ID ERRFI_HUMAN Reviewed; 462 AA. AC Q9UJM3; B2RDX9; Q9NTG9; Q9UD05; DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 168. DE RecName: Full=ERBB receptor feedback inhibitor 1; DE AltName: Full=Mitogen-inducible gene 6 protein; DE Short=MIG-6; GN Name=ERRFI1; Synonyms=MIG6; 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 [MRNA], AND SUBCELLULAR LOCATION. RX PubMed=7641805; DOI=10.1006/excr.1995.1261; RA Wick M., Buerger C., Funk M., Mueller R.; RT "Identification of a novel mitogen-inducible gene (mig-6): regulation RT during G1 progression and differentiation."; RL Exp. Cell Res. 219:527-535(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Van Laar T., Schouten T., van der Eb A.J., Terleth C.; RT "The gene for Mig-6 is regulated by methylmethanesulphonate and shows high RT expression in the liver."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 302-462. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251 AND SER-461, AND RP IDENTIFICATION BY MASS 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251 AND SER-461, AND 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251 AND SER-273, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 325-364 IN COMPLEX WITH EGFR, RP SUBUNIT, MUTAGENESIS OF MET-346; PHE-352 AND TYR-358, AND DOMAIN. RX PubMed=18046415; DOI=10.1038/nature05998; RA Zhang X., Pickin K.A., Bose R., Jura N., Cole P.A., Kuriyan J.; RT "Inhibition of the EGF receptor by binding of MIG6 to an activating kinase RT domain interface."; RL Nature 450:741-744(2007). CC -!- FUNCTION: Negative regulator of EGFR signaling in skin morphogenesis. CC Acts as a negative regulator for several EGFR family members, including CC ERBB2, ERBB3 and ERBB4. Inhibits EGFR catalytic activity by interfering CC with its dimerization. Inhibits autophosphorylation of EGFR, ERBB2 and CC ERBB4. Important for normal keratinocyte proliferation and CC differentiation. Plays a role in modulating the response to steroid CC hormones in the uterus. Required for normal response to progesterone in CC the uterus and for fertility. Mediates epithelial estrogen responses in CC the uterus by regulating ESR1 levels and activation. Important for CC regulation of endometrium cell proliferation. Important for normal CC prenatal and perinatal lung development (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with ERBB2 (By similarity). Interacts with EGFR. CC {ECO:0000250, ECO:0000269|PubMed:18046415}. CC -!- INTERACTION: CC Q9UJM3; O14757: CHEK1; NbExp=2; IntAct=EBI-2941912, EBI-974488; CC Q9UJM3; P00533: EGFR; NbExp=15; IntAct=EBI-2941912, EBI-297353; CC Q9UJM3; P04626: ERBB2; NbExp=4; IntAct=EBI-2941912, EBI-641062; CC Q9UJM3; P06241-3: FYN; NbExp=3; IntAct=EBI-2941912, EBI-10691738; CC Q9UJM3; P62993: GRB2; NbExp=16; IntAct=EBI-2941912, EBI-401755; CC Q9UJM3; P31947: SFN; NbExp=3; IntAct=EBI-2941912, EBI-476295; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7641805}. Cell CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; CC Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}. Note=Associated CC with the plasma membrane of basal skin keratinocytes. Translocates into CC the nucleus of differentiating suprabasal keratinocytes (By CC similarity). {ECO:0000250}. CC -!- INDUCTION: Levels are very low in quiescent cells. Up-regulated by CC mitogens. CC -!- DOMAIN: The EGFR-binding region prevents binding of a cyclin-like CC activator to the EGFR kinase domain, and thereby keeps EGFR in an CC inactive conformation. Also maintains EGFR in an inactive conformation CC by preventing formation of an asymmetric homodimer. CC {ECO:0000269|PubMed:18046415}. CC -!