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Protein

Epidermal growth factor receptor

Gene

EGFR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:2790960, PubMed:10805725, PubMed:27153536). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF (PubMed:2790960, PubMed:7679104, PubMed:8144591, PubMed:9419975, PubMed:15611079, PubMed:12297049, PubMed:27153536, PubMed:20837704). 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 (PubMed:27153536). May also activate the NF-kappa-B signaling cascade (PubMed:11116146). 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 (PubMed:11602604). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589). Plays a role in enhancing learning and memory performance (By similarity).By similarity20 Publications
Isoform 2 may act as an antagonist of EGF action.
(Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins.1 Publication

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation6 Publications

Activity regulationi

Endocytosis and inhibition of the activated EGFR by phosphatases like PTPRJ and PTPRK constitute immediate regulatory mechanisms. Upon EGF-binding phosphorylates EPS15 that regulates EGFR endocytosis and activity. Moreover, inducible feedback inhibitors including LRIG1, SOCS4, SOCS5 and ERRFI1 constitute alternative regulatory mechanisms for the EGFR signaling.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei745ATPCombined sources2 Publications1
Active sitei837Proton acceptorPROSITE-ProRule annotation1
Binding sitei855ATPCombined sources2 Publications1
Sitei1016Important for interaction with PIK3C2B1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi718 – 726ATPCombined sources1 Publication9
Nucleotide bindingi790 – 791ATPCombined sources2 Publications2

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein, Host cell receptor for virus entry, Kinase, Receptor, Transferase, Tyrosine-protein kinase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1 2681
ReactomeiR-HSA-1227986 Signaling by ERBB2
R-HSA-1236382 Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants
R-HSA-1236394 Signaling by ERBB4
R-HSA-1250196 SHC1 events in ERBB2 signaling
R-HSA-1251932 PLCG1 events in ERBB2 signaling
R-HSA-1257604 PIP3 activates AKT signaling
R-HSA-177929 Signaling by EGFR
R-HSA-179812 GRB2 events in EGFR signaling
R-HSA-180292 GAB1 signalosome
R-HSA-180336 SHC1 events in EGFR signaling
R-HSA-182971 EGFR downregulation
R-HSA-1963640 GRB2 events in ERBB2 signaling
R-HSA-1963642 PI3K events in ERBB2 signaling
R-HSA-212718 EGFR interacts with phospholipase C-gamma
R-HSA-2179392 EGFR Transactivation by Gastrin
R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-445144 Signal transduction by L1
R-HSA-5637810 Constitutive Signaling by EGFRvIII
R-HSA-5638303 Inhibition of Signaling by Overexpressed EGFR
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6785631 ERBB2 Regulates Cell Motility
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-8847993 ERBB2 Activates PTK6 Signaling
R-HSA-8856825 Cargo recognition for clathrin-mediated endocytosis
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-8857538 PTK6 promotes HIF1A stabilization
R-HSA-8863795 Downregulation of ERBB2 signaling
R-HSA-8866910 TFAP2 (AP-2) family regulates transcription of growth factors and their receptors
R-HSA-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus
SignaLinkiP00533
SIGNORiP00533

Protein family/group databases

MoonDBiP00533 Predicted

Names & Taxonomyi

Protein namesi
Recommended name:
Epidermal growth factor receptor (EC:2.7.10.1)
Alternative name(s):
Proto-oncogene c-ErbB-1
Receptor tyrosine-protein kinase erbB-1
Gene namesi
Name:EGFR
Synonyms:ERBB, ERBB1, HER1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000146648.15
HGNCiHGNC:3236 EGFR
MIMi131550 gene
neXtProtiNX_P00533

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini25 – 645ExtracellularSequence analysisAdd BLAST621
Transmembranei646 – 668HelicalSequence analysisAdd BLAST23
Topological domaini669 – 1210CytoplasmicSequence analysisAdd BLAST542

