Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Epidermal growth factor receptor  

UniProtKB / Swiss-Prot ID :  EGFR_HUMAN

Gene Name (Synonyms) : 
EGFR, ERBB, ERBB1, HER1  

Species :  Homo sapiens (Human). 

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. Endos 

Protein Function :  Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, 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. Isoform 2 may act as an antagonist of EGF action. 

Transmembrane Topology (topPTM) : EGFR_HUMAN 

Protein Sequence MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYV...
Predicted Secondary Structure CCCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHCCEEEEEEEEEEEE...
Protein Variant
LocationDescription
30Missing (variant EGFR vIII; found in alung cancer sample; somatic mutation;
98R -> Q (in dbSNP:rs17289589). VAR_019293
266P -> R (in dbSNP:rs17336639). VAR_019294
521R -> K (in dbSNP:rs2227983). VAR_019295
674V -> I (slightly increasedautophosphorylation; dbSNP:rs17337079).
709E -> A (found in a lung cancer sample). VAR_026084
709E -> K (found in a lung cancer sample). VAR_026085
719G -> A (found in a lung cancer sample). VAR_026086
719G -> C (found in a lung cancer sample;dbSNP:rs28929495).
719G -> D (found in a lung cancer sample). VAR_026088
719G -> S (found in a lung cancer sample;somatic mutation; strongly increased
724G -> S (found in a lung cancer sample). VAR_026089
734E -> K (found in a lung cancer sample). VAR_026090
746Missing (found in a lung cancer sample). VAR_026092
746Missing (found in a lung cancer sample). VAR_026091
747Missing (found in a lung cancer sample). VAR_026094
747L -> F (found in a lung cancer sample). VAR_026093
748R -> P (found in a lung cancer sample). VAR_026095
752Missing (found in a lung cancer sample). VAR_026096
787Q -> R (found in a lung cancer sample). VAR_026097
790T -> M (found in a lung cancer sample;increased kinase activity).
833L -> V (found in a lung cancer sample). VAR_026099
834V -> L (found in a lung cancer sample). VAR_026100
858L -> M (found in a lung cancer sample). VAR_026101
858L -> R (found in a lung cancer sample;somatic mutation; constitutively
861L -> Q (found in a lung cancer sample). VAR_026102
873G -> E (found in a lung cancer sample). VAR_026103
962R -> G (in dbSNP:rs17337451). VAR_019299
988H -> P (in dbSNP:rs17290699). VAR_019300
1034L -> R (in dbSNP:rs34352568). VAR_042095
1210A -> V (in dbSNP:rs35918369). VAR_042096
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
31S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)EKKVCQGTS
CCCCCCCCC
4.19HPRD
Link
56N-linked (Glc...)QRMFNNCEV
HHHHHCCEE
42.79HPRD
Link
56N-linked (GlcNAc...) (complex); atypical;partial.QRMFNNCEV
HHHHHCCEE
42.79UniProtKB
Link
58S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)MFNNCEVVL
HHHCCEEEE
4.39HPRD
Link
73N-linked (GlcNAc...).YVQRNYDLS
EECCCCCCC
19.99UniProtKB
Link
128N-linked (Glc...)NYDANKTGL
CCCCCCCCE
39.25HPRD
Link
128N-linked (GlcNAc...).NYDANKTGL
CCCCCCCCE
39.25UniProtKB
Link
151PhosphoserineAVRFSNNPA
CEEEEECCC
25.74Phosphositeplus
Link
157S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)NPALCNVES
CCCCCCCCC
6.11HPRD
Link
175N-linked (Glc...)DFLSNMSMD
CCCCCCCCC
28.79HPRD
Link
175N-linked (GlcNAc...).DFLSNMSMD
CCCCCCCCC
28.79UniProtKB
Link
187S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)HLGSCQKCD
CCCCCCCCC
4.21HPRD
Link
190S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)SCQKCDPSC
CCCCCCCCC
3.71HPRD
Link
190S-nitrosocysteineSCQKCDPSC
CCCCCCCCC
3.71dbSNO
Link
194S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CDPSCPNGS
CCCCCCCCC
3.55HPRD
Link
196N-linked (Glc...)PSCPNGSCW
CCCCCCCEE
60.38HPRD
Link
196N-linked (GlcNAc...).PSCPNGSCW
CCCCCCCEE
60.38UniProtKB
Link
199S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)PNGSCWGAG
CCCCEECCC
4.05HPRD
Link
207S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)GEENCQKLT
CCCCCCEEC
4.22HPRD
Link
215S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)TKIICAQQC
CCCCCCCCC
2.97HPRD
Link
219S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CAQQCSGRC
CCCCCCCCC
2.87HPRD
Link
223S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CSGRCRGKS
CCCCCCCCC
8.41HPRD
Link
229PhosphoserineGKSPSDCCH
CCCCCCCCC
50.82Phosphositeplus
Link
229Phosphoserine.GKSPSDCCH
CCCCCCCCC
50.82UniProtKB
Link
231S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)SPSDCCHNQ
CCCCCCCHH
2.74HPRD
Link
232S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)PSDCCHNQC
CCCCCCHHH
3.97HPRD
Link
236S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CHNQCAAGC
CCHHHCCCC
3.21HPRD
Link
240S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CAAGCTGPR
HCCCCCCCC
3.22HPRD
Link
248S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)RESDCLVCR
CCCCCEEEE
4.23HPRD
Link
251S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)DCLVCRKFR
CCEEEEEEC
2.24HPRD
Link
260S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)DEATCKDTC
CCCEEHHCC
4.90HPRD
Link
264S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CKDTCPPLM
EHHCCCCCC
4.72HPRD