- SIMILARITY: Belongs to the MIG6 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44147/ERRFI1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ276373; CAC20426.1; -; mRNA. DR EMBL; AL034417; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK315718; BAG38076.1; -; mRNA. DR EMBL; CH471130; EAW71593.1; -; Genomic_DNA. DR EMBL; BC025337; AAH25337.1; -; mRNA. DR EMBL; AL137274; CAB70672.1; -; mRNA. DR CCDS; CCDS94.1; -. DR PIR; T46346; T46346. DR RefSeq; NP_061821.1; NM_018948.3. DR RefSeq; XP_006710760.1; XM_006710697.2. DR PDB; 2RF9; X-ray; 3.50 A; C/D=315-374. DR PDB; 2RFD; X-ray; 3.60 A; C/D=340-364. DR PDB; 2RFE; X-ray; 2.90 A; E/F=325-364. DR PDB; 4I21; X-ray; 3.37 A; C/D=315-374. DR PDB; 4R3P; X-ray; 2.90 A; B=392-398. DR PDB; 4R3R; X-ray; 3.25 A; B=392-398. DR PDB; 4ZJV; X-ray; 2.70 A; C/D=330-399. DR PDBsum; 2RF9; -. DR PDBsum; 2RFD; -. DR PDBsum; 2RFE; -. DR PDBsum; 4I21; -. DR PDBsum; 4R3P; -. DR PDBsum; 4R3R; -. DR PDBsum; 4ZJV; -. DR AlphaFoldDB; Q9UJM3; -. DR SMR; Q9UJM3; -. DR BioGRID; 119923; 111. DR DIP; DIP-42379N; -. DR IntAct; Q9UJM3; 33. DR MINT; Q9UJM3; -. DR STRING; 9606.ENSP00000366702; -. DR iPTMnet; Q9UJM3; -. DR PhosphoSitePlus; Q9UJM3; -. DR BioMuta; ERRFI1; -. DR DMDM; 27923810; -. DR CPTAC; CPTAC-1566; -. DR EPD; Q9UJM3; -. DR jPOST; Q9UJM3; -. DR MassIVE; Q9UJM3; -. DR MaxQB; Q9UJM3; -. DR PaxDb; 9606-ENSP00000366702; -. DR PeptideAtlas; Q9UJM3; -. DR ProteomicsDB; 84632; -. DR Pumba; Q9UJM3; -. DR Antibodypedia; 27548; 243 antibodies from 29 providers. DR CPTC; Q9UJM3; 2 antibodies. DR DNASU; 54206; -. DR Ensembl; ENST00000377482.10; ENSP00000366702.5; ENSG00000116285.13. DR GeneID; 54206; -. DR KEGG; hsa:54206; -. DR MANE-Select; ENST00000377482.10; ENSP00000366702.5; NM_018948.4; NP_061821.1. DR UCSC; uc001aoz.4; human. DR AGR; HGNC:18185; -. DR CTD; 54206; -. DR DisGeNET; 54206; -. DR GeneCards; ERRFI1; -. DR HGNC; HGNC:18185; ERRFI1. DR HPA; ENSG00000116285; Tissue enhanced (liver, pancreas). DR MIM; 608069; gene. DR neXtProt; NX_Q9UJM3; -. DR OpenTargets; ENSG00000116285; -. DR PharmGKB; PA142671904; -. DR VEuPathDB; HostDB:ENSG00000116285; -. DR eggNOG; ENOG502QPQW; Eukaryota. DR GeneTree; ENSGT00440000033870; -. DR HOGENOM; CLU_604032_0_0_1; -. DR InParanoid; Q9UJM3; -. DR OMA; CWGSHSG; -. DR OrthoDB; 5345626at2759; -. DR PhylomeDB; Q9UJM3; -. DR TreeFam; TF335720; -. DR PathwayCommons; Q9UJM3; -. DR SignaLink; Q9UJM3; -. DR SIGNOR; Q9UJM3; -. DR BioGRID-ORCS; 54206; 14 hits in 1157 CRISPR screens. DR ChiTaRS; ERRFI1; human. DR EvolutionaryTrace; Q9UJM3; -. DR GeneWiki; ERRFI1; -. DR GenomeRNAi; 54206; -. DR Pharos; Q9UJM3; Tbio. DR PRO; PR:Q9UJM3; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9UJM3; Protein. DR Bgee; ENSG00000116285; Expressed in body of pancreas and 188 other cell types or tissues. DR ExpressionAtlas; Q9UJM3; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl. DR GO; GO:0006699; P:bile acid biosynthetic process; IEA:Ensembl. DR GO; GO:0051216; P:cartilage development; IEA:Ensembl. DR GO; GO:0016477; P:cell migration; IEA:Ensembl. DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl. DR GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl. DR GO; GO:0035988; P:chondrocyte proliferation; IEA:Ensembl. DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl. DR GO; GO:0060613; P:fat pad development; IEA:Ensembl. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl. DR GO; GO:0036022; P:limb joint morphogenesis; IEA:Ensembl. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0048286; P:lung alveolus development; ISS:UniProtKB. DR GO; GO:0060428; P:lung epithelium development; ISS:UniProtKB. DR GO; GO:0060426; P:lung vasculature development; ISS:UniProtKB. DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; IDA:UniProtKB. DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; IDA:UniProtKB. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:0050847; P:progesterone receptor signaling pathway; IEA:Ensembl. DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl. DR GO; GO:0045616; P:regulation of keratinocyte differentiation; ISS:UniProtKB. DR GO; GO:1904565; P:response to 1-oleoyl-sn-glycerol 3-phosphate; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0032868; P:response to insulin; IEA:Ensembl. DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0043589; P:skin morphogenesis; ISS:UniProtKB. DR GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl. DR GO; GO:0035847; P:uterine epithelium development; IEA:Ensembl. DR IDEAL; IID00286; -. DR InterPro; IPR015116; Cdc42-bd-like. DR InterPro; IPR021619; Mig-6. DR PANTHER; PTHR14254:SF5; ERBB RECEPTOR FEEDBACK INHIBITOR 1; 1. DR PANTHER; PTHR14254; GENE 33 POLYPEPTIDE; 1. DR Pfam; PF09027; GTPase_binding; 1. DR Pfam; PF11555; Inhibitor_Mig-6; 1. DR Genevisible; Q9UJM3; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cell membrane; Cytoplasm; Membrane; Nucleus; KW Phosphoprotein; Reference proteome; Tumor suppressor. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..462 FT /note="ERBB receptor feedback inhibitor 1" FT /id="PRO_0000096487" FT REGION 225..374 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 334..363 FT /note="Interaction with EGFR and ERBB2 and regulation of FT EGFR activation" FT REGION 415..448 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 329..347 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 127 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q99JZ7" FT MOD_RES 131 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q99JZ7" FT MOD_RES 251 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 273 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 302 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99JZ7" FT MOD_RES 461 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:21406692" FT VARIANT 109 FT /note="D -> N (in dbSNP:rs34781518)" FT /id="VAR_063039" FT VARIANT 158 FT /note="I -> L (in dbSNP:rs34974993)" FT /id="VAR_050975" FT MUTAGEN 346 FT /note="M->A: Abolishes inhibition of EGFR activity." FT /evidence="ECO:0000269|PubMed:18046415" FT MUTAGEN 352 FT /note="F->A: Abolishes inhibition of EGFR activity." FT /evidence="ECO:0000269|PubMed:18046415" FT MUTAGEN 358 FT /note="Y->A: Abolishes inhibition of EGFR activity." FT /evidence="ECO:0000269|PubMed:18046415" FT CONFLICT 7 FT /note="A -> T (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 36 FT /note="S -> C (in Ref. 1)" FT /evidence="ECO:0000305" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:4ZJV" FT TURN 356..358 FT /evidence="ECO:0007829|PDB:4ZJV" FT STRAND 378..382 FT /evidence="ECO:0007829|PDB:4ZJV" FT STRAND 390..397 FT /evidence="ECO:0007829|PDB:4ZJV" SQ SEQUENCE 462 AA; 50560 MW; 7AFA9F6CEB602912 CRC64; MSIAGVAAQE IRVPLKTGFL HNGRAMGNMR KTYWSSRSEF KNNFLNIDPI TMAYSLNSSA QERLIPLGHA SKSAPMNGHC FAENGPSQKS SLPPLLIPPS ENLGPHEEDQ VVCGFKKLTV NGVCASTPPL TPIKNSPSLF PCAPLCERGS RPLPPLPISE ALSLDDTDCE VEFLTSSDTD FLLEDSTLSD FKYDVPGRRS FRGCGQINYA YFDTPAVSAA DLSYVSDQNG GVPDPNPPPP QTHRRLRRSH SGPAGSFNKP AIRISNCCIH RASPNSDEDK PEVPPRVPIP PRPVKPDYRR WSAEVTSSTY SDEDRPPKVP PREPLSPSNS RTPSPKSLPS YLNGVMPPTQ SFAPDPKYVS SKALQRQNSE GSASKVPCIL PIIENGKKVS STHYYLLPER PPYLDKYEKF FREAEETNGG AQIQPLPADC GISSATEKPD SKTKMDLGGH VKRKHLSYVV SP //