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P01132

- EGF_MOUSE

UniProt

P01132 - EGF_MOUSE

Protein

Pro-epidermal growth factor

Gene

Egf

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6 By similarity.By similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. epidermal growth factor receptor binding Source: MGI
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of MAPKK activity Source: MGI
    2. angiogenesis Source: Ensembl
    3. branching morphogenesis of an epithelial tube Source: MGI
    4. epidermal growth factor receptor signaling pathway Source: MGI
    5. ERK1 and ERK2 cascade Source: Ensembl
    6. mammary gland alveolus development Source: MGI
    7. negative regulation of cholesterol efflux Source: BHF-UCL
    8. negative regulation of secretion Source: Ensembl
    9. peptidyl-tyrosine phosphorylation Source: MGI
    10. positive regulation of catenin import into nucleus Source: Ensembl
    11. positive regulation of cell proliferation Source: MGI
    12. positive regulation of cerebellar granule cell precursor proliferation Source: MGI
    13. positive regulation of DNA binding Source: UniProtKB
    14. positive regulation of epidermal growth factor-activated receptor activity Source: Ensembl
    15. positive regulation of hyaluronan biosynthetic process Source: Ensembl
    16. positive regulation of MAP kinase activity Source: Ensembl
    17. positive regulation of mitosis Source: Ensembl
    18. positive regulation of peptidyl-threonine phosphorylation Source: Ensembl
    19. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL
    20. positive regulation of transcription, DNA-templated Source: Ensembl
    21. regulation of calcium ion import Source: Ensembl
    22. regulation of peptidyl-tyrosine phosphorylation Source: MGI
    23. regulation of protein localization to cell surface Source: Ensembl
    24. regulation of protein transport Source: MGI
    25. STAT protein import into nucleus Source: UniProtKB

    Keywords - Molecular functioni

    Growth factor

    Enzyme and pathway databases

    ReactomeiREACT_188190. PLCG1 events in ERBB2 signaling.
    REACT_188191. Signaling by ERBB2.
    REACT_188528. GRB2 events in ERBB2 signaling.
    REACT_188574. SHC1 events in ERBB2 signaling.
    REACT_188579. Signaling by ERBB4.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_199123. Signaling by constitutively active EGFR.
    REACT_203917. EGFR downregulation.
    REACT_206286. GAB1 signalosome.
    REACT_215348. PI3K events in ERBB2 signaling.
    REACT_226341. PIP3 activates AKT signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pro-epidermal growth factor
    Short name:
    EGF
    Cleaved into the following chain:
    Gene namesi
    Name:Egf
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:95290. Egf.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: MGI
    3. integral component of membrane Source: UniProtKB-KW
    4. lysosomal membrane Source: Ensembl
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 12171189Pro-epidermal growth factorPRO_0000007542Add
    BLAST
    Chaini977 – 102953Epidermal growth factor1 PublicationPRO_0000007543Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi366 ↔ 377PROSITE-ProRule annotation
    Disulfide bondi373 ↔ 386PROSITE-ProRule annotation
    Disulfide bondi388 ↔ 401PROSITE-ProRule annotation
    Disulfide bondi407 ↔ 418PROSITE-ProRule annotation
    Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi414 ↔ 427PROSITE-ProRule annotation
    Disulfide bondi429 ↔ 442PROSITE-ProRule annotation
    Disulfide bondi445 ↔ 457PROSITE-ProRule annotation
    Disulfide bondi453 ↔ 467PROSITE-ProRule annotation
    Disulfide bondi469 ↔ 482PROSITE-ProRule annotation
    Disulfide bondi751 ↔ 762PROSITE-ProRule annotation
    Disulfide bondi758 ↔ 771PROSITE-ProRule annotation
    Disulfide bondi773 ↔ 786PROSITE-ProRule annotation
    Glycosylationi810 – 8101N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi842 ↔ 853PROSITE-ProRule annotation
    Disulfide bondi847 ↔ 862PROSITE-ProRule annotation
    Disulfide bondi864 ↔ 875PROSITE-ProRule annotation
    Disulfide bondi881 ↔ 895PROSITE-ProRule annotation
    Disulfide bondi888 ↔ 904PROSITE-ProRule annotation
    Disulfide bondi906 ↔ 917PROSITE-ProRule annotation
    Disulfide bondi923 ↔ 936PROSITE-ProRule annotation
    Disulfide bondi930 ↔ 945PROSITE-ProRule annotation
    Glycosylationi944 – 9441N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi947 ↔ 958PROSITE-ProRule annotation
    Disulfide bondi982 ↔ 9961 PublicationPROSITE-ProRule annotation
    Disulfide bondi990 ↔ 10071 PublicationPROSITE-ProRule annotation
    Disulfide bondi1009 ↔ 10181 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP01132.
    PaxDbiP01132.
    PRIDEiP01132.

    PTM databases

    PhosphoSiteiP01132.

    Miscellaneous databases

    PMAP-CutDBP01132.

    Expressioni

    Gene expression databases

    BgeeiP01132.
    CleanExiMM_EGF.
    GenevestigatoriP01132.

    Interactioni

    Subunit structurei

    Interacts with EGFR and promotes EGFR dimerization. Interacts with RHBDF1; may retain EGF in the endoplasmic reticulum and regulates its degradation through the endoplasmic reticulum-associated degradation (ERAD). Interacts with RHBDF2.1 Publication

    Protein-protein interaction databases

    DIPiDIP-5762N.
    IntActiP01132. 5 interactions.

