UniProt ID | EGFR_HUMAN | |
---|---|---|
UniProt AC | P00533 | |
Protein Name | Epidermal growth factor receptor | |
Gene Name | EGFR | |
Organism | Homo sapiens (Human). | |
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 . En |
|
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: 2790960] | |
Protein Sequence | MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
37 | Sumoylation | VCQGTSNKLTQLGTF CCCCCCCHHHHCCHH | 53.32 | - | |
37 | Sumoylation | VCQGTSNKLTQLGTF CCCCCCCHHHHCCHH | 53.32 | - | |
50 | Phosphorylation | TFEDHFLSLQRMFNN HHHHHHHHHHHHHCC | 22.85 | 24719451 | |
56 (in isoform 1) | N-linked_Glycosylation | - | 42.79 | - | |
56 | N-linked_Glycosylation | LSLQRMFNNCEVVLG HHHHHHHCCCEEEEC | 42.79 | 12731890 | |
56 | N-linked_Glycosylation | LSLQRMFNNCEVVLG HHHHHHHCCCEEEEC | 42.79 | 16799092 | |
56 (in isoform 2) | N-linked_Glycosylation | - | 42.79 | - | |
56 (in isoform 3) | N-linked_Glycosylation | - | 42.79 | - | |
73 | N-linked_Glycosylation | EITYVQRNYDLSFLK EEEEEECCCCHHHHH | 19.99 | 20837704 | |
77 | Phosphorylation | VQRNYDLSFLKTIQE EECCCCHHHHHHHHH | 26.15 | 21712546 | |
111 | Sulfoxidation | LQIIRGNMYYENSYA CEEEECCCCCCCCEE | 4.14 | 28465586 | |
112 | Phosphorylation | QIIRGNMYYENSYAL EEEECCCCCCCCEEE | 16.18 | - | |
113 | Phosphorylation | IIRGNMYYENSYALA EEECCCCCCCCEEEE | 9.62 | - | |
117 | Phosphorylation | NMYYENSYALAVLSN CCCCCCCEEEEEHHC | 19.74 | - | |
128 (in isoform 1) | N-linked_Glycosylation | - | 39.25 | - | |
128 | N-linked_Glycosylation | VLSNYDANKTGLKEL EHHCCCCCCCCCCCC | 39.25 | 12731890 | |
128 | N-linked_Glycosylation | VLSNYDANKTGLKEL EHHCCCCCCCCCCCC | 39.25 | 12731890 | |
128 (in isoform 2) | N-linked_Glycosylation | - | 39.25 | - | |
128 (in isoform 3) | N-linked_Glycosylation | - | 39.25 | - | |
133 | Acetylation | DANKTGLKELPMRNL CCCCCCCCCCCCCCH | 59.56 | 18530309 | |
151 | Phosphorylation | LHGAVRFSNNPALCN HHHHHHCCCCCCCCC | 25.74 | 21080693 | |
175 (in isoform 1) | N-linked_Glycosylation | - | 28.79 | - | |
175 | N-linked_Glycosylation | VSSDFLSNMSMDFQN HCHHHHHHCCCCHHH | 28.79 | 12731890 | |
175 | N-linked_Glycosylation | VSSDFLSNMSMDFQN HCHHHHHHCCCCHHH | 28.79 | 12731890 | |
175 (in isoform 2) | N-linked_Glycosylation | - | 28.79 | - | |
175 (in isoform 3) | N-linked_Glycosylation | - | 28.79 | - | |
190 | S-nitrosocysteine | HLGSCQKCDPSCPNG CCCCCCCCCCCCCCC | 3.71 | - | |
190 | S-nitrosylation | HLGSCQKCDPSCPNG CCCCCCCCCCCCCCC | 3.71 | 22178444 | |
196 (in isoform 1) | N-linked_Glycosylation | - | 60.38 | - | |
196 | N-linked_Glycosylation | KCDPSCPNGSCWGAG CCCCCCCCCCCCCCC | 60.38 | 12731890 | |
196 | N-linked_Glycosylation | KCDPSCPNGSCWGAG CCCCCCCCCCCCCCC | 60.38 | 12731890 | |
196 (in isoform 2) | N-linked_Glycosylation | - | 60.38 | - | |
196 (in isoform 3) | N-linked_Glycosylation | - | 60.38 | - | |
212 | Acetylation | ENCQKLTKIICAQQC HHHHHHHHHHHHHHC | 40.28 | 26051181 | |
212 | Ubiquitination | ENCQKLTKIICAQQC HHHHHHHHHHHHHHC | 40.28 | - | |
222 | Dimethylation | CAQQCSGRCRGKSPS HHHHCCCCCCCCCHH | 7.23 | - | |
222 | Methylation | CAQQCSGRCRGKSPS HHHHCCCCCCCCCHH | 7.23 | - | |
224 | Dimethylation | QQCSGRCRGKSPSDC HHCCCCCCCCCHHHC | 54.97 | - | |
224 | Methylation | QQCSGRCRGKSPSDC HHCCCCCCCCCHHHC | 54.97 | - | |
227 | Phosphorylation | SGRCRGKSPSDCCHN CCCCCCCCHHHCCCC | 32.24 | 30576142 | |
229 | Phosphorylation | RCRGKSPSDCCHNQC CCCCCCHHHCCCCCC | 50.82 | 21487020 | |
246 | Phosphorylation | GCTGPRESDCLVCRK CCCCCCCCCEEEECC | 34.60 | 30576142 | |
268 | Sulfoxidation | KDTCPPLMLYNPTTY CCCCCCEEEECCCEE | 4.62 | 28465586 | |
277 | Sulfoxidation | YNPTTYQMDVNPEGK ECCCEEEECCCCCCC | 4.35 | 28465586 | |
284 | Acetylation | MDVNPEGKYSFGATC ECCCCCCCCEEECEE | 35.74 | 12650313 | |
290 (in isoform 1) | Phosphorylation | - | 20.43 | - | |
290 | Phosphorylation | GKYSFGATCVKKCPR CCCEEECEEEECCCC | 20.43 | 18452278 | |
290 (in isoform 2) | Phosphorylation | - | 20.43 | - | |
290 (in isoform 3) | Phosphorylation | - | 20.43 | - | |
291 | S-nitrosocysteine | KYSFGATCVKKCPRN CCEEECEEEECCCCC | 4.13 | - | |
