dbPTM

MGN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MGN_HUMAN
UniProt AC	P61326
Protein Name	Protein mago nashi homolog
Gene Name	MAGOH
Organism	Homo sapiens (Human).
Sequence Length	146
Subcellular Localization	Nucleus . Nucleus speckle . Cytoplasm . Detected in granule-like structures in the dendroplasm (By similarity). Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and U
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 such as Bcl-X(S); the function is different from the established EJC assembly..
Protein Sequence	MESDFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKNDVMIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYYLVQDLKCLVFSLIGLHFKIKPI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MESDFYLR -------CCCCEEEE	11.39	22223895
3	Phosphorylation	-----MESDFYLRYY -----CCCCEEEEEE	31.55	23663014
6	Phosphorylation	--MESDFYLRYYVGH --CCCCEEEEEECCC	8.68	23663014
8	Methylation	MESDFYLRYYVGHKG CCCCEEEEEECCCCC	14.90	115482497
9	Phosphorylation	ESDFYLRYYVGHKGK CCCEEEEEECCCCCC	10.41	23663014
10	Phosphorylation	SDFYLRYYVGHKGKF CCEEEEEECCCCCCC	8.10	23663014
14	Methylation	LRYYVGHKGKFGHEF EEEECCCCCCCCCEE	58.84	23748837
14	Ubiquitination	LRYYVGHKGKFGHEF EEEECCCCCCCCCEE	58.84	23000965
16	Ubiquitination	YYVGHKGKFGHEFLE EECCCCCCCCCEEEE	53.64	21890473
16	Acetylation	YYVGHKGKFGHEFLE EECCCCCCCCCEEEE	53.64	25825284
16	Ubiquitination	YYVGHKGKFGHEFLE EECCCCCCCCCEEEE	53.64	23000965
31	Acetylation	FEFRPDGKLRYANNS EEECCCCCEEECCCC	36.85	25953088
31	Ubiquitination	FEFRPDGKLRYANNS EEECCCCCEEECCCC	36.85	21906983
34	Phosphorylation	RPDGKLRYANNSNYK CCCCCEEECCCCCCC	24.90	-
38	Phosphorylation	KLRYANNSNYKNDVM CEEECCCCCCCCCEE	41.15	27273156
40	Phosphorylation	RYANNSNYKNDVMIR EECCCCCCCCCEEEE	15.81	27155012
41	Ubiquitination	YANNSNYKNDVMIRK ECCCCCCCCCEEEEH	51.42	23000965
41	Acetylation	YANNSNYKNDVMIRK ECCCCCCCCCEEEEH	51.42	23236377
41	Ubiquitination	YANNSNYKNDVMIRK ECCCCCCCCCEEEEH	51.42	21890473
48	Ubiquitination	KNDVMIRKEAYVHKS CCCEEEEHHHHHCHH	35.45	27667366
51	Phosphorylation	VMIRKEAYVHKSVME EEEEHHHHHCHHHHH	12.27	20049867
54	Ubiquitination	RKEAYVHKSVMEELK EHHHHHCHHHHHHHH	34.40	32015554
54	Acetylation	RKEAYVHKSVMEELK EHHHHHCHHHHHHHH	34.40	26051181
61	Ubiquitination	KSVMEELKRIIDDSE HHHHHHHHHHCCHHH	44.84	29901268
71	Ubiquitination	IDDSEITKEDDALWP CCHHHCCCCCCCCCC	65.88	21906983
71	Acetylation	IDDSEITKEDDALWP CCHHHCCCCCCCCCC	65.88	26051181
98	Phosphorylation	VIGDEHISFTTSKIG EECCCCCEEECCCCC	20.60	21406692
100	Phosphorylation	GDEHISFTTSKIGSL CCCCCEEECCCCCCE	24.30	21406692
101	Phosphorylation	DEHISFTTSKIGSLI CCCCEEECCCCCCEE	26.47	21406692
102	Phosphorylation	EHISFTTSKIGSLID CCCEEECCCCCCEEE	21.15	21406692
106	Phosphorylation	FTTSKIGSLIDVNQS EECCCCCCEEECCCC	26.14	23401153
113	Phosphorylation	SLIDVNQSKDPEGLR CEEECCCCCCCCHHH	33.55	26074081
114	Ubiquitination	LIDVNQSKDPEGLRV EEECCCCCCCCHHHH	68.49	23000965
114	Acetylation	LIDVNQSKDPEGLRV EEECCCCCCCCHHHH	68.49	23954790
123	Phosphorylation	PEGLRVFYYLVQDLK CCHHHHHHHHHHHHH	7.95	23822953

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_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RBM8A_HUMAN	RBM8A	physical	10662555
RBM8A_HUMAN	RBM8A	physical	11707413
NXF1_HUMAN	NXF1	physical	11707413
