dbPTM

EGFR_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EGFR_MOUSE
UniProt AC	Q01279
Protein Name	Epidermal growth factor receptor
Gene Name	Egfr
Organism	Mus musculus (Mouse).
Sequence Length	1210
Subcellular Localization	Cell membrane Single-pass type I membrane protein . Endoplasmic reticulum membrane Single-pass type I membrane protein . Golgi apparatus membrane Single-pass type I membrane protein . Nucleus membrane Single-pass type I membrane protein . Endosome
Protein Description	Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. [PubMed: 8404850 Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (By similarity Plays a role in enhancing learning and memory performance]
Protein Sequence	MRPSGTARTTLLVLLTALCAAGGALEEKKVCQGTSNRLTQLGTFEDHFLSLQRMYNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNALYENTYALAILSNYGTNRTGLRELPMRNLQEILIGAVRFSNNPILCNMDTIQWRDIVQNVFMSNMSMDLQSHPSSCPKCDPSCPNGSCWGGGEENCQKLTKIICAQQCSHRCRGRSPSDCCHNQCAAGCTGPRESDCLVCQKFQDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGPDYYEVEEDGIRKCKKCDGPCRKVCNGIGIGEFKDTLSINATNIKHFKYCTAISGDLHILPVAFKGDSFTRTPPLDPRELEILKTVKEITGFLLIQAWPDNWTDLHAFENLEIIRGRTKQHGQFSLAVVGLNITSLGLRSLKEISDGDVIISGNRNLCYANTINWKKLFGTPNQKTKIMNNRAEKDCKAVNHVCNPLCSSEGCWGPEPRDCVSCQNVSRGRECVEKCNILEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGIMGENNTLVWKYADANNVCHLCHANCTYGCAGPGLQGCEVWPSGPKIPSIATGIVGGLLFIVVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQAHLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPYGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASDISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELILEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMEDVVDADEYLIPQQGFFNSPSTSRTPLLSSLSATSNNSTVACINRNGSCRVKEDAFLQRYSSDPTGAVTEDNIDDAFLPVPEYVNQSVPKRPAGSVQNPVYHNQPLHPAPGRDLHYQNPHSNAVGNPEYLNTAQPTCLSSGFNSPALWIQKGSHQMSLDNPDYQQDFFPKETKPNGIFKGPTAENAEYLRVAPPSSEFIGA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
128	N-linked_Glycosylation	ILSNYGTNRTGLREL HHHHCCCCCCCCCCC	34.84	-
157	S-palmitoylation	FSNNPILCNMDTIQW CCCCCEECCCCHHCH	4.03	28526873
175	N-linked_Glycosylation	VQNVFMSNMSMDLQS HHHHHHHCCCCCCCC	18.11	17330941
196	N-linked_Glycosylation	KCDPSCPNGSCWGGG CCCCCCCCCCCCCCC	60.38	-
215	S-palmitoylation	QKLTKIICAQQCSHR HHHHHHHHHHHCCHH	2.97	26165157
229	Phosphorylation	RCRGRSPSDCCHNQC HHCCCCHHHCCCCCC	44.52	-
270	Phosphorylation	TCPPLMLYNPTTYQM CCCCEEEECCCEEEE	12.72	15016810
291	S-palmitoylation	KYSFGATCVKKCPRN CCEEECEEEECCCCC	4.13	28526873
307	S-palmitoylation	VVTDHGSCVRACGPD EEECCCHHHHCCCCC	2.58	26165157
311	S-palmitoylation	HGSCVRACGPDYYEV CCHHHHCCCCCCEEE	5.95	28526873
316	Phosphorylation	RACGPDYYEVEEDGI HCCCCCCEEECHHCH	22.37	15378723
337	S-palmitoylation	DGPCRKVCNGIGIGE CCCHHHHCCCCCCCC	4.30	28526873
352	N-linked_Glycosylation	FKDTLSINATNIKHF CCCCEECCCCCCCEE	37.02	16944957
362	S-palmitoylation	NIKHFKYCTAISGDL CCCEEEEEEEECCCE	1.82	28526873
413	N-linked_Glycosylation	LIQAWPDNWTDLHAF EEEECCCCCCCCHHH	39.19	-
444	N-linked_Glycosylation	SLAVVGLNITSLGLR EEEEEECCEEHHCCC	29.57	16944957
454	Ubiquitination	SLGLRSLKEISDGDV HHCCCCHHHCCCCCE	55.00	22790023
470	S-palmitoylation	ISGNRNLCYANTINW EECCCCCEEECCCCH	3.26	28526873
487	Ubiquitination	LFGTPNQKTKIMNNR HHCCCCCCCHHHCCH	59.43	22790023
528	N-linked_Glycosylation	RDCVSCQNVSRGREC CCCCCCCCCCCHHHH	37.75	-
568	N-linked_Glycosylation	ECLPQAMNITCTGRG HHHCCCCCEEECCCC	29.45	-
603	N-linked_Glycosylation	PAGIMGENNTLVWKY CCCCCCCCCEEEEEE	40.85	-
623	N-linked_Glycosylation	VCHLCHANCTYGCAG CEEEECCCCCCCCCC	8.59	-
680	Phosphorylation	RHIVRKRTLRRLLQE HHHHHHHHHHHHHHH	27.87	-
695	Phosphorylation	RELVEPLTPSGEAPN CCCCCCCCCCCCCCC	26.56	25521595
697	Phosphorylation	LVEPLTPSGEAPNQA CCCCCCCCCCCCCHH	43.99	25521595
710	Ubiquitination	QAHLRILKETEFKKI HHHHHHHHHCCCCEE	61.28	22790023
722	Phosphorylation	KKIKVLGSGAFGTVY CEEEEECCCCCCCEE	23.84	29514104
727	Phosphorylation	LGSGAFGTVYKGLWI ECCCCCCCEECCEEC	17.76	20469934