291 | S-nitrosylation | KYSFGATCVKKCPRN CCEEECEEEECCCCC | 4.13 | 22178444 | |
293 | Ubiquitination | SFGATCVKKCPRNYV EEECEEEECCCCCEE | 51.29 | - | |
311 | S-nitrosocysteine | HGSCVRACGADSYEM CCHHHHCCCCCCEEC | 3.02 | - | |
311 | S-nitrosylation | HGSCVRACGADSYEM CCHHHHCCCCCCEEC | 3.02 | 22178444 | |
318 | Sulfoxidation | CGADSYEMEEDGVRK CCCCCEECHHHCCCC | 5.33 | 28465586 | |
329 | S-nitrosocysteine | GVRKCKKCEGPCRKV CCCCCCCCCCCHHHC | 4.46 | - | |
329 | S-nitrosylation | GVRKCKKCEGPCRKV CCCCCCCCCCCHHHC | 4.46 | 22178444 | |
346 | Acetylation | GIGIGEFKDSLSINA CCCCCCCCCCEECCC | 41.95 | 132865 | |
352 (in isoform 1) | N-linked_Glycosylation | - | 37.02 | - | |
352 | N-linked_Glycosylation | FKDSLSINATNIKHF CCCCEECCCCCCCCC | 37.02 | 12297049 | |
352 | N-linked_Glycosylation | FKDSLSINATNIKHF CCCCEECCCCCCCCC | 37.02 | 12297049 | |
352 (in isoform 2) | N-linked_Glycosylation | - | 37.02 | - | |
352 (in isoform 3) | N-linked_Glycosylation | - | 37.02 | - | |
354 | Phosphorylation | DSLSINATNIKHFKN CCEECCCCCCCCCCC | 32.75 | 24719451 | |
361 (in isoform 1) | N-linked_Glycosylation | - | 33.10 | - | |
361 | N-linked_Glycosylation | TNIKHFKNCTSISGD CCCCCCCCCCEECCC | 33.10 | 12731890 | |
361 | N-linked_Glycosylation | TNIKHFKNCTSISGD CCCCCCCCCCEECCC | 33.10 | 12731890 | |
361 (in isoform 2) | N-linked_Glycosylation | - | 33.10 | - | |
361 (in isoform 3) | N-linked_Glycosylation | - | 33.10 | - | |
380 | O-linked_Glycosylation | PVAFRGDSFTHTPPL EEEECCCCCCCCCCC | 34.56 | 30059200 | |
396 | 2-Hydroxyisobutyrylation | PQELDILKTVKEITG HHHCHHHHHHHHHHC | 52.16 | - | |
396 | Ubiquitination | PQELDILKTVKEITG HHHCHHHHHHHHHHC | 52.16 | - | |
413 (in isoform 1) | N-linked_Glycosylation | - | 48.34 | - | |
413 | N-linked_Glycosylation | LIQAWPENRTDLHAF HEEECCCCCCCCHHH | 48.34 | 12731890 | |
413 | N-linked_Glycosylation | LIQAWPENRTDLHAF HEEECCCCCCCCHHH | 48.34 | 12731890 | |
413 (in isoform 3) | N-linked_Glycosylation | - | 48.34 | - | |
444 (in isoform 1) | N-linked_Glycosylation | - | 28.17 | - | |
444 | N-linked_Glycosylation | SLAVVSLNITSLGLR EEEEEEECCCHHHCC | 28.17 | 12731890 | |
444 | N-linked_Glycosylation | SLAVVSLNITSLGLR EEEEEEECCCHHHCC | 28.17 | 12731890 | |
444 (in isoform 3) | N-linked_Glycosylation | - | 28.17 | - | |
457 | Phosphorylation | LRSLKEISDGDVIIS CCCCHHCCCCCEEEE | 36.31 | - | |
470 | S-nitrosocysteine | ISGNKNLCYANTINW EECCCCCEEECCCCH | 4.16 | - | |
470 | S-nitrosylation | ISGNKNLCYANTINW EECCCCCEEECCCCH | 4.16 | 22178444 | |
479 | Ubiquitination | ANTINWKKLFGTSGQ ECCCCHHHHHCCCCC | 40.43 | - | |
487 | Ubiquitination | LFGTSGQKTKIISNR HHCCCCCCEEEEECC | 56.14 | - | |
489 | Ubiquitination | GTSGQKTKIISNRGE CCCCCCEEEEECCCC | 45.11 | - | |
511 | Phosphorylation | QVCHALCSPEGCWGP CHHHHHCCCCCCCCC | 27.17 | 21080693 | |
528 (in isoform 1) | N-linked_Glycosylation | - | 40.21 | - | |
528 | N-linked_Glycosylation | RDCVSCRNVSRGREC CCCCCCCCCCCCCHH | 40.21 | 12731890 | |
528 | N-linked_Glycosylation | RDCVSCRNVSRGREC CCCCCCCCCCCCCHH | 40.21 | 12731890 | |
528 (in isoform 3) | N-linked_Glycosylation | - | 40.21 | - | |
538 | Ubiquitination | RGRECVDKCNLLEGE CCCHHHHHCCCCCCC | 12.48 | - | |
568 (in isoform 1) | N-linked_Glycosylation | - | 29.45 | - | |
568 | N-linked_Glycosylation | ECLPQAMNITCTGRG HHHCCCCCEEECCCC | 29.45 | 12731890 | |
568 | N-linked_Glycosylation | ECLPQAMNITCTGRG HHHCCCCCEEECCCC | 29.45 | 12731890 | |
568 (in isoform 3) | N-linked_Glycosylation | - | 29.45 | - | |
585 | Phosphorylation | NCIQCAHYIDGPHCV CCEEECCCCCCCCEE | 5.12 | 21080693 | |
603 (in isoform 1) | N-linked_Glycosylation | - | 40.85 | - | |
603 | N-linked_Glycosylation | PAGVMGENNTLVWKY CCCCCCCCCEEEEEE | 40.85 | 12731890 | |
603 | N-linked_Glycosylation | PAGVMGENNTLVWKY CCCCCCCCCEEEEEE | 40.85 | 12731890 | |
603 (in isoform 3) | N-linked_Glycosylation | - | 40.85 | - | |
623 (in isoform 1) | N-linked_Glycosylation | - | 13.70 | - | |
623 | N-linked_Glycosylation | VCHLCHPNCTYGCTG CEEECCCCCCCCCCC | 13.70 | 12731890 | |
623 | N-linked_Glycosylation | VCHLCHPNCTYGCTG CEEECCCCCCCCCCC | 13.70 | 16799092 | |
