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Reviewed, UniProtKB/Swiss-Prot P00533 (EGFR_HUMAN)

Last modified February 9, 2010. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Epidermal growth factor receptor
    EC=2.7.10.1
Alternative name(s):
    Receptor tyrosine-protein kinase erbB-1
    c-erbB-1
Gene names
Name: EGFR
Synonyms: ERBB1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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General annotation (Comments)

Function

Receptor for EGF, but also for other members of the EGF family, as TGF-alpha, amphiregulin, betacellulin, heparin-binding EGF-like growth factor, GP30 and vaccinia virus growth factor. Is involved in the control of cell growth and differentiation. Phosphorylates MUC1 in breast cancer cells and increases the interaction of MUC1 with SRC and CTNNB1/beta-catenin. Ref.33

Isoform 2 may act as an antagonist of EGF action. Ref.33

Catalytic activity

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

Subunit structure

Binds RIPK1. Interacts (via autophosphorylated C-terminal tail) with CBL. Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B. Interacts (autophosphorylated form) with PIK3C2B; the interaction may be indirect. Interacts with PELP1. Binds MUC1. Interacts with AP2M1. Interacts with GAB2. Ref.33 Ref.26 Ref.28 Ref.31 Ref.32 Ref.37 Ref.42

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Isoform 2: Secreted.

Tissue specificity

Ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers. Ref.40

Post-translational modification

Phosphorylation of Ser-695 is partial and occurs only if Thr-693 is phosphorylated. Ref.17 Ref.25 Ref.30 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39 Ref.41 Ref.43 Ref.44 Ref.45 Ref.47 Ref.49

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 occur.

Involvement in disease

Defects in EGFR are associated with lung cancer [MIM:211980].

Miscellaneous

Binding of EGF to the receptor leads to dimerization, internalization of the EGF-receptor complex, induction of the tyrosine kinase activity, stimulation of cell DNA synthesis, and cell proliferation.

Sequence similarities

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

Contains 1 protein kinase domain.

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Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Tumor suppressor
   DomainRepeat
Signal
Transmembrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processactivation of phospholipase A2 activity by calcium-mediated signaling

Traceable author statement. Source: UniProtKB

activation of phospholipase C activity

Traceable author statement. Source: UniProtKB

cell proliferation

Traceable author statement. Source: ProtInc

cell-cell adhesion

Inferred from mutant phenotype. Source: UniProtKB

epidermal growth factor receptor signaling pathway

Inferred from direct assay. Source: UniProtKB

ossification

Non-traceable author statement. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from direct assay. Source: UniProtKB

positive regulation of cell migration

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of cyclin-dependent protein kinase activity during G1/S

Inferred from direct assay. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from direct assay. Source: UniProtKB

positive regulation of nitric oxide biosynthetic process

Inferred from direct assay. Source: UniProtKB

positive regulation of phosphorylation

Inferred from direct assay. Source: UniProtKB

protein insertion into membrane

Traceable author statement. Source: UniProtKB

regulation of nitric-oxide synthase activity

Inferred from direct assay. Source: UniProtKB

regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype. Source: UniProtKB

response to UV-A

Inferred from direct assay. Source: UniProtKB

   Cellular componentShc-EGFR complex

Inferred from sequence or structural similarity. Source: UniProtKB

basolateral plasma membrane

Inferred from direct assay. Source: UniProtKB

endosome

Inferred from direct assay. Source: UniProtKB

extracellular space Ref.4

Non-traceable author statement. Source: UniProtKB

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: UniProtKB

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP/ERK kinase kinase activity

Non-traceable author statement. Source: UniProtKB

actin filament binding

Inferred from direct assay. Source: UniProtKB

double-stranded DNA binding Ref.22

Non-traceable author statement. Source: UniProtKB

epidermal growth factor receptor activity Ref.22 Ref.24

Inferred from direct assay. Source: UniProtKB

identical protein binding

Inferred from physical interaction. Source: IntAct

protein heterodimerization activity

Inferred from direct assay. Source: UniProtKB

protein phosphatase binding

Inferred from physical interaction. Source: UniProtKB

receptor signaling protein tyrosine kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P00533-1)

Also known as: p170;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P00533-2)

Also known as: p60; Truncated; TEGFR;

