EGFR
entrez
1956
canonical
uniprot
P00533
canonical
ensembl
ENSG00000146648
resolver
ensp
ENSP00000275493
resolver
ensp
ENSP00000342376
resolver
ensp
ENSP00000345973
resolver
ensp
ENSP00000413354
resolver
ensp
ENSP00000413843
resolver
ensp
ENSP00000415559
resolver
enst
ENST00000450046
resolver
enst
ENST00000455089
resolver
genesymbol
EGFR
resolver
genesymbol_syn
ERBB
resolver
genesymbol_syn
ERBB1
resolver
genesymbol_syn
HER1
resolver
hgnc
HGNC:3236
resolver
uniprot
B7Z2I3
resolver
uniprot
C9JYS6
resolver
uniprot
E7BSV0
resolver
uniprot
F2YGG7
resolver
uniprot
F6QWY5
resolver
uniprot
O00688
resolver
uniprot
O00732
resolver
uniprot
P06268
resolver
uniprot
Q14225
resolver
uniprot
Q504U8
resolver
uniprot
Q68GS5
resolver
uniprot
Q92795
resolver
uniprot
Q9BZS2
resolver
uniprot
Q9GZX1
resolver
uniprot
Q9H2C9
resolver
uniprot
Q9H3C9
resolver
uniprot
Q9UMD7
resolver
uniprot
Q9UMD8
resolver
uniprot
Q9UMG5
resolver
uniprot_entry
B7Z2I3_HUMAN
resolver
uniprot_entry
C9JYS6_HUMAN
resolver
uniprot_entry
E7BSV0_HUMAN
resolver
uniprot_entry
EGFR_HUMAN
resolver
uniprot_entry
F2YGG7_HUMAN
resolver
uniprot_entry
F6QWY5_HUMAN
resolver
uniprot_entry
Q504U8_HUMAN
resolver
uniprot_sec
O00688
resolver
uniprot_sec
O00732
resolver
uniprot_sec
P06268
resolver
uniprot_sec
Q14225
resolver
uniprot_sec
Q68GS5
resolver
uniprot_sec
Q92795
resolver
uniprot_sec
Q9BZS2
resolver
uniprot_sec
Q9GZX1
resolver
uniprot_sec
Q9H2C9
resolver
uniprot_sec
Q9H3C9
resolver
uniprot_sec
Q9UMD7
resolver
uniprot_sec
Q9UMD8
resolver
uniprot_sec
Q9UMG5
resolver
activity_regulation
ACTIVITY 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. Up-regulated by NEU3-mediated desialylation of N-linked glycan at Asn-528. {ECO:0000269|PubMed:15282549, ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:17334392, ECO:0000269|PubMed:18046415, ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:25922362}.
uniprot
proteins
amino_acid_sequence
MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA
uniprot
proteins
disease_involvement
DISEASE: Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis. {ECO:0000269|PubMed:15118125, ECO:0000269|PubMed:16533793, ECO:0000269|PubMed:16672372}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Neonatal nephrocutaneous inflammatory syndrome (NNCIS) [MIM:616069]: An autosomal recessive disorder characterized by intrauterine growth retardation, premature birth, fragile skin, recurrent skin infections and sepsis, failure to thrive, nephrocalcinosis, and nephromegaly with tubular dysfunction. Some patients have chronic diarrhea, and necrotizing enterocolitis. {ECO:0000269|PubMed:24691054}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:10805725, PubMed:12297050, PubMed:12620237, PubMed:12873986, PubMed:15374980, PubMed:15590694, PubMed:17115032, PubMed:19560417, PubMed:21258366, PubMed:27153536, PubMed:2790960, PubMed:35538033, PubMed:9488479). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF (PubMed:12297049, PubMed:15611079, PubMed:17909029, PubMed:20837704, PubMed:27153536, PubMed:2790960, PubMed:7679104, PubMed:8144591, PubMed:9419975). Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues (PubMed:10026169, PubMed:17349580, PubMed:18046415, PubMed:19560417, PubMed:19836242). The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades (PubMed:10026169, PubMed:17349580, PubMed:18046415, PubMed:19560417, PubMed:19836242). Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (PubMed:27153536). May also activate the NF-kappa-B signaling cascade (PubMed:11116146). 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 (PubMed:11602604). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589). Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration (PubMed:20462955). Acts as a positive regulator of cGAS-STING signaling by mediating tyrosine phosphorylation of STING1, promoting production of type I interferon (IFN-alpha and IFN-beta), while inhibiting STING1 ability to regulate autophagy (PubMed:32926474). Plays a role in enhancing learning and memory performance (By similarity). Plays a role in mammalian pain signaling (long-lasting hypersensitivity) (By similarity). {ECO:0000250|UniProtKB:Q01279, ECO:0000269|PubMed:10026169, ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11116146, ECO:0000269|PubMed:11483589, ECO:0000269|PubMed:11602604, ECO:0000269|PubMed:12297049, ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:12873986, ECO:0000269|PubMed:15374980, ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:15611079, ECO:0000269|PubMed:17115032, ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:18046415, ECO:0000269|PubMed:19560417, ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:20837704, ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:2790960, ECO:0000269|PubMed:32926474, ECO:0000269|PubMed:35538033, ECO:0000269|PubMed:7679104, ECO:0000269|PubMed:8144591, ECO:0000269|PubMed:9419975, ECO:0000269|PubMed:9488479}.; FUNCTION: [Isoform 2]: May act as an antagonist of EGF action. {ECO:0000269|PubMed:8918811}.; FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins. {ECO:0000269|PubMed:21516087}.