623 (in isoform 3) | N-linked_Glycosylation | - | 13.70 | - | |
645 | Phosphorylation | TNGPKIPSIATGMVG CCCCCCCHHHHHHHH | 28.47 | - | |
648 | Phosphorylation | PKIPSIATGMVGALL CCCCHHHHHHHHHHH | 24.92 | - | |
678 | Phosphorylation | RHIVRKRTLRRLLQE HHHHHHHHHHHHHHH | 27.87 | 10523301 | |
693 | Phosphorylation | RELVEPLTPSGEAPN CCCCCCCCCCCCCCC | 26.56 | 22167270 | |
695 | Phosphorylation | LVEPLTPSGEAPNQA CCCCCCCCCCCCCHH | 43.99 | 22167270 | |
708 | Acetylation | QALLRILKETEFKKI HHHHHHHHHCCCCEE | 61.28 | 21094134 | |
708 | Ubiquitination | QALLRILKETEFKKI HHHHHHHHHCCCCEE | 61.28 | 17940017 | |
713 | Ubiquitination | ILKETEFKKIKVLGS HHHHCCCCEEEEECC | 47.56 | 16543144 | |
714 | Ubiquitination | LKETEFKKIKVLGSG HHHCCCCEEEEECCC | 53.75 | 16543144 | |
716 | Ubiquitination | ETEFKKIKVLGSGAF HCCCCEEEEECCCCC | 40.04 | 16543144 | |
720 | Phosphorylation | KKIKVLGSGAFGTVY CEEEEECCCCCCCEE | 23.84 | 21945579 | |
725 | Phosphorylation | LGSGAFGTVYKGLWI ECCCCCCCEECCEEC | 17.76 | 21945579 | |
727 | Phosphorylation | SGAFGTVYKGLWIPE CCCCCCEECCEECCC | 10.12 | 16729043 | |
728 | Ubiquitination | GAFGTVYKGLWIPEG CCCCCEECCEECCCC | 43.10 | 17940017 | |
737 | Ubiquitination | LWIPEGEKVKIPVAI EECCCCCEEECCHHH | 60.74 | 16543144 | |
737 (in isoform 1) | Ubiquitination | - | 60.74 | 21890473 | |
739 | 2-Hydroxyisobutyrylation | IPEGEKVKIPVAIKE CCCCCEEECCHHHHH | 52.97 | - | |
739 | Ubiquitination | IPEGEKVKIPVAIKE CCCCCEEECCHHHHH | 52.97 | 17940017 | |
745 | 2-Hydroxyisobutyrylation | VKIPVAIKELREATS EECCHHHHHHHHCCC | 40.74 | - | |
745 | Methylation | VKIPVAIKELREATS EECCHHHHHHHHCCC | 40.74 | - | |
745 | Ubiquitination | VKIPVAIKELREATS EECCHHHHHHHHCCC | 40.74 | - | |
752 | Phosphorylation | KELREATSPKANKEI HHHHHCCCCCCCHHH | 31.30 | 22817900 | |
754 | Ubiquitination | LREATSPKANKEILD HHHCCCCCCCHHHHH | 65.44 | 16543144 | |
757 | Ubiquitination | ATSPKANKEILDEAY CCCCCCCHHHHHHHH | 51.49 | 16543144 | |
764 | Phosphorylation | KEILDEAYVMASVDN HHHHHHHHHHHCCCC | 6.68 | 21080693 | |
766 | Sulfoxidation | ILDEAYVMASVDNPH HHHHHHHHHCCCCHH | 1.18 | 28465586 | |
768 | Phosphorylation | DEAYVMASVDNPHVC HHHHHHHCCCCHHHH | 16.35 | 17653080 | |
797 | S-palmitoylation | TQLMPFGCLLDYVRE HHHCCHHHHHHHHHH | 3.31 | 29449326 | |
801 | Phosphorylation | PFGCLLDYVREHKDN CHHHHHHHHHHCCCC | 11.02 | - | |
823 | Ubiquitination | NWCVQIAKGMNYLED HHHHHHHHCCCHHHH | 61.39 | 17940017 | |
827 | Phosphorylation | QIAKGMNYLEDRRLV HHHHCCCHHHHHCHH | 11.54 | 21080693 | |
846 | Ubiquitination | AARNVLVKTPQHVKI HHCCCEECCCCCEEE | 50.78 | 17940017 | |
852 | Malonylation | VKTPQHVKITDFGLA ECCCCCEEECHHHHH | 37.45 | 26320211 | |
852 | Ubiquitination | VKTPQHVKITDFGLA ECCCCCEEECHHHHH | 37.45 | - | |
860 | Acetylation | ITDFGLAKLLGAEEK ECHHHHHHHHCCHHH | 49.65 | 21094134 | |
860 | Ubiquitination | ITDFGLAKLLGAEEK ECHHHHHHHHCCHHH | 49.65 | 21890473 | |
860 (in isoform 1) | Ubiquitination | - | 49.65 | 21890473 | |
867 | 2-Hydroxyisobutyrylation | KLLGAEEKEYHAEGG HHHCCHHHHHHCCCC | 55.89 | - | |
867 | Acetylation | KLLGAEEKEYHAEGG HHHCCHHHHHHCCCC | 55.89 | 21094134 | |
867 | Ubiquitination | KLLGAEEKEYHAEGG HHHCCHHHHHHCCCC | 55.89 | 16543144 | |
869 | Phosphorylation | LGAEEKEYHAEGGKV HCCHHHHHHCCCCCC | 19.87 | 16729043 | |
875 | Ubiquitination | EYHAEGGKVPIKWMA HHHCCCCCCCCCHHH | 56.55 | - | |
891 | Phosphorylation | ESILHRIYTHQSDVW HHHHHHHHHCCHHHH | 9.72 | 16729043 | |
892 | Phosphorylation | SILHRIYTHQSDVWS HHHHHHHHCCHHHHH | 15.86 | - | |
913 | Ubiquitination | ELMTFGSKPYDGIPA HHHHCCCCCCCCCCH | 48.23 | 17940017 | |
915 | Phosphorylation | MTFGSKPYDGIPASE HHCCCCCCCCCCHHH | 30.45 | 16729043 | |
925 | Phosphorylation | IPASEISSILEKGER CCHHHHHHHHHCCCC | 36.53 | 24719451 | |
929 | Ubiquitination | EISSILEKGERLPQP HHHHHHHCCCCCCCC | 63.73 | 16543144 | |
940 | Phosphorylation | LPQPPICTIDVYMIM CCCCCCCEEEEEEEE | 22.41 | - | |
944 | Phosphorylation | PICTIDVYMIMVKCW CCCEEEEEEEEEEHH | 4.16 | 16729043 | |
960 | Ubiquitination | IDADSRPKFRELIIE CCCCCCHHHHHHHHH | 56.81 | 17940017 | |
970 | Ubiquitination | ELIIEFSKMARDPQR HHHHHHHHHCCCCCC | 41.73 | 16543144 | |