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, Nucleus, Secreted

Pathology & Biotechi

Involvement in diseasei

Lung cancer (LNCR)3 Publications
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionA common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis.
See also OMIM:211980
Inflammatory skin and bowel disease, neonatal, 2 (NISBD2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by inflammatory features with neonatal onset, involving the skin, hair, and gut. The skin lesions involve perioral and perianal erythema, psoriasiform erythroderma, with flares of erythema, scaling, and widespread pustules. Gastrointestinal symptoms include malabsorptive diarrhea that is exacerbated by intercurrent gastrointestinal infections. The hair is short or broken, and the eyelashes and eyebrows are wiry and disorganized.
See also OMIM:616069
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072435428G → D in NISBD2; loss of function; the mutant does not localize to the cell membrane; has diffuse cytoplasmic localization. 1 PublicationCorresponds to variant dbSNP:rs606231253EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi275Y → A: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309. 1 Publication1
Mutagenesisi287F → A: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309. 1 Publication1
Mutagenesisi309R → S: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-275. Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-287. 1 Publication1
Mutagenesisi429R → E: Abolishes autophosphorylation and activation of downstream kinases. 1 Publication1
Mutagenesisi587 – 590DGPH → AGPA: Decreases intramolecular interactions and facilitates EGF binding. 1 Publication4
Mutagenesisi609K → A: Decreases intramolecular interactions and facilitates EGF binding. 1 Publication1
Mutagenesisi688L → A: Strongly reduced phosphorylation. 2 Publications1
Mutagenesisi689V → A: Reduced autophosphorylation. 1 Publication1
Mutagenesisi689V → M: Constitutively activated kinase. 1 Publication1
Mutagenesisi690E → A: Reduced phosphorylation. 2 Publications1
Mutagenesisi692L → A or P: Strongly reduced phosphorylation. 2 Publications1
Mutagenesisi693T → A: Increased phosphorylation. 1 Publication1
Mutagenesisi693T → D: Strongly reduced phosphorylation. 1 Publication1
Mutagenesisi694P → A: Strongly reduced phosphorylation. 1 Publication1
Mutagenesisi699P → A: Reduced phosphorylation. 1 Publication1
Mutagenesisi700N → A: Abolishes phosphorylation. 1 Publication1
Mutagenesisi704L → A: Abolishes phosphorylation. 1 Publication1
Mutagenesisi705R → A: Abolishes phosphorylation. 1 Publication1
Mutagenesisi706I → A: Abolishes phosphorylation. 1 Publication1
Mutagenesisi745K → A or M: Abolishes kinase activity. 1 Publication1
Mutagenesisi974D → A: Strongly reduced phosphorylation. 1
Mutagenesisi977R → A: Reduced phosphorylation. 1 Publication1
Mutagenesisi1005 – 1006ED → RK: Constitutively activated kinase. 1 Publication2
Mutagenesisi1016Y → F: 50% decrease in interaction with PIK3C2B. 65% decrease in interaction with PIK3C2B; when associated with F-1197. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1092. 1 Publication1
Mutagenesisi1048 – 1210Missing : Abolishes palmitoylation. 1 PublicationAdd BLAST163
Mutagenesisi1049C → A: Decreased palmitoylation. 1 Publication1
Mutagenesisi1067Q → G: No effect on interaction with CBLC. 1 Publication1
Mutagenesisi1068R → G: Strongly decreases interaction with CBLC. 1 Publication1
Mutagenesisi1069Y → F: Abolishes interaction with CBLC. 1 Publication1
Mutagenesisi1092Y → F: No change in interaction with PIK3C2B. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1016. 1 Publication1
Mutagenesisi1110Y → F: No change in interaction with PIK3C2B. 1 Publication1
Mutagenesisi1146C → A: Decreased palmitoylation. 1 Publication1
Mutagenesisi1172Y → F: No change in interaction with PIK3C2B. 1 Publication1
Mutagenesisi1197Y → F: No change in interaction with PIK3C2B. 65% decrease in interaction with PIK3C2B; when associated with F-1016. Abolishes interaction with PIK3C2B; when associated with F-1092 and F-1016. 1 Publication1

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNETi1956
MalaCardsiEGFR
MIMi211980 phenotype
616069 phenotype
OpenTargetsiENSG00000146648
Orphaneti251579 Giant cell glioblastoma
251576 Gliosarcoma
294023 Neonatal inflammatory skin and bowel disease
357191 Selection of therapeutic option in non-small cell lung carcinoma
PharmGKBiPA7360

Chemistry databases

ChEMBLiCHEMBL203
DrugBankiDB08916 Afatinib
DB00002 Cetuximab
DB05424 CI-1033
DB00530 Erlotinib
DB03496 Flavopiridol
DB00317 Gefitinib
DB05324 HuMax-EGFr
DB11737 Icotinib
DB04988 IGN311
DB05774 IMC-11F8
DB05900 INSM-18
DB01259 Lapatinib
DB00281 Lidocaine
DB05101 Matuzumab
DB07662 N-[4-(3-BROMO-PHENYLAMINO)-QUINAZOLIN-6-YL]-ACRYLAMIDE
DB09559 Necitumumab
DB13164 Olmutinib
DB09330 Osimertinib
DB01269 Panitumumab
DB05374 Rindopepimut
DB07602 S-{3-[(4-ANILINOQUINAZOLIN-6-YL)AMINO]-3-OXOPROPYL}-L-CYSTEINE
DB00072 Trastuzumab
DB05294 Vandetanib
GuidetoPHARMACOLOGYi1797