The sequence of this isoform differs from the canonical sequence as follows:
     404-405: FL → LS
     406-1210: Missing.
Isoform 3 (identifier: P00533-3)

Also known as: p110;

The sequence of this isoform differs from the canonical sequence as follows:
     628-705: CTGPGLEGCP...GEAPNQALLR → PGNESLKAML...SVIITASSCH
     706-1210: Missing.
Isoform 4 (identifier: P00533-4)

The sequence of this isoform differs from the canonical sequence as follows:
     628-628: C → S
     629-1210: Missing.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.18
Chain25 – 12101186Epidermal growth factor receptor
PRO_0000016665

Regions

Topological domain25 – 645621Extracellular Potential
Transmembrane646 – 66823 Potential
Topological domain669 – 1210542Cytoplasmic Potential
Repeat75 – 300226Approximate
Repeat390 – 600211Approximate
Domain712 – 979268Protein kinase
Nucleotide binding718 – 7269ATP By similarity
Compositional bias1025 – 107147Ser-rich

Sites

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

Amino acid modifications

Modified residue6781Phosphothreonine; by PKC
Modified residue6931Phosphothreonine Ref.17 Ref.30 Ref.34 Ref.38 Ref.41 Ref.43 Ref.44 Ref.45 Ref.47
Modified residue6951Phosphoserine Ref.17 Ref.44 Ref.45
Modified residue7251Phosphothreonine Ref.44
Modified residue8691Phosphotyrosine Ref.39
Modified residue9781Phosphotyrosine Ref.36
Modified residue9911Phosphoserine Ref.34 Ref.38 Ref.43 Ref.44 Ref.45
Modified residue9931Phosphothreonine Ref.45
Modified residue9951Phosphoserine Ref.38 Ref.45
Modified residue9981Phosphotyrosine Ref.35 Ref.38 Ref.45 Ref.49
Modified residue10161Phosphotyrosine Ref.49
Modified residue10251Phosphoserine Ref.44
Modified residue10261Phosphoserine Ref.34 Ref.44
Modified residue10371Phosphoserine Ref.44
Modified residue10391Phosphoserine Ref.44 Ref.45
Modified residue10411Phosphothreonine Ref.45
Modified residue10421Phosphoserine Ref.44 Ref.45
Modified residue10451Phosphoserine Ref.45
Modified residue10641Phosphoserine Ref.38 Ref.44 Ref.45
Modified residue10691Phosphotyrosine Ref.35 Ref.38
Modified residue10701Phosphoserine Ref.17
Modified residue10711Phosphoserine Ref.17
Modified residue10811Phosphoserine Ref.44
Modified residue10921Phosphotyrosine; by autocatalysis Ref.35 Ref.38 Ref.39 Ref.49
Modified residue11101Phosphotyrosine; by autocatalysis Ref.38 Ref.49
Modified residue11381Phosphotyrosine Ref.38 Ref.49
Modified residue11661Phosphoserine Ref.35 Ref.44 Ref.45
Modified residue11721Phosphotyrosine; by autocatalysis Ref.35 Ref.38 Ref.39 Ref.49
Modified residue11971Phosphotyrosine; by autocatalysis Ref.38 Ref.39 Ref.44 Ref.49
Glycosylation561N-linked (GlcNAc...) (complex); atypical; partial Ref.34 Ref.29
CAR_000227
Glycosylation1281N-linked (GlcNAc...) Ref.34 Ref.27
Glycosylation1751N-linked (GlcNAc...) Ref.34 Ref.27
Glycosylation1961N-linked (GlcNAc...) Ref.34
Glycosylation3521N-linked (GlcNAc...) Ref.34 Ref.29 Ref.48
Glycosylation3611N-linked (GlcNAc...) Ref.34 Ref.29
Glycosylation4131N-linked (GlcNAc...) Ref.34 Ref.27 Ref.48
Glycosylation4441N-linked (GlcNAc...) Ref.34 Ref.27
Glycosylation5281N-linked (GlcNAc...) Ref.34 Ref.27
Glycosylation5681N-linked (GlcNAc...); partial Ref.34 Ref.29 Ref.48
Glycosylation6031N-linked (GlcNAc...); partial Ref.34 Ref.29
Disulfide bond31 ↔ 58 Ref.21
Disulfide bond157 ↔ 187 Ref.21
Disulfide bond190 ↔ 199 Ref.21
Disulfide bond194 ↔ 207 Ref.21
Disulfide bond215 ↔ 223 Ref.21
Disulfide bond219 ↔ 231 Ref.21
Disulfide bond232 ↔ 240 Ref.21
Disulfide bond236 ↔ 248 Ref.21
Disulfide bond251 ↔ 260 Ref.21
Disulfide bond264 ↔ 291 Ref.21
Disulfide bond295 ↔ 307 Ref.21
Disulfide bond311 ↔ 326 Ref.21
Disulfide bond329 ↔ 333 Ref.21
Disulfide bond337 ↔ 362 Ref.21
Disulfide bond470 ↔ 499 Ref.21
Disulfide bond506 ↔ 515 Ref.21
Disulfide bond510 ↔ 523 Ref.21
Disulfide bond526 ↔ 535 Ref.21
Disulfide bond539 ↔ 555 Ref.21
Disulfide bond558 ↔ 571 Ref.21
Disulfide bond562 ↔ 579 Ref.21
Disulfide bond582 ↔ 591 Ref.21
Disulfide bond595 ↔ 617 Ref.21
Disulfide bond620 ↔ 628 Ref.21
Disulfide bond624 ↔ 636 Ref.21
Cross-link716Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.20
Cross-link737Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.20
Cross-link754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.20
Cross-link867Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.20
Cross-link929Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.20
Cross-link970Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.20