978 | Phosphorylation | MARDPQRYLVIQGDE HCCCCCCEEEEECCC | 10.48 | 16729043 | |
991 | Phosphorylation | DERMHLPSPTDSNFY CCCCCCCCCCCCHHH | 46.95 | 22167270 | |
993 | Phosphorylation | RMHLPSPTDSNFYRA CCCCCCCCCCHHHHH | 57.29 | 21945579 | |
995 | Phosphorylation | HLPSPTDSNFYRALM CCCCCCCCHHHHHHC | 31.17 | 21945579 | |
998 | Phosphorylation | SPTDSNFYRALMDEE CCCCCHHHHHHCCCC | 10.14 | 16729043 | |
1016 | Dephosphorylation | DVVDADEYLIPQQGF CCCCHHHHCCCCCCC | 15.52 | 14560030 | |
1016 | Phosphorylation | DVVDADEYLIPQQGF CCCCHHHHCCCCCCC | 15.52 | 16729043 | |
1025 | Phosphorylation | IPQQGFFSSPSTSRT CCCCCCCCCCCCCCC | 38.79 | 21080693 | |
1026 | Phosphorylation | PQQGFFSSPSTSRTP CCCCCCCCCCCCCCC | 20.08 | 21080693 | |
1028 | Phosphorylation | QGFFSSPSTSRTPLL CCCCCCCCCCCCCCC | 40.75 | 28176443 | |
1029 | Phosphorylation | GFFSSPSTSRTPLLS CCCCCCCCCCCCCCH | 26.13 | 29116813 | |
1030 | Phosphorylation | FFSSPSTSRTPLLSS CCCCCCCCCCCCCHH | 38.19 | 21080693 | |
1032 | Phosphorylation | SSPSTSRTPLLSSLS CCCCCCCCCCCHHHE | 20.32 | 23663014 | |
1036 | Phosphorylation | TSRTPLLSSLSATSN CCCCCCCHHHEECCC | 36.59 | 22617229 | |
1037 | Phosphorylation | SRTPLLSSLSATSNN CCCCCCHHHEECCCC | 26.72 | 21080693 | |
1039 | Phosphorylation | TPLLSSLSATSNNST CCCCHHHEECCCCCC | 31.30 | 25463755 | |
1041 | Phosphorylation | LLSSLSATSNNSTVA CCHHHEECCCCCCEE | 28.72 | 22617229 | |
1042 | Phosphorylation | LSSLSATSNNSTVAC CHHHEECCCCCCEEE | 33.46 | 25463755 | |
1045 | Phosphorylation | LSATSNNSTVACIDR HEECCCCCCEEEEEC | 28.63 | 26055452 | |
1046 | Phosphorylation | SATSNNSTVACIDRN EECCCCCCEEEEECC | 17.78 | 25463755 | |
1049 | S-palmitoylation | SNNSTVACIDRNGLQ CCCCCEEEEECCCCC | 2.63 | 29449326 | |
1057 | Phosphorylation | IDRNGLQSCPIKEDS EECCCCCCCCCCCCC | 27.23 | 21080693 | |
1061 | Acetylation | GLQSCPIKEDSFLQR CCCCCCCCCCCHHHH | 40.38 | 27452117 | |
1061 | Ubiquitination | GLQSCPIKEDSFLQR CCCCCCCCCCCHHHH | 40.38 | - | |
1064 | Phosphorylation | SCPIKEDSFLQRYSS CCCCCCCCHHHHHCC | 29.02 | 25159151 | |
1069 | Phosphorylation | EDSFLQRYSSDPTGA CCCHHHHHCCCCCCC | 10.28 | 18715874 | |
1070 | Phosphorylation | DSFLQRYSSDPTGAL CCHHHHHCCCCCCCC | 30.38 | 3138233 | |
1071 | Phosphorylation | SFLQRYSSDPTGALT CHHHHHCCCCCCCCC | 38.38 | 3138233 | |
1074 | Phosphorylation | QRYSSDPTGALTEDS HHHCCCCCCCCCCCC | 39.83 | 21080693 | |
1078 | Phosphorylation | SDPTGALTEDSIDDT CCCCCCCCCCCCCCC | 36.89 | 25159151 | |
1081 | Phosphorylation | TGALTEDSIDDTFLP CCCCCCCCCCCCCCC | 22.99 | 21080693 | |
1085 | Phosphorylation | TEDSIDDTFLPVPEY CCCCCCCCCCCCHHH | 24.27 | 25159151 | |
1092 | Phosphorylation | TFLPVPEYINQSVPK CCCCCHHHHCCCCCC | 10.09 | 8408058 | |
1096 | Phosphorylation | VPEYINQSVPKRPAG CHHHHCCCCCCCCCC | 35.58 | 28176443 | |
1099 | Ubiquitination | YINQSVPKRPAGSVQ HHCCCCCCCCCCCCC | 69.71 | - | |
1104 | Phosphorylation | VPKRPAGSVQNPVYH CCCCCCCCCCCCCCC | 23.72 | 21945579 | |
1110 | Phosphorylation | GSVQNPVYHNQPLNP CCCCCCCCCCCCCCC | 9.05 | 16729043 | |
1120 | Phosphorylation | QPLNPAPSRDPHYQD CCCCCCCCCCCCCCC | 51.96 | 26356563 | |
1125 | Phosphorylation | APSRDPHYQDPHSTA CCCCCCCCCCCCCCC | 21.72 | 16729043 | |
1130 | Phosphorylation | PHYQDPHSTAVGNPE CCCCCCCCCCCCCHH | 24.37 | 26356563 | |
1131 | Phosphorylation | HYQDPHSTAVGNPEY CCCCCCCCCCCCHHH | 23.48 | 26356563 | |
1138 | Phosphorylation | TAVGNPEYLNTVQPT CCCCCHHHHCCCCCC | 13.40 | 16729043 | |
1141 | Phosphorylation | GNPEYLNTVQPTCVN CCHHHHCCCCCCCCC | 20.23 | 25106551 | |
1145 | Phosphorylation | YLNTVQPTCVNSTFD HHCCCCCCCCCCCCC | 16.40 | 26356563 | |
1146 | S-palmitoylation | LNTVQPTCVNSTFDS HCCCCCCCCCCCCCC | 3.29 | 29449326 | |
1149 | Phosphorylation | VQPTCVNSTFDSPAH CCCCCCCCCCCCCCH | 15.28 | 26356563 | |
1150 | Phosphorylation | QPTCVNSTFDSPAHW CCCCCCCCCCCCCHH | 26.68 | 26356563 | |
1153 | Phosphorylation | CVNSTFDSPAHWAQK CCCCCCCCCCHHHHC | 21.57 | 29116813 | |
1160 | Ubiquitination | SPAHWAQKGSHQISL CCCHHHHCCCCEEEC | 55.42 | - | |
1162 | Phosphorylation | AHWAQKGSHQISLDN CHHHHCCCCEEECCC | 21.18 | 21945579 | |
1166 | Phosphorylation | QKGSHQISLDNPDYQ HCCCCEEECCCCCHH | 24.09 | 23927012 | |
