Receptor epidermnog faktora rasta

EGFR
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1IVO, 1M14, 1M17, 1MOX, 1NQL, 1XKK, 1YY9, 1Z9I, 2EB2, 2EB3, 2GS2, 2GS6, 2GS7, 2ITN, 2ITO, 2ITP, 2ITQ, 2ITT, 2ITU, 2ITV, 2ITW, 2ITY, 2ITZ, 2J5E, 2J5F, 2J6M, 2JIT, 2JIU, 2JIV, 2KS1, 2M0B, 2M20, 2RF9, 2RFD, 2RFE, 2RGP, 3B2U, 3B2V, 3BEL, 3BUO, 3C09, 3G5V, 3G5Y, 3GOP, 3GT8, 3IKA, 3LZB, 3NJP, 3OB2, 3OP0, 3P0Y, 3PFV, 3POZ, 3QWQ, 3UG1, 3UG2, 3VJN, 3VJO, 3VRP, 3VRR, 3W2O, 3W2P, 3W2Q, 3W2R, 3W2S, 3W32, 3W33, 4G5J, 4G5P, 4HJO, 4I1Z, 4I20, 4I21, 4I22, 4I23, 4I24, 4JQ7, 4JQ8, 4JR3, 4JRV, 4KRL, 4KRM, 4KRO, 4KRP, 4LI5, 4LL0, 4LQM, 4LRM, 4R3P, 4R3R, 4R5S, 4RIW, 4RIX, 4RIY, 4RJ4, 4RJ5, 4RJ6, 4RJ7, 4RJ8, 4TKS, 4WKQ, 4WRG, 4ZJV, 5CNN, 5CNO, 5CAN, 2N5S, 5CAL, 5C8M, 4UV7, 5CAV, 5CZI, 5EDQ, 5CAS, 5CAO, 5CAP, 5EM5, 5HG5, 5EDR, 5EM8, 5EDP, 5HG7, 5CAU, 5C8K, 5C8N, 5CZH, 5CAQ, 5EM6, 4UIP, 5HG9, 5EM7, 5HG8, 4ZSE, 5HIB, 5HIC, 5D41, 4WD5
Identifikatori
Aliasi	EGFR
Vanjski ID-jevi	OMIM: 131550 MGI: 95294 HomoloGene: 74545 GeneCards: EGFR
Lokacija gena (čovjek)
Hrom.	Hromosom 7 (čovjek)
Kraj	55,211,628 bp
Lokacija gena (miš)
Hrom.	Hromosom 11 (miš)
Kraj	16,868,158 bp
Obrazac RNK ekspresije
	https://ncbi.nlm.nih.gov/gene?cmd=retrieve&dopt=default&rn=1&list_uids=1956/ Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• kinase activity; • nitric-oxide synthase regulator activity; • transmembrane receptor protein tyrosine kinase activity; • protein phosphatase binding; • ATP binding; • protein kinase activity; • vezivanje enzima; • MAP kinase kinase kinase activity; • aktivnost sa transferazom; • chromatin binding; • actin filament binding; • double-stranded DNA binding; • transmembrane signaling receptor activity; • nucleotide binding; • signal transducer activity; • vezivanje identičnih proteina; • signaling receptor binding; • protein tyrosine kinase activity; • calmodulin binding; • protein kinase binding; • phosphatidylinositol-4,5-bisphosphate 3-kinase activity; • protein heterodimerization activity; • integrin binding; • epidermal growth factor binding; • GO:0008313 epidermal growth factor-activated receptor activity; • ubiquitin protein ligase binding; • cadherin binding; • virus receptor activity; • GO:0001948, GO:0016582 vezivanje za proteine;
Ćelijska komponenta	• citoplazma; • endozom; • multivesicular body, internal vesicle lumen; • Jedarna membrana; • membrana; • focal adhesion; • extracellular region; • perinuklearno područje citoplazme; • jedro; • cell surface; • Endoplazmatski retikulum; • integral component of membrane; • Golđijev aparat; • early endosome membrane; • receptor complex; • ćelijska membrana; • endocytic vesicle; • intracellular anatomical structure; • AP-2 adaptor complex; • endosome membrane; • endoplasmic reticulum membrane; • Golđijeva membrana; • basolateral plasma membrane; • Shc-EGFR complex; • Lipidni splav; • apical plasma membrane; • sinapsa; • Vanćelijsko; • clathrin-coated vesicle membrane; • integral component of plasma membrane; • basal plasma membrane; • GO:0009327 makromolekulani kompleks;
