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Reviewed (UniProtKB/Swiss-Prot)

Note: Proteins listed in ProtBank™ database are NOT off-the-shelf [catalog] proteins. Customized protein production request can be made for any protein in this database by clicking on the corresponding button under "Quick Quote". Please ensure sequence accuracy and/or make any necessary modifications prior to submitting your quote request

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Reviewed (UniProtKB/Swiss-Prot)


Name Gene Symbol Rec Full Name Protein Information Quick Quote  Price,
Turnaround
ERRFI_RAT, Rattus norvegicus (Norway rat) Errfi1 Receptor-associated late transducer Functions
wild_type
Starting from $1600,
4 weeks
Protein Domains
mutant
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Protein Names | ProteinIDs  | Organism | Gene Names  | GeneID | Genome Annotation(Ensembl) |  Protein Sequence | 
General annotation |  References | Order
Protein Names
Recommended name:
 ERBB receptor feedback inhibitor 1;
Alternative name(s):
 Gene 33 polypeptide
Mitogen-inducible gene 6 protein homolog
Receptor-associated late transducer
Protein IDs
(Accession numbers)
UniProtKB
 P05432
NCBI RefSeq

NP_001014093.1, NM_001014071.1.
Organism
Latin Name/
(Common Name)
Rattus norvegicus (Rat).
Taxonomic Identifier (NCBI)
 10116
Gene Names
 Errfi1 [GenPool]
GeneID

313729
Genome
Annotation (Ensembl)

ENSRNOT00000024606, ENSRNOP00000024606; ENSRNOG00000018275
Protein Sequence
 
SEQUENCE   459 AA;  49941 MW;  EBD90F11757AC549 CRC64;
MSTAGVAAQD IRVPLKTGFL HNGQALGNMK TCWGSRNEFE KNFLNIDPIT MAYNLNSPAP
EHLTTLGCAS PSAPGSGHFF AERGPSPKSS LPPLVIPPSE SSGQREEDQV LCGFKKLSVN
GVCASTPPLT PIQSCSSPFP CAAPCDRSSR PLPPLPISED PSLDEADCEV EFLTSADTDF
LLEDCVPSDF KYDVPGRRSF RGCGQINYAY FDSPTVSVAD LSCASDQNRV VPDPNPPPPQ
SHRRLRRSHS GPAGSFNKPA IRISSCTHRA SPSSDEDKPE IPPRVPIPPR PAKPDYRRWS
AEVTSNTYSD EDRPPKVPPR EPLSRSNSRT PSPKSLPSYL NGVMPPTQSF APDPKYVSSK
ALQRQSSEGS AKAPCILPII ENGKKVSSTH YYLLPERPPY LDKYEKYFRE AEEANPSTQI
QPLPAACGMV SATDKLASRM KMDVGGHGKR KHLSYVVSP
General annotation
Function
 Negative regulator of EGFR signaling in skin morphogenesis. Acts as a negative regulator for several EGFR family members, including ERBB2, ERBB3 and ERBB4. Inhibits EGFR catalytic activity by interfering with its dimerization. Inhibits autophosphorylation of EGFR, ERBB2 and ERBB4. Important for normal keratinocyte proliferation and differentiation. Plays a role in modulating the response to steroid hormones in the uterus. Required for normal response to progesterone in the uterus and for fertility. Mediates epithelial estrogen responses in the uterus by regulating ESR1 levels and activation. Important for regulation of endometrium cell proliferation. Important for normal prenatal and perinatal lung development (By similarity).
Cofactor
Subunit structure
 Interacts with EGFR and ERBB2.
Subcellular location

Cytoplasm (By similarity). Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Nucleus (By similarity). Note=Associated with the plasma membrane of basal skin keratinocytes. Translocates into the nucleus of differentiating suprabasal keratinocytes (By similarity).
Tissue specificity
Induction
 By cAMP, glucocorticoids, phorbol esters and insulin.
Domain
 The EGFR-binding region prevents binding of a cyclin-like activator to the EGFR kinase domain, and thereby keeps EGFR in an inactive conformation. Also maintains EGFR in an inactive conformation by preventing formation of an asymmetric homodimer (By similarity).
Post-translational modification