Polymorphism and mutation databases

BioMutaiEGFR
DMDMi2811086

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 243 PublicationsAdd BLAST24
ChainiPRO_000001666525 – 1210Epidermal growth factor receptorAdd BLAST1186

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi31 ↔ 58Combined sources3 Publications
GlycosylationiCAR_00022756N-linked (GlcNAc...) (complex) asparagine; atypical; partialCombined sources6 Publications1
Glycosylationi73N-linked (GlcNAc...) asparagine; atypicalCombined sources1 Publication1
Glycosylationi128N-linked (GlcNAc...) asparagine3 Publications1
Disulfide bondi157 ↔ 187Combined sources5 Publications
Glycosylationi175N-linked (GlcNAc...) asparagineCombined sources5 Publications1
Disulfide bondi190 ↔ 199Combined sources5 Publications
Disulfide bondi194 ↔ 207Combined sources5 Publications
Glycosylationi196N-linked (GlcNAc...) asparagineCombined sources5 Publications1
Disulfide bondi215 ↔ 223Combined sources5 Publications
Disulfide bondi219 ↔ 231Combined sources5 Publications
Modified residuei229Phosphoserine1 Publication1
Disulfide bondi232 ↔ 240Combined sources5 Publications
Disulfide bondi236 ↔ 248Combined sources5 Publications
Disulfide bondi251 ↔ 260Combined sources5 Publications
Disulfide bondi264 ↔ 291Combined sources5 Publications
Disulfide bondi295 ↔ 307Combined sources
Disulfide bondi311 ↔ 326Combined sources5 Publications
Disulfide bondi329 ↔ 333Combined sources
Disulfide bondi337 ↔ 362Combined sources5 Publications
Glycosylationi352N-linked (GlcNAc...) asparagineCombined sources8 Publications1
Glycosylationi361N-linked (GlcNAc...) asparagineCombined sources6 Publications1
Glycosylationi413N-linked (GlcNAc...) asparagineCombined sources4 Publications1
Glycosylationi444N-linked (GlcNAc...) asparagineCombined sources6 Publications1
Disulfide bondi470 ↔ 499Combined sources
Disulfide bondi506 ↔ 515Combined sources5 Publications
Disulfide bondi510 ↔ 523Combined sources5 Publications
Disulfide bondi526 ↔ 535Combined sources4 Publications
Glycosylationi528N-linked (GlcNAc...) asparagineCombined sources5 Publications1
Disulfide bondi539 ↔ 555Combined sources3 Publications
Disulfide bondi558 ↔ 571Combined sources3 Publications
Disulfide bondi562 ↔ 579Combined sources3 Publications
Glycosylationi568N-linked (GlcNAc...) asparagine; partialCombined sources5 Publications1
Disulfide bondi582 ↔ 591Combined sources3 Publications
Disulfide bondi595 ↔ 617Combined sources3 Publications
Glycosylationi603N-linked (GlcNAc...) asparagine; partialCombined sources4 Publications1
Disulfide bondi620 ↔ 628Combined sources3 Publications
Glycosylationi623N-linked (GlcNAc...) (high mannose) asparagine1 Publication1
Disulfide bondi624 ↔ 636Combined sources3 Publications
Modified residuei678Phosphothreonine; by PKC and PKD/PRKD11 Publication1
Modified residuei693Phosphothreonine; by PKD/PRKD1Combined sources3 Publications1
Modified residuei695PhosphoserineCombined sources1 Publication1
Cross-linki716Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki737Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki867Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki929Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki970Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei991PhosphoserineCombined sources1 Publication1
Modified residuei995PhosphoserineCombined sources1
Modified residuei998Phosphotyrosine; by autocatalysisCombined sources1 Publication1
Modified residuei1016Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1026PhosphoserineCombined sources1 Publication1
Modified residuei1039PhosphoserineCombined sources1
Modified residuei1041PhosphothreonineCombined sources1
Modified residuei1042PhosphoserineCombined sources1
Lipidationi1049S-palmitoyl cysteine1 Publication1
Modified residuei1064PhosphoserineCombined sources1
Modified residuei1069Phosphotyrosine1 Publication1
Modified residuei1070Phosphoserine1 Publication1
Modified residuei1071Phosphoserine1 Publication1
Modified residuei1081PhosphoserineCombined sources1
Modified residuei1092Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei1110Phosphotyrosine; by autocatalysis2 Publications1
Lipidationi1146S-palmitoyl cysteine1 Publication1
Modified residuei1166PhosphoserineCombined sources1
Modified residuei1172Phosphotyrosine; by autocatalysisCombined sources1 Publication1
Modified residuei1197Phosphotyrosine; by autocatalysisCombined sources3 Publications1
Modified residuei1199Omega-N-methylarginine1 Publication1

