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Sample Preparation and Post-separation Analysis



Searching in 'SWISS-2DPAGE' for entry matching: P00533




SWISS-2DPAGE:  P00533


P00533


General information about the entry
View entry in simple text format
Entry nameEGFR_HUMAN
Primary accession numberP00533
integrated into SWISS-2DPAGE on September 1, 1997 (release 6)
2D Annotations were last modified onMay 15, 2003 (version 1)
General Annotations were last modified on May 19, 2011 (version 13)
Name and origin of the protein
DescriptionRecName: Full=Epidermal growth factor receptor; EC=2.7.10.1; AltName: Full=Proto-oncogene c-ErbB-1; AltName: Full=Receptor tyrosine-protein kinase erbB-1; Flags: Precursor;.
Gene nameName=EGFR
Synonyms=ERBB1
Annotated speciesHomo sapiens (Human) [TaxID: 9606]
TaxonomyEukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
References
[1]   MAPPING ON GEL
MEDLINE=98163346; PubMed=9504818; [NCBI, ExPASy, EBI, Israel, Japan]
Reymond M.A., Sanchez J.-C., Hughes G.J., Riese J., Tortola S., Peinado M.A., Kirchner T., Hohenberger W., Hochstrasser D.F., Kockerling F.
''''''Standardized characterization of gene expression in human colorectal epithelium by two-dimensional electrophoresis'';'';''
Electrophoresis 18(1):2842-2848(1997)
2D PAGE maps for identified proteins
How to interpret a protein

CEC_HUMAN {Colorectal epithelia cells}
Homo sapiens (Human)
Tissue: Colon epithelium
CEC_HUMAN
  map experimental info
  protein estimated location
 
CEC_HUMAN

MAP LOCATIONS:
pI=5.85; Mw=151853
pI=5.93; Mw=151853
pI=5.73; Mw=150458

MAPPING (identification):
IMMUNODETECTION [1].

Copyright
This SWISS-2DPAGE entry is copyright the Swiss Institute of Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See http://world-2dpage.expasy.org/swiss-2dpage/docs/license.html or send email from license@isb-sib.ch).
Cross-references
UniProtKB/Swiss-ProtP00533; EGFR_HUMAN.
2D PAGE maps for identified proteins
  • How to interpret a protein map
  • You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw.
  • Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly.
  • Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed.