Natural variations

Alternative sequence404 – 4052FL → LS in isoform 2.
VSP_002887
Alternative sequence406 – 1210805Missing in isoform 2.
VSP_002888
Alternative sequence628 – 70578CTGPG…QALLR → PGNESLKAMLFCLFKLSSCN QSNDGSVSHQSGSPAAQESC LGWIPSLLPSEFQLGWGGCS HLHAWPSASVIITASSCH in isoform 3.
VSP_002889
Alternative sequence6281C → S in isoform 4.
VSP_002891
Alternative sequence629 – 1210582Missing in isoform 4.
VSP_002892
Alternative sequence706 – 1210505Missing in isoform 3.
VSP_002890
Natural variant981R → Q: dbSNP rs17289589. Ref.7
VAR_019293
Natural variant2661P → R: dbSNP rs17336639. Ref.7
VAR_019294
Natural variant5211R → K: dbSNP rs2227983. Ref.7 Ref.53
VAR_019295
Natural variant6741V → I: dbSNP rs17337079. Ref.7
VAR_019296
Natural variant7091E → A in lung cancer. Ref.52
VAR_026084
Natural variant7091E → K in lung cancer. Ref.52
VAR_026085
Natural variant7191G → A in lung cancer. Ref.52
VAR_026086
Natural variant7191G → C in lung cancer. dbSNP rs28929495. Ref.52
VAR_026087
Natural variant7191G → D in lung cancer. Ref.52
VAR_026088
Natural variant7191G → S in lung cancer; somatic mutation. Ref.52 Ref.51
VAR_019297
Natural variant7241G → S in lung cancer. Ref.52
VAR_026089
Natural variant7341E → K in lung cancer. Ref.52
VAR_026090
Natural variant746 – 7505Missing in lung cancer.
VAR_026092
Natural variant7461Missing in lung cancer.
VAR_026091
Natural variant747 – 7493Missing in lung cancer.
VAR_026094
Natural variant7471L → F in lung cancer. Ref.52
VAR_026093
Natural variant7481R → P in lung cancer. Ref.52
VAR_026095
Natural variant752 – 7598Missing in lung cancer.
VAR_026096
Natural variant7871Q → R in lung cancer. Ref.52
VAR_026097
Natural variant7901T → M in lung cancer. Ref.52
VAR_026098
Natural variant8331L → V in lung cancer. Ref.52
VAR_026099
Natural variant8341V → L in lung cancer. Ref.52
VAR_026100
Natural variant8581L → M in lung cancer. Ref.52
VAR_026101
Natural variant8581L → R in lung cancer; somatic mutation. Ref.52 Ref.51
VAR_019298
Natural variant8611L → Q in lung cancer. Ref.52
VAR_026102
Natural variant8731G → E in lung cancer. Ref.52
VAR_026103
Natural variant9621R → G: dbSNP rs17337451. Ref.7
VAR_019299
Natural variant9881H → P: dbSNP rs17290699. Ref.7
VAR_019300
Natural variant10341L → R: dbSNP rs34352568. Ref.53
VAR_042095
Natural variant12101A → V: dbSNP rs35918369. Ref.53
VAR_042096