Link
290PhosphothreonineSFGATCVKK
CCCCCHHHH
20.43HPRD
Link
291S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)FGATCVKKC
CCCCHHHHC
4.13HPRD
Link
291S-nitrosocysteineFGATCVKKC
CCCCHHHHC
4.13dbSNO
Link
295S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CVKKCPRNY
HHHHCCCCC
2.95HPRD
Link
307S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)DHGSCVRAC
CCCCEEEEC
2.58HPRD
Link
311S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CVRACGADS
EEEECCCCC
3.02HPRD
Link
311S-nitrosocysteineCVRACGADS
EEEECCCCC
3.02dbSNO
Link
326S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)GVRKCKKCE
CCEEEEECC
3.40HPRD
Link
329S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)KCKKCEGPC
EEEECCCCC
4.46HPRD
Link
329S-nitrosocysteineKCKKCEGPC
EEEECCCCC
4.46dbSNO
Link
333S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CEGPCRKVC
CCCCCCCEE
10.93HPRD
Link
337S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CRKVCNGIG
CCCEEEECC
4.30HPRD
Link-
352N-linked (Glc...)SLSINATNI
EEEECHHHH
37.02HPRD
Link-
352N-linked (GlcNAc...).SLSINATNI
EEEECHHHH
37.02UniProtKB
Link-
361N-linked (Glc...)KHFKNCTSI
HHCCCCEEE
33.10HPRD
Link-
361N-linked (GlcNAc...).KHFKNCTSI
HHCCCCEEE
33.10UniProtKB
Link-
362S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)HFKNCTSIS
HCCCCEEEE
3.04HPRD
Link-
413N-linked (Glc...)AWPENRTDL
ECCCCCCCC
48.34HPRD
Link-
413N-linked (GlcNAc...).AWPENRTDL
ECCCCCCCC
48.34UniProtKB
Link-
444N-linked (Glc...)VVSLNITSL
EECCCHHHH
28.17HPRD
Link-
444N-linked (GlcNAc...).VVSLNITSL
EECCCHHHH
28.17UniProtKB
Link-
470S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)NKNLCYANT
CCCCCHHHE
4.16HPRD
Link-
470S-nitrosocysteineNKNLCYANT
CCCCCHHHE
4.16dbSNO
Link-
499S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)GENSCKATG
CCCCCCCCC
5.39HPRD
Link-
506S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)TGQVCHALC
CCCCCCCCC
0.89HPRD
Link-
510S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CHALCSPEG
CCCCCCCCC
7.09HPRD
Link-
511PhosphoserineHALCSPEGC
CCCCCCCCC
27.17Phosphositeplus
Link-
515S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)SPEGCWGPE
CCCCCCCCC
3.46HPRD
Link-
523S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)EPRDCVSCR
CCCCEEEEE
2.28HPRD
Link-
526S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)DCVSCRNVS
CEEEEEEEC
1.50HPRD
Link-
528N-linked (Glc...)VSCRNVSRG
EEEEEECCC
40.21HPRD
Link-
528N-linked (GlcNAc...).VSCRNVSRG
EEEEEECCC
40.21UniProtKB
Link-
535S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)RGRECVDKC
CCCEEEEEC
4.64HPRD
Link-
539S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CVDKCNLLE
EEEECCCCC
3.62HPRD
Link-
555S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)ENSECIQCH
ECCCCCCCC
2.33HPRD
Link-
558S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)ECIQCHPEC
CCCCCCCHH
2.68HPRD
Link-
562S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CHPECLPQA
CCCHHCCCC
8.71HPRD
Link-
568N-linked (Glc...)PQAMNITCT
CCCCCCCCC
29.45HPRD
Link-
568N-linked (GlcNAc...); partial.PQAMNITCT
CCCCCCCCC
29.45UniProtKB
Link-
571S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)MNITCTGRG
CCCCCCCCC
3.17HPRD
Link-
579S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)GPDNCIQCA
CCCCCCCCC
2.72HPRD
Link-
582S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)NCIQCAHYI
CCCCCCEEE
0.97HPRD
Link-
585PhosphotyrosineQCAHYIDGP
CCCEEEECC
5.12Phosphositeplus
Link-
591S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)DGPHCVKTC
ECCEECCCC
3.65HPRD
Link-
595S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CVKTCPAGV
ECCCCCCCC
1.48HPRD
Link-
603N-linked (Glc...)VMGENNTLV
CCCCCCCCC
40.85HPRD
Link-
603N-linked (GlcNAc...); partial.VMGENNTLV
CCCCCCCCC
40.85UniProtKB
Link-
617S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)AGHVCHLCH
CCCCCCCCC
1.36HPRD
Link-
620S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)VCHLCHPNC
CCCCCCCCC
1.92HPRD
Link-
623N-linked (Glc...)LCHPNCTYG
CCCCCCCCC
13.70HPRD
Link-
624S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CHPNCTYGC
CCCCCCCCC
3.50HPRD
Link-
628S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CTYGCTGPG
CCCCCCCCC
2.54HPRD
Link-
636S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)GLEGCPTNG
CCCCCCCCC
2.47HPRD
Link-
678PhosphothreonineVRKRTLRRL
CHHHHHHHH
27.87Phosphositeplus
Link-
678Phosphothreonine (PKC_group;PKC_group;PKC_alpha;PKC_alpha)VRKRTLRRL
CHHHHHHHH
27.87PhosphoELM
Link-
678Phosphothreonine (PRKCD)VRKRTLRRL
CHHHHHHHH
27.87HPRD
Link-
678Phosphothreonine; by PKC and PKD/PRKD1.VRKRTLRRL
CHHHHHHHH
27.87UniProtKB
Link-
693PhosphothreonineVEPLTPSGE
HCCCCCCCC
26.56HPRD
Link-
693PhosphothreonineVEPLTPSGE
HCCCCCCCC
26.56HPRD
Link-
693PhosphothreonineVEPLTPSGE
HCCCCCCCC
26.56Phosphositeplus
Link-
693PhosphothreonineVEPLTPSGE
HCCCCCCCC
26.56SysPTM
Link-
693Phosphothreonine (MAPK3;MAPK1)VEPLTPSGE
HCCCCCCCC
26.56PhosphoELM
Link-
693Phosphothreonine; by PKD/PRKD1.VEPLTPSGE
HCCCCCCCC
26.56UniProtKB
Link-
695PhosphoserinePLTPSGEAP
CCCCCCCCC
43.99HPRD
Link-
695PhosphoserinePLTPSGEAP
CCCCCCCCC
43.99PhosphoELM
Link-
695PhosphoserinePLTPSGEAP