IF4A3_HUMAN	EIF4A3	physical	14730019
IF4A3_HUMAN	EIF4A3	physical	23084401
RBM8A_HUMAN	RBM8A	physical	23084401
CASC3_HUMAN	CASC3	physical	23084401
ACINU_HUMAN	ACIN1	physical	23084401
PININ_HUMAN	PNN	physical	23084401
RNPS1_HUMAN	RNPS1	physical	23084401
SAP18_HUMAN	SAP18	physical	23084401
PYM1_HUMAN	WIBG	physical	23084401
THOC4_HUMAN	ALYREF	physical	23084401
UIF_HUMAN	FYTTD1	physical	23084401
SRS10_HUMAN	SRSF10	physical	23084401
SRSF5_HUMAN	SRSF5	physical	23084401
SRSF1_HUMAN	SRSF1	physical	23084401
SRSF2_HUMAN	SRSF2	physical	23084401
SRSF3_HUMAN	SRSF3	physical	23084401
SRSF4_HUMAN	SRSF4	physical	23084401
SRSF6_HUMAN	SRSF6	physical	23084401
SRSF7_HUMAN	SRSF7	physical	23084401
SRSF8_HUMAN	SRSF8	physical	23084401
SRSF9_HUMAN	SRSF9	physical	23084401
SON_HUMAN	SON	physical	23084401
TRA2A_HUMAN	TRA2A	physical	23084401
TRA2B_HUMAN	TRA2B	physical	23084401
SRRM1_HUMAN	SRRM1	physical	23084401
SRRM2_HUMAN	SRRM2	physical	23084401
TR150_HUMAN	THRAP3	physical	23084401
FMR1_HUMAN	FMR1	physical	23084401
ILF3_HUMAN	ILF3	physical	23084401
ILF2_HUMAN	ILF2	physical	23084401
MATR3_HUMAN	MATR3	physical	23084401
HNRPC_HUMAN	HNRNPC	physical	23084401
CCDC9_HUMAN	CCDC9	physical	23084401
TSN_HUMAN	TSN	physical	23084401
ERH_HUMAN	ERH	physical	23084401
PGAM5_HUMAN	PGAM5	physical	23084401
RU17_HUMAN	SNRNP70	physical	23084401
SF3A1_HUMAN	SF3A1	physical	23084401
SF3B1_HUMAN	SF3B1	physical	23084401
SF3B2_HUMAN	SF3B2	physical	23084401
SF3B3_HUMAN	SF3B3	physical	23084401
PRP4B_HUMAN	PRPF4B	physical	23084401
PRP8_HUMAN	PRPF8	physical	23084401
SNR40_HUMAN	SNRNP40	physical	23084401
U520_HUMAN	SNRNP200	physical	23084401
U5S1_HUMAN	EFTUD2	physical	23084401
CDC5L_HUMAN	CDC5L	physical	23084401
CRNL1_HUMAN	CRNKL1	physical	23084401
PLRG1_HUMAN	PLRG1	physical	23084401
PPIE_HUMAN	PPIE	physical	23084401
PRP19_HUMAN	PRPF19	physical	23084401
SPF27_HUMAN	BCAS2	physical	23084401
SYF1_HUMAN	XAB2	physical	23084401
RBM22_HUMAN	RBM22	physical	23084401
SNW1_HUMAN	SNW1	physical	23084401
AQR_HUMAN	AQR	physical	23084401
CWC15_HUMAN	CWC15	physical	23084401
DHX15_HUMAN	DHX15	physical	23084401
PRP17_HUMAN	CDC40	physical	23084401
SRS12_HUMAN	SRSF12	physical	23084401
DREB_HUMAN	DBN1	physical	23084401
ACTB_HUMAN	ACTB	physical	23084401
ACTC_HUMAN	ACTC1	physical	23084401
CAMP3_HUMAN	CAMSAP3	physical	23084401
CAPZB_HUMAN	CAPZB	physical	23084401
CAZA1_HUMAN	CAPZA1	physical	23084401
E41L3_HUMAN	EPB41L3	physical	23084401
K1C10_HUMAN	KRT10	physical	23084401
K1C14_HUMAN	KRT14	physical	23084401
K1C19_HUMAN	KRT19	physical	23084401
K1C9_HUMAN	KRT9	physical	23084401
K22E_HUMAN	KRT2	physical	23084401
K2C1_HUMAN	KRT1	physical	23084401
K2C5_HUMAN	KRT5	physical	23084401
MAP1B_HUMAN	MAP1B	physical	23084401
SPI2A_HUMAN	SPIN2A	physical	23084401
SPIN1_HUMAN	SPIN1	physical	23084401
SPTN1_HUMAN	SPTAN1	physical	23084401
SPTB2_HUMAN	SPTBN1	physical	23084401
VIME_HUMAN	VIM	physical	23084401
MYH10_HUMAN	MYH10	physical	23084401
MYH9_HUMAN	MYH9	physical	23084401
POTEJ_HUMAN	POTEJ	physical	23084401
H2A1A_HUMAN	HIST1H2AA	physical	23084401
H2A1D_HUMAN	HIST1H2AD	physical	23084401
H31T_HUMAN	HIST3H3	physical	23084401
HNRH2_HUMAN	HNRNPH2	physical	23084401
HNRPF_HUMAN	HNRNPF	physical	23084401