External data extracted from UniProtKB/Swiss-Prot
Extracted from UniProtKB/Swiss-Prot, release: 2011_10
Entry nameEGFR_HUMAN
Primary accession numberP00533
Secondary accession number(s) O00688 O00732 P06268 Q14225 Q68GS5 Q92795 Q9BZS2 Q9GZX1 Q9H2C9 Q9H3C9 Q9UMD7 Q9UMD8 Q9UMG5
Sequence was last modified on November 1, 1997 (version 2)
Annotations were last modified on October 19, 2011 (version 176)
Name and origin of the protein
DescriptionRecName: Full=Epidermal growth factor receptor; EC=2.7.10.1; AltName: Full=Proto-oncogene c-ErbB-1; AltName: Full=Receptor tyrosine-protein kinase erbB-1; Flags: Precursor;
Gene nameName=EGFR
Synonyms=ERBB1
Encoded onName=EGFR; Synonyms=ERBB1
Keywords3D-structure; Alternative splicing; ATP-binding; Cell membrane; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; Isopeptide bond; Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; Secreted; Signal; Transferase; Transmembrane; Transmembrane helix; Tumor suppressor; Tyrosine-protein kinase; Ubl conjugation.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLX00588; CAA25240.1; -; mRNA
EMBLU95089; AAB53063.1; -; mRNA
EMBLU48722; AAC50802.1; -; mRNA
EMBLU48723; AAC50804.1; -; Genomic_DNA
EMBLU48724; AAC50796.1; -; Genomic_DNA
EMBLU48725; AAC50797.1; -; Genomic_DNA
EMBLU48726; AAC50798.1; -; Genomic_DNA
EMBLU48727; AAC50799.1; -; Genomic_DNA
EMBLU48728; AAC50800.1; -; Genomic_DNA
EMBLU48729; AAC50801.1; -; Genomic_DNA
EMBLAF288738; AAG35786.1; -; Genomic_DNA
EMBLAF288738; AAG35787.1; -; Genomic_DNA
EMBLAF288738; AAG35788.1; -; Genomic_DNA
EMBLAF288738; AAG35789.1; -; Genomic_DNA
EMBLAF288738; AAG35790.1; -; Genomic_DNA
EMBLAY698024; AAT97979.1; -; mRNA
EMBLAY588246; AAS83109.1; -; Genomic_DNA
EMBLAF277897; AAK01080.1; -; mRNA
EMBLAF125253; AAG43240.1; -; mRNA
EMBLAF125539; AAG43243.1; -; Genomic_DNA
EMBLAF125538; AAG43243.1; JOINED; Genomic_DNA
EMBLX06370; CAA29668.1; -; Genomic_DNA
EMBLX00663; CAA25282.1; -; mRNA
EMBLM38425; AAA63171.1; -; Genomic_DNA
EMBLM11234; AAA52370.1; -; Genomic_DNA
IPIIPI00018274; -; .
IPIIPI00221346; -; .
IPIIPI00221347; -; .
IPIIPI00221348; -; .
PIRA00641; GQHUE; .
RefSeqNP_005219.2; NM_005228.3; .
RefSeqNP_958439.1; NM_201282.1; .
RefSeqNP_958440.1; NM_201283.1; .
RefSeqNP_958441.1; NM_201284.1; .
UniGeneHs.488293; -; .
PDB1DNQ; Model; -; A=25-336
PDB1DNR; Model; -; A=337-645
PDB1IVO; X-ray; 3.30 A; A/B=25-646
PDB1M14; X-ray; 2.60 A; A=695-1022
PDB1M17; X-ray; 2.60 A; A=695-1022
PDB1MOX; X-ray; 2.50 A; A/B=25-525
PDB1NQL; X-ray; 2.80 A; A=25-642
PDB1XKK; X-ray; 2.40 A; A=695-1022
PDB1YY9; X-ray; 2.60 A; A=25-642
PDB1Z9I; NMR; -; A=669-721
PDB2EB2; X-ray; 2.50 A; A=695-1022
PDB2EB3; X-ray; 2.84 A; A=695-1022
PDB2EXP; Model; -; A=311-326
PDB2EXQ; Model; -; A=27-536
PDB2GS2; X-ray; 2.80 A; A=696-1022
PDB2GS6; X-ray; 2.60 A; A=696-1022
PDB2GS7; X-ray; 2.60 A; A/B=696-1022
PDB2ITN; X-ray; 2.47 A; A=696-1019
PDB2ITO; X-ray; 3.25 A; A=696-1022
PDB2ITP; X-ray; 2.74 A; A=696-1022
PDB2ITQ; X-ray; 2.68 A; A=696-1022
PDB2ITT; X-ray; 2.73 A; A=696-1022
PDB2ITU; X-ray; 2.80 A; A=696-1022
PDB2ITV; X-ray; 2.47 A; A=696-1022
PDB2ITW; X-ray; 2.88 A; A=696-1022
PDB2ITX; X-ray; 2.98 A; A=696-1022
PDB2ITY; X-ray; 3.42 A; A=696-1022
PDB2ITZ; X-ray; 2.72 A; A=696-1022
PDB2J5E; X-ray; 3.10 A; A=696-1022
PDB2J5F; X-ray; 3.00 A; A=696-1022
PDB2J6M; X-ray; 3.10 A; A=696-1022
PDB2JIT; X-ray; 3.10 A; A/B=696-1022
PDB2JIU; X-ray; 3.05 A; A/B=695-1022
PDB2JIV; X-ray; 3.50 A; A/B=695-1022
PDB2KS1; NMR; -; B=634-677
PDB2RF9; X-ray; 3.50 A; A/B=696-1022
PDB2RFD; X-ray; 3.60 A; A/B=702-1022
