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Protein

Epidermal growth factor receptor

Gene

EGFR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. 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. Plays a role in enhancing learning and memory performance (By similarity).By similarity
Isoform 2 may act as an antagonist of EGF action.

Catalytic activityi

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

Enzyme 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 sitei745ATP1
Active sitei837Proton acceptorPROSITE-ProRule annotation1
Binding sitei855ATP1
Sitei1016Important for interaction with PIK3C2B1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi718 – 726ATP9
Nucleotide bindingi790 – 791ATP2

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • chromatin binding Source: UniProtKB
  • double-stranded DNA binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • epidermal growth factor-activated receptor activity Source: UniProtKB
  • glycoprotein binding Source: Ensembl
  • identical protein binding Source: IntAct
  • MAP kinase kinase kinase activity Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: Reactome
  • protein heterodimerization activity Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • protein tyrosine kinase activity Source: UniProtKB
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • receptor signaling protein tyrosine kinase activity Source: InterPro
  • transmembrane receptor protein tyrosine kinase activity Source: Reactome
  • transmembrane signaling receptor activity Source: MGI
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • activation of phospholipase A2 activity by calcium-mediated signaling Source: UniProtKB
  • activation of phospholipase C activity Source: UniProtKB
  • astrocyte activation Source: Ensembl
  • cell proliferation Source: UniProtKB
  • cell surface receptor signaling pathway Source: MGI
  • cellular response to amino acid stimulus Source: Ensembl
  • cellular response to dexamethasone stimulus Source: Ensembl
  • cellular response to drug Source: Ensembl
  • cellular response to epidermal growth factor stimulus Source: UniProtKB
  • cellular response to estradiol stimulus Source: UniProtKB
  • cellular response to mechanical stimulus Source: Ensembl
  • cerebral cortex cell migration Source: Ensembl
  • circadian rhythm Source: Ensembl
  • digestive tract morphogenesis Source: Ensembl
  • diterpenoid metabolic process Source: Ensembl
  • embryonic placenta development Source: Ensembl
  • epidermal growth factor receptor signaling pathway Source: UniProtKB
  • ERBB2 signaling pathway Source: Reactome
  • eyelid development in camera-type eye Source: Ensembl
  • hair follicle development Source: Ensembl
  • hydrogen peroxide metabolic process Source: Ensembl
  • learning or memory Source: UniProtKB
  • liver regeneration Source: Ensembl
  • lung development Source: Ensembl
  • magnesium ion homeostasis Source: Ensembl
  • MAPK cascade Source: Reactome
  • midgut development Source: Ensembl
  • morphogenesis of an epithelial fold Source: Ensembl
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cardiocyte differentiation Source: BHF-UCL
  • negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
  • negative regulation of mitotic cell cycle Source: Ensembl
  • negative regulation of protein catabolic process Source: UniProtKB
  • neuron projection morphogenesis Source: Ensembl
  • ossification Source: UniProtKB
  • ovulation cycle Source: Ensembl
  • phosphatidylinositol-mediated signaling Source: Reactome
  • positive regulation of bone resorption Source: Ensembl
  • positive regulation of catenin import into nucleus Source: BHF-UCL
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: BHF-UCL
  • positive regulation of DNA repair Source: UniProtKB
  • positive regulation of DNA replication Source: UniProtKB
  • positive regulation of epithelial cell proliferation Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of fibroblast proliferation Source: Ensembl
  • positive regulation of inflammatory response Source: Ensembl
  • positive regulation of MAP kinase activity Source: UniProtKB
  • positive regulation of nitric oxide biosynthetic process Source: UniProtKB
  • positive regulation of phosphorylation Source: UniProtKB
  • positive regulation of production of miRNAs involved in gene silencing by miRNA Source: BHF-UCL
  • positive regulation of prolactin secretion Source: Ensembl
  • positive regulation of protein kinase B signaling Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of smooth muscle cell proliferation Source: Ensembl
  • positive regulation of superoxide anion generation Source: Ensembl
  • positive regulation of synaptic transmission, glutamatergic Source: Ensembl
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of vasoconstriction Source: Ensembl
  • positive regulation of vasodilation Source: Ensembl
  • protein autophosphorylation Source: UniProtKB
  • protein insertion into membrane Source: UniProtKB
  • regulation of cell motility Source: Reactome
  • regulation of nitric-oxide synthase activity Source: UniProtKB
  • regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  • regulation of phosphatidylinositol 3-kinase signaling Source: Reactome
  • response to calcium ion Source: Ensembl
  • response to cobalamin Source: Ensembl
  • response to hydroxyisoflavone Source: Ensembl
  • response to osmotic stress Source: Ensembl
  • response to oxidative stress Source: Ensembl
  • response to stress Source: UniProtKB
  • response to UV-A Source: BHF-UCL
  • salivary gland morphogenesis Source: Ensembl
  • signal transduction Source: UniProtKB
  • single organismal cell-cell adhesion Source: UniProtKB
  • tongue development Source: Ensembl
  • translation Source: Ensembl
  • wound healing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS07358-MONOMER.
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.
SignaLinkiP00533.
SIGNORiP00533.