Post-translational modificationi

Phosphorylated on Tyr residues in response to EGF (PubMed:27153536). Phosphorylation at Ser-695 is partial and occurs only if Thr-693 is phosphorylated. Phosphorylation at Thr-678 and Thr-693 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation. Dephosphorylation by PTPRJ prevents endocytosis and stabilizes the receptor at the plasma membrane. Autophosphorylation at Tyr-1197 is stimulated by methylation at Arg-1199 and enhances interaction with PTPN6. Autophosphorylation at Tyr-1092 and/or Tyr-1110 recruits STAT3. Dephosphorylated by PTPN1 and PTPN2.9 Publications
Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting (PubMed:27153536). Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs. Deubiquitination by OTUD7B prevents degradation. Ubiquitinated by RNF115 and RNF126 (By similarity).By similarity4 Publications
Palmitoylated on Cys residues by ZDHHC20. Palmitoylation inhibits internalization after ligand binding, and increases the persistence of tyrosine-phosphorylated EGFR at the cell membrane. Palmitoylation increases the amplitude and duration of EGFR signaling.1 Publication
Methylated. Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Lipoprotein, Methylation, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP00533
MaxQBiP00533
PaxDbiP00533
PeptideAtlasiP00533
PRIDEiP00533
ProteomicsDBi51261
51262 [P00533-2]
51263 [P00533-3]
51264 [P00533-4]

2D gel databases

SWISS-2DPAGEiP00533

PTM databases

GlyConnecti137
iPTMnetiP00533
PhosphoSitePlusiP00533
SwissPalmiP00533
UniCarbKBiP00533

Miscellaneous databases

PMAP-CutDBiP00533

Expressioni

Tissue specificityi

Ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers.1 Publication

Gene expression databases

BgeeiENSG00000146648 Expressed in 234 organ(s), highest expression level in placenta
ExpressionAtlasiP00533 baseline and differential
GenevisibleiP00533 HS