Experimental info

Mutagenesis10161Y → 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. Ref.31
Mutagenesis10921Y → F: No change in interaction with PIK3C2B. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1016. Ref.31
Mutagenesis11101Y → F: No change in interaction with PIK3C2B. Ref.31
Mutagenesis11721Y → F: No change in interaction with PIK3C2B. Ref.31
Mutagenesis11971Y → 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. Ref.31
Sequence conflict5401N → K in CAA25240. Ref.1

Secondary structure

1 .............................................................................................................................................................................. 1210
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (p170) [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: D8A2A50B4EFB6ED2

FASTA1,210134,277
        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 DFLSNMSMDF 

       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 GIGEFKDSLS 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 
FGTSGQKTKI ISNRGENSCK ATGQVCHALC SPEGCWGPEP RDCVSCRNVS RGRECVDKCN 

       550        560        570        580        590        600 
LLEGEPREFV ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM 

       610        620        630        640        650        660 
GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCPTNG 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

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Isoform 2 (p60) (Truncated) (TEGFR).

Checksum: F5DEB31787EF1822
Show »

FASTA40544,664
Isoform 3 (p110).

Checksum: 4CF149492FF1650C
Show »

FASTA70577,312
Isoform 4.

Checksum: 3A00A5511A3B6AE2
Show »

