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Protein

Epidermal growth factor receptor

Gene

EGFR

Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. 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. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin.

Catalytic activityi

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

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei745 – 7451ATPPROSITE-ProRule annotation
Active sitei837 – 8371Proton acceptorPROSITE-ProRule annotation
Binding sitei855 – 8551ATPPROSITE-ProRule annotation
Sitei1016 – 10161Important for interaction with PIK3C2BBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi718 – 7269ATPPROSITE-ProRule annotation
Nucleotide bindingi790 – 7912ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Epidermal growth factor receptor (EC:2.7.10.1)
Gene namesi
Name:EGFR
OrganismiMacaca mulatta (Rhesus macaque)
Taxonomic identifieri9544 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca
ProteomesiUP000006718 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 645621ExtracellularSequence AnalysisAdd
BLAST
Transmembranei646 – 66823HelicalSequence AnalysisAdd
BLAST
Topological domaini669 – 1210542CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 12101186Epidermal growth factor receptorPRO_0000160254Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 58By similarity
Glycosylationi128 – 1281N-linked (GlcNAc...)By similarity
Disulfide bondi157 ↔ 187By similarity
Glycosylationi175 – 1751N-linked (GlcNAc...)By similarity
Disulfide bondi190 ↔ 199By similarity
Disulfide bondi194 ↔ 207By similarity
Glycosylationi196 – 1961N-linked (GlcNAc...)By similarity
Disulfide bondi215 ↔ 223By similarity
Disulfide bondi219 ↔ 231By similarity
Modified residuei229 – 2291PhosphoserineBy similarity
Disulfide bondi232 ↔ 240By similarity
Disulfide bondi236 ↔ 248By similarity
Disulfide bondi251 ↔ 260By similarity
Disulfide bondi264 ↔ 291By similarity
Disulfide bondi295 ↔ 307By similarity
Disulfide bondi311 ↔ 326By similarity
Disulfide bondi329 ↔ 333By similarity
Disulfide bondi337 ↔ 362By similarity
Glycosylationi352 – 3521N-linked (GlcNAc...)By similarity
Glycosylationi361 – 3611N-linked (GlcNAc...)By similarity
Glycosylationi413 – 4131N-linked (GlcNAc...)By similarity
Glycosylationi444 – 4441N-linked (GlcNAc...)By similarity
Disulfide bondi470 ↔ 499By similarity
Disulfide bondi506 ↔ 515By similarity
Disulfide bondi510 ↔ 523By similarity
Disulfide bondi526 ↔ 535By similarity
Glycosylationi528 – 5281N-linked (GlcNAc...)By similarity
Disulfide bondi539 ↔ 555By similarity
Disulfide bondi558 ↔ 571By similarity
Disulfide bondi562 ↔ 579By similarity
Glycosylationi568 – 5681N-linked (GlcNAc...)By similarity
Disulfide bondi582 ↔ 591By similarity
Disulfide bondi595 ↔ 617By similarity
Glycosylationi603 – 6031N-linked (GlcNAc...)By similarity
Disulfide bondi620 ↔ 628By similarity
Disulfide bondi624 ↔ 636By similarity
Modified residuei678 – 6781Phosphothreonine; by PKC and PKD/PRKD1By similarity
Modified residuei693 – 6931Phosphothreonine; by PKD/PRKD1By similarity
Modified residuei695 – 6951PhosphoserineBy similarity
Cross-linki716 – 716Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki737 – 737Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki754 – 754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki867 – 867Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki929 – 929Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki970 – 970Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei991 – 9911PhosphoserineBy similarity
Modified residuei995 – 9951PhosphoserineBy similarity
Modified residuei998 – 9981Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1016 – 10161Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1026 – 10261PhosphoserineBy similarity
Modified residuei1039 – 10391PhosphoserineBy similarity
Modified residuei1041 – 10411PhosphothreonineBy similarity
Modified residuei1042 – 10421PhosphoserineBy similarity
Modified residuei1064 – 10641PhosphoserineBy similarity
Modified residuei1070 – 10701PhosphoserineBy similarity
Modified residuei1071 – 10711PhosphoserineBy similarity
Modified residuei1081 – 10811PhosphoserineBy similarity
Modified residuei1092 – 10921Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1110 – 11101Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1166 – 11661PhosphoserineBy similarity
Modified residuei1172 – 11721Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1197 – 11971Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1199 – 11991Omega-N-methylarginine; alternateBy similarity
Modified residuei1199 – 11991Omega-N-methylated arginine; alternateBy similarity