Organism-specific databases

HPAiCAB000035
CAB068186
CAB073534
HPA001200
HPA018530

Interactioni

Subunit structurei

Binding of the ligand triggers homo- and/or heterodimerization of the receptor triggering its autophosphorylation. Heterodimer with ERBB2 (PubMed:10805725). Interacts with ERRFI1; inhibits dimerization of the kinase domain and autophosphorylation (PubMed:18046415). Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B (PubMed:10805725). Interacts with GRB2; an adapter protein coupling the receptor to downstream signaling pathways. Interacts with GAB2; involved in signaling downstream of EGFR. Interacts with STAT3; mediates EGFR downstream signaling in cell proliferation. Interacts with RIPK1; involved in NF-kappa-B activation. Interacts (autophosphorylated) with CBL, CBLB and CBLC; involved in EGFR ubiquitination and regulation. Interacts with SOCS5; regulates EGFR degradation through ELOC- and ELOB-mediated ubiquitination and proteasomal degradation. Interacts with PRMT5; methylates EGFR and enhances interaction with PTPN6. Interacts (phosphorylated) with PTPN6; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with COPG1; essential for regulation of EGF-dependent nuclear transport of EGFR by retrograde trafficking from the Golgi to the ER. Interacts with TNK2; this interaction is dependent on EGF stimulation and kinase activity of EGFR. Interacts with PCNA; positively regulates PCNA (PubMed:17115032). Interacts with PELP1. Interacts with MUC1. Interacts with AP2M1. Interacts with FER. May interact with EPS8; mediates EPS8 phosphorylation. Interacts (via SH2 domains) with GRB2, NCK1 and NCK2 (PubMed:10026169). Interacts with ATX2. Interacts with GAREM1. Interacts (ubiquitinated) with ANKRD13A/B/D; the interaction is direct and may regulate EGFR internalization after EGF stimulation. Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Interacts (via C-terminal cytoplasmic kinase domain) with ZPR1 (via zinc fingers). Interacts with RNF115 and RNF126 (PubMed:23418353). Interacts with GPRC5A (via its transmembrane domain) (PubMed:25311788). Interacts with FAM83B; positively regulates EGFR inducing its autophosphorylation in absence of stimulation by EGF (PubMed:23912460). Interacts with LAPTM4B; positively correlates with EGFR activation (PubMed:28479384). Interacts with STX19 (PubMed:16420529).40 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself26EBI-297353,EBI-297353
Q53FC73EBI-297353,EBI-9356749
Q96BE02EBI-297353,EBI-9356686
ABL1P005192EBI-297353,EBI-375543
ABL2P426848EBI-297353,EBI-1102694
AGERQ151092EBI-297353,EBI-1646426
AGO2Q9UKV811EBI-297353,EBI-528269
AHNAKQ096663EBI-297353,EBI-2555881
AKAP12Q029522EBI-297353,EBI-2562430
ANKS1AQ926255EBI-297353,EBI-1048612
AP2M1Q96CW14EBI-297353,EBI-297683
APBB1O002134EBI-297353,EBI-81694
APBB2Q928706EBI-297353,EBI-79277
APBB3O957042EBI-297353,EBI-286427
APPL1Q9UKG12EBI-297353,EBI-741243
AURKAO149654EBI-297353,EBI-448680
AXLP305304EBI-297353,EBI-2850927
BECN1Q144577EBI-297353,EBI-949378
BLKP514512EBI-297353,EBI-2105445
CALM3P621584EBI-297353,EBI-397435
Calm3P621616EBI-297353,EBI-397530From a different organism.
CAMLGP490692EBI-297353,EBI-1748958
CAV1Q031356EBI-297353,EBI-603614
CBLP2268122EBI-297353,EBI-518228
CblP226822EBI-297353,EBI-640919From Mus musculus.
CDC37Q165439EBI-297353,EBI-295634
CDH1P128303EBI-297353,EBI-727477
CHIAQ9BZP62EBI-297353,EBI-14357960
CISHQ9NSE23EBI-297353,EBI-617866
CLNKQ7Z7G12EBI-297353,EBI-7878194
CRKP461083EBI-297353,EBI-886
CRKP46108-13EBI-297353,EBI-287556
CRKLP461093EBI-297353,EBI-910
CTNNA1P352214EBI-297353,EBI-701918
CTNND1O607164EBI-297353,EBI-701927
CTTNQ142473EBI-297353,EBI-351886