Involvement in disease

References

  • "Structure of a multihormonally regulated rat gene.";,Tindal M.H., Lee K.-L., Isham K.R., Cadilla C., Kenney F.T.;,Gene 71:413-420(1988)., PubMeb:3224831 DOI:10.1016/0378-1119(88)90058-3

  • "Rat gene 33: analysis of its structure, messenger RNA and basalpromoter activity.";,Chrapkiewicz N.B., Davis C.M., Chu D.T.W., Granner D.K.;,Nucleic Acids Res. 17:6651-6667(1989)., PubMeb:2780291 DOI:10.1093/nar/17.16.6651

  • "Molecular cloning and analysis of full-length cDNAs cognate to a ratgene under multihormonal control.";,Lee K.-L., Makkinje A., Ch'Ang L.-Y., Kenney F.T.;,Arch. Biochem. Biophys. 269:106-113(1989)., PubMeb:2916834 DOI:10.1016/0003-9861(89)90091-X

  • "The status, quality, and expansion of the NIH full-length cDNAproject: the Mammalian Gene Collection (MGC).";,Genome Res. 14:2121-2127(2004).,PubMeb:15489334 DOI:10.1101/gr.2596504

  • "Inhibition of ErbB-2 mitogenic and transforming activity by RALT, amitogen-induced signal transducer which binds to the ErbB-2 kinasedomain.";,Fiorentino L., Pertica C., Fiorini M., Talora C., Crescenzi M.,Castellani L., Alema S., Benedetti P., Segatto O.;,Mol. Cell. Biol. 20:7735-7750(2000).,PubMeb:11003669 DOI:10.1128/MCB.20.20.7735-7750.2000

  • "The evolutionarily conserved EBR module of RALT/MIG6 mediatessuppression of the EGFR catalytic activity.";,Anastasi S., Baietti M.F., Frosi Y., Alema S., Segatto O.;,Oncogene 26:7833-7846(2007).,PubMeb:17599051 DOI:10.1038/sj.onc.1210590

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Protein Domain Databases
InterPro

IPR015116, GTPase_binding.

IPR021619, Inhibitor_Mig-6.
Gene3D
PANTHER
Pfam

PF09027, GTPase_binding; 1.

PF11555, Inhibitor_Mig-6; 1.
PRINTS
SUPFAM
PROSITE
3D Structure
Database (PDB)
Entry
Method
Resolution (A)
Chain
Positions
PDBsum
Sequence
Annotation
Feature key
Position(s)
Length
Description
Polypeptide chain 1 - 459 459 ERBB receptor feedback inhibitor 1. /FTId=PRO_0000096489.
Region 332 - 361 30 Interaction with EGFR and ERBB2 and
Posttranslational modification of a residue 126 1 Phosphothreonine (By similarity).
Posttranslational modification of a residue 130 1 Phosphothreonine (By similarity).
Posttranslational modification of a residue 250 1 Phosphoserine (By similarity).
Posttranslational modification of a residue 271 1 Phosphoserine (By similarity).
Posttranslational modification of a residue 391 1 Phosphotyrosine (By similarity).
Posttranslational modification of a residue 392 1 Phosphotyrosine (By similarity).
Posttranslational modification of a residue 458 1 Phosphoserine (By similarity).
Natural variance 67 - 142 76 Missing (in isoform 2). /FTId=VSP_011893.
Different sources report differing sequences 18 1 G -> K (in Ref. 3; no nucleotide entry).
Different sources report differing sequences 192 1 Y -> T (in Ref. 3; no nucleotide entry).
Different sources report differing sequences 302 1 E -> L (in Ref. 3; no nucleotide entry).
Different sources report differing sequences 311 1 E -> L (in Ref. 3; no nucleotide entry).
Different sources report differing sequences 396 1 E -> L (in Ref. 3; no nucleotide entry).
Different sources report differing sequences 410 1 E -> L (in Ref. 3; no nucleotide entry).
Protein-protein
Interaction
Databases
DIP
IntAct
MINT
STRING

P05432
Binary Interactions
With
Entry
#Exp.
IntAct
Enzyme and Pathway Databases
Pathway
Interaction DB
Reactome
Phylogenomic Database
HOVERGEN

HBG031710
InParanoid

P05432
OMA

TDCEVEF
OrthoDB

EOG4CVG6X
Proteomics
Database (PRIDE)

P05432
Comparative
Toxicogenomics
Database (CTD)

54206
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