uniprot
proteins
mass_dalton
134277
uniprot
proteins
mutagenesis
MUTAGEN 275; /note="Y->A: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309."; /evidence="ECO:0000269|PubMed:12297050"; MUTAGEN 287; /note="F->A: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309."; /evidence="ECO:0000269|PubMed:12297050"; MUTAGEN 309; /note="R->S: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-275. Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-287."; /evidence="ECO:0000269|PubMed:12297050"; MUTAGEN 429; /note="R->E: Abolishes autophosphorylation and activation of downstream kinases."; /evidence="ECO:0000269|PubMed:12297050"; MUTAGEN 525..1210; /note="Missing: Increased EGF binding."; /evidence="ECO:0000269|PubMed:19718021"; MUTAGEN 587..590; /note="DGPH->AGPA: Decreases intramolecular interactions and facilitates EGF binding."; /evidence="ECO:0000269|PubMed:12620237"; MUTAGEN 587; /note="D->A: Increased EGF binding; when associated with A-590 and A-609."; /evidence="ECO:0000269|PubMed:19718021"; MUTAGEN 590; /note="H->A: Increased EGF binding; when associated with A-587; A-590 and A-609."; /evidence="ECO:0000269|PubMed:19718021"; MUTAGEN 609; /note="K->A: Decreases intramolecular interactions and facilitates EGF binding. Increased EGF binding; when associated with A-587; A-590 and A-609."; /evidence="ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:19718021"; MUTAGEN 688; /note="L->A: Strongly reduced phosphorylation."; /evidence="ECO:0000269|PubMed:19560417, ECO:0000269|PubMed:19563760"; MUTAGEN 689; /note="V->A: Reduced autophosphorylation."; /evidence="ECO:0000269|PubMed:19560417"; MUTAGEN 689; /note="V->M: Constitutively activated kinase."; /evidence="ECO:0000269|PubMed:19560417"; MUTAGEN 690; /note="E->A: Reduced phosphorylation."; /evidence="ECO:0000269|PubMed:19560417, ECO:0000269|PubMed:19563760"; MUTAGEN 692; /note="L->A,P: Strongly reduced phosphorylation."; /evidence="ECO:0000269|PubMed:19560417, ECO:0000269|PubMed:19563760"; MUTAGEN 693; /note="T->A: Increased phosphorylation."; /evidence="ECO:0000269|PubMed:19560417"; MUTAGEN 693; /note="T->D: Strongly reduced phosphorylation."; /evidence="ECO:0000269|PubMed:19560417"; MUTAGEN 694; /note="P->A: Strongly reduced phosphorylation."; /evidence="ECO:0000269|PubMed:19560417"; MUTAGEN 699; /note="P->A: Reduced phosphorylation."; /evidence="ECO:0000269|PubMed:19560417"; MUTAGEN 700; /note="N->A: Abolishes phosphorylation."; /evidence="ECO:0000269|PubMed:19560417"; MUTAGEN 704; /note="L->A: Abolishes phosphorylation."; /evidence="ECO:0000269|PubMed:19560417"; MUTAGEN 705; /note="R->A: Abolishes phosphorylation."; /evidence="ECO:0000269|PubMed:19560417"; MUTAGEN 706; /note="I->A: Abolishes phosphorylation."; /evidence="ECO:0000269|PubMed:19560417"; MUTAGEN 745; /note="K->A,M: Abolishes kinase activity."; /evidence="ECO:0000269|PubMed:19560417"; MUTAGEN 974; /note="D->A: Strongly reduced phosphorylation."; MUTAGEN 977; /note="R->A: Reduced phosphorylation."; /evidence="ECO:0000269|PubMed:19563760"; MUTAGEN 1005..1006; /note="ED->RK: Constitutively activated kinase."; /evidence="ECO:0000269|PubMed:19563760"; MUTAGEN 1016; /note="Y->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."; /evidence="ECO:0000269|PubMed:10805725"; MUTAGEN 1048..1210; /note="Missing: Abolishes