CCCCCCCCC
43.99Phosphositeplus
Link-
695PhosphoserinePLTPSGEAP
CCCCCCCCC
43.99SysPTM
Link-
695Phosphoserine.PLTPSGEAP
CCCCCCCCC
43.99UniProtKB
Link-
708Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LRILKETEF
HHCCCHHHE
61.28Phosphositeplus
Link-
713Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ETEFKKIKV
HHHEEEEEE
47.56Phosphositeplus
Link-
714Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TEFKKIKVL
HHEEEEEEE
53.75Phosphositeplus
Link-
716Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FKKIKVLGS
EEEEEEEEC
40.04Phosphositeplus
Link-
716Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FKKIKVLGS
EEEEEEEEC
40.04UbiProtDB
Link-
716Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).FKKIKVLGS
EEEEEEEEC
40.04UniProtKB
Link-
720PhosphoserineKVLGSGAFG
EEEECCCCC
23.84HPRD
Link-
725PhosphothreonineGAFGTVYKG
CCCCEEEEE
17.76HPRD
Link-
725PhosphothreonineGAFGTVYKG
CCCCEEEEE
17.76SysPTM
Link-
725Phosphothreonine.GAFGTVYKG
CCCCEEEEE
17.76UniProtKB
Link-
727PhosphotyrosineFGTVYKGLW
CCEEEEEEE
10.12HPRD
Link-
727PhosphotyrosineFGTVYKGLW
CCEEEEEEE
10.12Phosphositeplus
Link-
728Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GTVYKGLWI
CEEEEEEEC
43.10Phosphositeplus
Link-
737Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PEGEKVKIP
CCCCEEEEE
60.74Phosphositeplus
Link-
737Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PEGEKVKIP
CCCCEEEEE
60.74UbiProtDB
Link-
737Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).PEGEKVKIP
CCCCEEEEE
60.74UniProtKB
Link-
739Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GEKVKIPVA
CCEEEEEEE
52.97Phosphositeplus
Link-
752PhosphoserineREATSPKAN
CCCCCHHHH
31.30Phosphositeplus
Link-
754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ATSPKANKE
CCCHHHHHH
65.44Phosphositeplus
Link-
754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ATSPKANKE
CCCHHHHHH
65.44UbiProtDB
Link-
754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).ATSPKANKE
CCCHHHHHH
65.44UniProtKB
Link-
757Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PKANKEILD
HHHHHHHHH
51.49Phosphositeplus
Link-
764PhosphotyrosineLDEAYVMAS
HHHHHHHHH
6.68Phosphositeplus
Link-
768PhosphoserineYVMASVDNP
HHHHHCCCC
16.35Phosphositeplus
Link-
768Phosphoserine (CaM-KII_alpha)YVMASVDNP
HHHHHCCCC
16.35PhosphoELM
Link-
768Phosphoserine (CAMK2A)YVMASVDNP
HHHHHCCCC
16.35HPRD
Link-
823Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VQIAKGMNY
HHHHHHHHH
61.39Phosphositeplus
Link-
827PhosphotyrosineKGMNYLEDR
HHHHHHHHC
11.54Phosphositeplus
Link-
846Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NVLVKTPQH
CEEECCCCE
50.78Phosphositeplus
Link-
860Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FGLAKLLGA
CCEEEECCC
49.65Phosphositeplus
Link-
867Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GAEEKEYHA
CCCCCEEEE
55.89Phosphositeplus
Link-
867Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GAEEKEYHA
CCCCCEEEE
55.89UbiProtDB
Link-
867Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).GAEEKEYHA
CCCCCEEEE
55.89UniProtKB
Link-
869PhosphotyrosineEEKEYHAEG
CCCEEEEEC
19.87Phosphositeplus
Link-
869PhosphotyrosineEEKEYHAEG
CCCEEEEEC
19.87SysPTM
Link-
869Phosphotyrosine (SRC)EEKEYHAEG
CCCEEEEEC
19.87HPRD
Link-
869Phosphotyrosine (SRC)EEKEYHAEG
CCCEEEEEC
19.87PhosphoELM
Link-
869Phosphotyrosine.EEKEYHAEG
CCCEEEEEC
19.87UniProtKB
Link-
891PhosphotyrosineLHRIYTHQS
HCCCCCCHH
9.72HPRD
Link-
913Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TFGSKPYDG
HCCCCCCCC
48.23Phosphositeplus
Link-
915Phosphotyrosine (SRC)GSKPYDGIP
CCCCCCCCC
30.45HPRD
Link-
915Phosphotyrosine (SRC)GSKPYDGIP
CCCCCCCCC
30.45PhosphoELM
Link-
929Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SILEKGERL
HHHHCCCCC
63.73Phosphositeplus
Link-
929Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SILEKGERL
HHHHCCCCC
63.73UbiProtDB
Link-
929Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).SILEKGERL
HHHHCCCCC
63.73UniProtKB
Link-
944PhosphotyrosineTIDVYMIMV
CHHHHHHHH
4.16Phosphositeplus
Link-
944Phosphotyrosine (SRC)TIDVYMIMV
CHHHHHHHH
4.16HPRD
Link-
944Phosphotyrosine (SRC)TIDVYMIMV
CHHHHHHHH
4.16PhosphoELM
Link-
960Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DSRPKFREL
HHCCCHHHH
56.81Phosphositeplus
Link-
970Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IEFSKMARD
HHHHHHHHC
41.73Phosphositeplus
Link-
970Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IEFSKMARD
HHHHHHHHC
41.73UbiProtDB
Link-
970Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).IEFSKMARD
HHHHHHHHC
41.73UniProtKB
Link-
978PhosphotyrosineDPQRYLVIQ
CCHHHHCCC
10.48HPRD
Link-
978PhosphotyrosineDPQRYLVIQ
CCHHHHCCC
10.48PhosphoELM
Link-
978PhosphotyrosineDPQRYLVIQ
CCHHHHCCC
10.48Phosphositeplus
Link-
978Phosphotyrosine.DPQRYLVIQ
CCHHHHCCC
10.48UniProtKB
Link-
991PhosphoserineMHLPSPTDS
CCCCCCCCC
46.95HPRD
Link-
991PhosphoserineMHLPSPTDS
CCCCCCCCC
46.95PhosphoELM
Link-
991PhosphoserineMHLPSPTDS
CCCCCCCCC
46.95Phosphositeplus
Link-
991PhosphoserineMHLPSPTDS
CCCCCCCCC
46.95SysPTM
Link-
991Phosphoserine.MHLPSPTDS
CCCCCCCCC
46.95UniProtKB
Link-
993PhosphothreonineLPSPTDSNF