FASTA62869,228

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References

« Hide 'large scale' references
[1]"Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells."
Ullrich A., Coussens L., Hayflick J.S., Dull T.J., Gray A., Tam A.W., Lee J., Yarden Y., Libermann T.A., Schlessinger J., Downward J., Mayes E.L.V., Whittle N., Waterfield M.D., Seeburg P.H.
Nature 309:418-425(1984) [PubMed: 6328312] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Possible role of variant RNA transcripts in the regulation of epidermal growth factor receptor expression in human placenta."
Ilekis J.V., Stark B.C., Scoccia B.
Mol. Reprod. Dev. 41:149-156(1995) [PubMed: 7654368] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Placenta.
[3]"A 1.8 kb alternative transcript from the human epidermal growth factor receptor gene encodes a truncated form of the receptor."
Reiter J.L., Maihle N.J.
Nucleic Acids Res. 24:4050-4056(1996) [PubMed: 8918811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
Tissue: Placenta.
[4]"Expression of a truncated epidermal growth factor receptor-like protein (TEGFR) in ovarian cancer."
Ilekis J.V., Gariti J., Niederberger C., Scoccia B.
Gynecol. Oncol. 65:36-41(1997) [PubMed: 9103388] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2).
Tissue: Placenta.
[5]"Comparative genomic sequence analysis and isolation of human and mouse alternative EGFR transcripts encoding truncated receptor isoforms."
Reiter J.L., Threadgill D.W., Eley G.D., Strunk K.E., Danielsen A.J., Schehl Sinclair C., Pearsall R.S., Green P.J., Yee D., Lampland A.L., Balasubramaniam S., Crossley T.D., Magnuson T.R., James C.D., Maihle N.J.
Genomics 71:1-20(2001) [PubMed: 11161793] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 3 AND 4).
Tissue: Placenta.
[6]"Cloning of the cDNA for a short EGF receptor from human placenta."
Xu L., Hong A., He X.
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[7]NIEHS SNPs program
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-98; ARG-266; LYS-521; ILE-674; GLY-962 AND PRO-988.
[8]"Human and mouse alternative EGFR transcripts encoding only the extracellular domain of the receptor."
Reiter J.L., Threadgill D.W., Danielsen A.J., Schehl C.M., Lampland A.L., Balasubramaniam S., Crossley T.O., Magnuson T.R., Maihle N.J.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 575-687.
[9]"Expression cloning of human EGF receptor complementary DNA: gene amplification and three related messenger RNA products in A431 cells."
Lin C.R., Chen W.S., Kruiger W., Stolarsky L.S., Weber W., Evans R.M., Verma I.M., Gill G.N., Rosenfeld M.G.
Science 224:843-848(1984) [PubMed: 6326261] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 713-924.
[10]"Human epidermal growth factor receptor cDNA is homologous to a variety of RNAs overproduced in A431 carcinoma cells."
Xu Y.H., Ishii S., Clark A.J.L., Sullivan M., Wilson R.K., Ma D.P., Roe B.A., Merlino G.T., Pastan I.
Nature 309:806-810(1984) [PubMed: 6330563] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 150-962.
[11]"Isolation of an evolutionarily conserved epidermal growth factor receptor cDNA from human A431 carcinoma cells."
Simmen F.A., Gope M.L., Schulz T.Z., Wright D.A., Carpenter G., O'Malley B.W.
Biochem. Biophys. Res. Commun. 124:125-132(1984) [PubMed: 6093780] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1028-1210.
[12]"The human EGF receptor gene: structure of the 110 kb locus and identification of sequences regulating its transcription."
Haley J.D., Whittle N., Bennett P., Kinchington D., Ullrich A., Waterfield M.D.
Oncogene Res. 1:375-396(1987) [PubMed: 3329716] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
[13]"Contributory effects of de novo transcription and premature transcript termination in the regulation of human epidermal growth factor receptor proto-oncogene RNA synthesis."
Haley J.D., Waterfield M.D.
J. Biol. Chem. 266:1746-1753(1991) [PubMed: 1988448] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
[14]"Characterization and sequence of the promoter region of the human epidermal growth factor receptor gene."
Ishii S., Xu Y.H., Stratton R.H., Roe B.A., Merlino G.T., Pastan I.
Proc. Natl. Acad. Sci. U.S.A. 82:4920-4924(1985) [PubMed: 2991899] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
[15]"Production of an epidermal growth factor receptor-related protein."
Weber W., Gill G.N., Spiess J.
Science 224:294-297(1984) [PubMed: 6324343] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 25-49.
[16]Kohda D.
Submitted (SEP-1997) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 540.
[17]"Epidermal growth factor receptor threonine and serine residues phosphorylated in vivo."
Heisermann G.J., Gill G.N.
J. Biol. Chem. 263:13152-13158(1988) [PubMed: 3138233] [Abstract]