Post-translational modificationi

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 occurs. Deubiquitinated by OTUD7B, preventing degradation. Ubiquitinated by RNF115 and RNF126.By similarity
Phosphorylated. Autophosphorylates. Dephosphorylated by PTPN1 and PTPN2 (By similarity).By similarity
Methylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Expressioni

Tissue specificityi

Hypothalamus.

Developmental stagei

Levels in the medial basal hypothalamus and preoptic area are elevated during neonatal life (1 week-6 months), decrease during juvenile development (8-18 months) and markedly increase during the expected time of puberty (30-36 months).

Gene expression databases

ExpressionAtlasiP55245. baseline.

Interactioni

Subunit structurei

Binding of the ligand triggers homo- and/or heterodimerization of the receptor triggering its autophosphorylation. Heterodimer with ERBB2. Interacts with ERRFI1; inhibits dimerization of the kinase domain and autophosphorylation. Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B. Interacts with GRB2; an adapter protein coupling the receptor to downstream signaling pathways. Interacts with GAB2; involved in signaling downstream of EGFR. Interacts with STAT3; mediates EGFR downstream signaling in cell proliferation. Interacts with RIPK1; involved in NF-kappa-B activation. Interacts (autophosphorylated) with CBL, CBLB and CBLC; involved in EGFR ubiquitination and regulation. Interacts with SOCS5; regulates EGFR degradation through TCEB1- and TCEB2-mediated ubiquitination and proteasomal degradation. Interacts with PRMT5; methylates EGFR and enhances interaction with PTPN6. Interacts (phosphorylated) with PTPN6; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with COPG1; essential for regulation of EGF-dependent nuclear transport of EGFR by retrograde trafficking from the Golgi to the ER. Interacts with TNK2; this interaction is dependent on EGF stimulation and kinase activity of EGFR. Interacts with PCNA; positively regulates PCNA. Interacts with PELP1. Interacts with MUC1. Interacts with AP2M1. Interacts with FER. May interact with EPS8; mediates EPS8 phosphorylation. Interacts (via SH2 domains) with GRB2, NCK1 and NCK2. Interacts with ATX2. Interacts with GAREM. Interacts (ubiquitinated) with ANKRD13A/B/D; the interaction is direct and may regulate EGFR internalization after EGF stimulation. Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Interacts (via C-terminal cytoplasmic kinase domain) with ZPR1 (via zinc fingers). Interacts with RNF115 and RNF126.By similarity

Protein-protein interaction databases

STRINGi9544.ENSMMUP00000029471.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati75 – 300226ApproximateAdd
BLAST
Repeati390 – 600211ApproximateAdd
BLAST
Domaini712 – 979268Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni688 – 70417Important for dimerization, phosphorylation and activationBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000230982.
InParanoidiP55245.
OrthoDBiEOG7V49XM.
TreeFamiTF106002.