DOK6Q6PKX42EBI-297353,EBI-2880244
EGFP0113321EBI-297353,EBI-640857
EPS8Q129292EBI-297353,EBI-375576
ERBB2P0462625EBI-297353,EBI-641062
ERBB3P2186013EBI-297353,EBI-720706
ERBB4Q153032EBI-297353,EBI-80371
ERCC1P0799221EBI-297353,EBI-750962
ERRFI1Q9UJM313EBI-297353,EBI-2941912
ESR1P033722EBI-297353,EBI-78473
ESR1P03372-44EBI-297353,EBI-4309277
EXOC4Q96A652EBI-297353,EBI-355383
FGRP097692EBI-297353,EBI-1383732
FKBP8Q143183EBI-297353,EBI-724839
GAB1Q134803EBI-297353,EBI-517684
GABARAPL2P605202EBI-297353,EBI-720116
GAPDHP044066EBI-297353,EBI-354056
GOLM1Q8NBJ413EBI-297353,EBI-712073
GPNMBQ149563EBI-297353,EBI-7250369
GPNMBQ14956-12EBI-297353,EBI-16191078
GRAP2O757912EBI-297353,EBI-740418
GRB2P6299336EBI-297353,EBI-401755
HCKP086312EBI-297353,EBI-346340
HDAC6Q9UBN711EBI-297353,EBI-301697
HDAC7Q8WUI42EBI-297353,EBI-1048378
HSP90AA1P079005EBI-297353,EBI-296047
HSP90AB1P082388EBI-297353,EBI-352572
HSP90AB1Q6PK502EBI-297353,EBI-9356629
HSPA1BP081076EBI-297353,EBI-629985
HSPA8P111425EBI-297353,EBI-351896
HSPA9P386464EBI-297353,EBI-354932
HSPB1P047923EBI-297353,EBI-352682
IGFBP3P179363EBI-297353,EBI-715709
IQGAP1P469404EBI-297353,EBI-297509
IRS4O146542EBI-297353,EBI-356594
LAPTM4BQ86VI410EBI-297353,EBI-3267258
LATO435612EBI-297353,EBI-1222766
LCP2Q130942EBI-297353,EBI-346946
LINGO1Q96FE52EBI-297353,EBI-719955
LRRK1Q38SD22EBI-297353,EBI-1050422
LYNP079486EBI-297353,EBI-79452
LYNP07948-12EBI-297353,EBI-6895930
MAPK8IP1Q9UQF23EBI-297353,EBI-78404
MAPK8IP2Q133874EBI-297353,EBI-722813
MAST1Q9Y2H92EBI-297353,EBI-3385920
METP085818EBI-297353,EBI-1039152
MIFP141743EBI-297353,EBI-372712
MUC1P159413EBI-297353,EBI-2804728
NCK1P163333EBI-297353,EBI-389883
NEDD4P469343EBI-297353,EBI-726944
NR3C1P041502EBI-297353,EBI-493507
PDGFRAP162343EBI-297353,EBI-2861522
PIK3C2BO007509EBI-297353,EBI-641107
PIK3R1P279865EBI-297353,EBI-79464
PIK3R2O004593EBI-297353,EBI-346930
PIK3R3Q925696EBI-297353,EBI-79893
PLCG1P191746EBI-297353,EBI-79387
PLCG2P168855EBI-297353,EBI-617403
PRKCAP172522EBI-297353,EBI-1383528
PrkdcP973134EBI-297353,EBI-2272005From Mus musculus.
PTK2Q053973EBI-297353,EBI-702142
PTPN1P180317EBI-297353,EBI-968788
Ptpn1P2041711EBI-297353,EBI-916819From Rattus norvegicus.
PTPN12Q052093EBI-297353,EBI-2266035
PTPN22Q9Y2R22EBI-297353,EBI-1211241
PTPRGP234702EBI-297353,EBI-2258115
RABGEF1Q9UJ414EBI-297353,EBI-913954
RAPH1Q70E732EBI-297353,EBI-3940924
RASA1P209367EBI-297353,EBI-1026476
RIN1Q136713EBI-297353,EBI-366017
ROR1Q019738EBI-297353,EBI-6082337
RUBCNQ926223EBI-297353,EBI-2952709
RubcnQ80U622EBI-297353,EBI-3506572From Mus musculus.
SFNP319478EBI-297353,EBI-476295
SH2B1Q9NRF22EBI-297353,EBI-310491
SH2B3Q9UQQ22EBI-297353,EBI-7879749
SH2D3AQ9BRG22EBI-297353,EBI-2339271
SHC1P2935328EBI-297353,EBI-78835
SHC1P29353-74EBI-297353,EBI-9691288
SHC2P980773EBI-297353,EBI-7256023
SHC4Q6S5L82EBI-297353,EBI-9453524
SLAQ132392EBI-297353,EBI-726214
SLC5A1P138663EBI-297353,EBI-1772443
SRCP129317EBI-297353,EBI-621482
STAT1P422246EBI-297353,EBI-1057697
STAT3P4076314EBI-297353,EBI-518675
STAT5AP422293EBI-297353,EBI-749537
STIP1P319482EBI-297353,EBI-1054052
STUB1Q9UNE73EBI-297353,EBI-357085
SYKP434056EBI-297353,EBI-78302
TGFAP011352EBI-297353,EBI-1034374
TLN1Q9Y4902EBI-297353,EBI-2462036
TLR2O606032EBI-297353,EBI-973722
TNS3Q68CZ24EBI-297353,EBI-1220488
TOM1L1O756746EBI-297353,EBI-712991
TRAF2Q129333EBI-297353,EBI-355744
Trpv3Q8K4242EBI-297353,EBI-2650739From Mus musculus.
TUBA1AQ71U363EBI-297353,EBI-302552
TXNP105994EBI-297353,EBI-594644
UCHL1P099362EBI-297353,EBI-714860
VAPAQ9P0L02EBI-297353,EBI-1059156
YES1P079473EBI-297353,EBI-515331
YWHAQP273486EBI-297353,EBI-359854
YWHAZP631045EBI-297353,EBI-347088
ZAP70P434032EBI-297353,EBI-1211276

GO - Molecular functioni