729	Phosphorylation	SGAFGTVYKGLWIPE CCCCCCEECCEECCC	10.12	29514104
730	Ubiquitination	GAFGTVYKGLWIPEG CCCCCEECCEECCCC	43.10	22790023
739	Ubiquitination	LWIPEGEKVKIPVAI EECCCCCEEECCHHH	60.74	22790023
741	Ubiquitination	IPEGEKVKIPVAIKE CCCCCEEECCHHHHH	52.97	22790023
747	Ubiquitination	VKIPVAIKELREATS EECCHHHHHHHHCCC	40.74	22790023
759	Ubiquitination	ATSPKANKEILDEAY CCCCCCCHHHHHHHH	51.49	22790023
848	Ubiquitination	AARNVLVKTPQHVKI HHCCCEECCCCCEEE	50.78	22790023
854	Ubiquitination	VKTPQHVKITDFGLA ECCCCCEEECHHHHH	37.45	22790023
862	Ubiquitination	ITDFGLAKLLGAEEK ECHHHHHHHHCCHHH	49.65	22790023
869	Ubiquitination	KLLGAEEKEYHAEGG HHHCCHHHHHHCCCC	55.89	22790023
871	Phosphorylation	LGAEEKEYHAEGGKV HCCHHHHHHCCCCCC	19.87	14647453
877	Ubiquitination	EYHAEGGKVPIKWMA HHHCCCCCCCCCHHH	56.55	22790023
931	Ubiquitination	DISSILEKGERLPQP HHHHHHHCCCCCCCC	63.73	22790023
972	Ubiquitination	ELILEFSKMARDPQR HHHHHHHHHCCCCCC	41.73	22790023
989	Oxidation	VIQGDERMHLPSPTD EEECCCCCCCCCCCC	3.42	17242355
993	Phosphorylation	DERMHLPSPTDSNFY CCCCCCCCCCCCHHH	46.95	25521595
995	Phosphorylation	RMHLPSPTDSNFYRA CCCCCCCCCCHHHHH	57.29	26239621
997	Phosphorylation	HLPSPTDSNFYRALM CCCCCCCCHHHHHHC	31.17	22817900
1000	Phosphorylation	SPTDSNFYRALMDEE CCCCCHHHHHHCCHH	10.14	22817900
1018	Phosphorylation	DVVDADEYLIPQQGF HCCCHHHCCCCCCCC	15.52	17139251
1028	Phosphorylation	PQQGFFNSPSTSRTP CCCCCCCCCCCCCCC	18.31	21743459
1030	Phosphorylation	QGFFNSPSTSRTPLL CCCCCCCCCCCCCCC	38.54	23649490
1031	Phosphorylation	GFFNSPSTSRTPLLS CCCCCCCCCCCCCCH	26.13	23984901
1032	Phosphorylation	FFNSPSTSRTPLLSS CCCCCCCCCCCCCHH	38.19	23649490
1034	Phosphorylation	NSPSTSRTPLLSSLS CCCCCCCCCCCHHCE	20.32	22942356
1038	Phosphorylation	TSRTPLLSSLSATSN CCCCCCCHHCEECCC	36.59	23984901
1039	Phosphorylation	SRTPLLSSLSATSNN CCCCCCHHCEECCCC	26.72	23984901
1041	Phosphorylation	TPLLSSLSATSNNST CCCCHHCEECCCCCC	31.30	21743459
1043	Phosphorylation	LLSSLSATSNNSTVA CCHHCEECCCCCCEE	28.72	21743459
1044	Phosphorylation	LSSLSATSNNSTVAC CHHCEECCCCCCEEE	33.46	25521595
1047	Phosphorylation	LSATSNNSTVACINR CEECCCCCCEEEECC	28.63	25521595
1048	Phosphorylation	SATSNNSTVACINRN EECCCCCCEEEECCC	17.78	25521595
1051	S-palmitoylation	SNNSTVACINRNGSC CCCCCEEEECCCCCE	2.17	-
1057	Phosphorylation	ACINRNGSCRVKEDA EEECCCCCEEECCCC	11.42	23140645
1061	Ubiquitination	RNGSCRVKEDAFLQR CCCCEEECCCCCHHH	30.44	22790023
1069	Phosphorylation	EDAFLQRYSSDPTGA CCCCHHHHCCCCCCC	10.28	17139251
1070	Phosphorylation	DAFLQRYSSDPTGAV CCCHHHHCCCCCCCC	30.38	19878607
1071	Phosphorylation	AFLQRYSSDPTGAVT CCHHHHCCCCCCCCC	38.38	19878607
1074	Phosphorylation	QRYSSDPTGAVTEDN HHHCCCCCCCCCCCC	42.64	26239621
1078	Phosphorylation	SDPTGAVTEDNIDDA CCCCCCCCCCCCCCC	36.77	23984901
1092	Phosphorylation	AFLPVPEYVNQSVPK CCCCCHHHCCCCCCC	9.91	17139251
1096	Phosphorylation	VPEYVNQSVPKRPAG CHHHCCCCCCCCCCC	34.87	30352176
1104	Phosphorylation	VPKRPAGSVQNPVYH CCCCCCCCCCCCCCC	23.72	22499769
1110	Phosphorylation	GSVQNPVYHNQPLHP CCCCCCCCCCCCCCC	9.05	22499769
1138	Phosphorylation	NAVGNPEYLNTAQPT CCCCCHHHCCCCCCC	13.40	-
1145	Phosphorylation	YLNTAQPTCLSSGFN HCCCCCCCHHHCCCC	17.63	23984901
1146	S-palmitoylation	LNTAQPTCLSSGFNS CCCCCCCHHHCCCCC	4.40	-
1148	Phosphorylation	TAQPTCLSSGFNSPA CCCCCHHHCCCCCCC	30.48	23984901
1149	Phosphorylation	AQPTCLSSGFNSPAL CCCCHHHCCCCCCCE	34.16	23984901
1153	Phosphorylation	CLSSGFNSPALWIQK HHHCCCCCCCEEEEC	14.86	23984901
1162	Phosphorylation	ALWIQKGSHQMSLDN CEEEECCCCCCCCCC	19.99	22942356
1166	Phosphorylation	QKGSHQMSLDNPDYQ ECCCCCCCCCCCCHH	26.46	25521595
1172	Phosphorylation	MSLDNPDYQQDFFPK CCCCCCCHHCCCCCC	14.88	25521595
1179	Ubiquitination	YQQDFFPKETKPNGI HHCCCCCCCCCCCCC	73.24	22790023
1182	Ubiquitination	DFFPKETKPNGIFKG CCCCCCCCCCCCCCC	37.26	22790023
1188	Ubiquitination	TKPNGIFKGPTAENA CCCCCCCCCCCHHCC	63.16	22790023
1197	Phosphorylation	PTAENAEYLRVAPPS CCHHCCCEEEECCCC	9.44	25521595
1199	Methylation	AENAEYLRVAPPSSE HHCCCEEEECCCCCC	22.96	-