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

HGNCiHGNC:3236. EGFR.

Subcellular locationi

Topology

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

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • basolateral plasma membrane Source: BHF-UCL
  • cell-cell adherens junction Source: BHF-UCL
  • cell surface Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • early endosome membrane Source: UniProtKB
  • endocytic vesicle Source: Ensembl
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • endosome Source: UniProtKB
  • endosome membrane Source: UniProtKB
  • extracellular space Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • membrane raft Source: UniProtKB
  • multivesicular body, internal vesicle lumen Source: UniProtKB
  • nuclear membrane Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: Ensembl
  • plasma membrane Source: HGNC
  • receptor complex Source: MGI
  • Shc-EGFR complex Source: BHF-UCL
  • synapse Source: Ensembl
Complete GO annotation...

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 rs606231253dbSNPEnsembl.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
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
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.
DB00530. Erlotinib.
DB00317. Gefitinib.
DB01259. Lapatinib.
DB00281. Lidocaine.
DB09559. Necitumumab.
DB09330. Osimertinib.
DB01269. Panitumumab.
DB00072. Trastuzumab.
DB05294. Vandetanib.
GuidetoPHARMACOLOGYi1797.

Polymorphism and mutation databases

BioMutaiEGFR.
DMDMi2811086.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 242 PublicationsAdd BLAST24
ChainiPRO_000001666525 – 1210Epidermal growth factor receptorAdd BLAST1186

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi31 ↔ 58
GlycosylationiCAR_00022756N-linked (GlcNAc...) (complex); atypical; partial5 Publications1
Glycosylationi73N-linked (GlcNAc...); atypical1 Publication1
Glycosylationi128N-linked (GlcNAc...)3 Publications1
Disulfide bondi157 ↔ 187
Glycosylationi175N-linked (GlcNAc...)5 Publications1
Disulfide bondi190 ↔ 199
Disulfide bondi194 ↔ 207
Glycosylationi196N-linked (GlcNAc...)4 Publications1
Disulfide bondi215 ↔ 223
Disulfide bondi219 ↔ 231
Modified residuei229Phosphoserine1 Publication1
Disulfide bondi232 ↔ 240
Disulfide bondi236 ↔ 248
Disulfide bondi251 ↔ 260
Disulfide bondi264 ↔ 291
Disulfide bondi295 ↔ 307
Disulfide bondi311 ↔ 326
Disulfide bondi329 ↔ 333
Disulfide bondi337 ↔ 362
Glycosylationi352N-linked (GlcNAc...)7 Publications1
Glycosylationi361N-linked (GlcNAc...)6 Publications1
Glycosylationi413N-linked (GlcNAc...)4 Publications1
Glycosylationi444N-linked (GlcNAc...)6 Publications1
Disulfide bondi470 ↔ 499
Disulfide bondi506 ↔ 515
Disulfide bondi510 ↔ 523
Disulfide bondi526 ↔ 535
Glycosylationi528N-linked (GlcNAc...)5 Publications1
Disulfide bondi539 ↔ 555
Disulfide bondi558 ↔ 571
Disulfide bondi562 ↔ 579
Glycosylationi568N-linked (GlcNAc...); partial5 Publications1
Disulfide bondi582 ↔ 591
Disulfide bondi595 ↔ 617
Glycosylationi603N-linked (GlcNAc...); partial4 Publications1
Disulfide bondi620 ↔ 628
Glycosylationi623N-linked (GlcNAc...) (high mannose)1 Publication1
Disulfide bondi624 ↔ 636
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
Modified residuei1064PhosphoserineCombined sources1
Modified residuei1069Phosphotyrosine1 Publication1
Modified residuei1070Phosphoserine1 Publication1
Modified residuei1071Phosphoserine1 Publication1
Modified residuei1081PhosphoserineCombined sources1
Modified residuei1092Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1110Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei1166PhosphoserineCombined sources1
Modified residuei1172Phosphotyrosine; by autocatalysisCombined sources1
Modified residuei1197Phosphotyrosine; by autocatalysisCombined sources2 Publications1
Modified residuei1199Omega-N-methylarginine1 Publication1

