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Protein

Epidermal growth factor receptor

Gene

EGFR

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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:3260329). Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF (By similarity). Ligand binding triggers receptor homo-and/or heterodimerization and autophosphorylation on key cytoplasmic residues (By similarity). The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades (By similarity). Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (By similarity). May also activate the NF-kappa-B signaling cascade (By similarity). Plays a role in enhancing learning and memory performance (By similarity).By similarity1 Publication

Catalytic activityi

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

Enzyme regulationi

Endocytosis and inhibition of the activated EGFR by phosphatases constitute immediate regulatory mechanisms. Moreover, inducible feedback inhibitors may constitute alternative regulatory mechanisms for the EGFR signaling.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Epidermal growth factor receptor (EC:2.7.10.1)
Short name:
CER
Gene namesi
Name:EGFR
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini31 – 654ExtracellularSequence analysisAdd BLAST624
Transmembranei655 – 667HelicalSequence analysisAdd BLAST13
Topological domaini668 – ›703CytoplasmicSequence analysisAdd BLAST›36

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Add BLAST30
ChainiPRO_000001666731 – ›703Epidermal growth factor receptorAdd BLAST›673

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi134N-linked (GlcNAc...)Sequence analysis1
Glycosylationi190N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi197 ↔ 206By similarity
Glycosylationi200N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi201 ↔ 214By similarity
Disulfide bondi222 ↔ 230By similarity
Disulfide bondi226 ↔ 238By similarity
Disulfide bondi239 ↔ 247By similarity
Disulfide bondi243 ↔ 255By similarity
Disulfide bondi258 ↔ 267By similarity
Disulfide bondi271 ↔ 298By similarity
Disulfide bondi302 ↔ 314By similarity
Disulfide bondi318 ↔ 333By similarity
Disulfide bondi336 ↔ 340By similarity
Glycosylationi359N-linked (GlcNAc...)Sequence analysis1
Glycosylationi368N-linked (GlcNAc...)Sequence analysis1
Glycosylationi420N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi513 ↔ 522By similarity
Disulfide bondi517 ↔ 530By similarity
Disulfide bondi533 ↔ 542By similarity
Disulfide bondi546 ↔ 562By similarity
Disulfide bondi565 ↔ 581By similarity
Disulfide bondi569 ↔ 589By similarity
Glycosylationi573N-linked (GlcNAc...)Sequence analysis1
Glycosylationi578N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi592 ↔ 601By similarity
Disulfide bondi605 ↔ 627By similarity
Glycosylationi613N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi630 ↔ 638By similarity
Glycosylationi633N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi634 ↔ 646By similarity
Glycosylationi648N-linked (GlcNAc...)Sequence analysis1
Modified residuei687PhosphothreonineBy similarity1
Modified residuei702PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylated. Autophosphorylates (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP13387.
PRIDEiP13387.

PTM databases

iPTMnetiP13387.

Expressioni

Gene expression databases

BgeeiENSGALG00000012363.

Interactioni

Subunit structurei

Binding of the ligand triggers homo- and/or heterodimerization of the receptor triggering its autophosphorylation.By similarity

Protein-protein interaction databases

STRINGi9031.ENSGALP00000020165.

Structurei

3D structure databases

ProteinModelPortaliP13387.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1025. Eukaryota.
ENOG410XNSR. LUCA.
HOGENOMiHOG000230982.
HOVERGENiHBG000490.
InParanoidiP13387.
KOiK04361.
PhylomeDBiP13387.

Family and domain databases

Gene3Di3.80.20.20. 2 hits.
InterProiIPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR032778. GF_recep_IV.
IPR009030. Growth_fac_rcpt_.
IPR032675. L_dom-like.
IPR000494. Rcpt_L-dom.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF14843. GF_recep_IV. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
SMARTiSM00261. FU. 5 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF57184. SSF57184. 2 hits.

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13387-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVRSPLSAS GPRGAAVLVL LLLGVALCSA VEEKKVCQGT NNKLTQLGHV
60 70 80 90 100
EDHFTSLQRM YNNCEVVLSN LEITYVEHNR DLTFLKTIQE VAGYVLIALN
110 120 130 140 150
MVDVIPLENL QIIRGNVLYD NSFALAVLSN YHMNKTQGLR ELPMKRLSEI
160 170 180 190 200
LNGGVKISNN PKLCNMDTVL WNDIIDTSRK PLTVLDFASN LSSCPKCHPN
210 220 230 240 250
CTEDHCWGAG EQNCQTLTKV ICAQQCSGRC RGKVPSDCCH NQCAAGCTGP
260 270 280 290 300
RESDCLACRK FRDDATCKDT CPPLVLYNPT TYQMDVNPEG KYSFGATCVR
310 320 330 340 350
ECPHNYVVTD HGSCVRSCNT DTYEVEENGV RKCKKCDGLC SKVCNGIGIG
360 370 380 390 400
ELKGILSINA TNIDSFKNCT KINGDVSILP VAFLGDAFTK TLPLDPKKLD
410 420 430 440 450
VFRTVKEISG FLLIQAWPDN ATDLYAFENL EIIRGRTKQH GQYSLAVVNL
460 470 480 490 500
KIQSLGLRSL KEISDGDIAI MKNKNLCYAD TMNWRSLFAT QSQKTKIIQN
510 520 530 540 550
RNKNDCTADR HVCDPLCSDV GCWGPGPFHC FSCRFFSRQK ECVKQCNILQ
560 570 580 590 600
GEPREFERDS KCLPCHSECL VQNSTAYNTT CSGPGPDHCM KCAHFIDGPH
610 620 630 640 650
CVKACPAGVL GENDTLVWKY ADANAVCQLC HPNCTRGCKG PGLEGCPNGS
660 670 680 690 700
KTPSIAAGVV GGLLCLVVVG LGIGLYLRRR HIVRKRTLRR LLQERELVEP

LTP
Length:703
Mass (Da):77,427
Last modified:January 1, 1990 - v1
Checksum:iAFF2DE11B735A690
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei7031

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20386 mRNA. Translation: AAA48760.1.
RefSeqiNP_990828.2. NM_205497.2.
UniGeneiGga.35024.

Genome annotation databases

GeneIDi396494.
KEGGigga:396494.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20386 mRNA. Translation: AAA48760.1.
RefSeqiNP_990828.2. NM_205497.2.
UniGeneiGga.35024.

3D structure databases

ProteinModelPortaliP13387.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000020165.

PTM databases

iPTMnetiP13387.

Proteomic databases

PaxDbiP13387.
PRIDEiP13387.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396494.
KEGGigga:396494.

Organism-specific databases

CTDi1956.

Phylogenomic databases

eggNOGiKOG1025. Eukaryota.
ENOG410XNSR. LUCA.
HOGENOMiHOG000230982.
HOVERGENiHBG000490.
InParanoidiP13387.
KOiK04361.
PhylomeDBiP13387.

Gene expression databases

BgeeiENSGALG00000012363.

Family and domain databases

Gene3Di3.80.20.20. 2 hits.
InterProiIPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR032778. GF_recep_IV.
IPR009030. Growth_fac_rcpt_.
IPR032675. L_dom-like.
IPR000494. Rcpt_L-dom.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF14843. GF_recep_IV. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
SMARTiSM00261. FU. 5 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF57184. SSF57184. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiEGFR_CHICK
AccessioniPrimary (citable) accession number: P13387
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 30, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.