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
680	T	Phosphorylation	Kinase	PRKD1	Q62101	Uniprot
680	T	Phosphorylation	Kinase	PKC	-	Uniprot
695	T	Phosphorylation	Kinase	PRKD1	Q62101	Uniprot
695	T	Phosphorylation	Kinase	MAPK1	P63085	GPS
871	Y	Phosphorylation	Kinase	SRC	P05480	PSP
871	Y	Phosphorylation	Kinase	SRC	Q9WUD9	PSP
1069	Y	Phosphorylation	Kinase	EGFR	Q01279	PSP
1197	Y	Phosphorylation	Kinase	EGFR	Q01279	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	Cbl	P22682	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
11	K	ubiquitylation	23418353
Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs.
29	K	ubiquitylation	23418353
Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs.
48	K	ubiquitylation	23418353
Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs.
63	K	ubiquitylation	23418353
Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs.
680	T	Phosphorylation	-
Phosphorylation at Thr-680 and Thr-695 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation.
695	T	Phosphorylation	-
Phosphorylation at Ser-697 is partial and occurs only if Thr-695 is phosphorylated.
695	T	Phosphorylation	-
Phosphorylation at Thr-680 and Thr-695 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation.
697	S	Phosphorylation	-
Phosphorylation at Ser-697 is partial and occurs only if Thr-695 is phosphorylated.
1199	R	Methylation	-
Autophosphorylation at Tyr-1199 is stimulated by methylation at Arg-1199 and enhances interaction with PTPN6.
1199	R	Methylation	-
Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197.
1199	R	Phosphorylation	-
Autophosphorylation at Tyr-1199 is stimulated by methylation at Arg-1199 and enhances interaction with PTPN6.
1199	R	Phosphorylation	-
Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197.

