ERRFI_HUMAN
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 03-AUG-2022, entry version 160.
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=13; IntAct=EBI-2941912, EBI-297353;
CC Q9UJM3; P04626: ERBB2; NbExp=3; 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="http://atlasgeneticsoncology.org/Genes/ERRFI1ID44147ch1p36.html";
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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; 108.
DR DIP; DIP-42379N; -.
DR IntAct; Q9UJM3; 34.
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; Q9UJM3; -.
DR PeptideAtlas; Q9UJM3; -.
DR PRIDE; Q9UJM3; -.
DR ProteomicsDB; 84632; -.
DR Antibodypedia; 27548; 214 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 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; MKTCWGS; -.
DR OrthoDB; 644164at2759; -.
DR PhylomeDB; Q9UJM3; -.
DR TreeFam; TF335720; -.
DR PathwayCommons; Q9UJM3; -.
DR SignaLink; Q9UJM3; -.
DR SIGNOR; Q9UJM3; -.
DR BioGRID-ORCS; 54206; 13 hits in 1077 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 186 other tissues.
DR ExpressionAtlas; Q9UJM3; baseline and differential.
DR Genevisible; Q9UJM3; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0071474; P:cellular hyperosmotic response; IEA:Ensembl.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; 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:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IEA:Ensembl.
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:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IEA:Ensembl.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0061469; P:regulation of type B pancreatic cell proliferation; IEA:Ensembl.
DR GO; GO:0043589; P:skin morphogenesis; ISS:UniProtKB.
DR IDEAL; IID00286; -.
DR InterPro; IPR015116; Cdc42-bd-like.
DR InterPro; IPR021619; Mig-6.
DR Pfam; PF09027; GTPase_binding; 1.
DR Pfam; PF11555; Inhibitor_Mig-6; 1.
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