Post-translational modificationi

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 PTPN2.8 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. 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 similarity3 Publications
Methylated. Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197.3 Publications

Keywords - PTMi

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

Proteomic databases

EPDiP00533.
MaxQBiP00533.
PaxDbiP00533.
PeptideAtlasiP00533.
PRIDEiP00533.

2D gel databases

SWISS-2DPAGEP00533.

PTM databases

iPTMnetiP00533.
PhosphoSitePlusiP00533.
SwissPalmiP00533.
UniCarbKBiP00533.

Miscellaneous databases

PMAP-CutDBP00533.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000146648.
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. Interacts with ERRFI1; inhibits dimerization of the kinase domain and autophosphorylation. Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B. 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 TCEB1- and TCEB2-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. 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. 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. Interacts with GPRC5A (via its transmembrane domain)(PubMed:25311788). Interacts with FAM83B; positively regulates EGFR inducing its autophospharylation in absence of stimulation by EGF (PubMed:23912460).38 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself23EBI-297353,EBI-297353
Q53FC73EBI-297353,EBI-9356749
Q96BE02EBI-297353,EBI-9356686
ABL1P005192EBI-297353,EBI-375543
ABL2P426848EBI-297353,EBI-1102694
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
CAV1Q031355EBI-297353,EBI-603614
CBLP2268121EBI-297353,EBI-518228
CblP226822EBI-297353,EBI-640919From a different organism.
CDC37Q165439EBI-297353,EBI-295634
CDH1P128303EBI-297353,EBI-727477
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
CYTH2Q994185EBI-297353,EBI-448974
DOK6Q6PKX42EBI-297353,EBI-2880244
EGFP0113316EBI-297353,EBI-640857
EPS8Q129292EBI-297353,EBI-375576
ERBB2P0462621EBI-297353,EBI-641062
ERBB3P2186012EBI-297353,EBI-720706
ERBB4Q153032EBI-297353,EBI-80371
ERCC1P0799221EBI-297353,EBI-750962
ERRFI1Q9UJM38EBI-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
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
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
METP085817EBI-297353,EBI-1039152
MUC1P159413EBI-297353,EBI-2804728
NCK1P163333EBI-297353,EBI-389883
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 a different organism.
PTK2Q053973EBI-297353,EBI-702142
PTPN1P180317EBI-297353,EBI-968788
Ptpn1P2041711EBI-297353,EBI-916819From a different organism.
PTPN12Q052093EBI-297353,EBI-2266035
PTPN22Q9Y2R22EBI-297353,EBI-1211241
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 a different organism.
SFNP319478EBI-297353,EBI-476295
SH2B1Q9NRF22EBI-297353,EBI-310491
SH2B3Q9UQQ22EBI-297353,EBI-7879749
SH2D3AQ9BRG22EBI-297353,EBI-2339271
SHC1P2935326EBI-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 a different organism.
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

  • actin filament binding Source: UniProtKB
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108276. 845 interactors.
DIPiDIP-405N.
IntActiP00533. 479 interactors.
MINTiMINT-206389.
STRINGi9606.ENSP00000275493.

Chemistry databases

BindingDBiP00533.