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 EGFR_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PRKN_HUMAN	PARK2	physical	16862145
EPS15_MOUSE	Eps15	physical	16862145
CBL_MOUSE	Cbl	physical	17372273
CBL_MOUSE	Cbl	physical	17139251
MK14_MOUSE	Mapk14	physical	17139251
ARHG7_MOUSE	Arhgef7	physical	16892055
PA2GA_MOUSE	Pla2g2a	genetic	11818567
ERBB2_MOUSE	Erbb2	physical	21044682
JAK2_MOUSE	Jak2	physical	9038232
GRB2_MOUSE	Grb2	physical	9363897
SOCS5_MOUSE	Socs5	physical	15695332
CBL_MOUSE	Cbl	physical	23457600
STAT1_HUMAN	STAT1	physical	7657660
CBL_MOUSE	Cbl	physical	7657591
CBL_MOUSE	Cbl	physical	23027125
GRB2_MOUSE	Grb2	physical	23027125
ASPP1_MOUSE	Ppp1r13b	physical	23027125
PTN11_MOUSE	Ptpn11	physical	23027125
ERBB2_MOUSE	Erbb2	physical	23027125
SOS1_MOUSE	Sos1	physical	23027125
GRB2_MOUSE	Grb2	physical	20676128
SHC1_MOUSE	Shc1	physical	20676128
EGFR_MOUSE	Egfr	physical	20676128

Drug and Disease Associations

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

Regulatory Network of EGFR_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."; Bernhard O.K., Kapp E.A., Simpson R.J.; J. Proteome Res. 6:987-995(2007). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-175, AND MASSSPECTROMETRY.	17330941 [Abstract]
"Proteome-wide characterization of N-glycosylation events by diagonalchromatography."; Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.; J. Proteome Res. 5:2438-2447(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352 AND ASN-444, AND MASSSPECTROMETRY.	16944957 [Abstract]

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