CCCCCCCCC
57.29HPRD
Link-
993PhosphothreonineLPSPTDSNF
CCCCCCCCC
57.29PhosphoELM
Link-
993PhosphothreonineLPSPTDSNF
CCCCCCCCC
57.29Phosphositeplus
Link-
993PhosphothreonineLPSPTDSNF
CCCCCCCCC
57.29SysPTM
Link-
993Phosphothreonine.LPSPTDSNF
CCCCCCCCC
57.29UniProtKB
Link-
995PhosphoserineSPTDSNFYR
CCCCCCCCC
31.17HPRD
Link-
995PhosphoserineSPTDSNFYR
CCCCCCCCC
31.17PhosphoELM
Link-
995PhosphoserineSPTDSNFYR
CCCCCCCCC
31.17Phosphositeplus
Link-
995PhosphoserineSPTDSNFYR
CCCCCCCCC
31.17SysPTM
Link-
995Phosphoserine.SPTDSNFYR
CCCCCCCCC
31.17UniProtKB
Link-
998PhosphotyrosineDSNFYRALM
CCCCCCCCC
10.14PhosphoELM
Link-
998PhosphotyrosineDSNFYRALM
CCCCCCCCC
10.14Phosphositeplus
Link-
998PhosphotyrosineDSNFYRALM
CCCCCCCCC
10.14SysPTM
Link-
998Phosphotyrosine (SRC)DSNFYRALM
CCCCCCCCC
10.14HPRD
Link-
998Phosphotyrosine; by autocatalysis.DSNFYRALM
CCCCCCCCC
10.14UniProtKB
Link-
1016DePhosphotyrosineDADEYLIPQ
CCHHHCCCC
15.52HPRD
Link-
1016PhosphotyrosineDADEYLIPQ
CCHHHCCCC
15.52HPRD
Link-
1016PhosphotyrosineDADEYLIPQ
CCHHHCCCC
15.52Phosphositeplus
Link-
1016Phosphotyrosine (EGFR)DADEYLIPQ
CCHHHCCCC
15.52HPRD
Link-
1016Phosphotyrosine (SRC)DADEYLIPQ
CCHHHCCCC
15.52PhosphoELM
Link-
1016Phosphotyrosine; by autocatalysis.DADEYLIPQ
CCHHHCCCC
15.52UniProtKB
Link-
1025PhosphoserineQGFFSSPST
CCCCCCCCC
38.79HPRD
Link-
1025PhosphoserineQGFFSSPST
CCCCCCCCC
38.79PhosphoELM
Link-
1025PhosphoserineQGFFSSPST
CCCCCCCCC
38.79Phosphositeplus
Link-
1025PhosphoserineQGFFSSPST
CCCCCCCCC
38.79SysPTM
Link-
1025Phosphoserine.QGFFSSPST
CCCCCCCCC
38.79UniProtKB
Link-
1026PhosphoserineGFFSSPSTS
CCCCCCCCC
20.08HPRD
Link-
1026PhosphoserineGFFSSPSTS
CCCCCCCCC
20.08Phosphositeplus
Link-
1026PhosphoserineGFFSSPSTS
CCCCCCCCC
20.08SysPTM
Link-
1026Phosphoserine (CDK1)GFFSSPSTS
CCCCCCCCC
20.08PhosphoELM
Link-
1026Phosphoserine.GFFSSPSTS
CCCCCCCCC
20.08UniProtKB
Link-
1028PhosphoserineFSSPSTSRT
CCCCCCCCC
40.75HPRD
Link-
1028PhosphoserineFSSPSTSRT
CCCCCCCCC
40.75PhosphoELM
Link-
1030PhosphoserineSPSTSRTPL
CCCCCCCCC
38.19Phosphositeplus
Link-
1036PhosphoserineTPLLSSLSA
CCCCCCCCC
36.59HPRD
Link-
1036PhosphoserineTPLLSSLSA
CCCCCCCCC
36.59SysPTM
Link-
1037PhosphoserinePLLSSLSAT
CCCCCCCCC
26.72HPRD
Link-
1037PhosphoserinePLLSSLSAT
CCCCCCCCC
26.72PhosphoELM
Link-
1037PhosphoserinePLLSSLSAT
CCCCCCCCC
26.72Phosphositeplus
Link-
1037PhosphoserinePLLSSLSAT
CCCCCCCCC
26.72SysPTM
Link-
1037Phosphoserine.PLLSSLSAT
CCCCCCCCC
26.72UniProtKB
Link-
1039PhosphoserineLSSLSATSN
CCCCCCCCC
31.30HPRD
Link-
1039PhosphoserineLSSLSATSN
CCCCCCCCC
31.30PhosphoELM
Link-
1039PhosphoserineLSSLSATSN
CCCCCCCCC
31.30Phosphositeplus
Link-
1039PhosphoserineLSSLSATSN
CCCCCCCCC
31.30SysPTM
Link-
1039Phosphoserine.LSSLSATSN
CCCCCCCCC
31.30UniProtKB
Link-
1041PhosphothreonineSLSATSNNS
CCCCCCCCC
28.72HPRD
Link-
1041PhosphothreonineSLSATSNNS
CCCCCCCCC
28.72PhosphoELM
Link-
1041PhosphothreonineSLSATSNNS
CCCCCCCCC
28.72Phosphositeplus
Link-
1041PhosphothreonineSLSATSNNS
CCCCCCCCC
28.72SysPTM
Link-
1041Phosphothreonine.SLSATSNNS
CCCCCCCCC
28.72UniProtKB
Link-
1042PhosphoserineLSATSNNST
CCCCCCCCC
33.46HPRD
Link-
1042PhosphoserineLSATSNNST
CCCCCCCCC
33.46PhosphoELM
Link-
1042PhosphoserineLSATSNNST
CCCCCCCCC
33.46Phosphositeplus
Link-
1042PhosphoserineLSATSNNST
CCCCCCCCC
33.46SysPTM
Link-
1042Phosphoserine.LSATSNNST
CCCCCCCCC
33.46UniProtKB
Link-
1045PhosphoserineTSNNSTVAC
CCCCCCCCC
28.63HPRD
Link-
1045PhosphoserineTSNNSTVAC
CCCCCCCCC
28.63PhosphoELM
Link-
1045PhosphoserineTSNNSTVAC
CCCCCCCCC
28.63Phosphositeplus
Link-
1045PhosphoserineTSNNSTVAC
CCCCCCCCC
28.63SysPTM
Link-
1045Phosphoserine.TSNNSTVAC
CCCCCCCCC
28.63UniProtKB
Link-
1046PhosphothreonineSNNSTVACI
CCCCCCCCC
17.78Phosphositeplus
Link-
1057PhosphoserineNGLQSCPIK
CCCCCCCCC
27.23Phosphositeplus
Link-
1064PhosphoserineIKEDSFLQR
CCCCCCCCC
29.02PhosphoELM
Link-
1064PhosphoserineIKEDSFLQR
CCCCCCCCC
29.02Phosphositeplus
Link-
1064PhosphoserineIKEDSFLQR
CCCCCCCCC
29.02SysPTM
Link-
1064Phosphoserine (CAMK2A)IKEDSFLQR
CCCCCCCCC
29.02HPRD
Link-
1064Phosphoserine.IKEDSFLQR
CCCCCCCCC
29.02UniProtKB
Link-
1069PhosphotyrosineFLQRYSSDP
CCCCCCCCC
10.28HPRD
Link-
1069PhosphotyrosineFLQRYSSDP
CCCCCCCCC
10.28PhosphoELM
Link-
1069PhosphotyrosineFLQRYSSDP
CCCCCCCCC
10.28Phosphositeplus
Link-
1069PhosphotyrosineFLQRYSSDP
CCCCCCCCC
10.28SysPTM
Link-
1069Phosphotyrosine (EGFR)FLQRYSSDP
CCCCCCCCC
10.28HPRD
Link-
1069Phosphotyrosine (ERBB2)FLQRYSSDP
CCCCCCCCC
10.28HPRD
Link-
1069Phosphotyrosine (JAK2)FLQRYSSDP
CCCCCCCCC
10.28HPRD
Link-
1069Phosphotyrosine.FLQRYSSDP
CCCCCCCCC
10.28UniProtKB
Link-
1070PhosphoserineLQRYSSDPT
CCCCCCCCC
30.38Phosphositeplus
Link-
1070Phosphoserine (CaM-KII_alpha)LQRYSSDPT
CCCCCCCCC
30.38PhosphoELM
Link-
1070Phosphoserine (CAMK2A)LQRYSSDPT
CCCCCCCCC
30.38HPRD
Link-
1070Phosphoserine (CAMK2G)LQRYSSDPT
CCCCCCCCC
30.38HPRD
Link-
1070Phosphoserine.LQRYSSDPT
CCCCCCCCC
30.38UniProtKB
Link-
1071PhosphoserineQRYSSDPTG
CCCCCCCCC
38.38Phosphositeplus
Link-
1071Phosphoserine (CaM-KII_alpha)QRYSSDPTG
CCCCCCCCC
38.38PhosphoELM
Link-
1071Phosphoserine (CAMK2A)QRYSSDPTG