1172 | Phosphorylation | ISLDNPDYQQDFFPK EECCCCCHHCCCCCC | 14.88 | 16729043 | |
1179 | Acetylation | YQQDFFPKEAKPNGI HHCCCCCCCCCCCCC | 66.21 | 20513767 | |
1179 | Ubiquitination | YQQDFFPKEAKPNGI HHCCCCCCCCCCCCC | 66.21 | - | |
1182 | Acetylation | DFFPKEAKPNGIFKG CCCCCCCCCCCCCCC | 39.86 | 20513767 | |
1182 | Ubiquitination | DFFPKEAKPNGIFKG CCCCCCCCCCCCCCC | 39.86 | - | |
1188 | Acetylation | AKPNGIFKGSTAENA CCCCCCCCCCCHHCC | 50.46 | 20513767 | |
1188 | Methylation | AKPNGIFKGSTAENA CCCCCCCCCCCHHCC | 50.46 | - | |
1188 | Ubiquitination | AKPNGIFKGSTAENA CCCCCCCCCCCHHCC | 50.46 | - | |
1190 | Phosphorylation | PNGIFKGSTAENAEY CCCCCCCCCHHCCCE | 25.65 | 21945579 | |
1191 | Phosphorylation | NGIFKGSTAENAEYL CCCCCCCCHHCCCEE | 46.81 | 21945579 | |
1197 | Dephosphorylation | STAENAEYLRVAPQS CCHHCCCEEEECCCC | 9.44 | 9733788 | |
1197 | Phosphorylation | STAENAEYLRVAPQS CCHHCCCEEEECCCC | 9.44 | 16574647 | |
1199 | Methylation | AENAEYLRVAPQSSE HHCCCEEEECCCCCC | 22.96 | 21258366 | |
1204 | Phosphorylation | YLRVAPQSSEFIGA- EEEECCCCCCCCCC- | 30.67 | 21945579 | |
1205 | Phosphorylation | LRVAPQSSEFIGA-- EEECCCCCCCCCC-- | 31.14 | 21945579 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
229 | S | Phosphorylation | Kinase | AKT1 | P31749 | PSP |
229 | S | Phosphorylation | Kinase | AKT2 | P31751 | PSP |
678 | T | Phosphorylation | Kinase | PKN1 | Q16512 | PSP |
678 | T | Phosphorylation | Kinase | KPCA | P17252 | PhosphoELM |
678 | T | Phosphorylation | Kinase | PRKCA | P20444 | GPS |
678 | T | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
678 | T | Phosphorylation | Kinase | PRKD1 | Q15139 | Uniprot |
678 | T | Phosphorylation | Kinase | PKC | - | Uniprot |
678 | T | Phosphorylation | Kinase | PKCE | Q02156 | PSP |
678 | T | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
678 | T | Phosphorylation | Kinase | PKN3 | Q6P5Z2 | PSP |
693 | T | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
693 | T | Phosphorylation | Kinase | PRKD1 | Q15139 | Uniprot |
693 | T | Phosphorylation | Kinase | MAPK3 | P27361 | GPS |
693 | T | Phosphorylation | Kinase | MAPK14 | Q16539 | GPS |
693 | T | Phosphorylation | Kinase | P38-SUBFAMILY | - | GPS |
693 | T | Phosphorylation | Kinase | PKG2 | Q13237 | PSP |
727 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
764 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
768 | S | Phosphorylation | Kinase | CAMK2A | P11275 | PSP |
768 | S | Phosphorylation | Kinase | CAMK2-FAMILY | - | GPS |
768 | S | Phosphorylation | Kinase | KCC2A | Q9UQM7 | PhosphoELM |
869 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
869 | Y | Phosphorylation | Kinase | SRC | P05480 | PSP |
869 | Y | Phosphorylation | Kinase | EGFR | P00533 | PSP |
869 | Y | Phosphorylation | Kinase | SRC64 | - | PhosphoELM |
892 | T | Phosphorylation | Kinase | PRKAA1 | Q13131 | GPS |
915 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
915 | Y | Phosphorylation | Kinase | SRC64 | - | PhosphoELM |
944 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
944 | Y | Phosphorylation | Kinase | SRC64 | - | PhosphoELM |
998 | Y | Phosphorylation | Kinase | EGFR | P00533 | GPS |
1016 | Y | Phosphorylation | Kinase | ABL1 | P00519 | GPS |
1016 | Y | Phosphorylation | Kinase | SRC64 | - | PhosphoELM |
1016 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
1016 | Y | Phosphorylation | Kinase | EGFR | P00533 | PSP |
1026 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
1039 | S | Phosphorylation | Kinase | MAPK11 | Q15759 | GPS |
1039 | S | Phosphorylation | Kinase | MAPK14 | Q16539 | GPS |
1041 | T | Phosphorylation | Kinase | MAPK11 | Q15759 | GPS |
1041 | T | Phosphorylation | Kinase | MAPK14 | Q16539 | GPS |
1070 | S | Phosphorylation | Kinase | CAMK2-FAMILY | - | GPS |
1070 | S | Phosphorylation | Kinase | KCC2A | Q9UQM7 | PhosphoELM |
1070 | S | Phosphorylation | Kinase | CAMK2A | P11275 | PSP |
1071 | S | Phosphorylation | Kinase | CAMK2-FAMILY | - | GPS |
1071 | S | Phosphorylation | Kinase | KCC2A | Q9UQM7 | PhosphoELM |