Structurei

Secondary structure

11210
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 43Combined sources4
Helixi44 – 55Combined sources12
Beta strandi60 – 69Combined sources10
Helixi77 – 81Combined sources5
Beta strandi84 – 87Combined sources4
Beta strandi89 – 93Combined sources5
Helixi101 – 103Combined sources3
Turni114 – 116Combined sources3
Beta strandi117 – 122Combined sources6
Beta strandi125 – 129Combined sources5
Beta strandi145 – 152Combined sources8
Helixi159 – 161Combined sources3
Helixi164 – 166Combined sources3
Helixi170 – 173Combined sources4
Helixi195 – 197Combined sources3
Beta strandi199 – 204Combined sources6
Beta strandi211 – 214Combined sources4
Beta strandi223 – 227Combined sources5
Helixi228 – 230Combined sources3
Beta strandi236 – 238Combined sources3
Beta strandi240 – 244Combined sources5
Turni245 – 247Combined sources3
Beta strandi248 – 256Combined sources9
Beta strandi259 – 263Combined sources5
Beta strandi267 – 271Combined sources5
Turni272 – 275Combined sources4
Beta strandi276 – 279Combined sources4
Beta strandi285 – 287Combined sources3
Beta strandi290 – 294Combined sources5
Turni296 – 298Combined sources3
Beta strandi299 – 301Combined sources3
Beta strandi303 – 305Combined sources3
Beta strandi306 – 310Combined sources5
Beta strandi313 – 315Combined sources3
Beta strandi318 – 320Combined sources3
Beta strandi323 – 325Combined sources3
Beta strandi330 – 332Combined sources3
Beta strandi336 – 338Combined sources3
Turni340 – 342Combined sources3
Helixi343 – 345Combined sources3
Beta strandi349 – 351Combined sources3
Turni353 – 355Combined sources3
Helixi356 – 359Combined sources4
Beta strandi363 – 367Combined sources5
Beta strandi369 – 371Combined sources3
Helixi373 – 377Combined sources5
Turni380 – 383Combined sources4
Helixi389 – 397Combined sources9
Beta strandi400 – 403Combined sources4
Beta strandi405 – 407Combined sources3
Helixi418 – 420Combined sources3
Turni433 – 435Combined sources3
Beta strandi436 – 442Combined sources7
Beta strandi458 – 464Combined sources7
Helixi472 – 474Combined sources3
Helixi477 – 480Combined sources4
Beta strandi481 – 483Combined sources3
Beta strandi488 – 494Combined sources7
Helixi496 – 501Combined sources6
Turni507 – 509Combined sources3
Beta strandi515 – 519Combined sources5
Helixi520 – 522Combined sources3
Beta strandi523 – 526Combined sources4
Beta strandi531 – 533Combined sources3
Beta strandi535 – 537Combined sources3
Beta strandi540 – 546Combined sources7
Beta strandi548 – 551Combined sources4
Beta strandi554 – 557Combined sources4
Beta strandi560 – 562Combined sources3
Beta strandi566 – 568Combined sources3
Beta strandi570 – 575Combined sources6
Beta strandi578 – 587Combined sources10
Beta strandi590 – 594Combined sources5
Beta strandi597 – 602Combined sources6
Beta strandi606 – 611Combined sources6
Beta strandi615 – 619Combined sources5
Beta strandi629 – 632Combined sources4
Helixi633 – 635Combined sources3
Beta strandi643 – 646Combined sources4
Helixi648 – 669Combined sources22
Beta strandi671 – 673Combined sources3
Helixi679 – 684Combined sources6
Helixi685 – 687Combined sources3
