FA83B_HUMAN
ID FA83B_HUMAN Reviewed; 1011 AA.
AC Q5T0W9; Q2M1P3; Q96DQ2;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein FAM83B {ECO:0000305};
GN Name=FAM83B {ECO:0000312|HGNC:HGNC:21357};
GN Synonyms=C6orf143 {ECO:0000312|HGNC:HGNC:21357};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-640 AND ASN-907.
RC TISSUE=Heart, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-811.
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422; SER-424; SER-466;
RP SER-664; THR-782; SER-802 AND SER-852, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466 AND THR-782, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP FUNCTION, INTERACTION WITH RAF1, SUBCELLULAR LOCATION, AND REGION.
RX PubMed=22886302; DOI=10.1172/jci60517;
RA Cipriano R., Graham J., Miskimen K.L., Bryson B.L., Bruntz R.C.,
RA Scott S.A., Brown H.A., Stark G.R., Jackson M.W.;
RT "FAM83B mediates EGFR- and RAS-driven oncogenic transformation.";
RL J. Clin. Invest. 122:3197-3210(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334; SER-466; SER-543;
RP SER-664; THR-782; SER-802; SER-869 AND SER-915, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP FUNCTION, AND INTERACTION WITH AKT1; PIK3CA AND PIK3R1.
RX PubMed=23676467; DOI=10.18632/oncotarget.1027;
RA Cipriano R., Miskimen K.L., Bryson B.L., Foy C.R., Bartel C.A.,
RA Jackson M.W.;
RT "FAM83B-mediated activation of PI3K/AKT and MAPK signaling cooperates to
RT promote epithelial cell transformation and resistance to targeted
RT therapies.";
RL Oncotarget 4:729-738(2013).
RN [11]
RP FUNCTION, INTERACTION WITH EGFR, AND MUTAGENESIS OF LYS-230.
RX PubMed=23912460; DOI=10.1038/onc.2013.293;
RA Cipriano R., Bryson B.L., Miskimen K.L., Bartel C.A., Hernandez-Sanchez W.,
RA Bruntz R.C., Scott S.A., Lindsley C.W., Brown H.A., Jackson M.W.;
RT "Hyperactivation of EGFR and downstream effector phospholipase D1 by
RT oncogenic FAM83B.";
RL Oncogene 33:3298-3306(2014).
CC -!- FUNCTION: Probable proto-oncogene that functions in the epidermal
CC growth factor receptor/EGFR signaling pathway. May activate both the
CC EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling
CC cascades. {ECO:0000269|PubMed:22886302, ECO:0000269|PubMed:23676467,
CC ECO:0000269|PubMed:23912460}.
CC -!- SUBUNIT: Interacts with EGFR; the interaction is disrupted by EGF
CC stimulation (PubMed:23912460). Interacts with RAF1; displaces 14-3-3
CC proteins from RAF1 and activates RAF1 within the RAS/MAPK signaling
CC cascade (PubMed:22886302). Interacts with AKT1, PIK3CA and PIK3R1;
CC activates the PI3K/AKT signaling cascade (PubMed:23676467).
CC {ECO:0000269|PubMed:22886302, ECO:0000269|PubMed:23676467,
CC ECO:0000269|PubMed:23912460}.
CC -!- INTERACTION:
CC Q5T0W9; P48729: CSNK1A1; NbExp=8; IntAct=EBI-2556565, EBI-1383726;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22886302}. Membrane
CC {ECO:0000269|PubMed:22886302}.
CC -!- SIMILARITY: Belongs to the FAM83 family. {ECO:0000305}.
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DR EMBL; AL512363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04439.1; -; Genomic_DNA.
DR EMBL; BC101628; AAI01629.1; -; mRNA.
DR EMBL; BC112275; AAI12276.1; -; mRNA.
DR EMBL; AK055204; BAB70873.1; -; mRNA.
DR CCDS; CCDS34479.1; -.
DR RefSeq; NP_001010872.1; NM_001010872.2.
DR RefSeq; XP_006715085.1; XM_006715022.3.
DR RefSeq; XP_011512696.1; XM_011514394.2.
DR RefSeq; XP_011512697.1; XM_011514395.2.
DR RefSeq; XP_016865967.1; XM_017010478.1.
DR PDB; 5LZK; X-ray; 1.57 A; A/B=117-294.