1071 | S | Phosphorylation | Kinase | CAMK2A | P11275 | PSP |
1081 | S | Phosphorylation | Kinase | CAMK2A | P11275 | PSP |
1081 | S | Phosphorylation | Kinase | CAMK2-FAMILY | - | GPS |
1081 | S | Phosphorylation | Kinase | KCC2A | Q9UQM7 | PhosphoELM |
1092 | Y | Phosphorylation | Kinase | SRC | P05480 | PSP |
1092 | Y | Phosphorylation | Kinase | ABL1 | P00519 | GPS |
1092 | Y | Phosphorylation | Kinase | EGFR | P00533 | PSP |
1092 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
1110 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
1110 | Y | Phosphorylation | Kinase | EGFR | P00533 | PSP |
1125 | Y | Phosphorylation | Kinase | SRC64 | - | PhosphoELM |
1125 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
1166 | S | Phosphorylation | Kinase | KCC2A | Q9UQM7 | PhosphoELM |
1166 | S | Phosphorylation | Kinase | CAMK2-FAMILY | - | GPS |
1166 | S | Phosphorylation | Kinase | CAMK2A | P11275 | PSP |
1172 | Y | Phosphorylation | Kinase | EGFR | P00533 | PSP |
1197 | Y | Phosphorylation | Kinase | EGFR | P00533 | PSP |
1197 | Y | Phosphorylation | Kinase | ABL1 | P00519 | GPS |
- | K | Ubiquitination | E3 ubiquitin ligase | RNF126 | Q9BV68 | PMID:23418353 |
- | K | Ubiquitination | E3 ubiquitin ligase | RNF115 | Q9Y4L5 | PMID:23418353 |
- | K | Ubiquitination | E3 ubiquitin ligase | CBLB | Q13191 | PMID:10542134 |
- | K | Ubiquitination | E3 ubiquitin ligase | NEDD4 | P46934 | PMID:20086093 |
- | K | Ubiquitination | E3 ubiquitin ligase | CBL | P22681 | PMID:10428778 |
- | K | Ubiquitination | E3 ubiquitin ligase | SOCS5 | O75159 | PMID:15590694 |
- | K | Ubiquitination | E3 ubiquitin ligase | ITCH | Q96J02 | PMID:12226085 |
- | K | Ubiquitination | E3 ubiquitin ligase | CBLC | Q9ULV8 | PMID:22199232 |
- | K | Ubiquitination | E3 ubiquitin ligase | SMURF2 | Q9HAU4 | PMID:21750651 |
- | K | Ubiquitination | E3 ubiquitin ligase | CGRRF1 | Q99675 | PMID:31801577 |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
11 | K | ubiquitylation |
| 16543144 |
29 | K | ubiquitylation |
| 16543144 |
48 | K | ubiquitylation |
| 16543144 |
63 | K | ubiquitylation |
| 16543144 |
678 | T | Phosphorylation |
| 10523301 |
693 | T | Phosphorylation |
| 3138233 |
693 | T | Phosphorylation |
| 3138233 |
695 | S | Phosphorylation |
| 3138233 |
1199 | R | Methylation |
| 21258366 |
1199 | R | Methylation |
| 21258366 |
1199 | R | Phosphorylation |
| 21258366 |
1199 | R | Phosphorylation |
| 21258366 |
* 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_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
H00016 | Oral cancer | |||||
H00017 | Esophageal cancer | |||||
H00018 | Gastric cancer | |||||
H00022 | Bladder cancer | |||||
H00028 | Choriocarcinoma | |||||
H00030 | Cervical cancer | |||||
H00042 | Glioma | |||||
H00055 | Laryngeal cancer | |||||
OMIM Disease | ||||||
211980 | Lung cancer (LNCR) | |||||
616069 | Inflammatory skin and bowel disease, neonatal, 2 (NISBD2) | |||||
Kegg Drug | ||||||
D01977 | Gefitinib (JAN/USAN/INN); Iressa (TN) | |||||
D03350 | Canertinib dihydrochloride (USAN) | |||||
D03455 | Cetuximab (genetical recombination) (JAN); Cetuximab (USAN/INN); Erbitux (TN) | |||||
D04023 | Erlotinib hydrochloride (JAN/USAN); Tarceva (TN) | |||||
D04024 | Lapatinib tosilate hydrate (JAN); Lapatinib ditosylate (USAN); Tykerb (TN) | |||||
D05350 | Panitumumab (genetical recombination) (JAN); Panitumumab (USAN/INN); Vectibix (TN) | |||||
D05399 | Pelitinib (USAN/INN) | |||||
D06407 | Vandetanib (JAN/USAN/INN); Caprelsa (TN) | |||||
D07907 | Erlotinib (INN); Tarceva (TN) | |||||
D08108 | Lapatinib (INN) | |||||
D08950 | Neratinib (INN/USAN) | |||||
D09689 | Varlitinib (USAN/INN) | |||||
D09690 | Varlitinib tosylate (USAN) | |||||
D09724 | Afatinib (USAN/INN) | |||||
D09733 | Afatinib maleate (JAN); Afatinib dimaleate (USAN) | |||||
D09883 | Dacomitinib (USAN/INN) | |||||
D10018 | Necitumumab (USAN/INN) | |||||
D10031 | Zalutumumab (USAN/INN) | |||||
D10439 | Imgatuzumab (USAN/INN) | |||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Methylation | |