Cited for: PROTEIN SEQUENCE OF 687-705; 986-998; 1000-1023; 1026-1030 AND 1068-1077, PHOSPHORYLATION AT THR-693; SER-695; SER-1070 AND SER-1071.
[18]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-39.
[19]"Identification of residues in the nucleotide binding site of the epidermal growth factor receptor/kinase."
Russo M.W., Lukas T.J., Cohen S., Staros J.V.
J. Biol. Chem. 260:5205-5208(1985) [PubMed: 2985580] [Abstract]
Cited for: PROTEIN SEQUENCE OF 740-744 AND 746-747.
[20]"Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain."
Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.
Mol. Cell 21:737-748(2006) [PubMed: 16543144] [Abstract]
Cited for: PROTEIN SEQUENCE OF 861-875 AND 914-932, UBIQUITINATION AT LYS-716; LYS-737; LYS-754; LYS-867; LYS-929 AND LYS-970, MASS SPECTROMETRY.
[21]"Disulfide bond structure of human epidermal growth factor receptor."
Abe Y., Odaka M., Inagaki F., Lax I., Schlessinger J., Kohda D.
J. Biol. Chem. 273:11150-11157(1998) [PubMed: 9556602] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS.
[22]"ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA."
Mroczkowski B., Mosig G., Cohen S.
Nature 309:270-273(1984) [PubMed: 6325948] [Abstract]
Cited for: RECEPTOR ACTIVITY.
[23]"Receptors for epidermal growth factor and other polypeptide mitogens."
Carpenter G.
Annu. Rev. Biochem. 56:881-914(1987) [PubMed: 3039909] [Abstract]
Cited for: REVIEW.
[24]"Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation."
Chen W.S., Lazar C.S., Lund K.A., Welsh J.B., Chang C.P., Walton G.M., Der C.J., Wiley H.S., Gill G.N., Rosenfeld M.G.
Cell 59:33-43(1989) [PubMed: 2790960] [Abstract]
Cited for: LIGAND-BINDING.
[25]"All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor."
Margolis B.L., Lax I., Kris R., Dombalagian M., Honegger A.M., Howk R., Givol D., Ullrich A., Schlessinger J.
J. Biol. Chem. 264:10667-10671(1989) [PubMed: 2543678] [Abstract]
Cited for: PHOSPHORYLATION.
[26]"Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and association with epidermal growth factor (EGF) receptor upon EGF stimulation."
Galisteo M.L., Dikic I., Batzer A.G., Langdon W.Y., Schlessinger J.
J. Biol. Chem. 270:20242-20245(1995) [PubMed: 7657591] [Abstract]
Cited for: INTERACTION WITH CBL.
[27]"Analysis of the glycosylation patterns of the extracellular domain of the epidermal growth factor receptor expressed in Chinese hamster ovary fibroblasts."
Smith K.D., Davies M.J., Bailey D., Renouf D.V., Hounsell E.F.
Growth Factors 13:121-132(1996) [PubMed: 8962717] [Abstract]
Cited for: GLYCOSYLATION AT ASN-128; ASN-175; ASN-413; ASN-444 AND ASN-528.
[28]"Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant mu2 subunit and its effects on endocytosis."
Nesterov A., Carter R.E., Sorkina T., Gill G.N., Sorkin A.
EMBO J. 18:2489-2499(1999) [PubMed: 10228163] [Abstract]
Cited for: INTERACTION WITH AP2M1.
[29]"Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor."
Sato C., Kim J.-H., Abe Y., Saito K., Yokoyama S., Kohda D.
J. Biochem. 127:65-72(2000) [PubMed: 10731668] [Abstract]
Cited for: GLYCOSYLATION AT ASN-56; ASN-352; ASN-361; ASN-568 AND ASN-603.
[30]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, MASS SPECTROMETRY.
Tissue: Epithelium.
[31]"Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors."
Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D., Domin J.
Mol. Cell. Biol. 20:3817-3830(2000) [PubMed: 10805725] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH PIK3C2A AND ERBB2, IDENTIFICATION IN A COMPLEX WITH PIK3C2B AND ERBB2, INTERACTION WITH PIK3C2B, MUTAGENESIS OF TYR-1016; TYR-1092; TYR-1110; TYR-1172 AND TYR-1197.
[32]"The epidermal growth factor receptor engages receptor interacting protein and nuclear factor-kappa B (NF-kappa B)-inducing kinase to activate NF-kappa B. Identification of a novel receptor-tyrosine kinase signalosome."
Habib A.A., Chatterjee S., Park S.-K., Ratan R.R., Lefebvre S., Vartanian T.
J. Biol. Chem. 276:8865-8874(2001) [PubMed: 11116146] [Abstract]
Cited for: INTERACTION WITH RIPK1.
[33]"The epidermal growth factor receptor regulates interaction of the human DF3/MUC1 carcinoma antigen with c-Src and beta-catenin."
Li Y., Ren J., Yu W., Li Q., Kuwahara H., Yin L., Carraway K.L. III, Kufe D.
J. Biol. Chem. 276:35239-35242(2001) [PubMed: 11483589] [Abstract]
Cited for: INTERACTION WITH MUC1, FUNCTION.
[34]"Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR)."
Wu S.L., Kim J., Hancock W.S., Karger B.
J. Proteome Res. 4:1155-1170(2005) [PubMed: 16083266] [Abstract]
Cited for: GLYCOSYLATION AT ASN-56; ASN-128; ASN-175; ASN-196; ASN-352; ASN-361; ASN-413; ASN-444; ASN-528; ASN-568 AND ASN-603, PHOSPHORYLATION AT THR-693; SER-991 AND SER-1026, MASS SPECTROMETRY.
[35]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-998; TYR-1069; TYR-1092; SER-1166 AND TYR-1172, MASS SPECTROMETRY.
Tissue: Epithelium.