PDB2RFE; X-ray; 2.90 A; A/B/C/D=702-1022
PDB2RGP; X-ray; 2.00 A; A=702-1016
PDB3B2U; X-ray; 2.58 A; A/B/E/I/M/P/S/V=335-538
PDB3B2V; X-ray; 3.30 A; A=25-642
PDB3BEL; X-ray; 2.30 A; A=702-1016
PDB3BUO; X-ray; 2.60 A; A/C=1063-1075
PDB3C09; X-ray; 3.20 A; A/D=335-538
PDB3G5V; X-ray; 2.00 A; C=311-326
PDB3G5Y; X-ray; 1.59 A; E=311-326
PDB3GOP; X-ray; 2.80 A; A=669-1022
PDB3GT8; X-ray; 2.96 A; A/B/C/D=696-1022
PDB3IKA; X-ray; 2.90 A; A/B=694-1022
PDB3LZB; X-ray; 2.70 A; A/B/C/D/E/F/G/H=696-983
PDB3NJP; X-ray; 3.30 A; A/B=25-638
PDB3OB2; X-ray; 2.10 A; A=1063-1074
PDB3OP0; X-ray; 2.52 A; C/D=1066-1076
PDB3PFV; X-ray; 2.27 A; C/D=1066-1076
PDB3POZ; X-ray; 1.50 A; A=696-1022
PDBsum1DNQ; -; .
PDBsum1DNR; -; .
PDBsum1IVO; -; .
PDBsum1M14; -; .
PDBsum1M17; -; .
PDBsum1MOX; -; .
PDBsum1NQL; -; .
PDBsum1XKK; -; .
PDBsum1YY9; -; .
PDBsum1Z9I; -; .
PDBsum2EB2; -; .
PDBsum2EB3; -; .
PDBsum2EXP; -; .
PDBsum2EXQ; -; .
PDBsum2GS2; -; .
PDBsum2GS6; -; .
PDBsum2GS7; -; .
PDBsum2ITN; -; .
PDBsum2ITO; -; .
PDBsum2ITP; -; .
PDBsum2ITQ; -; .
PDBsum2ITT; -; .
PDBsum2ITU; -; .
PDBsum2ITV; -; .
PDBsum2ITW; -; .
PDBsum2ITX; -; .
PDBsum2ITY; -; .
PDBsum2ITZ; -; .
PDBsum2J5E; -; .
PDBsum2J5F; -; .
PDBsum2J6M; -; .
PDBsum2JIT; -; .
PDBsum2JIU; -; .
PDBsum2JIV; -; .
PDBsum2KS1; -; .
PDBsum2RF9; -; .
PDBsum2RFD; -; .
PDBsum2RFE; -; .
PDBsum2RGP; -; .
PDBsum3B2U; -; .
PDBsum3B2V; -; .
PDBsum3BEL; -; .
PDBsum3BUO; -; .
PDBsum3C09; -; .
PDBsum3G5V; -; .
PDBsum3G5Y; -; .
PDBsum3GOP; -; .
PDBsum3GT8; -; .
PDBsum3IKA; -; .
PDBsum3LZB; -; .
PDBsum3NJP; -; .
PDBsum3OB2; -; .
PDBsum3OP0; -; .
PDBsum3PFV; -; .
PDBsum3POZ; -; .
ProteinModelPortalP00533; -; .
SMRP00533; 26-1003; .
DisProtDP00309; -; .
DIPDIP-405N; -; .
DIPDIP-5764N; -; .
IntActP00533; 125; .
MINTMINT-206389; -; .
STRINGP00533; -; .
GlycoSuiteDBP00533; -; .
PhosphoSiteP00533; -; .
SWISS-2DPAGEP00533; -; .
PeptideAtlasP00533; -; .
PRIDEP00533; -; .
EnsemblENST00000275493; ENSP00000275493; ENSG00000146648; .
GeneID1956; -; .
KEGGhsa:1956; -; .
UCSCuc003tqi.1; human; .
UCSCuc003tqj.1; human; .
UCSCuc003tqk.1; human; .
CTD1956; -; .
GeneCardsGC07P054860; -; .
H-InvDBHIX0025338; -; .
HGNCHGNC:3236; EGFR; .
HPACAB000035; -; .
HPAHPA001200; -; .
HPAHPA018530; -; .
MIM131550; gene; .
MIM211980; phenotype; .
neXtProtNX_P00533; -; .
Orphanet360; Glioblastoma; .
PharmGKBPA7360; -; .
HOVERGENHBG000490; -; .
InParanoidP00533; -; .
OMAMRRRHIV; -; .
PhylomeDBP00533; -; .
BRENDA2.7.10.1; 2681; .
Pathway_Interaction_DBa6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling; .
Pathway_Interaction_DBarf6cyclingpathway; Arf6 signaling events; .
Pathway_Interaction_DBendothelinpathway; Endothelins; .
Pathway_Interaction_DBlysophospholipid_pathway; LPA receptor mediated events; .
Pathway_Interaction_DBtelomerasepathway; Regulation of Telomerase; .
Pathway_Interaction_DBptp1bpathway; Signaling events mediated by PTP1B; .
Pathway_Interaction_DBsyndecan_3_pathway; Syndecan-3-mediated signaling events; .
Pathway_Interaction_DBtxa2pathway; Thromboxane A2 receptor signaling; .
ReactomeREACT_18266; Axon guidance; .
ReactomeREACT_9417; Signaling by EGFR; .
DrugBankDB00002; Cetuximab; .
DrugBankDB00530; Erlotinib; .
DrugBankDB00317; Gefitinib; .
DrugBankDB01259; Lapatinib; .
DrugBankDB00281; Lidocaine; .
DrugBankDB01269; Panitumumab; .
DrugBankDB00072; Trastuzumab; .
NextBio7931; -; .
PMAP-CutDBP00533; -; .
ArrayExpressP00533; -; .
BgeeP00533; -; .
GenevestigatorP00533; -; .
GermOnlineENSG00000146648; Homo sapiens; .
GOGO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL; .