DR PDB; 5QHI; X-ray; 1.73 A; A/B=117-294.
DR PDB; 5QHJ; X-ray; 1.68 A; A/B=117-294.
DR PDB; 5QHK; X-ray; 1.61 A; A/B=117-294.
DR PDB; 5QHL; X-ray; 1.68 A; A/B=117-294.
DR PDB; 5QHM; X-ray; 1.79 A; A=117-294.
DR PDB; 5QHN; X-ray; 1.73 A; A=117-294.
DR PDB; 5QHO; X-ray; 1.66 A; A=117-294.
DR PDB; 5QHP; X-ray; 2.06 A; A=117-294.
DR PDB; 5QHQ; X-ray; 1.96 A; A=117-294.
DR PDB; 5QHR; X-ray; 1.68 A; A=117-294.
DR PDB; 5QHS; X-ray; 1.95 A; A=117-294.
DR PDBsum; 5LZK; -.
DR PDBsum; 5QHI; -.
DR PDBsum; 5QHJ; -.
DR PDBsum; 5QHK; -.
DR PDBsum; 5QHL; -.
DR PDBsum; 5QHM; -.
DR PDBsum; 5QHN; -.
DR PDBsum; 5QHO; -.
DR PDBsum; 5QHP; -.
DR PDBsum; 5QHQ; -.
DR PDBsum; 5QHR; -.
DR PDBsum; 5QHS; -.
DR AlphaFoldDB; Q5T0W9; -.
DR SMR; Q5T0W9; -.
DR BioGRID; 128805; 137.
DR IntAct; Q5T0W9; 35.
DR MINT; Q5T0W9; -.
DR STRING; 9606.ENSP00000304078; -.
DR iPTMnet; Q5T0W9; -.
DR PhosphoSitePlus; Q5T0W9; -.
DR BioMuta; FAM83B; -.
DR DMDM; 74744366; -.
DR EPD; Q5T0W9; -.
DR jPOST; Q5T0W9; -.
DR MassIVE; Q5T0W9; -.
DR MaxQB; Q5T0W9; -.
DR PaxDb; Q5T0W9; -.
DR PeptideAtlas; Q5T0W9; -.
DR PRIDE; Q5T0W9; -.
DR ProteomicsDB; 64210; -.
DR ABCD; Q5T0W9; 1 sequenced antibody.
DR Antibodypedia; 31026; 59 antibodies from 15 providers.
DR DNASU; 222584; -.
DR Ensembl; ENST00000306858.8; ENSP00000304078.7; ENSG00000168143.9.
DR GeneID; 222584; -.
DR KEGG; hsa:222584; -.
DR MANE-Select; ENST00000306858.8; ENSP00000304078.7; NM_001010872.3; NP_001010872.1.
DR UCSC; uc003pck.5; human.
DR CTD; 222584; -.
DR DisGeNET; 222584; -.
DR GeneCards; FAM83B; -.
DR HGNC; HGNC:21357; FAM83B.
DR HPA; ENSG00000168143; Tissue enhanced (esophagus, skin).
DR neXtProt; NX_Q5T0W9; -.
DR OpenTargets; ENSG00000168143; -.
DR PharmGKB; PA134987811; -.
DR VEuPathDB; HostDB:ENSG00000168143; -.
DR eggNOG; ENOG502RPYE; Eukaryota.
DR GeneTree; ENSGT00940000157889; -.
DR HOGENOM; CLU_011804_0_0_1; -.
DR InParanoid; Q5T0W9; -.
DR OMA; QFQPSQI; -.
DR OrthoDB; 103194at2759; -.
DR PhylomeDB; Q5T0W9; -.
DR TreeFam; TF330777; -.
DR PathwayCommons; Q5T0W9; -.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; Q5T0W9; -.
DR BioGRID-ORCS; 222584; 7 hits in 1072 CRISPR screens.
DR ChiTaRS; FAM83B; human.
DR GenomeRNAi; 222584; -.
DR Pharos; Q5T0W9; Tbio.
DR PRO; PR:Q5T0W9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5T0W9; protein.
DR Bgee; ENSG00000168143; Expressed in skin of abdomen and 70 other tissues.
DR Genevisible; Q5T0W9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IPI:UniProtKB.
DR GO; GO:0036313; F:phosphatidylinositol 3-kinase catalytic subunit binding; IPI:UniProtKB.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR012461; FAM83_N.
