logo CaMPDB: Calpain for Modulatory Proteolysis Database

SB0050 : EGFR, ErbB-1, Epidermal growth factor receptor

[ CaMP Format ]

* Basic Information

OrganismHomo sapiens (human)
Protein Namesepidermal growth factor receptor isoform a precursor [Homo sapiens]; epidermal growth factor receptor isoform a precursor; avian erythroblastic leukemia viral (v-erb-b) oncogene homolog; cell proliferation-inducing protein 61; cell growth inhibiting protein 40; proto-oncogene c-ErbB-1; receptor tyrosine-protein kinase erbB-1; Epidermal growth factor receptor;; Proto-oncogene c-ErbB-1; Receptor tyrosine-protein kinase erbB-1
Gene NamesEGFR; ERBB, ERBB1, HER1; ERBB; ERBB1; HER1; epidermal growth factor receptor
Gene Locus7p12; chromosome 7
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_005219 NM_005228 1956 P00533 131550 HGNC:3236 N/A hsa:1956

* Information From OMIM

Description: EGFR and its ligands are cell signaling molecules involved in diverse cellular functions, including cell proliferation, differentiation, motility, and survival, and in tissue development (Wang et al., 2004).

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* Structure Information

1. Primary Information

Length: 1210 aa

Average Mass: 134.276 kDa

Monoisotopic Mass: 134.190 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
Receptor L domain 1. 571671.00.7
Growth factor receptor domain IV 1. 29434218.010.6
Furin-like cysteine rich region 1. 55459849.011.7
Furin-like cysteine rich region 2. 61863649.03.6
GRB2-binding adapter (GAPT) 1. 65068713.00.3
--- cleavage 683 (inside GRB2-binding adapter (GAPT) 650..687) ---
--- cleavage 733 ---
Phosphotransferase enzyme family 1. 824860162.00.0

