dbPTM

NGEF_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NGEF_MOUSE
UniProt AC	Q8CHT1
Protein Name	Ephexin-1
Gene Name	Ngef
Organism	Mus musculus (Mouse).
Sequence Length	710
Subcellular Localization	Cytoplasm. Membrane. Cell projection, growth cone. Associated with membranes. Localizes to axonal growth cones (By similarity)..
Protein Description	Acts as a guanine nucleotide exchange factor (GEF) which differentially activates the GTPases RHOA, RAC1 and CDC42. Plays a role in axon guidance regulating ephrin-induced growth cone collapse and dendritic spine morphogenesis. Upon activation by ephrin through EPHA4, the GEF activity switches toward RHOA resulting in its activation. Activated RHOA promotes cone retraction at the expense of RAC1- and CDC42-stimulated growth cone extension..
Protein Sequence	METKNSEDWGKPQRKSESSSRKSNHGPAEMRPALPPENREAPETGEETQNEEPRRLIPIQRHSLFNRAVRHRHKARSTSERRASDQADLPKMGKSVNERSAFNLPQGRLSPWRTPAQRDTGAQEASESSSTPGNGTTPEECPALTDSPTTLTEALQMIHPIPADSWRNLIEQIGLLYQEYRDKSTLQEIETRRQQDAEIQGNSDGSQVGEDAGEEEEEEEEGEEEELASPPERRALPQICLLSNPHSRFNLWQDLPEIQSSGVLDILQPEEIRLQEAMFELVTSEASYYKSLNLLVSHFMENERLKKILHPSEAHILFSNVLDVMAVSERFLLELEHRMEENIVISDVCDIVYRYAADHFSVYITYVSNQTYQERTYKQLLQEKAAFRELIAQLELDPKCKGLPFSSFLILPFQRITRLKLLVQNILKRVEERSEREGTALDAHKELEMVVKACNEGVRKMSRTEQMISIQKKMEFKIKSVPIISHSRWLLKQGELQQMSGPKTSRTLRTKKLFREIYLFLFNDLLVICRQIPGDKYQVFDSAPRGLLRVEELEDQGQTLANVFILRLLENADDREATYMLKASSQSEMKRWMTSLAPNRRTKFVSFTSRLLDCPQVQCVHPYVAQQPDELTLELADILNILEKTEDGWIFGERLHDQERGWFPSSMTEEILNPKIRSQNLKECFRVHKMEDPQRSQNKDRRKLGSRNRQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
63	Phosphorylation	LIPIQRHSLFNRAVR CCCHHHHHHHHHHHH	36.52	21743459
84	Phosphorylation	STSERRASDQADLPK CHHHHHHHCCCCCCC	28.57	25521595
137	Phosphorylation	STPGNGTTPEECPAL CCCCCCCCHHHCCCC	30.05	-
177	Phosphorylation	IEQIGLLYQEYRDKS HHHHHHHHHHHCCHH	12.35	-
180	Phosphorylation	IGLLYQEYRDKSTLQ HHHHHHHHCCHHHHH	14.48	-
206	Phosphorylation	IQGNSDGSQVGEDAG CCCCCCCCCCCCCCC	27.04	29899451
229	Phosphorylation	GEEEELASPPERRAL CCHHHHCCCHHHHCC	54.32	29899451
363	Phosphorylation	AADHFSVYITYVSNQ HHHHEEEEEEECCCC	6.07	-
366	Phosphorylation	HFSVYITYVSNQTYQ HEEEEEEECCCCCCH	7.72	-
399	Ubiquitination	AQLELDPKCKGLPFS HHHCCCCCCCCCCCC	48.52	-
428	Ubiquitination	LLVQNILKRVEERSE HHHHHHHHHHHHHHH	51.07	-
445	Acetylation	GTALDAHKELEMVVK CCCCHHHHHHHHHHH	66.76	7721483
462	Phosphorylation	NEGVRKMSRTEQMIS HHHHHHCCHHHHHHH	38.80	29899451
464	Phosphorylation	GVRKMSRTEQMISIQ HHHHCCHHHHHHHHH	24.22	22324799
492	Ubiquitination	SHSRWLLKQGELQQM ECHHHHHHHCCHHHH	54.83	-
518	Phosphorylation	KKLFREIYLFLFNDL HHHHHHHHHHHHCCH	6.15	-
537	Phosphorylation	RQIPGDKYQVFDSAP HCCCCCCCEEECCCC	18.04	-
579	Phosphorylation	ADDREATYMLKASSQ CCHHHHHHHHHCCCH	13.90	-
584	Phosphorylation	ATYMLKASSQSEMKR HHHHHHCCCHHHHHH	27.59	-
585	Phosphorylation	TYMLKASSQSEMKRW HHHHHCCCHHHHHHH	42.45	-
587	Phosphorylation	MLKASSQSEMKRWMT HHHCCCHHHHHHHHH	41.42	-
595	Phosphorylation	EMKRWMTSLAPNRRT HHHHHHHHHCCCCCH	13.36	28059163
603	Ubiquitination	LAPNRRTKFVSFTSR HCCCCCHHEEEHHHH	41.79	-
606	Phosphorylation	NRRTKFVSFTSRLLD CCCHHEEEHHHHHHC	26.41	21082442
608	Phosphorylation	RTKFVSFTSRLLDCP CHHEEEHHHHHHCCC	12.87	22324799
623	Phosphorylation	QVQCVHPYVAQQPDE CCEECCHHHCCCCCH	8.11	-
678	Phosphorylation	ILNPKIRSQNLKECF HHCHHHHCCCHHHHH	27.22	22324799
696	Phosphorylation	KMEDPQRSQNKDRRK CCCCCCHHCCHHHHH	32.62	25521595
706	Phosphorylation	KDRRKLGSRNRQ--- HHHHHHHHCCCC---	36.50	22324799

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
177	Y	Phosphorylation	Kinase	EPHA4	P54764	PSP
177	Y	Phosphorylation	Kinase	FGFR2	P21802	PSP
177	Y	Phosphorylation	Kinase	SRC	P12931	PSP
177	Y	Phosphorylation	Kinase	SRC	P05480	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of NGEF_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NGEF_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606, AND MASSSPECTROMETRY.	16452087 [Abstract]