[36]"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC."
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J.
Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-978, MASS SPECTROMETRY.
Tissue: Hepatocyte.
[37]"Functional implications of altered subcellular localization of PELP1 in breast cancer cells."
Vadlamudi R.K., Manavathi B., Balasenthil S., Nair S.S., Yang Z., Sahin A.A., Kumar R.
Cancer Res. 65:7724-7732(2005) [PubMed: 16140940] [Abstract]
Cited for: INTERACTION WITH PELP1.
[38]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-991; SER-995; TYR-998; SER-1064; TYR-1069; TYR-1092; TYR-1110; TYR-1138; TYR-1172 AND TYR-1197, MASS SPECTROMETRY.
Tissue: Epithelium.
[39]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-869; TYR-1092; TYR-1172 AND TYR-1197, MASS SPECTROMETRY.
[40]"Impaired basolateral sorting of pro-EGF causes isolated recessive renal hypomagnesemia."
Groenestege W.M.T., Thebault S., van der Wijst J., van den Berg D., Janssen R., Tejpar S., van den Heuvel L.P., van Cutsem E., Hoenderop J.G., Knoers N.V., Bindels R.J.
J. Clin. Invest. 117:2260-2267(2007) [PubMed: 17671655] [Abstract]
Cited for: TISSUE SPECIFICITY.
[41]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, MASS SPECTROMETRY.
[42]"Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein."
Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M., James D.E., Daly R.J.
EMBO J. 27:2305-2316(2008) [PubMed: 19172738] [Abstract]
Cited for: INTERACTION WITH GAB2.
[43]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693 AND SER-991, MASS SPECTROMETRY.
[44]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-695; THR-725; SER-991; SER-1025; SER-1026; SER-1037; SER-1039; SER-1042; SER-1064; SER-1081; SER-1166 AND TYR-1197, MASS SPECTROMETRY.
[45]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-695; SER-991; THR-993; SER-995; TYR-998; SER-1039; THR-1041; SER-1042; SER-1045; SER-1064 AND SER-1166, MASS SPECTROMETRY.
[46]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[47]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, MASS SPECTROMETRY.
[48]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352; ASN-413 AND ASN-568, MASS SPECTROMETRY.
Tissue: Liver.
[49]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-998; TYR-1016; TYR-1092; TYR-1110; TYR-1138; TYR-1172 AND TYR-1197, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[50]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, MASS SPECTROMETRY.
[51]"EGFR mutations in lung cancer: correlation with clinical response to gefitinib therapy."
Paez J.G., Janne P.A., Lee J.C., Tracy S., Greulich H., Gabriel S., Herman P., Kaye F.J., Lindeman N., Boggon T.J., Naoki K., Sasaki H., Fujii Y., Eck M.J., Sellers W.R., Johnson B.E., Meyerson M.
Science 304:1497-1500(2004) [PubMed: 15118125] [Abstract]
Cited for: VARIANTS LUNG CANCER SER-719 AND ARG-858.
[52]"Distinct epidermal growth factor receptor and KRAS mutation patterns in non-small cell lung cancer patients with different tobacco exposure and clinicopathologic features."
Tam I.Y.S., Chung L.P., Suen W.S., Wang E., Wong M.C.M., Ho K.K., Lam W.K., Chiu S.W., Girard L., Minna J.D., Gazdar A.F., Wong M.P.
Clin. Cancer Res. 12:1647-1653(2006) [PubMed: 16533793] [Abstract]
Cited for: VARIANTS LUNG CANCER ALA-709; LYS-709; ALA-719; ASP-719; CYS-719; SER-719; SER-724; LYS-734; GLU-746 DEL; PHE-747; 747-LEU--GLU-749 DEL; PRO-748; 752-SER--ILE-759 DEL; ARG-787; MET-790; VAL-833; LEU-834; MET-858; ARG-858; GLN-861 AND GLU-873.
[53]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-521; ARG-1034 AND VAL-1210.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X00588 mRNA. Translation: CAA25240.1.
U95089 mRNA. Translation: AAB53063.1.
U48722 mRNA. Translation: AAC50802.1.
U48723 Genomic DNA. Translation: AAC50804.1.
U48724 Genomic DNA. Translation: AAC50796.1.
U48725 Genomic DNA. Translation: AAC50797.1.
U48726 Genomic DNA. Translation: AAC50798.1.
U48727 Genomic DNA. Translation: AAC50799.1.
U48728 Genomic DNA. Translation: AAC50800.1.
U48729 Genomic DNA. Translation: AAC50801.1.
AF288738 Genomic DNA. Translation: AAG35786.1.
AF288738 Genomic DNA. Translation: AAG35787.1.
AF288738 Genomic DNA. Translation: AAG35788.1.
AF288738 Genomic DNA. Translation: AAG35789.1.
AF288738 Genomic DNA. Translation: AAG35790.1.
AY698024 mRNA. Translation: AAT97979.1.
AY588246 Genomic DNA. Translation: AAS83109.1.
AF277897 mRNA. Translation: AAK01080.1.
AF125253 mRNA. Translation: AAG43240.1.
AF125539, AF125538 Genomic DNA. Translation: AAG43243.1.
X06370 Genomic DNA. Translation: CAA29668.1.
X00663 mRNA. Translation: CAA25282.1.
M38425 Genomic DNA. Translation: AAA63171.1.
M11234 Genomic DNA. Translation: AAA52370.1.
IPIIPI00018274.
IPI00221346.
IPI00221347.
IPI00221348.
PIRGQHUE. A00641.
RefSeqNP_005219.2.
NP_958439.1.
NP_958440.1.
NP_958441.1.
UniGeneHs.488293