Reference | PubMed |
"Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylationnegatively modulates EGFR-mediated ERK activation."; Hsu J.M., Chen C.T., Chou C.K., Kuo H.P., Li L.Y., Lin C.Y., Lee H.J.,Wang Y.N., Liu M., Liao H.W., Shi B., Lai C.C., Bedford M.T.,Tsai C.H., Hung M.C.; Nat. Cell Biol. 13:174-181(2011). Cited for: FUNCTION IN CELL PROLIFERATION AND CELL MIGRATION, METHYLATION ATARG-1199 BY PRMT5, AND INTERACTION WITH PRMT5 AND PTPN6. | |
N-linked Glycosylation | |
Reference | PubMed |
"Structural evidence for loose linkage between ligand binding andkinase activation in the epidermal growth factor receptor."; Lu C., Mi L.Z., Grey M.J., Zhu J., Graef E., Yokoyama S.,Springer T.A.; Mol. Cell. Biol. 30:5432-5443(2010). Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-638 IN COMPLEX WITH EGF,FUNCTION, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-56;ASN-73; ASN-175; ASN-196; ASN-352; ASN-361; ASN-444 AND ASN-528. | |
"EGF activates its receptor by removing interactions that autoinhibitectodomain dimerization."; Ferguson K.M., Berger M.B., Mendrola J.M., Cho H.S., Leahy D.J.,Lemmon M.A.; Mol. Cell 11:507-517(2003). Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-642 IN COMPLEX WITH EGF,FUNCTION, SUBUNIT, MUTAGENESIS OF 587-ASP--HIS-590 AND LYS-609,DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-352; ASN-361; ASN-444;ASN-528; ASN-568 AND ASN-603. | |
"Crystal structure of the complex of human epidermal growth factor andreceptor extracellular domains."; Ogiso H., Ishitani R., Nureki O., Fukai S., Yamanaka M., Kim J.H.,Saito K., Sakamoto A., Inoue M., Shirouzu M., Yokoyama S.; Cell 110:775-787(2002). Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-646 IN COMPLEX WITH EGF,FUNCTION IN MAPK1 AND/OR MAPK3 ACTIVATION, SUBUNIT, SUBCELLULARLOCATION, MUTAGENESIS OF TYR-275; PHE-287; ARG-309 AND ARG-429,DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-56; ASN-175; ASN-196;ASN-352; ASN-361 AND ASN-444. | |
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352; ASN-413 AND ASN-568,AND MASS SPECTROMETRY. | |
"Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MSplatform for high sequence coverage of complex proteins with extensivepost-translational modifications-comprehensive analysis of beta-caseinand epidermal growth factor receptor (EGFR)."; Wu S.L., Kim J., Hancock W.S., Karger B.; J. Proteome Res. 4:1155-1170(2005). Cited for: GLYCOSYLATION AT ASN-56; ASN-128; ASN-175; ASN-196; ASN-352; ASN-361;ASN-413; ASN-444; ASN-528; ASN-568 AND ASN-603, PHOSPHORYLATION ATTHR-693; SER-991 AND SER-1026, AND MASS SPECTROMETRY. | |
"Characterization of the N-oligosaccharides attached to the atypicalAsn-X-Cys sequence of recombinant human epidermal growth factorreceptor."; Sato C., Kim J.-H., Abe Y., Saito K., Yokoyama S., Kohda D.; J. Biochem. 127:65-72(2000). Cited for: GLYCOSYLATION AT ASN-56; ASN-352; ASN-361; ASN-568 AND ASN-603. | |
"Analysis of the glycosylation patterns of the extracellular domain ofthe epidermal growth factor receptor expressed in Chinese hamsterovary fibroblasts."; Smith K.D., Davies M.J., Bailey D., Renouf D.V., Hounsell E.F.; Growth Factors 13:121-132(1996). Cited for: GLYCOSYLATION AT ASN-128; ASN-175; ASN-413; ASN-444 AND ASN-528. | |
Phosphorylation | |
Reference | PubMed |
"Nuclear translocation of epidermal growth factor receptor by Akt-dependent phosphorylation enhances breast cancer-resistant proteinexpression in gefitinib-resistant cells."; Huang W.C., Chen Y.J., Li L.Y., Wei Y.L., Hsu S.C., Tsai S.L.,Chiu P.C., Huang W.P., Wang Y.N., Chen C.H., Chang W.C., Chang W.C.,Chen A.J., Tsai C.H., Hung M.C.; J. Biol. Chem. 286:20558-20568(2011). Cited for: PHOSPHORYLATION AT SER-229. | |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-695; SER-991;THR-993; SER-995; TYR-998; SER-1039; THR-1041; SER-1042; SER-1045;SER-1064 AND SER-1166, AND MASS SPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-695; THR-725;SER-991; SER-1025; SER-1026; SER-1037; SER-1039; SER-1042; SER-1064;SER-1081; SER-1166 AND TYR-1197, AND MASS SPECTROMETRY. | |