palmitoylation."; /evidence="ECO:0000269|PubMed:27153536"; MUTAGEN 1049; /note="C->A: Decreased palmitoylation."; /evidence="ECO:0000269|PubMed:27153536"; MUTAGEN 1067; /note="Q->G: No effect on interaction with CBLC."; /evidence="ECO:0000269|PubMed:22888118"; MUTAGEN 1068; /note="R->G: Strongly decreases interaction with CBLC."; /evidence="ECO:0000269|PubMed:22888118"; MUTAGEN 1069; /note="Y->F: Abolishes interaction with CBLC."; /evidence="ECO:0000269|PubMed:22888118"; MUTAGEN 1092; /note="Y->F: No change in interaction with PIK3C2B. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1016."; /evidence="ECO:0000269|PubMed:10805725"; MUTAGEN 1110; /note="Y->F: No change in interaction with PIK3C2B."; /evidence="ECO:0000269|PubMed:10805725"; MUTAGEN 1146; /note="C->A: Decreased palmitoylation."; /evidence="ECO:0000269|PubMed:27153536"; MUTAGEN 1172; /note="Y->F: No change in interaction with PIK3C2B."; /evidence="ECO:0000269|PubMed:10805725"; MUTAGEN 1197; /note="Y->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."; /evidence="ECO:0000269|PubMed:10805725
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on Tyr residues in response to EGF (PubMed:20462955, PubMed:27153536). Phosphorylation at Ser-695 is partial and occurs only if Thr-693 is phosphorylated. Phosphorylation at Thr-678 and Thr-693 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation. Dephosphorylation by PTPRJ prevents endocytosis and stabilizes the receptor at the plasma membrane. Autophosphorylation at Tyr-1197 is stimulated by methylation at Arg-1199 and enhances interaction with PTPN6. Autophosphorylation at Tyr-1092 and/or Tyr-1110 recruits STAT3. Dephosphorylated by PTPN1 and PTPN2. {ECO:0000269|PubMed:10523301, ECO:0000269|PubMed:12873986, ECO:0000269|PubMed:16083266, ECO:0000269|PubMed:19563760, ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:2543678, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:3138233}.; PTM: Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting (PubMed:27153536). Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs. Deubiquitination by OTUD7B prevents degradation. Ubiquitinated by RNF115 and RNF126 (By similarity). Ubiquitinated by ZNRF1 or CBL at different lysines in response to EGF stimulation; leading to recruitment of the ESCRT machinery and subsequent degradation in the lysosomes (PubMed:33996800). Deubiquitinated by UCHL1 leading to the inhibition of its degradation (By similarity). {ECO:0000250|UniProtKB:Q01279, ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:22179831, ECO:0000269|PubMed:22298428, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:33996800}.; PTM: Palmitoylated on Cys residues by ZDHHC20. Palmitoylation inhibits internalization after ligand binding, and increases the persistence of tyrosine-phosphorylated EGFR at the cell membrane. Palmitoylation increases the amplitude and duration of EGFR signaling. {ECO:0000269|PubMed:27153536}.; PTM: Neddylated; by NEDD8 (PubMed:28891468). Neddylation results in localization to the cell membrane when activated by EGF. Neddylation also increases protein stability (PubMed:28891468). {ECO:0000269|PubMed:28891468}.; PTM: Methylated. Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197. {ECO:0000269|PubMed:19563760, ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:21258366}.