Beta strandi688 – 692Combined sources5
Beta strandi694 – 697Combined sources4
Beta strandi703 – 706Combined sources4
Helixi709 – 711Combined sources3
Beta strandi712 – 721Combined sources10
Beta strandi724 – 731Combined sources8
Turni734 – 736Combined sources3
Beta strandi740 – 747Combined sources8
Beta strandi748 – 750Combined sources3
Turni753 – 755Combined sources3
Helixi756 – 767Combined sources12
Beta strandi772 – 774Combined sources3
Beta strandi777 – 791Combined sources15
Beta strandi794 – 797Combined sources4
Helixi798 – 805Combined sources8
Helixi806 – 808Combined sources3
Helixi811 – 830Combined sources20
Helixi840 – 842Combined sources3
Beta strandi843 – 847Combined sources5
Beta strandi850 – 853Combined sources4
Helixi858 – 862Combined sources5
Turni863 – 865Combined sources3
Helixi867 – 871Combined sources5
Beta strandi873 – 876Combined sources4
Helixi878 – 880Combined sources3
Helixi883 – 888Combined sources6
Helixi893 – 908Combined sources16
Turni909 – 911Combined sources3
Turni914 – 917Combined sources4
Helixi920 – 922Combined sources3
Helixi923 – 929Combined sources7
Beta strandi937 – 939Combined sources3
Helixi941 – 949Combined sources9
Beta strandi951 – 953Combined sources3
Helixi955 – 957Combined sources3
Helixi961 – 972Combined sources12
Helixi975 – 978Combined sources4
Helixi984 – 986Combined sources3
Turni992 – 998Combined sources7
Beta strandi1004 – 1010Combined sources7
Helixi1013 – 1016Combined sources4
Beta strandi1068 – 1070Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DNQmodel-A25-336[»]
1DNRmodel-A337-645[»]
1IVOX-ray3.30A/B25-646[»]
1M14X-ray2.60A695-1022[»]
1M17X-ray2.60A695-1022[»]
1MOXX-ray2.50A/B25-525[»]
1NQLX-ray2.80A25-642[»]
1XKKX-ray2.40A695-1022[»]
1YY9X-ray2.60A25-642[»]
1Z9INMR-A669-721[»]
2EB2X-ray2.50A695-1022[»]
2EB3X-ray2.84A695-1022[»]
2EXPmodel-A311-326[»]
2EXQmodel-A27-536[»]
2GS2X-ray2.80A696-1022[»]
2GS6X-ray2.60A696-1022[»]
2GS7X-ray2.60A/B696-1022[»]
2ITNX-ray2.47A696-1019[»]
2ITOX-ray3.25A696-1022[»]
2ITPX-ray2.74A696-1022[»]
2ITQX-ray2.68A696-1022[»]
2ITTX-ray2.73A696-1022[»]
2ITUX-ray2.80A696-1022[»]
2ITVX-ray2.47A696-1022[»]
2ITWX-ray2.88A696-1022[»]
2ITXX-ray2.98A696-1022[»]
2ITYX-ray3.42A696-1022[»]
2ITZX-ray2.72A696-1022[»]
2J5EX-ray3.10A696-1022[»]
2J5FX-ray3.00A696-1022[»]
2J6MX-ray3.10A696-1022[»]
2JITX-ray3.10A/B696-1022[»]
2JIUX-ray3.05A/B695-1022[»]
2JIVX-ray3.50A/B695-1022[»]
2KS1NMR-B634-677[»]
2M0BNMR-A/B634-677[»]
2M20NMR-A/B642-697[»]
2N5SNMR-A642-690[»]
2RF9X-ray3.50A/B696-1022[»]
2RFDX-ray3.60A/B702-1022[»]
2RFEX-ray2.90A/B/C/D702-1022[»]
2RGPX-ray2.00A702-1016[»]
3B2UX-ray2.58A/B/E/I/M/P/S/V335-538[»]
3B2VX-ray3.30A25-642[»]
3BELX-ray2.30A702-1016[»]
3BUOX-ray2.60A/C1063-1075[»]
3C09X-ray3.20A/D336-538[»]
3G5VX-ray2.00C311-326[»]
3G5YX-ray1.59E311-326[»]
3GOPX-ray2.80A669-1022[»]
3GT8X-ray2.96A/B/C/D696-1022[»]
3IKAX-ray2.90A/B694-1022[»]
3LZBX-ray2.70A/B/C/D/E/F/G/H696-983[»]
3NJPX-ray3.30A/B25-638[»]
3OB2X-ray2.10A1063-1074[»]
3OP0X-ray2.52C/D1066-1076[»]
3P0YX-ray1.80A334-538[»]
3PFVX-ray2.27C/D1066-1076[»]
3POZX-ray1.50A696-1022[»]
3QWQX-ray2.75A1-642[»]