DR Pfam; PF07894; FAM83; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Membrane; Phosphoprotein; Proto-oncogene;
KW Reference proteome.
FT CHAIN 1..1011
FT /note="Protein FAM83B"
FT /id="PRO_0000297562"
FT REGION 1..284
FT /note="Required for interaction with RAF1 and for the
FT function"
FT /evidence="ECO:0000269|PubMed:22886302"
FT REGION 555..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 782
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 410
FT /note="N -> S (in dbSNP:rs13211183)"
FT /id="VAR_034638"
FT VARIANT 435
FT /note="S -> R (in dbSNP:rs9475076)"
FT /id="VAR_034639"
FT VARIANT 640
FT /note="K -> T (in dbSNP:rs239798)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034640"
FT VARIANT 907
FT /note="T -> N (in dbSNP:rs9475077)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034641"
FT MUTAGEN 230
FT /note="K->A: Loss of the ability to interact with and
FT activate EGFR."
FT /evidence="ECO:0000269|PubMed:23912460"
FT CONFLICT 349
FT /note="D -> G (in Ref. 4; BAB70873)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="K -> E (in Ref. 4; BAB70873)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="R -> S (in Ref. 4; BAB70873)"
FT /evidence="ECO:0000305"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:5LZK"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:5LZK"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:5LZK"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:5LZK"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:5LZK"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:5LZK"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:5LZK"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:5LZK"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:5LZK"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:5LZK"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:5LZK"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:5LZK"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:5LZK"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:5LZK"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:5LZK"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:5LZK"
FT STRAND 255..263
FT /evidence="ECO:0007829|PDB:5LZK"
FT HELIX 265..279
FT /evidence="ECO:0007829|PDB:5LZK"
SQ SEQUENCE 1011 AA; 114799 MW; 7EF02DC36F95CFC3 CRC64;
METSSMLSSL NDECKSDNYI EPHYKEWYRV AIDILIEHGL EAYQEFLVQE RVSDFLAEEE
INYILKNVQK VAQSTAHGTD DSCDDTLSSG TYWPVESDVE APNLDLGWPY VMPGLLGGTH
IDLLFHPPRA HLLTIKETIR KMIKEARKVI ALVMDIFTDV DIFKEIVEAS TRGVSVYILL
DESNFNHFLN MTEKQGCSVQ RLRNIRVRTV KGQDYLSKTG AKFHGKMEQK FLLVDCQKVM
YGSYSYMWSF EKAHLSMVQI ITGQLVESFD EEFRTLYARS CVPSSFAQEE SARVKHGKAL
WENGTYQHSV SSLASVSSQR NLFGRQDKIH KLDSSYFKNR GIYTLNEHDK YNIRSHGYKP
HFVPNFNGPN AIRQFQPNQI NENWKRHSYA GEQPETVPYL LLNRALNRTN NPPGNWKKPS
DSLSVASSSR EGYVSHHNTP AQSFANRLAQ RKTTNLADRN SNVRRSFNGT DNHIRFLQQR
MPTLEHTTKS FLRNWRIESY LNDHSEATPD SNGSALGDRF EGYDNPENLK ANALYTHSRL
RSSLVFKPTL PEQKEVNSCT TGSSNSTIIG SQGSETPKEV PDTPTNVQHL TDKPLPESIP
KLPLQSEAPK MHTLQVPENH SVALNQTTNG HTESNNYIYK TLGVNKQTEN LKNQQTENLL
KRRSFPLFDN SKANLDPGNS KHYVYSTLTR NRVRQPEKPK EDLLKSSKSM HNVTHNLEED
EEEVTKRNSP SGTTTKSVSI AALLDVNKEE SNKELASKKE VKGSPSFLKK GSQKLRSLLS
LTPDKKENLS KNKAPAFYRL CSSSDTLVSE GEENQKPKKS DTKVDSSPRR KHSSSSNSQG
SIHKSKEDVT VSPSQEINAP PDENKRTPSP GPVESKFLER AGDASAPRFN TEQIQYRDSR
EINAVVTPER RPTSSPRPTS SELLRSHSTD RRVYSRFEPF CKIESSIQPT SNMPNTSINR
PEIKSATMGN SYGRSSPLLN YNTGVYRSYQ PNENKFRGFM QKFGNFIHKN K