CCCCCCCCC
38.38HPRD
Link-
1071Phosphoserine (CAMK2G)QRYSSDPTG
CCCCCCCCC
38.38HPRD
Link-
1071Phosphoserine.QRYSSDPTG
CCCCCCCCC
38.38UniProtKB
Link-
1074PhosphothreonineSSDPTGALT
CCCCCCCCC
39.83Phosphositeplus
Link-
1078PhosphothreonineTGALTEDSI
CCCCCCCCC
36.89HPRD
Link-
1078PhosphothreonineTGALTEDSI
CCCCCCCCC
36.89PhosphoELM
Link-
1081PhosphoserineLTEDSIDDT
CCCCCCCCC
22.99Phosphositeplus
Link-
1081PhosphoserineLTEDSIDDT
CCCCCCCCC
22.99SysPTM
Link-
1081Phosphoserine (CaM-KII_alpha)LTEDSIDDT
CCCCCCCCC
22.99PhosphoELM
Link-
1081Phosphoserine (CAMK2A)LTEDSIDDT
CCCCCCCCC
22.99HPRD
Link-
1081Phosphoserine.LTEDSIDDT
CCCCCCCCC
22.99UniProtKB
Link-
1085PhosphothreonineSIDDTFLPV
CCCCCCCCC
24.27HPRD
Link-
1085PhosphothreonineSIDDTFLPV
CCCCCCCCC
24.27PhosphoELM
Link-
1085PhosphothreonineSIDDTFLPV
CCCCCCCCC
24.27Phosphositeplus
Link-
1092PhosphotyrosinePVPEYINQS
CCCCCCCCC
10.09Phosphositeplus
Link-
1092PhosphotyrosinePVPEYINQS
CCCCCCCCC
10.09SysPTM
Link-
1092Phosphotyrosine (EGFR)PVPEYINQS
CCCCCCCCC
10.09HPRD
Link-
1092Phosphotyrosine (EGFR)PVPEYINQS
CCCCCCCCC
10.09PhosphoELM
Link-
1092Phosphotyrosine (SRC)PVPEYINQS
CCCCCCCCC
10.09HPRD
Link-
1092Phosphotyrosine; by autocatalysis.PVPEYINQS
CCCCCCCCC
10.09UniProtKB
Link-
1096PhosphoserineYINQSVPKR
CCCCCCCCC
35.58Phosphositeplus
Link-
1104PhosphoserineRPAGSVQNP
CCCCCCCCC
23.72PhosphoELM
Link-
1104PhosphoserineRPAGSVQNP
CCCCCCCCC
23.72Phosphositeplus
Link-
1110PhosphotyrosineQNPVYHNQP
CCCCCCCCC
9.05Phosphositeplus
Link-
1110PhosphotyrosineQNPVYHNQP
CCCCCCCCC
9.05SysPTM
Link-
1110Phosphotyrosine (EGFR)QNPVYHNQP
CCCCCCCCC
9.05HPRD
Link-
1110Phosphotyrosine (EGFR)QNPVYHNQP
CCCCCCCCC
9.05PhosphoELM
Link-
1110Phosphotyrosine; by autocatalysis.QNPVYHNQP
CCCCCCCCC
9.05UniProtKB
Link-
1120Phosphoserine (CAMK2A)NPAPSRDPH
CCCCCCCCE
51.96HPRD
Link-
1125PhosphotyrosineRDPHYQDPH
CCCEEECCC
21.72Phosphositeplus
Link-
1125Phosphotyrosine (SRC)RDPHYQDPH
CCCEEECCC
21.72HPRD
Link-
1125Phosphotyrosine (SRC;SRC;SRC)RDPHYQDPH
CCCEEECCC
21.72PhosphoELM
Link-
1138PhosphotyrosineGNPEYLNTV
CCHHHHHCC
13.40HPRD
Link-
1138PhosphotyrosineGNPEYLNTV
CCHHHHHCC
13.40Phosphositeplus
Link-
1138PhosphotyrosineGNPEYLNTV
CCHHHHHCC
13.40SysPTM
Link-
1138Phosphotyrosine.GNPEYLNTV
CCHHHHHCC
13.40UniProtKB
Link-
1162PhosphoserineAQKGSHQIS
CCCCCCCCC
21.18Phosphositeplus
Link-
1166PhosphoserineSHQISLDNP
CCCCCCCCC
24.09Phosphositeplus
Link-
1166PhosphoserineSHQISLDNP
CCCCCCCCC
24.09SysPTM
Link-
1166Phosphoserine (CaM-KII_alpha)SHQISLDNP
CCCCCCCCC
24.09PhosphoELM
Link-
1166Phosphoserine (CAMK2A)SHQISLDNP
CCCCCCCCC
24.09HPRD
Link-
1166Phosphoserine.SHQISLDNP
CCCCCCCCC
24.09UniProtKB
Link-
1172PhosphotyrosineDNPDYQQDF
CCCCCCCCC
14.88Phosphositeplus
Link-
1172PhosphotyrosineDNPDYQQDF
CCCCCCCCC
14.88SysPTM
Link-
1172Phosphotyrosine (EGFR)DNPDYQQDF
CCCCCCCCC
14.88HPRD
Link-
1172Phosphotyrosine (EGFR)DNPDYQQDF
CCCCCCCCC
14.88PhosphoELM
Link-
1172Phosphotyrosine; by autocatalysis.DNPDYQQDF
CCCCCCCCC
14.88UniProtKB
Link-
1179N6-acetyllysineDFFPKEAKP
CCCCCCCCC
66.21Phosphositeplus
Link-
1182N6-acetyllysinePKEAKPNGI
CCCCCCCCC
39.86Phosphositeplus
Link-
1188N6-acetyllysineNGIFKGSTA
CCCCCCCCC
50.46Phosphositeplus
Link-
1190PhosphoserineIFKGSTAEN
CCCCCCCCC
25.65PhosphoELM
Link-
1190PhosphoserineIFKGSTAEN
CCCCCCCCC
25.65Phosphositeplus
Link-
1191PhosphothreonineFKGSTAENA
CCCCCCCCC
46.81Phosphositeplus
Link-
1197DePhosphotyrosineENAEYLRVA
CCCCEECCC
9.44HPRD
Link-
1197PhosphotyrosineENAEYLRVA
CCCCEECCC
9.44Phosphositeplus
Link-
1197PhosphotyrosineENAEYLRVA
CCCCEECCC
9.44SysPTM
Link-
1197Phosphotyrosine (EGFR)ENAEYLRVA
CCCCEECCC
9.44HPRD
Link-
1197Phosphotyrosine (EGFR)ENAEYLRVA
CCCCEECCC
9.44PhosphoELM
Link-
1197Phosphotyrosine; by autocatalysis.ENAEYLRVA
CCCCEECCC
9.44UniProtKB
Link-
1199Omega-N-methylated arginine.AEYLRVAPQ
CCEECCCCC
22.96UniProtKB
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
TLR4_HUMANphysical interactionMINT-3981896MINT17126326
APBB1_HUMANphysical interactionMINT-74468MINT16273093
P85B_HUMANphysical interactionMINT-74619MINT16273093
PLS1_HUMANphysical interactionMINT-15400MINT12009895
SH21A_HUMANphysical interactionMINT-74718MINT16273093
SH3L1_HUMANphysical interactionMINT-61483MINT16729043
APBB3_HUMANphysical interactionMINT-74476MINT16273093
EGF_HUMANphysical interactionMINT-25095MINT12620237
FES_HUMANphysical interactionMINT-74535MINT16273093
RASA1_HUMANphysical interactionMINT-74694MINT16273093
RASA1_HUMANphysical interactionMINT-74695MINT16273093
RASA1_HUMANphysical interactionMINT-74696MINT16273093
RASA1_HUMANphysical interactionMINT-74710MINT16273093
RASA1_HUMANphysical interactionMINT-74711MINT16273093
ARBK1_HUMANphysical interactionMINT-51491MINT15620700
ARBK1_HUMANphysical interactionMINT-51492MINT15620700
ARBK1_HUMANphysical interactionMINT-51490MINT15620700
P85A_HUMANphysical interactionMINT-74598MINT16273093
SHC1_HUMANphysical interactionMINT-1782352MINT9544989
SHC1_HUMANphysical interactionMINT-1782377MINT9544989
SHC1_HUMANphysical interactionMINT-17353MINT8662998
SHC1_HUMANphysical interactionMINT-74727MINT16273093