3UG1X-ray2.75A695-1022[»]
3UG2X-ray2.50A695-1022[»]
3VJNX-ray2.34A695-1022[»]
3VJOX-ray2.64A695-1022[»]
3VRPX-ray1.52B1062-1074[»]
3VRRX-ray2.00C1062-1074[»]
3W2OX-ray2.35A698-1022[»]
3W2PX-ray2.05A698-1022[»]
3W2QX-ray2.20A698-1022[»]
3W2RX-ray2.05A698-1022[»]
3W2SX-ray1.90A696-1022[»]
3W32X-ray1.80A696-1022[»]
3W33X-ray1.70A696-1022[»]
4G5JX-ray2.80A696-1022[»]
4G5PX-ray3.17A/B696-1022[»]
4HJOX-ray2.75A696-1022[»]
4I1ZX-ray3.00A695-1022[»]
4I20X-ray3.34A695-1022[»]
4I21X-ray3.37A/B695-1022[»]
4I22X-ray1.71A695-1022[»]
4I23X-ray2.80A695-1022[»]
4I24X-ray1.80A/B695-1022[»]
4JQ7X-ray2.73A696-1021[»]
4JQ8X-ray2.83A696-1021[»]
4JR3X-ray2.70A696-1021[»]
4JRVX-ray2.80A696-1021[»]
4KRLX-ray2.85A335-538[»]
4KRMX-ray2.66A/C/E/G/I/K335-538[»]
4KROX-ray3.05A25-642[»]
4KRPX-ray2.82A25-642[»]
4LI5X-ray2.64A696-1020[»]
4LL0X-ray4.00A/B694-1022[»]
4LQMX-ray2.50A694-1022[»]
4LRMX-ray3.53A/B/C/D/E694-1022[»]
4R3PX-ray2.90A696-1018[»]
4R3RX-ray3.25A696-1018[»]
4R5SX-ray3.00A696-1022[»]
4RIWX-ray3.10B/D682-1022[»]
4RIXX-ray3.10B/D682-1022[»]
4RIYX-ray2.98B/D682-1022[»]
4RJ4X-ray2.78A695-1022[»]
4RJ5X-ray3.10A695-1022[»]
4RJ6X-ray2.70A695-1022[»]
4RJ7X-ray2.55A695-1022[»]
4RJ8X-ray2.50A695-1022[»]
4TKSX-ray3.20A695-1022[»]
4UIPX-ray2.95A26-637[»]
4UV7X-ray2.10A25-645[»]
4WD5X-ray3.30A/B694-1022[»]
4WKQX-ray1.85A696-1022[»]
4WRGX-ray1.90A696-1022[»]
4ZAUX-ray2.80A696-1022[»]
4ZJVX-ray2.70A/B695-1022[»]
4ZSEX-ray1.97A/B/C/D695-1022[»]
5C8KX-ray3.00A695-1022[»]
5C8MX-ray2.90A695-1022[»]
5C8NX-ray2.40A695-1022[»]
5CALX-ray2.70A695-1022[»]
5CANX-ray2.80A695-1022[»]
5CAOX-ray2.60A695-1022[»]
5CAPX-ray2.40A695-1022[»]
5CAQX-ray2.50A695-1022[»]
5CASX-ray2.10A695-1022[»]
5CAUX-ray2.25A695-1022[»]
5CAVX-ray2.73A695-1022[»]
5CNNX-ray1.90A/B696-1042[»]
5CNOX-ray1.55A/B/X696-1022[»]
5CZHX-ray2.80A694-1022[»]
5CZIX-ray2.60A694-1022[»]
5D41X-ray2.31A/B695-1022[»]
5EDPX-ray2.90A695-1022[»]
5EDQX-ray2.80A695-1022[»]
5EDRX-ray2.60A695-1022[»]
5EM5X-ray2.65A695-1022[»]
5EM6X-ray2.78A695-1022[»]
5EM7X-ray2.81A695-1022[»]
5EM8X-ray2.80A695-1022[»]
5FEDX-ray2.65A696-1022[»]
5FEEX-ray2.70A696-1022[»]
5FEQX-ray3.40A696-1022[»]
5HCXX-ray2.60A696-1022[»]
5HCYX-ray2.46A696-1022[»]
5HCZX-ray2.62A696-1022[»]
5HG5X-ray1.52A695-1022[»]
5HG7X-ray1.85A695-1022[»]
5HG8X-ray1.42A695-1022[»]
5HG9X-ray2.15A695-1022[»]
5HIBX-ray2.85A695-1022[»]
5HICX-ray2.60A695-1022[»]
5J9YX-ray2.80A697-1019[»]
5J9ZX-ray2.50A696-1020[»]
5JEBX-ray3.30A696-1022[»]
5SX4X-ray2.80M/N335-525[»]
5SX5X-ray2.50M/N335-525[»]
DisProtiDP00309.
ProteinModelPortaliP00533.
SMRiP00533.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00533.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati75 – 300ApproximateAdd BLAST226
Repeati390 – 600ApproximateAdd BLAST211
Domaini712 – 979Protein kinasePROSITE-ProRule annotationAdd BLAST268

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni688 – 704Important for dimerization, phosphorylation and activationAdd BLAST17

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1025. Eukaryota.
ENOG410XNSR. LUCA.
GeneTreeiENSGT00760000118799.
HOVERGENiHBG000490.
InParanoidiP00533.
KOi