Biološki proces	• positive regulation of protein phosphorylation; • negative regulation of epidermal growth factor receptor signaling pathway; • positive regulation of MAP kinase activity; • protein phosphorylation; • cell surface receptor signaling pathway; • protein insertion into membrane; • Ćelijska proliferacija; • morphogenesis of an epithelial fold; • ossification; • GO:1903363 negative regulation of protein catabolic process; • transmembrane receptor protein tyrosine kinase signaling pathway; • positive regulation of fibroblast proliferation; • activation of phospholipase C activity; • epidermis development; • learning or memory; • protein autophosphorylation; • positive regulation of phosphorylation; • cerebral cortex cell migration; • digestive tract morphogenesis; • hair follicle development; • Fosforilacija; • positive regulation of epithelial cell proliferation; • embryonic placenta development; • eyelid development in camera-type eye; • GO:0043006 activation of phospholipase A2 activity; • positive regulation of DNA replication; • response to UV-A; • regulation of peptidyl-tyrosine phosphorylation; • positive regulation of cell migration; • positive regulation of nitric oxide biosynthetic process; • cellular response to estradiol stimulus; • GO:1900404 positive regulation of DNA repair; • response to stress; • regulation of nitric-oxide synthase activity; • salivary gland morphogenesis; • MAPK cascade; • cellular response to epidermal growth factor stimulus; • multicellular organism development; • regulation of cell population proliferation; • GO:0000767 cell morphogenesis; • cellular response to amino acid stimulus; • GO:0072468 Transdukcija signala; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II; • lung development; • positive regulation of synaptic transmission, glutamatergic; • positive regulation of ERK1 and ERK2 cascade; • phosphatidylinositol phosphate biosynthetic process; • Jednodnevni biološki ritam; • positive regulation of superoxide anion generation; • positive regulation of cell population proliferation; • positive regulation of vasoconstriction; • response to osmotic stress; • tongue development; • negative regulation of apoptotic process; • response to cobalamin; • liver regeneration; • response to calcium ion; • Zarastanje rana; • cellular response to dexamethasone stimulus; • negative regulation of mitotic cell cycle; • cellular response to growth factor stimulus; • hydrogen peroxide metabolic process; • GO:0001306 response to oxidative stress; • response to lipid; • regulation of cell motility; • GO:0007243 intracellular signal transduction; • GO:1904578 response to organic cyclic