SHC1_HUMANphysical interactionMINT-74729MINT16273093
SHC1_HUMANphysical interactionMINT-74730MINT16273093
SHC1_HUMANphysical interactionMINT-74731MINT16273093
SHC1_HUMANphysical interactionMINT-74732MINT16273093
SHC1_HUMANphysical interactionMINT-61482MINT16729043
SHC1_HUMANphysical interactionMINT-61489MINT16729043
SHC1_HUMANphysical interactionMINT-61495MINT16729043
SHC1_HUMANphysical interactionMINT-61501MINT16729043
SHC1_HUMANphysical interactionMINT-61503MINT16729043
IRS1_HUMANphysical interactionMINT-74551MINT16273093
ABL2_HUMANphysical interactionMINT-74437MINT16273093
ZAP70_HUMANphysical interactionMINT-74807MINT16273093
KSYK_HUMANphysical interactionMINT-74757MINT16273093
KSYK_HUMANphysical interactionMINT-74762MINT16273093
KSYK_HUMANphysical interactionMINT-74763MINT16273093
CRKL_HUMANphysical interactionMINT-61486MINT16729043
BLK_HUMANphysical interactionMINT-74484MINT16273093
STA5B_HUMANphysical interactionMINT-61490MINT16729043
BMX_HUMANphysical interactionMINT-74487MINT16273093
GRB2_HUMANphysical interactionMINT-61498MINT16729043
1433Z_HUMANphysical interactionMINT-50934MINT15225635
1433Z_HUMANphysical interactionMINT-50936MINT15225635
1433Z_HUMANphysical interactionMINT-50935MINT15225635
SHC2_HUMANphysical interactionMINT-74523MINT16273093
SHC2_HUMANphysical interactionMINT-74524MINT16273093
PTN11_HUMANphysical interactionMINT-74689MINT16273093
GRB10_HUMANphysical interactionMINT-16801MINT9506989
GRB10_HUMANphysical interactionMINT-16802MINT9506989
PTK6_HUMANphysical interactionMINT-74687MINT16273093
Q5T4P2_HUMANphysical interactionMINT-74640MINT16273093
Q5T4P2_HUMANphysical interactionMINT-74648MINT16273093
Q5T4P2_HUMANphysical interactionMINT-74658MINT16273093
Q5T4P2_HUMANphysical interactionMINT-74659MINT16273093
DOK6_HUMANphysical interactionMINT-74517MINT16273093
DOK6_HUMANphysical interactionMINT-74518MINT16273093
MIST_HUMANphysical interactionMINT-74583MINT16273093
SGSM2_HUMANphysical interactionMINT-64866MINT16169070
CKLF8_HUMANphysical interactionMINT-72809MINT16263120
CKLF8_HUMANphysical interactionMINT-72808MINT16263120
TENS4_HUMANphysical interactionMINT-74506MINT16273093
DOK4_HUMANphysical interactionMINT-74513MINT16273093
PDC6I_HUMANphysical interactionMINT-68513MINT15557335
RIN2_HUMANphysical interactionMINT-74715MINT16273093
SHC3_HUMANphysical interactionMINT-74741MINT16273093
ANKS1_HUMANphysical interactionMINT-74459MINT16273093
ANKS1_HUMANphysical interactionMINT-74460MINT16273093
APBB2_HUMANphysical interactionMINT-74474MINT16273093
Q96D37_HUMANphysical interactionMINT-74796MINT16273093
SH22A_HUMANphysical interactionMINT-74720MINT16273093
CISH_HUMANphysical interactionMINT-74491MINT16273093
SH2B3_HUMANphysical interactionMINT-74566MINT16273093
TLN1_HUMANphysical interactionMINT-74789MINT16273093
TLN1_HUMANphysical interactionMINT-74790MINT16273093
GRB2_HUMANphysical interactionDIP:85EDIP1322798
TGFA_HUMANphysical interaction
physical interaction
DIP:9950EDIP10775655
8663070
AREG_HUMANphysical interaction
physical interaction
DIP:9951EDIP10085134
8663535
EGF_HUMANdirect interaction
direct interaction
DIP:58935EDIP17697999
17697999
4F2_HUMANphysical interaction
physical interaction
physical interaction
EBI-1188138
EBI-1188189
EBI-7
intact16799092
16799092
15657067
LYN_HUMANphysical interaction
physical interaction
EBI-1188138
EBI-1188189
intact16799092
16799092
CAV1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
EBI-1188138
EBI-1188189
EBI-7
intact16799092
16799092
15657067
15657067
AT1A1_HUMANphysical interactionEBI-1188138
intact16799092
S10A9_HUMANphysical interaction
physical interaction
EBI-1188138
EBI-1188189
intact16799092
16799092
GRB2_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical int
EBI-1188138
EBI-1188189
EBI-7
intact16799092
16799092
15657067
15657067
12577067
12577067
14679214
8887653
SEC13_HUMANphysical interactionEBI-1188138
intact16799092
ICAM1_HUMANphysical interactionEBI-1188138
intact16799092
CAV2_HUMANphysical interactionEBI-1188138
intact16799092
HXC10_HUMANphysical interactionEBI-1188138
intact16799092
G3P_HUMANphysical interaction
physical interaction
EBI-1188138
EBI-1188189
intact16799092
16799092
CD166_HUMANphysical interactionEBI-1188138
intact16799092
CLH2_HUMANphysical interactionEBI-1188138
intact16799092
TBA4A_HUMANphysical interactionEBI-1188138
intact16799092
AT1B1_HUMANphysical interactionEBI-1188138
intact16799092
CLCA_HUMANphysical interaction
physical interaction
EBI-1188138
EBI-1188189
intact16799092
16799092
1433S_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
EBI-1188138
EBI-1188189
EBI-7
intact16799092
16799092
15657067
15657067
P3C2A_HUMANphysical interactionEBI-641139
intact10805725
TBB5_HUMANphysical interactionEBI-702075
intact15657067
BCAR1_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
XPO2_HUMANphysical interactionEBI-702075
intact15657067
MPCP_HUMANphysical interactionEBI-702075
intact15657067
DNJA2_HUMANphysical interactionEBI-702075
intact15657067
HSP71_HUMANphysical interactionEBI-702075
intact15657067
UBIQ_HUMANphysical interactionEBI-702075