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693 AND SER-991, ANDMASS SPECTROMETRY. | |
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-991; TYR-998; SER-1166;TYR-1069; TYR-1172 AND TYR-1197, AND MASS SPECTROMETRY. | |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-991; SER-995;TYR-998; SER-1064; TYR-1069; TYR-1092; TYR-1110; TYR-1138; TYR-1172AND TYR-1197, AND MASS SPECTROMETRY. | |
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-998; TYR-1069; TYR-1092;SER-1166 AND TYR-1172, AND MASS SPECTROMETRY. | |
"Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MSplatform for high sequence coverage of complex proteins with extensivepost-translational modifications-comprehensive analysis of beta-caseinand epidermal growth factor receptor (EGFR)."; Wu S.L., Kim J., Hancock W.S., Karger B.; J. Proteome Res. 4:1155-1170(2005). Cited for: GLYCOSYLATION AT ASN-56; ASN-128; ASN-175; ASN-196; ASN-352; ASN-361;ASN-413; ASN-444; ASN-528; ASN-568 AND ASN-603, PHOSPHORYLATION ATTHR-693; SER-991 AND SER-1026, AND MASS SPECTROMETRY. | |
"Epidermal growth factor receptor threonine and serine residuesphosphorylated in vivo."; Heisermann G.J., Gill G.N.; J. Biol. Chem. 263:13152-13158(1988). Cited for: PROTEIN SEQUENCE OF 687-705; 986-998; 1000-1023; 1026-1030 AND1068-1077, AND PHOSPHORYLATION AT THR-693; SER-695; SER-1070 ANDSER-1071. | |
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, AND MASSSPECTROMETRY. | |
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, AND MASSSPECTROMETRY. | |
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, AND MASSSPECTROMETRY. | |
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, AND MASSSPECTROMETRY. | |
"Cell-type specific phosphorylation of threonines T654 and T669 by PKDdefines the signal capacity of the EGF receptor."; Bagowski C.P., Stein-Gerlach M., Choidas A., Ullrich A.; EMBO J. 18:5567-5576(1999). Cited for: PHOSPHORYLATION AT THR-678 AND THR-693. | |
"Mechanism for activation of the EGF receptor catalytic domain by thejuxtamembrane segment."; Jura N., Endres N.F., Engel K., Deindl S., Das R., Lamers M.H.,Wemmer D.E., Zhang X., Kuriyan J.; Cell 137:1293-1307(2009). Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 696-1022, CATALYTICACTIVITY, PHOSPHORYLATION AT TYR-998; TYR-1016 AND TYR-1197,MUTAGENESIS OF LEU-688; GLU-690; LEU-692; ARG-977 AND1005-GLU-ASP-1006, AND SUBUNIT. | |
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-998; TYR-1016; TYR-1092;TYR-1110; TYR-1138; TYR-1172 AND TYR-1197, AND MASS SPECTROMETRY. | |
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-869; TYR-1092; TYR-1172AND TYR-1197, AND MASS SPECTROMETRY. | |
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC."; Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.; Proteomics 5:3589-3599(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-978, AND MASSSPECTROMETRY. | |
"Identification and characterization of signal transducer andactivator of transcription 3 recruitment sites within the epidermalgrowth factor receptor."; Shao H., Cheng H.Y., Cook R.G., Tweardy D.J.; Cancer Res. 63:3923-3930(2003). Cited for: FUNCTION IN CELL PROLIFERATION, INTERACTION WITH STAT3, ANDPHOSPHORYLATION AT TYR-1092 AND TYR-1110. | |
"All autophosphorylation sites of epidermal growth factor (EGF)receptor and HER2/neu are located in their carboxyl-terminal tails.Identification of a novel site in EGF receptor."; Margolis B.L., Lax I., Kris R., Dombalagian M., Honegger A.M.,Howk R., Givol D., Ullrich A., Schlessinger J.; J. Biol. Chem. 264:10667-10671(1989). Cited for: AUTOPHOSPHORYLATION AT TYR-1110. | |
Ubiquitylation | |
Reference | PubMed |
"Differential regulation of EGF receptor internalization anddegradation by multiubiquitination within the kinase domain."; Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.; Mol. Cell 21:737-748(2006). Cited for: PROTEIN SEQUENCE OF 861-875 AND 914-932, UBIQUITINATION AT LYS-716;LYS-737; LYS-754; LYS-867; LYS-929 AND LYS-970, AND MASS SPECTROMETRY. |