GOGO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell; .
GOGO:0005768; C:endosome; IDA:UniProtKB; .
GOGO:0005615; C:extracellular space; NAS:UniProtKB; .
GOGO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell; .
GOGO:0016021; C:integral to membrane; IEA:UniProtKB-KW; .
GOGO:0045121; C:membrane raft; IDA:UniProtKB; .
GOGO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell; .
GOGO:0070435; C:Shc-EGFR complex; ISS:BHF-UCL; .
GOGO:0051015; F:actin filament binding; IDA:UniProtKB; .
GOGO:0005524; F:ATP binding; IEA:UniProtKB-KW; .
GOGO:0003690; F:double-stranded DNA binding; NAS:UniProtKB; .
GOGO:0005006; F:epidermal growth factor-activated receptor activity; IDA:UniProtKB; .
GOGO:0004710; F:MAP/ERK kinase kinase activity; NAS:UniProtKB; .
GOGO:0046982; F:protein heterodimerization activity; IDA:UniProtKB; .
GOGO:0019903; F:protein phosphatase binding; IPI:UniProtKB; .
GOGO:0004716; F:receptor signaling protein tyrosine kinase activity; IEA:InterPro; .
GOGO:0043006; P:activation of phospholipase A2 activity by calcium-mediated signaling; TAS:UniProtKB; .
GOGO:0007202; P:activation of phospholipase C activity; TAS:UniProtKB; .
GOGO:0007411; P:axon guidance; TAS:Reactome; .
GOGO:0008283; P:cell proliferation; TAS:ProtInc; .
GOGO:0016337; P:cell-cell adhesion; IMP:UniProtKB; .
GOGO:0043066; P:negative regulation of apoptosis; IMP:UniProtKB; .
GOGO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome; .
GOGO:0001503; P:ossification; NAS:UniProtKB; .
GOGO:0035413; P:positive regulation of catenin import into nucleus; IMP:BHF-UCL; .
GOGO:0030335; P:positive regulation of cell migration; IMP:UniProtKB; .
GOGO:0031659; P:positive regulation of cyclin-dependent protein kinase activity involved in G1/S; IDA:BHF-UCL; .
GOGO:0050679; P:positive regulation of epithelial cell proliferation; IDA:UniProtKB; .
GOGO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB; .
GOGO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:UniProtKB; .
GOGO:0042327; P:positive regulation of phosphorylation; IDA:UniProtKB; .
GOGO:0051897; P:positive regulation of protein kinase B signaling cascade; IMP:BHF-UCL; .
GOGO:0046777; P:protein autophosphorylation; IMP:UniProtKB; .
GOGO:0051205; P:protein insertion into membrane; TAS:UniProtKB; .
GOGO:0050999; P:regulation of nitric-oxide synthase activity; IDA:UniProtKB; .
GOGO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:UniProtKB; .
GOGO:0006950; P:response to stress; NAS:UniProtKB; .
GOGO:0070141; P:response to UV-A; IDA:BHF-UCL; .
InterProIPR000494; EGF_rcpt_L; .
InterProIPR006211; Furin-like_Cys-rich_dom; .
InterProIPR006212; Furin_repeat; .
InterProIPR009030; Growth_fac_rcpt; .
InterProIPR011009; Kinase-like_dom; .
InterProIPR000719; Prot_kinase_cat_dom; .
InterProIPR017441; Protein_kinase_ATP_BS; .
InterProIPR001245; Ser-Thr/Tyr_kinase; .
InterProIPR008266; Tyr_kinase_AS; .
InterProIPR020635; Tyr_kinase_cat_dom; .
InterProIPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt; .
PfamPF00757; Furin-like; 1; .
PfamPF07714; Pkinase_Tyr; 1; .
PfamPF01030; Recep_L_domain; 2; .
PIRSFPIRSF000619; TyrPK_EGF-R; 1; .
PRINTSPR00109; TYRKINASE; .
SMARTSM00261; FU; 3; .
SMARTSM00219; TyrKc; 1; .
SUPFAMSSF57184; Grow_fac_recept; 2; .
SUPFAMSSF56112; Kinase_like; 1; .
PROSITEPS00107; PROTEIN_KINASE_ATP; 1; .
PROSITEPS50011; PROTEIN_KINASE_DOM; 1; .
PROSITEPS00109; PROTEIN_KINASE_TYR; 1; .



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SWISS-2DPAGE (search AC)


Database constructed and maintained by SIB, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the ExPASy web server