intact15657067
EPHB4_HUMANphysical interactionEBI-702075
intact15657067
XPOT_HUMANphysical interactionEBI-702075
intact15657067
ATPB_HUMANphysical interactionEBI-702075
intact15657067
TBRG4_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
BCAR3_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
ACK1_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
CDCP1_HUMANphysical interactionEBI-702075
intact15657067
LRC59_HUMANphysical interactionEBI-702075
intact15657067
TRI29_HUMANphysical interactionEBI-702075
intact15657067
ATX10_HUMANphysical interactionEBI-702075
intact15657067
CKAP4_HUMANphysical interactionEBI-702075
intact15657067
YES_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
S10AB_HUMANphysical interactionEBI-702075
intact15657067
ERBB2_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical int
EBI-702075
EBI-702413
EBI-875
intact15657067
15657067
10572067
16843263
16843263
16843263
16843263
16843263
FHL2_HUMANphysical interactionEBI-702075
intact15657067
1433T_HUMANphysical interactionEBI-702075
intact15657067
SHC1_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
CTND1_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
1433E_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
HSPB1_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702075
intact15657067
15657067
STAT3_HUMANphysical interactionEBI-702075
intact15657067
CTNA1_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
AT2A2_HUMANphysical interactionEBI-702075
intact15657067
1433Z_HUMANphysical interaction
physical interaction
physical interaction
colocalization
EBI-702075
EBI-702413
EBI-446
intact15657067
15657067
15225635
15225635
CDC2_HUMANphysical interactionEBI-702075
intact15657067
CBLB_HUMANphysical interactionEBI-702075
intact15657067
EFNB1_HUMANphysical interactionEBI-702075
intact15657067
IMB1_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
K2C1_HUMANphysical interactionEBI-702075
intact15657067
HNRPF_HUMANphysical interactionEBI-702075
intact15657067
H2B1C_HUMANphysical interactionEBI-702075
intact15657067
PAXI_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
THIO_HUMANphysical interactionEBI-702075
intact15657067
K2C6A_HUMANphysical interactionEBI-702075
intact15657067
TBA1A_HUMANphysical interactionEBI-702075
intact15657067
FAK1_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
HNRPK_HUMANphysical interactionEBI-702075
intact15657067
PEX19_HUMANphysical interactionEBI-702075
intact15657067
DNJA3_HUMANphysical interactionEBI-702075
intact15657067
EI2BG_HUMANphysical interactionEBI-702075
intact15657067
EPHA2_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
FAK2_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
HSP7C_HUMANphysical interactionEBI-702075
intact15657067
HNRH1_HUMANphysical interactionEBI-702075
intact15657067
H14_HUMANphysical interactionEBI-702075
intact15657067
CBL_HUMANphysical interaction
direct interaction
direct interaction
EBI-702075
EBI-678899
EBI-641
intact15657067
7657591
7657591
ADT2_HUMANphysical interactionEBI-702075
intact15657067
K2C5_HUMANphysical interactionEBI-702075
intact15657067
GRP78_HUMANphysical interactionEBI-702075
intact15657067
K1C17_HUMANphysical interactionEBI-702075
intact15657067
GRP75_HUMANphysical interactionEBI-702075
intact15657067
PKP2_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
HS90B_HUMANphysical interactionEBI-702075
intact15657067
EF1A1_HUMANphysical interaction
physical interaction
EBI-702075
EBI-702413
intact15657067
15657067
DNJA1_HUMANphysical interactionEBI-702075
intact15657067
CH60_HUMANphysical interactionEBI-702075
intact15657067
K1C14_HUMANphysical interactionEBI-702075
intact15657067
ERBB4_HUMANphysical interaction
physical interaction
EBI-875497
EBI-875456
intact10572067
10572067
ERBB3_HUMANphysical interaction
physical interaction
EBI-875494
EBI-875451
intact10572067
10572067
EP15_HUMANphysical interactionEBI-921718
intact16499958
ACTS_HUMANin vitro
in vivo
HPRD:00579HPRD1808202
1383230
AREG_HUMANin vivoHPRD:00579HPRD10085134
GRB2_HUMANin vitro
in vivo
HPRD:00579HPRD1322798
7527043
8662998
12577067
14679214
8887653
11726515
8810325
CD44_HUMANin vivoHPRD:00579HPRD12093135
CALM_HUMANin vitro
in vivo
HPRD:00579HPRD12153558
CTNB1_HUMANin vivoHPRD:00579HPRD9233779
MPIP1_HUMANin vitro
in vivo
HPRD:00579HPRD11912208
EZRI_HUMANin vitro
in vivo
HPRD:00579HPRD1382070
12560083
HBEGF_HUMANin vivoHPRD:00579HPRD12725245
EGF_HUMANin vitroHPRD:00579HPRD12093292
12620237
10788520
16274239
41_HUMANin vitro
in vivo
HPRD:00579HPRD1647028
PGS2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:00579HPRD12105206
9988678
EGFR_HUMANin vitro
in vivo
HPRD:00579HPRD11279102
12397069
12009895
8940083
11114724
8845374
11983694
9363897
10635327
16274239
RASA1_HUMANin vitro
in vivo
HPRD:00579HPRD1633149
1850098
MUC1_HUMANin vitro
in vivo
HPRD:00579HPRD11483589
11278868
CRK_HUMANin vitro
in vivo
HPRD:00579HPRD9642287
12198159
11956190
8875975
9480911
ERBB2_HUMANin vitro
in vivo
HPRD:00579HPRD11500850
12354693
1706616
11500516