uniprot
proteins
protein_family
EGF receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10026169
uniprot
proteins
pubmed
10228163
uniprot
proteins
pubmed
10523301
uniprot
proteins
pubmed
10731668
uniprot
proteins
pubmed
10805725
uniprot
proteins
pubmed
11116146
uniprot
proteins
pubmed
11161793
uniprot
proteins
pubmed
11483589
uniprot
proteins
pubmed
11602604
uniprot
proteins
pubmed
12297049
uniprot
proteins
pubmed
12297050
uniprot
proteins
pubmed
12620237
uniprot
proteins
pubmed
12731890
uniprot
proteins
pubmed
12873986
uniprot
proteins
pubmed
15118125
uniprot
proteins
pubmed
15282549
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15374980
uniprot
proteins
pubmed
15590694
uniprot
proteins
pubmed
15611079
uniprot
proteins
pubmed
15623594
uniprot
proteins
pubmed
15837620
uniprot
proteins
pubmed
15840573
uniprot
proteins
pubmed
16083266
uniprot
proteins
pubmed
16140940
uniprot
proteins
pubmed
16205628
uniprot
proteins
pubmed
16420529
uniprot
proteins
pubmed
16533793
uniprot
proteins
pubmed
16543144
uniprot
proteins
pubmed
16672372
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17115032
uniprot
proteins
pubmed
17182860
uniprot
proteins
pubmed
17334392
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17349580
uniprot
proteins
pubmed
17671655
uniprot
proteins
pubmed
17909029
uniprot
proteins
pubmed
18046415
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18227510
uniprot
proteins
pubmed
18602463
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19172738
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19509291
uniprot
proteins
pubmed
19560417
uniprot
proteins
pubmed
19563760
uniprot
proteins
pubmed
19718021
uniprot
proteins
pubmed
19749156
uniprot
proteins
pubmed
19836242
uniprot
proteins
pubmed
1988448
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20462955
uniprot
proteins
pubmed
20471394
uniprot
proteins
pubmed
20551055
uniprot
proteins
pubmed
20674546
uniprot
proteins
pubmed
20837704
uniprot
proteins
pubmed
21258366
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21487020
uniprot
proteins
pubmed
21516087
uniprot
proteins
pubmed
21518868
uniprot
proteins
pubmed
22179831
uniprot
proteins
pubmed
22298428
uniprot
proteins
pubmed
22888118
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23418353
uniprot
proteins
pubmed
23589287
uniprot
proteins
pubmed
23774213
uniprot
proteins
pubmed
23912460
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24691054
uniprot
proteins
pubmed
25187647
uniprot
proteins
pubmed
25311788
uniprot
proteins
pubmed
2543678
uniprot
proteins
pubmed
25922362
uniprot
proteins
pubmed
26918609
uniprot
proteins
pubmed
26988023
uniprot
proteins
pubmed
27153536
uniprot
proteins
pubmed
2790960
uniprot
proteins
pubmed
28479384
uniprot
proteins
pubmed
28891468
uniprot
proteins
pubmed
29192674
uniprot
proteins
pubmed
2985580
uniprot
proteins
pubmed
2991899
uniprot
proteins
pubmed
30352854
uniprot
proteins
pubmed
3039909
uniprot
proteins
pubmed
3138233
uniprot
proteins
pubmed
32926474
uniprot
proteins
pubmed
3329716
uniprot
proteins
pubmed
33996800
uniprot
proteins
pubmed
35538033
uniprot
proteins
pubmed
39073202
uniprot
proteins
pubmed
6093780
uniprot
proteins
pubmed
6324343
uniprot
proteins
pubmed
6325948
uniprot
proteins
pubmed
6326261
uniprot
proteins
pubmed
6328312
uniprot
proteins
pubmed
6330563
uniprot
proteins
pubmed
7654368
uniprot
proteins
pubmed
7657591
uniprot
proteins
pubmed
7679104
uniprot
proteins
pubmed
8144591
uniprot
proteins
pubmed
8650580
uniprot
proteins
pubmed
8918811
uniprot
proteins
pubmed
8962717
uniprot
proteins
pubmed
9103388
uniprot
proteins
pubmed
9419975
uniprot
proteins
pubmed
9488479
uniprot
proteins
pubmed
9556602
uniprot
proteins
pubmed
9852145
uniprot
proteins
sequence_length
1210
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:23589287, ECO:0000269|PubMed:26918609, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:2790960, ECO:0000269|PubMed:35538033}; Single-pass type I membrane protein {ECO:0000269|PubMed:27153536}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:27153536}; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Nucleus membrane; Single-pass type I membrane protein. Endosome {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:27153536}. Endosome membrane. Nucleus {ECO:0000269|PubMed:17115032, ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:20551055, ECO:0000269|PubMed:20674546}. Note=In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER (PubMed:17909029, PubMed:20674546). Endocytosed upon activation by ligand (PubMed:17182860, PubMed:17909029, PubMed:27153536, PubMed:2790960). Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) (PubMed:20551055). {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:20674546, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:2790960}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
uniprot
proteins
transmembrane_region
TRANSMEM 646..668; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins