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P55245

- EGFR_MACMU

UniProt

P55245 - EGFR_MACMU

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Protein
Epidermal growth factor receptor
Gene
EGFR
Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed - 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.

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 – 7451ATP By similarity
Active sitei837 – 8371Proton acceptor By similarity
Binding sitei855 – 8551ATP By similarity
Sitei1016 – 10161Important for interaction with PIK3C2B By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi718 – 7269ATP By similarity
Nucleotide bindingi790 – 7912ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. chromatin binding Source: UniProtKB
  3. epidermal growth factor-activated receptor activity Source: Ensembl
  4. nitric-oxide synthase regulator activity Source: Ensembl
  5. protein tyrosine kinase activity Source: UniProtKB
  6. receptor signaling protein tyrosine kinase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. cell morphogenesis Source: Ensembl
  2. cell proliferation Source: Ensembl
  3. cellular response to epidermal growth factor stimulus Source: UniProtKB
  4. cellular response to estradiol stimulus Source: UniProtKB
  5. cerebral cortex cell migration Source: Ensembl
  6. digestive tract morphogenesis Source: Ensembl
  7. embryonic placenta development Source: Ensembl
  8. epidermal growth factor receptor signaling pathway Source: UniProtKB
  9. hair follicle development Source: Ensembl
  10. learning or memory Source: UniProtKB
  11. morphogenesis of an epithelial fold Source: Ensembl
  12. negative regulation of apoptotic process Source: Ensembl
  13. negative regulation of protein catabolic process Source: Ensembl
  14. positive regulation of DNA repair Source: Ensembl
  15. positive regulation of DNA replication Source: Ensembl
  16. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  17. positive regulation of MAP kinase activity Source: Ensembl
  18. positive regulation of catenin import into nucleus Source: Ensembl
  19. positive regulation of cell migration Source: Ensembl
  20. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: Ensembl
  21. positive regulation of epithelial cell proliferation Source: Ensembl
  22. positive regulation of fibroblast proliferation Source: Ensembl
  23. positive regulation of nitric oxide biosynthetic process Source: Ensembl
  24. positive regulation of protein kinase B signaling Source: Ensembl
  25. positive regulation of protein phosphorylation Source: UniProtKB
  26. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  27. protein autophosphorylation Source: Ensembl
  28. regulation of nitric-oxide synthase activity Source: Ensembl
  29. regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  30. response to UV-A Source: Ensembl
  31. salivary gland morphogenesis Source: Ensembl
  32. single organismal cell-cell adhesion Source: Ensembl
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: Unplaced

Subcellular locationi

Cell membrane; Single-pass type I membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass type I membrane protein By similarity. Golgi apparatus membrane; Single-pass type I membrane protein By similarity. Nucleus membrane; Single-pass type I membrane protein By similarity. Endosome. Endosome membrane By similarity. Nucleus By similarity
Note: In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) By similarity.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 645621Extracellular Reviewed prediction
Add
BLAST
Transmembranei646 – 66823Helical; Reviewed prediction
Add
BLAST
Topological domaini669 – 1210542Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. basolateral plasma membrane Source: Ensembl
  3. endocytic vesicle Source: Ensembl
  4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  5. endosome Source: UniProtKB
  6. endosome membrane Source: UniProtKB-SubCell
  7. integral component of membrane Source: UniProtKB-KW
  8. membrane raft Source: Ensembl
  9. nuclear membrane Source: UniProtKB-SubCell
  10. nucleus Source: UniProtKB
  11. perinuclear region of cytoplasm Source: Ensembl
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 – 2424 Reviewed prediction
Add
BLAST
Chaini25 – 12101186Epidermal growth factor receptor
PRO_0000160254Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 58 By similarity
Glycosylationi73 – 731N-linked (GlcNAc...); atypical By similarity
Glycosylationi128 – 1281N-linked (GlcNAc...) By similarity
Disulfide bondi157 ↔ 187 By similarity
Glycosylationi175 – 1751N-linked (GlcNAc...) By similarity
Disulfide bondi190 ↔ 199 By similarity
Disulfide bondi194 ↔ 207 By similarity
Glycosylationi196 – 1961N-linked (GlcNAc...) By similarity
Disulfide bondi215 ↔ 223 By similarity
Disulfide bondi219 ↔ 231 By similarity
Modified residuei229 – 2291Phosphoserine By similarity
Disulfide bondi232 ↔ 240 By similarity
Disulfide bondi236 ↔ 248 By similarity
Disulfide bondi251 ↔ 260 By similarity
Disulfide bondi264 ↔ 291 By similarity
Disulfide bondi295 ↔ 307 By similarity
Disulfide bondi311 ↔ 326 By similarity
Disulfide bondi329 ↔ 333 By similarity
Disulfide bondi337 ↔ 362 By 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 ↔ 499 By similarity
Disulfide bondi506 ↔ 515 By similarity
Disulfide bondi510 ↔ 523 By similarity
Disulfide bondi526 ↔ 535 By similarity
Glycosylationi528 – 5281N-linked (GlcNAc...) By similarity
Disulfide bondi539 ↔ 555 By similarity
Disulfide bondi558 ↔ 571 By similarity
Disulfide bondi562 ↔ 579 By similarity
Glycosylationi568 – 5681N-linked (GlcNAc...) By similarity
Disulfide bondi582 ↔ 591 By similarity
Disulfide bondi595 ↔ 617 By similarity
Glycosylationi603 – 6031N-linked (GlcNAc...) By similarity
Disulfide bondi620 ↔ 628 By similarity
Disulfide bondi624 ↔ 636 By similarity
Modified residuei678 – 6781Phosphothreonine; by PKC and PKD/PRKD1 By similarity
Modified residuei693 – 6931Phosphothreonine; by PKD/PRKD1 By similarity
Modified residuei695 – 6951Phosphoserine By 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 – 9911Phosphoserine By similarity
Modified residuei995 – 9951Phosphoserine By similarity
Modified residuei998 – 9981Phosphotyrosine; by autocatalysis By similarity
Modified residuei1016 – 10161Phosphotyrosine; by autocatalysis By similarity
Modified residuei1026 – 10261Phosphoserine By similarity
Modified residuei1039 – 10391Phosphoserine By similarity
Modified residuei1041 – 10411Phosphothreonine By similarity
Modified residuei1042 – 10421Phosphoserine By similarity
Modified residuei1064 – 10641Phosphoserine By similarity
Modified residuei1070 – 10701Phosphoserine By similarity
Modified residuei1071 – 10711Phosphoserine By similarity
Modified residuei1081 – 10811Phosphoserine By similarity
Modified residuei1092 – 10921Phosphotyrosine; by autocatalysis By similarity
Modified residuei1110 – 11101Phosphotyrosine; by autocatalysis By similarity
Modified residuei1166 – 11661Phosphoserine By similarity
Modified residuei1172 – 11721Phosphotyrosine; by autocatalysis By similarity
Modified residuei1197 – 11971Phosphotyrosine; by autocatalysis By similarity
Modified residuei1199 – 11991Omega-N-methylated arginine By 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-955', but linkage through 'Lys-940', 'Lys-903' and 'Lys-921' also occur. Deubiquitinated by OTUD7B, preventing degradation By similarity.
Phosphorylated. Autophosphorylates. Dephosphorylated by PTPN1 and PTPN2 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).

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) By similarity.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati75 – 300226Approximate
Add
BLAST
Repeati390 – 600211Approximate
Add
BLAST
Domaini712 – 979268Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni688 – 70417Important for dimerization, phosphorylation and activation By similarity
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000230982.
InParanoidiP55245.
TreeFamiTF106002.

Family and domain databases

Gene3Di3.80.20.20. 2 hits.
InterProiIPR000494. EGF_rcpt_L.
IPR006211. 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.
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

MRPSGTAGAA LLALLAALCP ASRALEEKKV CQGTSNKLTQ LGTFEDHFLS     50
LQRMFNNCEV VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP 100
LENLQIIRGN MYYENSYALA VLSNYDANKT GLKELPMRNL QEILHGAVRF 150
SNNPALCNVE SIQWRDIVSS EFLSNMSMDF QNHLGSCQKC DPSCPNGSCW 200
GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC TGPRESDCLV 250
CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV 300
VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDTLS 350
INATNIKHFK NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE 400
ITGFLLIQAW PENRTDLHAF ENLEIIRGRT KQHGQFSLAV VSLNITSLGL 450
RSLKEISDGD VIISGNKNLC YANTINWKKL FGTSSQKTKI ISNRGENSCK 500
ATGQVCHALC SPEGCWGPEP RDCVSCQNVS RGRECVDKCN VLEGEPREFV 550
ENSECIQCHP ECLPQVMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM 600
GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCARNG PKIPSIATGM 650
VGALLLLLVV ALGIGLFMRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN 700
QALLRILKET EFKKIKVLGS GAFGTVYKGL WIPEGEKVKI PVAIKELREA 750
TSPKANKEIL DEAYVMASVD NPHVCRLLGI CLTSTVQLIT QLMPFGCLLD 800
YVREHKDNIG SQYLLNWCVQ IAKGMNYLED RRLVHRDLAA RNVLVKTPQH 850
VKITDFGLAK LLGAEEKEYH AEGGKVPIKW MALESILHRI YTHQSDVWSY 900
GVTVWELMTF GSKPYDGIPA SEISSILEKG ERLPQPPICT IDVYMIMVKC 950
WMIDADSRPK FRELIIEFSK MARDPQRYLV IQGDERMHLP SPTDSNFYRA 1000
LMDEEDMDDV VDADEYLIPQ QGFFSSPSTS RTPLLSSLSA TSNNSTVACI 1050
DRNGLQSCPI KEDSFLQRYS SDPTGALTED SIDDTFLPVP EYINQSVPKR 1100
PAGSVQNPVY HNQPLNPAPS RDPHYQDPHS TAVGNPEYLN TVQPTCVNST 1150
FDSPAHWAQK GSHQISLDNP DYQQDFFPKE AKPNGIFKGS TAENAEYLRV 1200
APQSSEFIGA 1210
Length:1,210
Mass (Da):134,350
Last modified:January 22, 2014 - v2
Checksum:iE114E9CEE96D64CC
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti541 – 5411V → I in EHH17303. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
JH286850 Genomic DNA. No translation available.
CM001255 Genomic DNA. Translation: EHH17303.1 .
JU327815 mRNA. Translation: AFE71571.1 .
S75916 mRNA. Translation: AAB33095.1 .
PIRi I78540.
UniGenei Mmu.3397.

3D structure databases

ModBasei Search...

Chemistry

BindingDBi P55245.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000230982.
InParanoidi P55245.
TreeFami TF106002.

Family and domain databases

Gene3Di 3.80.20.20. 2 hits.
InterProi IPR000494. EGF_rcpt_L.
IPR006211. 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.
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 ]
Pfami PF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view ]
PIRSFi PIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00261. FU. 4 hits.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 9, 2014
This is version 118 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