CBL_HUMANin vivoHPRD:00579HPRD8662998
11994282
11239464
9890970
10092522
10799548
PLCG1_HUMANin vitro
in vivo
HPRD:00579HPRD9207933
8885868
8657103
1689310
7682059
15144186
12601080
PTN1_HUMANin vitro
in vivo
HPRD:00579HPRD8621392
7540771
10889023
12573287
11506178
9355745
VAV2_HUMANin vitro
in vivo
HPRD:00579HPRD10618391
10938113
12454019
11516622
STAT1_HUMANin vitro
in vivo
HPRD:00579HPRD12070153
7657660
11294897
10918587
15322115
7543024
11839738
12817007
7690989
12637327
PLD2_HUMANin vitro
in vivo
HPRD:00579HPRD9837959
RGS16_HUMANin vitro
in vivo
HPRD:00579HPRD11602604
12588871
STA5B_HUMANin vitro
in vivo
HPRD:00579HPRD10558875
11751923
HGS_HUMANin vitroHPRD:00579HPRD12953068
GAB1_HUMANin vitro
in vivo
HPRD:00579HPRD11432805
10734310
IPKA_HUMANin vitroHPRD:00579HPRD2434500
STAM2_HUMANin vitro
in vivo
HPRD:00579HPRD11687594
10993906
SCAM1_HUMANin vivoHPRD:00579HPRD9658162
SCAM3_HUMANin vitro
in vivo
HPRD:00579HPRD9658162
15144186
EP15_HUMANin vitro
in vivo
HPRD:00579HPRD9049247
10953014
MET_HUMANin vitro
in vivo
HPRD:00579HPRD10722725
ERBB4_HUMANin vitroHPRD:00579HPRD10572067
PAK1_HUMANin vitro
in vivo
HPRD:00579HPRD12522133
CTND1_HUMANin vitro
in vivo
HPRD:00579HPRD14996911
P85B_HUMANin vivoHPRD:00579HPRD11172806
STAT3_HUMANin vitroHPRD:00579HPRD12873986
TNR6_HUMANin vitro
in vivo
HPRD:00579HPRD12586732
MP2K1_HUMANin vitro
in vivo
HPRD:00579HPRD12556561
EPHA2_HUMANin vivoHPRD:00579HPRD15657067
MK01_HUMANin vitro
in vivo
HPRD:00579HPRD12556561
ANDR_HUMANin vivoHPRD:00579HPRD12534934
PLD1_HUMANin vivoHPRD:00579HPRD11459228
H31T_HUMANin vitro
in vivo
HPRD:00579HPRD12577067
KPCD1_HUMANin vivoHPRD:00579HPRD10523301
2984676
2987962
CAV2_HUMANin vivoHPRD:00579HPRD16799092
CLCA_HUMANin vivoHPRD:00579HPRD16799092
CLH2_HUMANin vivoHPRD:00579HPRD16799092
HXC10_HUMANin vivoHPRD:00579HPRD16799092
LYN_HUMANin vivoHPRD:00579HPRD16799092
S10A7_HUMANin vivoHPRD:00579HPRD16799092
S10A9_HUMANin vivoHPRD:00579HPRD16799092
SEC13_HUMANin vivoHPRD:00579HPRD16799092
G3P_HUMANin vivoHPRD:00579HPRD16799092
1433S_HUMANin vivoHPRD:00579HPRD16799092
4F2_HUMANin vivoHPRD:00579HPRD16799092
AT1A1_HUMANin vivoHPRD:00579HPRD16799092
AT1B1_HUMANin vivoHPRD:00579HPRD16799092
ICAM1_HUMANin vivoHPRD:00579HPRD16799092
TBA4A_HUMANin vivoHPRD:00579HPRD16799092
CD166_HUMANin vivoHPRD:00579HPRD16799092
CAV1_HUMANin vitro
in vivo
HPRD:00579HPRD9374534
16799092
PGS2_HUMANENSP00000275493STRING
ESR1_HUMANENSP00000275493STRING
MK01_HUMANENSP00000275493STRING
TGFB1_HUMANENSP00000275493STRING
P85B_HUMANENSP00000275493STRING
ZPR1_HUMANENSP00000275493STRING
HBEGF_HUMANENSP00000275493STRING
NCK2_HUMANENSP00000275493STRING
EGR1_HUMANENSP00000275493STRING
EREG_HUMANENSP00000275493STRING
INS_HUMANENSP00000275493STRING
INS_HUMANENSP00000275493STRING
IL6_HUMANENSP00000275493STRING
CADH1_HUMANENSP00000275493STRING
MK03_HUMANENSP00000275493STRING
CBL_HUMANENSP00000275493STRING
CBLB_HUMANENSP00000275493STRING
CBLB_HUMANENSP00000275493STRING
AREG_HUMANENSP00000275493STRING
STAT3_HUMANENSP00000275493STRING
TENA_HUMANENSP00000275493STRING
EGF_HUMANENSP00000275493STRING
ERBB3_HUMANENSP00000275493STRING
P53_HUMANENSP00000275493STRING
ERBB2_HUMANENSP00000275493STRING
CALM_HUMANENSP00000275493STRING
RAB5A_HUMANENSP00000275493STRING
LRIG1_HUMANENSP00000275493STRING
AGTR1_HUMANENSP00000275493STRING
P85A_HUMANENSP00000275493STRING
RASA1_HUMANENSP00000275493STRING
CD44_HUMANENSP00000275493STRING
EPS8_HUMANENSP00000275493STRING
NCK1_HUMANENSP00000275493STRING
K2C8_HUMANENSP00000275493STRING
K2C8_HUMANENSP00000275493STRING
STA5B_HUMANENSP00000275493STRING
TGFA_HUMANENSP00000275493STRING
CRK_HUMANENSP00000275493STRING
CRK_HUMANENSP00000275493STRING
MP2K1_HUMANENSP00000275493STRING
IGF1B_HUMANENSP00000275493STRING
MPIP1_HUMANENSP00000275493STRING
IRS1_HUMANENSP00000275493STRING
FOS_HUMANENSP00000275493STRING
IL8_HUMANENSP00000275493STRING
TEAD2_HUMANENSP00000275493STRING
GRB7_HUMANENSP00000275493STRING
BTC_HUMANENSP00000275493STRING
ARBK1_HUMANENSP00000275493STRING
VEGFA_HUMANENSP00000275493STRING
APOA_HUMANENSP00000275493STRING
SP1_HUMANENSP00000275493STRING
ACK1_HUMANENSP00000275493STRING
SOCS2_HUMANENSP00000275493STRING
FAK1_HUMANENSP00000275493STRING
CTNB1_HUMANENSP00000275493STRING
PLS1_HUMANENSP00000275493STRING
TNR6_HUMANENSP00000275493STRING
MK08_HUMANENSP00000275493STRING
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Disease Reference
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
211980Lung cancer (LNCR)
616069Inflammatory skin and bowel disease, neonatal, 2 (NISBD2)
Drug Reference
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)
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"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
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
"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.
"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.
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
Ubiquitylation
ReferencePubMed
"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.
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