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P55245 (EGFR_MACMU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Epidermal growth factor receptor

EC=2.7.10.1
Gene names
Name:EGFR
OrganismMacaca mulatta (Rhesus macaque) [Reference proteome]
Taxonomic identifier9544 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

Sequence length1210 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Catalytic activity

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

Enzyme regulation

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.

Subunit structure

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 GAREM. 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 By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass type I membrane protein By similarity. Golgi apparatus membrane; Single-pass type I membrane protein By similarity. Nucleus membrane; Single-pass type I membrane protein By similarity. Endosome. Endosome membrane By similarity. Nucleus By similarity. Note: In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) By similarity.

Tissue specificity

Hypothalamus.

Developmental stage

Levels in the medial basal hypothalamus and preoptic area are elevated during neonatal life (1 week-6 months), decrease during juvenile development (8-18 months) and markedly increase during the expected time of puberty (30-36 months).

Post-translational modification

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-955', but linkage through 'Lys-940', 'Lys-903' and 'Lys-921' also occur. Deubiquitinated by OTUD7B, preventing degradation By similarity.

Phosphorylated. Autophosphorylates. Dephosphorylated by PTPN1 and PTPN2 By similarity.

Methylated By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Endoplasmic reticulum
Endosome
Golgi apparatus
Membrane
Nucleus
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

cellular response to epidermal growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to estradiol stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cerebral cortex cell migration

Inferred from electronic annotation. Source: Ensembl

digestive tract morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic placenta development

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

hair follicle development

Inferred from electronic annotation. Source: Ensembl

learning or memory

Inferred from sequence or structural similarity. Source: UniProtKB

morphogenesis of an epithelial fold

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein catabolic process

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: GOC

positive regulation of DNA repair

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of catenin import into nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of nitric-oxide synthase activity

Inferred from electronic annotation. Source: Ensembl

regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

response to UV-A

Inferred from electronic annotation. Source: Ensembl

salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

endocytic vesicle

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Inferred from sequence or structural similarity. Source: UniProtKB

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane raft

Inferred from electronic annotation. Source: Ensembl

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

epidermal growth factor-activated receptor activity

Inferred from electronic annotation. Source: Ensembl

nitric-oxide synthase regulator activity

Inferred from electronic annotation. Source: Ensembl

protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

receptor signaling protein tyrosine kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 12101186Epidermal growth factor receptor
PRO_0000160254

Regions

Topological domain25 – 645621Extracellular Potential
Transmembrane646 – 66823Helical; Potential
Topological domain669 – 1210542Cytoplasmic Potential
Repeat75 – 300226Approximate
Repeat390 – 600211Approximate
Domain712 – 979268Protein kinase
Nucleotide binding718 – 7269ATP By similarity
Nucleotide binding790 – 7912ATP By similarity
Region688 – 70417Important for dimerization, phosphorylation and activation By similarity

Sites

Active site8371Proton acceptor By similarity
Binding site7451ATP By similarity
Binding site8551ATP By similarity
Site10161Important for interaction with PIK3C2B By similarity