compound; • magnesium ion homeostasis; • Biosinteza bjelančevina; • positive regulation of production of miRNAs involved in gene silencing by miRNA; • positive regulation of smooth muscle cell proliferation; • positive regulation of bone resorption; • midgut development; • positive regulation of inflammatory response; • liver development; • diterpenoid metabolic process; • ERBB2 signaling pathway; • response to estradiol; • positive regulation of cell growth; • positive regulation of prolactin secretion; • astrocyte activation; • cellular response to mechanical stimulus; • response to hydroxyisoflavone; • neuron projection morphogenesis; • ovulation cycle; • GO:0044324, GO:0003256, GO:1901213, GO:0046019, GO:0046020, GO:1900094, GO:0061216, GO:0060994, GO:1902064, GO:0003258, GO:0072212 regulation of transcription by RNA polymerase II; • peptidyl-tyrosine phosphorylation; • membrane organization; • positive regulation of protein kinase C activity; • negative regulation of ERBB signaling pathway; • positive regulation of protein localization to plasma membrane; • negative regulation of cardiocyte differentiation; • GO:0072353 cellular response to reactive oxygen species; • GO:0060469, GO:0009371 positive regulation of transcription, DNA-templated; • regulation of JNK cascade; • regulation of ERK1 and ERK2 cascade; • cellular response to cadmium ion; • positive regulation of NIK/NF-kappaB signaling; • viral entry into host cell; • epidermal growth factor receptor signaling pathway; • positive regulation of peptidyl-serine phosphorylation; • peptidyl-tyrosine autophosphorylation; • cell-cell adhesion; • regulation of phosphatidylinositol 3-kinase signaling; • positive regulation of protein kinase B signaling; • positive regulation of nitric oxide mediated signal transduction; • Ćelijska diferencijacija; • positive regulation of cyclin-dependent protein serine/threonine kinase activity; • negative regulation of Notch signaling pathway; • positive regulation of canonical Wnt signaling pathway; • positive regulation of G1/S transition of mitotic cell cycle;
	Izvori:Amigo / QuickGO
Ortolozi
	1956,https://ncbi.nlm.nih.gov/gene?cmd=retrieve&dopt=default&rn=1&list_uids=1956; 1956,https://ncbi.nlm.nih.gov/gene?cmd=retrieve&dopt=default&rn=1&list_uids=1956
	13649
	ENSG00000146648
	ENSMUSG00000020122
	P00533
	Q01279
NM_001346897; NM_001346898; NM_001346899; NM_001346900; NM_001346941;
	NM_005228; NM_201282; NM_201283; NM_201284
	NM_007912; NM_207655
NP_001333826; NP_001333827; NP_001333828; NP_001333829; NP_001333870;
	NP_005219; NP_958439; NP_958440; NP_958441
	NP_031938; NP_997538
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Receptor epidermnog faktora rasta (EGFR, ErbB-1, HER1 kod ljudi je transmembranski protein, receptor za članove epidermnog faktora rasta porodice EGF vanćelijskog proteinskog liganda.^[5]