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
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/D335-538[»]
3GOPX-ray2.80A669-1022[»]
3GT8X-ray2.96A/B/C/D696-1022[»]
DisProtDP00309.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-405N.
DIP-5764N.
IntActP00533. 113 interactions.
STRINGP00533.

PTM databases

GlycoSuiteDBP00533.
PhosphoSiteP00533.

2-D gel databases

SWISS-2DPAGEP00533.

Proteomic databases

PeptideAtlasP00533.
PRIDEP00533.

Genome annotation databases

EnsemblENST00000275493; ENSP00000275493; ENSG00000146648; Homo sapiens. [Genome view]
GeneID1956.
KEGGhsa:1956.
UCSCuc003tqi.1. human.
uc003tqj.1. human.
uc003tqk.1. human.

Organism-specific databases

CTD1956.
GeneCardsGC07P055054.
H-InvDBHIX0025274.
HIX0025338.
HGNCHGNC:3236. EGFR.
HPACAB000035.
HPA001200.
HPA018530.
MIM131550. gene.
211980. phenotype.
Orphanet360. Glioblastoma.
PharmGKBPA7360.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP00533.
InParanoidP00533.
OMAEFKKIKV.
PhylomeDBP00533.

Enzyme and pathway databases

BRENDA2.7.10.1. 247.
Pathway_Interaction_DBa6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
arf6cyclingpathway. Arf6 signaling events.
endothelinpathway. Endothelins.
lysophospholipid_pathway. LPA receptor mediated events.
telomerasepathway. Regulation of Telomerase.
ptp1bpathway. Signaling events mediated by PTP1B.
syndecan_3_pathway. Syndecan-3-mediated signaling events.
txa2pathway. Thromboxane A2 receptor signaling.
ReactomeREACT_9417. Signaling by EGFR.

Gene expression databases

ArrayExpressP00533.
BgeeP00533.
GenevestigatorP00533.
GermOnlineENSG00000146648. Homo sapiens.

Family and domain databases

InterProIPR000494. EGF_rcpt_L.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
[Graphical view]
PANTHERPTHR23256. Tyr_prot_kinase. 1 hit.
PfamPF00757. Furin-like. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFPIRSF000619. TyrPK_EGF-R. 1 hit.
SMARTSM00261. FU. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00002. Cetuximab.
DB00530. Erlotinib.
DB00317. Gefitinib.
DB01259. Lapatinib.
DB00281. Lidocaine.
DB01269. Panitumumab.
DB00072. Trastuzumab.
NextBio7931.
PMAP-CutDBP00533.
SOURCESearch...

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Entry information

Entry nameEGFR_HUMAN
AccessionPrimary (citable) accession number: P00533
Secondary accession number(s): O00688 expand/collapse secondary AC list , O00732, P06268, Q14225, Q68GS5, Q92795, Q9BZS2, Q9GZX1, Q9H2C9, Q9H3C9, Q9UMD7, Q9UMD8, Q9UMG5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: February 9, 2010
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Relevant documents

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents