MGN2_HUMAN - dbPTM
MGN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MGN2_HUMAN
UniProt AC Q96A72
Protein Name Protein mago nashi homolog 2
Gene Name MAGOHB
Organism Homo sapiens (Human).
Sequence Length 148
Subcellular Localization Nucleus.
Protein Description Involved in mRNA splicing and in the nonsense-mediated decay (NMD) pathway..
Protein Sequence MAVASDFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKNDVMIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYYLVQDLKCLVFSLIGLHFKIKPI
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
2Acetylation------MAVASDFYL
------CCCCCCEEE
12.9422223895
16UbiquitinationLRYYVGHKGKFGHEF
EEEECCCCCCCCCEE
58.84-
18AcetylationYYVGHKGKFGHEFLE
EECCCCCCCCCEEEE
53.64-
18UbiquitinationYYVGHKGKFGHEFLE
EECCCCCCCCCEEEE
53.6421890473
33UbiquitinationFEFRPDGKLRYANNS
EEECCCCCEEECCCC
36.8521890473
36PhosphorylationRPDGKLRYANNSNYK
CCCCCEEECCCCCCC
24.90-
40PhosphorylationKLRYANNSNYKNDVM
CEEECCCCCCCCCEE
41.1527273156
42PhosphorylationRYANNSNYKNDVMIR
EECCCCCCCCCEEEE
15.8127155012
43UbiquitinationYANNSNYKNDVMIRK
ECCCCCCCCCEEEEH
51.4221890473
53PhosphorylationVMIRKEAYVHKSVME
EEEEHHHHHCHHHHH
12.2720049867
56UbiquitinationRKEAYVHKSVMEELK
EHHHHHCHHHHHHHH
34.40-
63UbiquitinationKSVMEELKRIIDDSE
HHHHHHHHHHCCHHH
44.84-
73UbiquitinationIDDSEITKEDDALWP
CCHHHCCCCCCCCCC
65.8821890473
100PhosphorylationVIGDEHISFTTSKIG
EECCCCCEEECCCCC
20.6021406692
102PhosphorylationGDEHISFTTSKIGSL
CCCCCEEECCCCCCE
24.3021406692
103PhosphorylationDEHISFTTSKIGSLI
CCCCEEECCCCCCEE
26.4721406692
104PhosphorylationEHISFTTSKIGSLID
CCCEEECCCCCCEEE
21.1521406692
108PhosphorylationFTTSKIGSLIDVNQS
EECCCCCCEEECCCC
26.1423401153
115PhosphorylationSLIDVNQSKDPEGLR
CEEECCCCCCCCHHH
33.5526074081
116UbiquitinationLIDVNQSKDPEGLRV
EEECCCCCCCCHHHH
68.4921906983
116AcetylationLIDVNQSKDPEGLRV
EEECCCCCCCCHHHH
68.4937092765
125PhosphorylationPEGLRVFYYLVQDLK
CCHHHHHHHHHHHHH
7.95-
132UbiquitinationYYLVQDLKCLVFSLI
HHHHHHHHHHHHHHH
33.54-

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 MGN2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MGN2_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 MGN2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBM8A_HUMANRBM8Aphysical
22939629
DX39B_HUMANDDX39Bphysical
22939629
ZN398_HUMANZNF398physical
25416956
ZN250_HUMANZNF250physical
25416956
C102B_HUMANCCDC102Bphysical
25416956
K1C40_HUMANKRT40physical
25416956
TRI42_HUMANTRIM42physical
25416956
RBM8A_HUMANRBM8Aphysical
26496610
PYM1_HUMANWIBGphysical
26496610
EFGM_HUMANGFM1physical
26496610

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MGN2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASSSPECTROMETRY.

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