Receptor epidermnog faktora rasta je član receptora porodice ErbB, potporodice od četiri blisko povezane receptorske tirozin-kinaze: EGFR (ErbB-1), HER2/neu (ErbB-2), 3 HER (ErbB-3) i HER-4 (ErbB-4). Kod mnogih tipova raka, mutacije koje utiču na ekspresiju ili aktivnost EGFR-a mogu dovesti do raka.^[6]

Epidermni faktor rasta i njegov receptor otkrio je Stanley Cohen sa Vanderbilt University. Cohen je 1986. godine podijelio Nobelovu nagradu za fiziologiju ili medicinu sa Ritom Levi-Montalcini za njihovo otkriće faktora rasta.

Nedostatak signalizacije EGFR-a i drugih receptorska tirozin-kinaza kod ljudi povezan je s bolestima kao što je Alzheimerova bolest, dok je prekomjerna ekspresija povezana s razvojem širokog spektra tumora. Prekid EGFR signalizacije, bilo blokiranjem EGFR mjesta vezanja na vanćelijskom domenu receptora ili inhibicijom aktivnosti unutarćelijskih tirozin-kinaza, može spriječiti rast tumora koji eksprimiraju EGFR i poboljšati stanje pacijenta.

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 1.210 aminokiselina, a molekulska težina 134.277 Da.^[6]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MRPSGTAGAA	LLALLAALCP	ASRALEEKKV	CQGTSNKLTQ	LGTFEDHFLS
LQRMFNNCEV	VLGNLEITYV	QRNYDLSFLK	TIQEVAGYVL	IALNTVERIP
LENLQIIRGN	MYYENSYALA	VLSNYDANKT	GLKELPMRNL	QEILHGAVRF
SNNPALCNVE	SIQWRDIVSS	DFLSNMSMDF	QNHLGSCQKC	DPSCPNGSCW
GAGEENCQKL	TKIICAQQCS	GRCRGKSPSD	CCHNQCAAGC	TGPRESDCLV
CRKFRDEATC	KDTCPPLMLY	NPTTYQMDVN	PEGKYSFGAT	CVKKCPRNYV
VTDHGSCVRA	CGADSYEMEE	DGVRKCKKCE	GPCRKVCNGI	GIGEFKDSLS
INATNIKHFK	NCTSISGDLH	ILPVAFRGDS	FTHTPPLDPQ	ELDILKTVKE
ITGFLLIQAW	PENRTDLHAF	ENLEIIRGRT	KQHGQFSLAV	VSLNITSLGL
RSLKEISDGD	VIISGNKNLC	YANTINWKKL	FGTSGQKTKI	ISNRGENSCK
ATGQVCHALC	SPEGCWGPEP	RDCVSCRNVS	RGRECVDKCN	LLEGEPREFV
ENSECIQCHP	ECLPQAMNIT	CTGRGPDNCI	QCAHYIDGPH	CVKTCPAGVM
GENNTLVWKY	ADAGHVCHLC	HPNCTYGCTG	PGLEGCPTNG	PKIPSIATGM
VGALLLLLVV	ALGIGLFMRR	RHIVRKRTLR	RLLQERELVE	PLTPSGEAPN
QALLRILKET	EFKKIKVLGS	GAFGTVYKGL	WIPEGEKVKI	PVAIKELREA
TSPKANKEIL	DEAYVMASVD	NPHVCRLLGI	CLTSTVQLIT	QLMPFGCLLD
YVREHKDNIG	SQYLLNWCVQ	IAKGMNYLED	RRLVHRDLAA	RNVLVKTPQH
VKITDFGLAK	LLGAEEKEYH	AEGGKVPIKW	MALESILHRI	YTHQSDVWSY
GVTVWELMTF	GSKPYDGIPA	SEISSILEKG	ERLPQPPICT	IDVYMIMVKC
WMIDADSRPK	FRELIIEFSK	MARDPQRYLV	IQGDERMHLP	SPTDSNFYRA
LMDEEDMDDV	VDADEYLIPQ	QGFFSSPSTS	RTPLLSSLSA	TSNNSTVACI
DRNGLQSCPI	KEDSFLQRYS	SDPTGALTED	SIDDTFLPVP	EYINQSVPKR
PAGSVQNPVY	HNQPLNPAPS	RDPHYQDPHS	TAVGNPEYLN	TVQPTCVNST
FDSPAHWAQK	GSHQISLDNP	DYQQDFFPKE	AKPNGIFKGS	TAENAEYLRV
APQSSEFIGA

Funkcija

Receptor epidermalnog faktora rasta (EGFR) je transmembranski protein koji se aktivira vezivanjem njegovih specifičnih liganda, uključujući epidermni faktor rasta i transformirajući faktor rasta α (TGFα). ErbB2 nema poznatu direktnu aktivaciju liganda i može biti u konstitutivnom aktiviranom stanju ili postati aktivan nakon heterodimerizacije sa drugim članovima porodice kao što je EGFR. Nakon aktivacije svojim ligandima faktora rasta, EGFR prolazi kroz tranziciju iz neaktivnog monomernog oblika u aktivni homodimer.^[7] – although there is some evidence that preformed inactive dimers may also exist before ligand binding.^[8] Pored formiranja homodimera nakon vezivanja liganda, EGFR se može upariti sa drugim članom porodice ErbB receptora, kao što je ErbB2/Her2/neu, kako bi se stvorio aktivirani heterodimer. Postoje i dokazi koji ukazuju na to da se formiraju klasteri aktiviranih EGFR-ova, iako ostaje nejasno da li je ovo grupiranje važno za samu aktivaciju ili se javlja nakon aktivacije pojedinačnih dimera.