Family and domain databases

Gene3Di3.80.20.20. 2 hits.
InterProiIPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFiPIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00261. FU. 4 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P55245-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPSGTAGAA LLALLAALCP ASRALEEKKV CQGTSNKLTQ LGTFEDHFLS
60 70 80 90 100
LQRMFNNCEV VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP
110 120 130 140 150
LENLQIIRGN MYYENSYALA VLSNYDANKT GLKELPMRNL QEILHGAVRF
160 170 180 190 200
SNNPALCNVE SIQWRDIVSS EFLSNMSMDF QNHLGSCQKC DPSCPNGSCW
210 220 230 240 250
GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC TGPRESDCLV
260 270 280 290 300
CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV
310 320 330 340 350
VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDTLS
360 370 380 390 400
INATNIKHFK NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE
410 420 430 440 450
ITGFLLIQAW PENRTDLHAF ENLEIIRGRT KQHGQFSLAV VSLNITSLGL
460 470 480 490 500
RSLKEISDGD VIISGNKNLC YANTINWKKL FGTSSQKTKI ISNRGENSCK
510 520 530 540 550
ATGQVCHALC SPEGCWGPEP RDCVSCQNVS RGRECVDKCN VLEGEPREFV
560 570 580 590 600
ENSECIQCHP ECLPQVMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM
610 620 630 640 650
GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCARNG PKIPSIATGM
660 670 680 690 700
VGALLLLLVV ALGIGLFMRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN
710 720 730 740 750
QALLRILKET EFKKIKVLGS GAFGTVYKGL WIPEGEKVKI PVAIKELREA
760 770 780 790 800
TSPKANKEIL DEAYVMASVD NPHVCRLLGI CLTSTVQLIT QLMPFGCLLD
810 820 830 840 850
YVREHKDNIG SQYLLNWCVQ IAKGMNYLED RRLVHRDLAA RNVLVKTPQH
860 870 880 890 900
VKITDFGLAK LLGAEEKEYH AEGGKVPIKW MALESILHRI YTHQSDVWSY
910 920 930 940 950
GVTVWELMTF GSKPYDGIPA SEISSILEKG ERLPQPPICT IDVYMIMVKC
960 970 980 990 1000
WMIDADSRPK FRELIIEFSK MARDPQRYLV IQGDERMHLP SPTDSNFYRA
1010 1020 1030 1040 1050
LMDEEDMDDV VDADEYLIPQ QGFFSSPSTS RTPLLSSLSA TSNNSTVACI
1060 1070 1080 1090 1100
DRNGLQSCPI KEDSFLQRYS SDPTGALTED SIDDTFLPVP EYINQSVPKR
1110 1120 1130 1140 1150
PAGSVQNPVY HNQPLNPAPS RDPHYQDPHS TAVGNPEYLN TVQPTCVNST
1160 1170 1180 1190 1200
FDSPAHWAQK GSHQISLDNP DYQQDFFPKE AKPNGIFKGS TAENAEYLRV
1210
APQSSEFIGA
Length:1,210
Mass (Da):134,350
Last modified:January 22, 2014 - v2
Checksum:iE114E9CEE96D64CC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti541 – 5411V → I in EHH17303 (PubMed:22002653).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JH286850 Genomic DNA. No translation available.
CM001255 Genomic DNA. Translation: EHH17303.1.
JU327815 mRNA. Translation: AFE71571.1.
S75916 mRNA. Translation: AAB33095.1.
PIRiI78540.
UniGeneiMmu.3397.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JH286850 Genomic DNA. No translation available.
CM001255 Genomic DNA. Translation: EHH17303.1.
JU327815 mRNA. Translation: AFE71571.1.
S75916 mRNA. Translation: AAB33095.1.
PIRiI78540.
UniGeneiMmu.3397.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9544.ENSMMUP00000029471.

Chemistry

BindingDBiP55245.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000230982.
InParanoidiP55245.
OrthoDBiEOG7V49XM.
TreeFamiTF106002.

Gene expression databases

ExpressionAtlasiP55245. baseline.

Family and domain databases

Gene3Di3.80.20.20. 2 hits.
InterProiIPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFiPIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00261. FU. 4 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Evolutionary and biomedical insights from the rhesus macaque genome."
    Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C., Makova K.D., Miller W., Milosavljevic A.
    , Palermo R.E., Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., Zwieg A.S.
    Science 316:222-234(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 17573.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "De novo assembly of the rhesus macaque transcriptome from NextGen mRNA sequences."
    Pandey S., Maudhoo M.D., Guda C., Ferguson B., Fox H., Norgren R.B.
    Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-1210.
    Tissue: Caudate nucleus.
  4. "Developmental expression of the genes encoding transforming growth factor alpha and its receptor in the hypothalamus of female rhesus macaques."
    Ma Y.J., Costa M.E., Ojeda S.R.
    Neuroendocrinology 60:346-359(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 893-977.
    Tissue: Hypothalamus.

Entry informationi

Entry nameiEGFR_MACMU
AccessioniPrimary (citable) accession number: P55245
Secondary accession number(s): F6YXS7, G7ML99, H9FAB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 22, 2014
Last modified: July 22, 2015
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.