Amino acid modifications

Modified residue2291Phosphoserine By similarity
Modified residue6781Phosphothreonine; by PKC and PKD/PRKD1 By similarity
Modified residue6931Phosphothreonine; by PKD/PRKD1 By similarity
Modified residue6951Phosphoserine By similarity
Modified residue9911Phosphoserine By similarity
Modified residue9951Phosphoserine By similarity
Modified residue9981Phosphotyrosine; by autocatalysis By similarity
Modified residue10161Phosphotyrosine; by autocatalysis By similarity
Modified residue10261Phosphoserine By similarity
Modified residue10391Phosphoserine By similarity
Modified residue10411Phosphothreonine By similarity
Modified residue10421Phosphoserine By similarity
Modified residue10641Phosphoserine By similarity
Modified residue10701Phosphoserine By similarity
Modified residue10711Phosphoserine By similarity
Modified residue10811Phosphoserine By similarity
Modified residue10921Phosphotyrosine; by autocatalysis By similarity
Modified residue11101Phosphotyrosine; by autocatalysis By similarity
Modified residue11661Phosphoserine By similarity
Modified residue11721Phosphotyrosine; by autocatalysis By similarity
Modified residue11971Phosphotyrosine; by autocatalysis By similarity
Modified residue11991Omega-N-methylated arginine By similarity
Glycosylation731N-linked (GlcNAc...); atypical By similarity
Glycosylation1281N-linked (GlcNAc...) By similarity
Glycosylation1751N-linked (GlcNAc...) By similarity
Glycosylation1961N-linked (GlcNAc...) By similarity
Glycosylation3521N-linked (GlcNAc...) By similarity
Glycosylation3611N-linked (GlcNAc...) By similarity
Glycosylation4131N-linked (GlcNAc...) By similarity
Glycosylation4441N-linked (GlcNAc...) By similarity
Glycosylation5281N-linked (GlcNAc...) By similarity
Glycosylation5681N-linked (GlcNAc...) By similarity
Glycosylation6031N-linked (GlcNAc...) By similarity
Disulfide bond31 ↔ 58 By similarity
Disulfide bond157 ↔ 187 By similarity
Disulfide bond190 ↔ 199 By similarity
Disulfide bond194 ↔ 207 By similarity
Disulfide bond215 ↔ 223 By similarity
Disulfide bond219 ↔ 231 By similarity
Disulfide bond232 ↔ 240 By similarity
Disulfide bond236 ↔ 248 By similarity
Disulfide bond251 ↔ 260 By similarity
Disulfide bond264 ↔ 291 By similarity
Disulfide bond295 ↔ 307 By similarity
Disulfide bond311 ↔ 326 By similarity
Disulfide bond329 ↔ 333 By similarity
Disulfide bond337 ↔ 362 By similarity
Disulfide bond470 ↔ 499 By similarity
Disulfide bond506 ↔ 515 By similarity
Disulfide bond510 ↔ 523 By similarity
Disulfide bond526 ↔ 535 By similarity
Disulfide bond539 ↔ 555 By similarity
Disulfide bond558 ↔ 571 By similarity
Disulfide bond562 ↔ 579 By similarity
Disulfide bond582 ↔ 591 By similarity
Disulfide bond595 ↔ 617 By similarity
Disulfide bond620 ↔ 628 By similarity
Disulfide bond624 ↔ 636 By similarity
Cross-link716Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link737Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link867Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link929Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link970Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict5411V → I in EHH17303. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P55245 [UniParc].

Last modified January 22, 2014. Version 2.
Checksum: E114E9CEE96D64CC

FASTA1,210134,350
        10         20         30         40         50         60 
MRPSGTAGAA LLALLAALCP ASRALEEKKV CQGTSNKLTQ LGTFEDHFLS LQRMFNNCEV 

        70         80         90        100        110        120 
VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN MYYENSYALA 

       130        140        150        160        170        180 
VLSNYDANKT GLKELPMRNL QEILHGAVRF SNNPALCNVE SIQWRDIVSS EFLSNMSMDF 

       190        200        210        220        230        240 
QNHLGSCQKC DPSCPNGSCW GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC 

       250        260        270        280        290        300 
TGPRESDCLV CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV 

       310        320        330        340        350        360 
VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDTLS INATNIKHFK 

       370        380        390        400        410        420 
NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE ITGFLLIQAW PENRTDLHAF 

       430        440        450        460        470        480 
ENLEIIRGRT KQHGQFSLAV VSLNITSLGL RSLKEISDGD VIISGNKNLC YANTINWKKL 

       490        500        510        520        530        540 
FGTSSQKTKI ISNRGENSCK ATGQVCHALC SPEGCWGPEP RDCVSCQNVS RGRECVDKCN 

       550        560        570        580        590        600 
VLEGEPREFV ENSECIQCHP ECLPQVMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM 

       610        620        630        640        650        660 
GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCARNG PKIPSIATGM VGALLLLLVV 

       670        680        690        700        710        720 
ALGIGLFMRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN QALLRILKET EFKKIKVLGS 

       730        740        750        760        770        780 
GAFGTVYKGL WIPEGEKVKI PVAIKELREA TSPKANKEIL DEAYVMASVD NPHVCRLLGI 

       790        800        810        820        830        840 
CLTSTVQLIT QLMPFGCLLD YVREHKDNIG SQYLLNWCVQ IAKGMNYLED RRLVHRDLAA 

       850        860        870        880        890        900 
RNVLVKTPQH VKITDFGLAK LLGAEEKEYH AEGGKVPIKW MALESILHRI YTHQSDVWSY 

       910        920        930        940        950        960 
GVTVWELMTF GSKPYDGIPA SEISSILEKG ERLPQPPICT IDVYMIMVKC WMIDADSRPK 

       970        980        990       1000       1010       1020 
FRELIIEFSK MARDPQRYLV IQGDERMHLP SPTDSNFYRA LMDEEDMDDV VDADEYLIPQ 

      1030       1040       1050       1060       1070       1080 
QGFFSSPSTS RTPLLSSLSA TSNNSTVACI DRNGLQSCPI KEDSFLQRYS SDPTGALTED 

      1090       1100       1110       1120       1130       1140 
SIDDTFLPVP EYINQSVPKR PAGSVQNPVY HNQPLNPAPS RDPHYQDPHS TAVGNPEYLN 

      1150       1160       1170       1180       1190       1200 
TVQPTCVNST FDSPAHWAQK GSHQISLDNP DYQQDFFPKE AKPNGIFKGS TAENAEYLRV 

      1210 
APQSSEFIGA 

« Hide

References

« Hide 'large scale' references
[1]"Evolutionary and biomedical insights from the rhesus macaque genome."
Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C., Makova K.D., Miller W., Milosavljevic A. expand/collapse author list , Palermo R.E., Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., Zwieg A.S.
Science 316:222-234(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 17573.
[2]"Genome sequencing and comparison of two nonhuman primate animal models, the cynomolgus and Chinese rhesus macaques."
Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z., Thompson J.R., Meng Y., Bai Y. expand/collapse author list , Wang J., Zhuo M., Wang T., Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.
Nat. Biotechnol. 29:1019-1023(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"De novo assembly of the rhesus macaque transcriptome from NextGen mRNA sequences."
Pandey S., Maudhoo M.D., Guda C., Ferguson B., Fox H., Norgren R.B.
Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-1210.
Tissue: Caudate nucleus.
[4]"Developmental expression of the genes encoding transforming growth factor alpha and its receptor in the hypothalamus of female rhesus macaques."
Ma Y.J., Costa M.E., Ojeda S.R.
Neuroendocrinology 60:346-359(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 893-977.
Tissue: Hypothalamus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
JH286850 Genomic DNA. No translation available.
CM001255 Genomic DNA. Translation: EHH17303.1.
JU327815 mRNA. Translation: AFE71571.1.
S75916 mRNA. Translation: AAB33095.1.
PIRI78540.
UniGeneMmu.3397.

3D structure databases

ProteinModelPortalP55245.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP55245.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000230982.
InParanoidP55245.
TreeFamTF106002.

Family and domain databases

Gene3D3.80.20.20. 2 hits.
InterProIPR000494. EGF_rcpt_L.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
[Graphical view]
PfamPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFPIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00261. FU. 4 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEGFR_MACMU
AccessionPrimary (citable) accession number: P55245
Secondary accession number(s): F6YXS7, G7ML99, H9FAB2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 22, 2014
Last modified: April 16, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families