3. Sequence Information

Fasta Sequence: SB0050.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 1DNQ (Model; -; A=25-336), 1DNR (Model; -; A=337-645), 1IVO (X-ray; 330 A; A/B=25-646), 1M14 (X-ray; 260 A; A=695-1022), 1M17 (X-ray; 260 A; A=695-1022), 1MOX (X-ray; 250 A; A/B=25-525), 1NQL (X-ray; 280 A; A=25-642), 1XKK (X-ray; 240 A; A=695-1022), 1YY9 (X-ray; 260 A; A=25-642), 1Z9I (NMR; -; A=669-721), 2EB2 (X-ray; 250 A; A=695-1022), 2EB3 (X-ray; 284 A; A=695-1022), 2EXP (Model; -; A=311-326), 2EXQ (Model; -; A=27-536), 2GS2 (X-ray; 280 A; A=696-1022), 2GS6 (X-ray; 260 A; A=696-1022), 2GS7 (X-ray; 260 A; A/B=696-1022), 2ITN (X-ray; 247 A; A=696-1019), 2ITO (X-ray; 325 A; A=696-1022), 2ITP (X-ray; 274 A; A=696-1022), 2ITQ (X-ray; 268 A; A=696-1022), 2ITT (X-ray; 273 A; A=696-1022), 2ITU (X-ray; 280 A; A=696-1022), 2ITV (X-ray; 247 A; A=696-1022), 2ITW (X-ray; 288 A; A=696-1022), 2ITX (X-ray; 298 A; A=696-1022), 2ITY (X-ray; 342 A; A=696-1022), 2ITZ (X-ray; 272 A; A=696-1022), 2J5E (X-ray; 310 A; A=696-1022), 2J5F (X-ray; 300 A; A=696-1022), 2J6M (X-ray; 310 A; A=696-1022), 2JIT (X-ray; 310 A; A/B=696-1022), 2JIU (X-ray; 305 A; A/B=695-1022), 2JIV (X-ray; 350 A; A/B=695-1022), 2KS1 (NMR; -; B=634-677), 2M0B (NMR; -; A/B=634-677), 2M20 (NMR; -; A/B=642-697), 2RF9 (X-ray; 350 A; A/B=696-1022), 2RFD (X-ray; 360 A; A/B=702-1022), 2RFE (X-ray; 290 A; A/B/C/D=702-1022), 2RGP (X-ray; 200 A; A=702-1016), 3B2U (X-ray; 258 A; A/B/E/I/M/P/S/V=335-538), 3B2V (X-ray; 330 A; A=25-642), 3BEL (X-ray; 230 A; A=702-1016), 3BUO (X-ray; 260 A; A/C=1063-1075), 3C09 (X-ray; 320 A; A/D=336-538), 3G5V (X-ray; 200 A; C=311-326), 3G5Y (X-ray; 159 A; E=311-326), 3GOP (X-ray; 280 A; A=669-1022), 3GT8 (X-ray; 296 A; A/B/C/D=696-1022), 3IKA (X-ray; 290 A; A/B=694-1022), 3LZB (X-ray; 270 A; A/B/C/D/E/F/G/H=696-983), 3NJP (X-ray; 330 A; A/B=25-638), 3OB2 (X-ray; 210 A; A=1063-1074), 3OP0 (X-ray; 252 A; C/D=1066-1076), 3P0Y (X-ray; 180 A; A=334-538), 3PFV (X-ray; 227 A; C/D=1066-1076), 3POZ (X-ray; 150 A; A=696-1022), 3QWQ (X-ray; 275 A; A=1-642), 3UG1 (X-ray; 275 A; A=695-1022), 3UG2 (X-ray; 250 A; A=695-1022), 3VJN (X-ray; 234 A; A=695-1022), 3VJO (X-ray; 264 A; A=695-1022), 3VRP (X-ray; 152 A; B=1062-1074), 3VRR (X-ray; 200 A; C=1062-1074), 3W2O (X-ray; 235 A; A=698-1022), 3W2P (X-ray; 205 A; A=698-1022), 3W2Q (X-ray; 220 A; A=698-1022), 3W2R (X-ray; 205 A; A=698-1022), 3W2S (X-ray; 190 A; A=696-1022), 3W32 (X-ray; 180 A; A=696-1022), 3W33 (X-ray; 170 A; A=696-1022), 4G5J (X-ray; 280 A; A=696-1022), 4G5P (X-ray; 317 A; A/B=696-1022), 4HJO (X-ray; 275 A; A=696-1022), 4I1Z (X-ray; 300 A; A=695-1022), 4I20 (X-ray; 334 A; A=695-1022), 4I21 (X-ray; 337 A; A/B=695-1022), 4I22 (X-ray; 171 A; A=695-1022), 4I23 (X-ray; 280 A; A=695-1022), 4I24 (X-ray; 180 A; A/B=695-1022), 4JQ7 (X-ray; 273 A; A=696-1021), 4JQ8 (X-ray; 283 A; A=696-1021), 4JR3 (X-ray; 270 A; A=696-1021), 4JRV (X-ray; 280 A; A=696-1021), 4KRL (X-ray; 285 A; A=335-538), 4KRM (X-ray; 266 A; A/C/E/G/I/K=335-538), 4KRO (X-ray; 305 A; A=25-642), 4KRP (X-ray; 282 A; A=25-642), 4LI5 (X-ray; 264 A; A=696-1020), 4LL0 (X-ray; 400 A; A/B=694-1022), 4LQM (X-ray; 250 A; A=694-1022), 4LRM (X-ray; 353 A; A/B/C/D/E=694-1022), 4R5S (X-ray; 300 A; A=696-1022), 4RIW (X-ray; 310 A; B/D=682-1022), 4RIX (X-ray; 310 A; B/D=682-1022), 4RIY (X-ray; 298 A; B/D=682-1022), 4RJ4 (X-ray; 278 A; A=695-1022), 4RJ5 (X-ray; 310 A; A=695-1022), 4RJ6 (X-ray; 270 A; A=695-1022), 4RJ7 (X-ray; 255 A; A=695-1022), 4RJ8 (X-ray; 250 A; A=695-1022), 4TKS (X-ray; 320 A; A=695-1022), 4WKQ (X-ray; 185 A; A=696-1022), 4WRG (X-ray; 190 A; A=696-1022)

* Cleavage Information

7 [sites] cleaved by Calpain 2

Source Reference: [PubMed ID: 8055914] Gregoriou M, Willis AC, Pearson MA, Crawford C, The calpain cleavage sites in the epidermal growth factor receptor kinase domain. Eur J Biochem. 1994 Jul 15;223(2):455-64.

Cleavage sites (±10aa)


Leu683 Gln

iTraq-117 Signal 3131.0 () for VRKRTLRRLL

iTraq-117 Signal 3354.7 () for QERELVEPLT

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)


Pro733 Glu

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)


Ser1030 Arg

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)


Pro1059 Ile

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)


Phe1086 Leu

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)


Phe1151 Asp

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)


Gly1185 Ile

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)

* References

[PubMed ID: 25002532] Schaeffer D, Somarelli JA, Hanna G, Palmer GM, Garcia-Blanco MA, Cellular migration and invasion uncoupled: increased migration is not an inexorable consequence of epithelial-to-mesenchymal transition. Mol Cell Biol. 2014 Sep 15;34(18):3486-99. doi: 10.1128/MCB.00694-14. Epub 2014

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