Dimerizacija EGFR-a stimuliše njegovu unutarćelijsku aktivnost protein-tirozin kinaze. Kao rezultat, dolazi do autofosforilacije nekoliko tirozinskih (Y) ostataka na C-terminalnom domenu EGFR. To uključuje Y992, Y1045, Y1068, Y1148 i Y1173, kao što je prikazano na susjednom dijagramu.^[9] Ova autofosforilacija izaziva nizvodnu aktivaciju i signalizaciju nekoliko drugih proteina koji se povezuju sa fosforiliranim tirozinima preko vlastitih fosfotirozin-vezujućih SH2-domena. Ovi nizvodni signalni proteini pokreću nekoliko kaskada transdukcija signala, uglavnom MAPK, Akt i JNK puteve, što dovodi do DNK sinteze i proliferacija ćelija.^[10] Takvi proteini moduliraju fenotipove kao što su ćelijska migracija, adhezija i proliferacija. Aktivacija receptora je važna za urođeni imunski odgovor u ljudskoj koži. Domen kinaze EGFR-a također može unakrsno fosforilirati tirozinske ostatke drugih receptora s kojima je agregiran i može se sam aktivirati na taj način.

Biološke uloge

EGFR je neophodan za razvoj cjevastih mliječnih žlijezda,^[11]^[12]^[13] i agonisti EGFR-a kao što su amfiregulin, TGF-α i heregulin induciraju i duktusni i lobuloalveolski razvoj, čak i u odsustvu estrogena i progesterona.^[14]^[15]

Klinički značaj

Kancer

Mutacije koje dovode do prekomjerne ekspresije EGFR-a (poznate kao nadregulacija ili pojačanje) povezane su s brojnim karcinomima, uključujući adenokarcinom pluća (40% slučajeva), anusni rak,^[16] glioblastom (50%) i epitelni tumori glave i vrata (80–100%).^[17] Ove somatske mutacije koje uključuju EGFR dovode do njegove stalne aktivacije, što uzrokuje nekontrolirane diobe ćelija.^[18] Kod glioblastoma se često opaža specifična mutacija EGFR, zvana EGFRvIII.^[19] Mutacije, pojačanja ili pogrešna regulacija EGFR-a ili članova porodice su uključeni u oko 30% svih epitelnih karcinoma.^[20]

Upalna bolest

Aberantna EGFR signalizacija je implicirana kod psorijaze, ekcema i ateroskleroze.^[21]^[22] Međutim, njegove tačne uloge u ovim uslovima su loše definisane.

Monogenska bolest

Utvrđeno je da jedno dijete koje pokazuje upalu epitela više organa ima homozigotnu mutaciju gubitka funkcije u "EGFR" genu. Patogenost EGFR mutacije je potvrđena in vitro eksperimentima i funkcionalnom analizom biopsije kože. Njegov teški fenotip odražava mnoga ranija istraživanja funkcije EGFR. Njegove kliničke karakteristike su uključivale papulopustulni osip, suhu kožu, hroničnu dijareju, abnormalnosti rasta dlake, poteškoće s disanjem i neravnotežu elektrolita.^[23]

Zacjeljivanje rana i fibroza

Pokazalo se da EGFR ima ključnu ulogu u diferencijaciji TGF beta 1, zavisnoj od fibroblasta do miofibroblasta.^[24]^[25] Aberantna perzistencija miofibroblasta unutar tkiva može dovesti do progresivnog tkiva fibroze, oštećenja funkcije tkiva ili organa (npr. kože hipertrofični ili keloidni ožiljci, ciroza jetre, fibroza miokarda, hronična bolest bubrega).