RBMX_HUMAN	RBMX	physical	23084401
HNRPK_HUMAN	HNRNPK	physical	23084401
HNRPL_HUMAN	HNRNPL	physical	23084401
HNRPM_HUMAN	HNRNPM	physical	23084401
HNRPU_HUMAN	HNRNPU	physical	23084401
HNRH1_HUMAN	HNRNPH1	physical	23084401
ANM1_HUMAN	PRMT1	physical	23084401
CHTOP_HUMAN	CHTOP	physical	23084401
ANM5_HUMAN	PRMT5	physical	23084401
ICLN_HUMAN	CLNS1A	physical	23084401
MEP50_HUMAN	WDR77	physical	23084401
ADT2_HUMAN	SLC25A5	physical	23084401
BLM_HUMAN	BLM	physical	23084401
BOLA2_HUMAN	BOLA2	physical	23084401
DOCK4_HUMAN	DOCK4	physical	23084401
F263_HUMAN	PFKFB3	physical	23084401
FAS_HUMAN	FASN	physical	23084401
GRP75_HUMAN	HSPA9	physical	23084401
HSP7C_HUMAN	HSPA8	physical	23084401
JAK1_HUMAN	JAK1	physical	23084401
MOB2_HUMAN	MOB2	physical	23084401
PPM1B_HUMAN	PPM1B	physical	23084401
PRDX1_HUMAN	PRDX1	physical	23084401
RAN_HUMAN	RAN	physical	23084401
RIOK1_HUMAN	RIOK1	physical	23084401
ST38L_HUMAN	STK38L	physical	23084401
STK38_HUMAN	STK38	physical	23084401
RBM39_HUMAN	RBM39	physical	23084401
DDX17_HUMAN	DDX17	physical	23084401
YBOX1_HUMAN	YBX1	physical	23084401
ZC3HD_HUMAN	ZC3H13	physical	23084401
DDX3X_HUMAN	DDX3X	physical	23084401
FBRL_HUMAN	FBL	physical	23084401
YBOX3_HUMAN	YBX3	physical	23084401
RL4_HUMAN	RPL4	physical	23084401
RL10_HUMAN	RPL10	physical	23084401
RL13_HUMAN	RPL13	physical	23084401
RL13A_HUMAN	RPL13A	physical	23084401
RL15_HUMAN	RPL15	physical	23084401
RL17_HUMAN	RPL17	physical	23084401
RL18_HUMAN	RPL18	physical	23084401
RL19_HUMAN	RPL19	physical	23084401
RL21_HUMAN	RPL21	physical	23084401
RL24_HUMAN	RPL24	physical	23084401
RL26_HUMAN	RPL26	physical	23084401
RL26L_HUMAN	RPL26L1	physical	23084401
RL27A_HUMAN	RPL27A	physical	23084401
RL28_HUMAN	RPL28	physical	23084401
RL3_HUMAN	RPL3	physical	23084401
RL6_HUMAN	RPL6	physical	23084401
RL7_HUMAN	RPL7	physical	23084401
RL7A_HUMAN	RPL7A	physical	23084401
RL8_HUMAN	RPL8	physical	23084401
RS6_HUMAN	RPS6	physical	23084401
RS8_HUMAN	RPS8	physical	23084401
RS11_HUMAN	RPS11	physical	23084401
RS2_HUMAN	RPS2	physical	23084401
RS24_HUMAN	RPS24	physical	23084401
RS3_HUMAN	RPS3	physical	23084401
RS9_HUMAN	RPS9	physical	23084401
RSMB_HUMAN	SNRPB	physical	23084401
SMD1_HUMAN	SNRPD1	physical	23084401
SMD2_HUMAN	SNRPD2	physical	23084401
SMD3_HUMAN	SNRPD3	physical	23084401
RBM10_HUMAN	RBM10	physical	23084401
SCYL2_HUMAN	SCYL2	physical	23084401
YTDC1_HUMAN	YTHDC1	physical	23084401
EF1A1_HUMAN	EEF1A1	physical	23084401
IF4B_HUMAN	EIF4B	physical	23084401
RBM8A_HUMAN	RBM8A	physical	22365833
TAD2A_HUMAN	TADA2A	physical	25416956
RBM8A_HUMAN	RBM8A	physical	25416956
UBB_HUMAN	UBB	physical	26186194
SCRN3_HUMAN	SCRN3	physical	26186194
PININ_HUMAN	PNN	physical	26186194
PYM1_HUMAN	WIBG	physical	26186194
RBM8A_HUMAN	RBM8A	physical	26186194
CASC3_HUMAN	CASC3	physical	26186194
DFFB_HUMAN	DFFB	physical	26186194
PYM1_HUMAN	WIBG	physical	28514442
SCRN3_HUMAN	SCRN3	physical	28514442
DFFB_HUMAN	DFFB	physical	28514442
RBM8A_HUMAN	RBM8A	physical	28514442
CASC3_HUMAN	CASC3	physical	28514442
UBB_HUMAN	UBB	physical	28514442
PININ_HUMAN	PNN	physical	28514442

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 MGN_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114, AND MASS SPECTROMETRY.	19608861 [Abstract]