223806337
106PhosphorylationFTTSKIGSLIDVNQS
EECCCCCCEEECCCC
26.1422942356
114UbiquitinationLIDVNQSKDPEGLRV
EEECCCCCCCCHHHH
68.4922790023
114AcetylationLIDVNQSKDPEGLRV
EEECCCCCCCCHHHH
68.4923236377

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 MGN_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MGN_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 MGN_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DNM3B_HUMANDNMT3Bphysical
26496610
GOGA4_HUMANGOLGA4physical
26496610
ITA1_HUMANITGA1physical
26496610
M3K4_HUMANMAP3K4physical
26496610
6PGD_HUMANPGDphysical
26496610
ZN207_HUMANZNF207physical
26496610
KIF3B_HUMANKIF3Bphysical
26496610
CROCC_HUMANCROCCphysical
26496610
RBM8A_HUMANRBM8Aphysical
26496610
APBP2_HUMANAPPBP2physical
26496610
HPS5_HUMANHPS5physical
26496610
HS74L_HUMANHSPA4Lphysical
26496610
ZN609_HUMANZNF609physical
26496610
KI26A_HUMANKIF26Aphysical
26496610
MGN2_HUMANMAGOHBphysical
26496610
FEM1A_HUMANFEM1Aphysical
26496610
KI16B_HUMANKIF16Bphysical
26496610
KIF17_HUMANKIF17physical
26496610
RBSK_HUMANRBKSphysical
26496610
S35E1_HUMANSLC35E1physical
26496610
TPC13_HUMANTRAPPC13physical
26496610
PYM1_HUMANWIBGphysical
26496610
SNX29_HUMANSNX29physical
26496610
TGS1_HUMANTGS1physical
26496610
IPIL2_HUMANITPRIPL2physical
26496610

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

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Related Literatures of Post-Translational Modification

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