Medicinska primjena

Meta lijekova

Identifikacija EGFR-a kao onkogena dovela je do razvoja antikancerogenih lijekova usmjerenih protiv EGFR-a (koji se nazivaju "EGFR inhibitori", EGFRi), uključujući gefitinib,^[26] erlotinib, afatinib, brigatinib i ikotinib^[27] za rak pluća i cetuksimab za rak debelog crijeva. Nedavno je AstraZeneca razvila Osimertinib, treću generaciju inhibitora tirozin-kinaze.^[28]

Mnogi terapijski pristupi usmjereni su na EGFR. Cetuksimab i panitumumab su primjeri inhibitorskih monoklonska antitijela. Međutim, prvi je tipa IgG1, a drugi tipa IgG2; posljedice na ćelijsku citotoksičnost zavisnu od antitijela mogu biti sasvim različite.^[29] Ostali monoklonski agensi u kliničkom razvoju su zalutumumab, nimotuzumab i matuzumab. Monoklonska antitijela blokiraju domen za vezivanje vanćelijskog liganda. Sa blokiranim mjestom vezivanja, signalne molekule se više ne mogu vezati tamo i aktivirati tirozin-kinazu.

Drugi metod je korištenje malih molekula za inhibiciju EGFR tirozin-kinaze, koja se nalazi na citoplazmatskoj strani receptora. Bez aktivnosti kinaze, EGFR nije u stanju da se aktivira, što je preduslov za vezivanje nizvodnih adapterskih proteina. Navodno zaustavljanjem signalne kaskade u ćelijama koje se oslanjaju na ovaj put za ćelijski rast, proliferacija i migracija tumora je smanjena. Gefitinib, erlotinib, brigatinib i lapatinib (mješoviti EGFR i ERBB2 inhibitor) su primjeri inhibitora malih molekula kinaze.

CimaVax-EGF, aktivna vakcina koja cilja EGF kao glavni ligand EGF-a, koristi drugačiji pristup, podižući antitijela protiv samog EGF-a, čime se poriču EGFR zavisni karcinomi proliferativni stimulus;^[30] koristi se kao terapija raka protiv karcinoma nemalih ćelija pluća (najčešći oblik raka pluća) na Kubi, a prolazi dalje ispitivanje za moguće licenciranje u Japanu, Evropi i Sjedinjenim Državama.^[31]

Postoji nekoliko dostupnih kvantitativnih metoda koje koriste detekciju fosforilacije proteina za identifikaciju inhibitora porodice EGFR.^[32]

Novi lijekovi kao što su osimertinib, gefitinib, erlotinib i brigatinib direktno ciljaju EGFR. Pacijenti su podijeljeni na EGFR-pozitivne i EGFR-negativne, na osnovu toga da li test tkiva pokazuje mutaciju. EGFR-pozitivni pacijenti pokazali su stopu odgovora od 60%, što premašuje stopu odgovora za konvencionalnu hemoterapiju.^[33]

Međutim, mnogi pacijenti razvijaju otpornost. Dva primarna izvora rezistencije su mutacija T790M i MET onkogen.^[33] Međutim, od 2010. nije postojao konsenzus o prihvaćenom pristupu borbi protiv otpora niti odobrenje FDA za određenu kombinaciju. Rezultati kliničkog ispitivanja faze II prijavljeni za brigatinib koji cilja na mutaciju T790M, a brigatinib je dobio status probojne terapije kod FDA u februaru 2015. godine.

Najčešći štetni efekat EGFR inhibitora, koji se nalazi kod više od 90% pacijenata, je papulopustulni osip koji se širi preko lica i trupa; prisustvo osipa je u korelaciji sa antitumorskim dejstvom lijeka.^[34] Kod 10% do 15% pacijenata efekti mogu biti ozbiljni i zahtijevaju liječenje.^[35]^[36]

Neki testovi imaju za cilj predviđanje koristi od EGFR tretmana, kao što je Veristrat.^[37]

Laboratorijsko istraživanje koje koristi genetički modifikovane matične ćelije za ciljanje EGFR kod miševa objavljeno je 2014. da obećava.^[38] EGFR is a well-established target for monoclonal antibodies and specific tyrosine kinase inhibitors.^[39]

Meta agenasa za snimanje

Razvijeni su agensi za snimanje koji identifikuju karcinome zavisne od EGFR, koristeći označeni EGF.^[40] Izvodljivost snimanja ekspresije in vivo EGFR pokazano je u nekoliko studija.^[41]^[42]

Predloženo je da određeni nalazi kompjuterizirane tomografije kao što su opaciteti brušenog stakla, zračni bronhogram, spikulirane ivice, vaskularna konvergencija i pleuralna retrakcija mogu predvidjeti prisustvo EGFR mutacije kod pacijenata s karcinomom pluća nemalih ćelija.^[43]

Interakcije

Pokazalo se da receptor epidermalnog faktora rasta reaguje sa:

AR,^[44]^[45]
ARF4,^[46]
CAV1,^[47]
CAV3,^[47]
CBL,^[48]^[49]^[50]^[51]^[52]
CBLB,^[49]^[53]
CBLC,^[54]^[55]
CD44,^[24]
CDC25A,^[56]
CRK,^[53]^[57]
CTNNB1,^[58]^[59]^[60]
DCN,^[61]^[62]
EGF,^[63]^[64]
GRB14,^[65]
Grb2,^[53]^[63]^[65]^[66]^[67]^[68]^[69]^[70]^[71]^[72]
JAK2,^[73]
MUC1,^[74]^[75]
NCK1,^[66]^[76]^[77]
NCK2^[66]^[78]^[79]
PKC-alfa,^[80]
PLCG1,^[48]^[81]
PLSCR1,^[82]
PTPN1,^[83]^[84]
PTPN11,^[53]^[85]
PTPN6,^[85]^[86]
PTPRK,^[87]
SH2D3A,^[88]
SH3KBP1,^[89]^[90]
SHC1,^[53]^[91]
SOS1,^[71]^[92]^[93]
Src,^[73]^[94]^[95]
STAT1,^[73]^[96]
STAT3,^[73]^[97]
STAT5A,^[53]^[73]
UBC,^[50]^[51]^[98] i
WAS,^[99]
PAR2.^[100]

Kod voćnih mušica, receptor epidermnog faktora rasta stupa u interakciju sa Spic.^[101]

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000146648 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020122 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Herbst RS (2004). "Review of epidermal growth factor receptor biology". International Journal of Radiation Oncology, Biology, Physics. 59 (2 Suppl): 21–6. doi:10.1016/j.ijrobp.2003.11.041. PMID 15142631.
^ ^a ^b Zhang H, Berezov A, Wang Q, Zhang G, Drebin J, Murali R, Greene MI (august 2007). "ErbB receptors: from oncogenes to targeted cancer treatment". The Journal of Clinical Investigation. 117 (8): 2051–8. doi:10.1172/JCI32278. PMC 1934579. PMID 17671639.
^ Yarden Y, Schlessinger J (mart 1987). "Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor". Biochemistry. 26 (5): 1443–51. doi:10.1021/bi00379a035. PMID 3494473.
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Vanjski linkovi

Epidermal Growth Factor Receptor na US National Library of Medicine Medical Subject Headings (MeSH)
P00533

Portal Biologija

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p r u Enzimi
Teme	Aktivno mjesto Alosterna regulacija Difuzijski limitirani enzim EC broj Enzimska kataliza Inhibicija enzimskih reakcija Kinetika enzima Koenzim Kooperativnost Lineweaver–Burkov dijagram Michaelis–Mentenova kinetika Mjesto vezanja Spisak enzima
Tipovi	EC1 Oksidoreduktaze/spisak EC2 Transferaze/spisak EC3 Hidrolaze/spisak EC4 Lijaze/spisak EC5 Izomeraze/spisak EC6 Ligaze/spisak