    Structurei

    Secondary structure

    1
    1217
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi987 – 9904
    Beta strandi991 – 9933
    Beta strandi995 – 9984
    Turni1000 – 10023
    Beta strandi1003 – 10086
    Turni1015 – 10173
    Beta strandi1023 – 10264

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A3PNMR-A980-1024[»]
    1EGFNMR-A977-1029[»]
    1EPGNMR-A977-1029[»]
    1EPHNMR-A977-1029[»]
    1EPINMR-A977-1029[»]
    1EPJNMR-A977-1029[»]
    1GK5NMR-A977-1018[»]
    3EGFNMR-A977-1029[»]
    ProteinModelPortaliP01132.
    SMRiP01132. Positions 977-1029.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01132.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini29 – 10381010ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1059 – 1217159CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1039 – 105820HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati93 – 13442LDL-receptor class B 1Add
    BLAST
    Repeati135 – 17642LDL-receptor class B 2Add
    BLAST
    Repeati177 – 21943LDL-receptor class B 3Add
    BLAST
    Domaini327 – 36135EGF-like 1; incompletePROSITE-ProRule annotationAdd
    BLAST
    Domaini362 – 40241EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini403 – 44341EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini441 – 48343EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Repeati489 – 52941LDL-receptor class B 4Add
    BLAST
    Repeati530 – 57243LDL-receptor class B 5Add
    BLAST
    Repeati573 – 61543LDL-receptor class B 6Add
    BLAST
    Repeati616 – 65944LDL-receptor class B 7Add
    BLAST
    Repeati660 – 70243LDL-receptor class B 8Add
    BLAST
    Domaini747 – 78741EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini838 – 87639EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini877 – 91842EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini919 – 95941EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini978 – 101942EGF-like 9PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1024 – 10296Not required for full biological activity

    Sequence similaritiesi

    Contains 9 EGF-like domains.PROSITE-ProRule annotation
    Contains 8 LDL-receptor class B repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG325841.
    GeneTreeiENSGT00750000117524.
    HOGENOMiHOG000112345.
    HOVERGENiHBG003858.
    InParanoidiQ569W5.
    KOiK04357.
    OMAiKIYFAHT.
    OrthoDBiEOG7Q2N4J.
    TreeFamiTF315253.

    Family and domain databases

    Gene3Di2.120.10.30. 2 hits.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR000033. LDLR_classB_rpt.
    IPR016317. Pro-epidermal_GF.
    [Graphical view]
    PfamiPF00008. EGF. 1 hit.
    PF07645. EGF_CA. 2 hits.
    PF00058. Ldl_recept_b. 3 hits.
    [Graphical view]
    PIRSFiPIRSF001778. Pro-epidermal_growth_factor. 1 hit.
    SMARTiSM00181. EGF. 5 hits.
    SM00179. EGF_CA. 2 hits.
    SM00135. LY. 9 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 2 hits.
    PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 6 hits.
    PS50026. EGF_3. 5 hits.
    PS01187. EGF_CA. 3 hits.
    PS51120. LDLRB. 8 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P01132-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPWGRRPTWL LLAFLLVFLK ISILSVTAWQ TGNCQPGPLE RSERSGTCAG     50
    PAPFLVFSQG KSISRIDPDG TNHQQLVVDA GISADMDIHY KKERLYWVDV 100
    ERQVLLRVFL NGTGLEKVCN VERKVSGLAI DWIDDEVLWV DQQNGVITVT 150
    DMTGKNSRVL LSSLKHPSNI AVDPIERLMF WSSEVTGSLH RAHLKGVDVK 200
    TLLETGGISV LTLDVLDKRL FWVQDSGEGS HAYIHSCDYE GGSVRLIRHQ 250
    ARHSLSSMAF FGDRIFYSVL KSKAIWIANK HTGKDTVRIN LHPSFVTPGK 300
    LMVVHPRAQP RTEDAAKDPD PELLKQRGRP CRFGLCERDP KSHSSACAEG 350
    YTLSRDRKYC EDVNECATQN HGCTLGCENT PGSYHCTCPT GFVLLPDGKQ 400
    CHELVSCPGN VSKCSHGCVL TSDGPRCICP AGSVLGRDGK TCTGCSSPDN 450
    GGCSQICLPL RPGSWECDCF PGYDLQSDRK SCAASGPQPL LLFANSQDIR 500
    HMHFDGTDYK VLLSRQMGMV FALDYDPVES KIYFAQTALK WIERANMDGS 550
    QRERLITEGV DTLEGLALDW IGRRIYWTDS GKSVVGGSDL SGKHHRIIIQ 600
    ERISRPRGIA VHPRARRLFW TDVGMSPRIE SASLQGSDRV LIASSNLLEP 650
    SGITIDYLTD TLYWCDTKRS VIEMANLDGS KRRRLIQNDV GHPFSLAVFE 700
    DHLWVSDWAI PSVIRVNKRT GQNRVRLQGS MLKPSSLVVV HPLAKPGADP 750
    CLYRNGGCEH ICQESLGTAR CLCREGFVKA WDGKMCLPQD YPILSGENAD 800
    LSKEVTSLSN STQAEVPDDD GTESSTLVAE IMVSGMNYED DCGPGGCGSH 850
    ARCVSDGETA ECQCLKGFAR DGNLCSDIDE CVLARSDCPS TSSRCINTEG 900
    GYVCRCSEGY EGDGISCFDI DECQRGAHNC GENAACTNTE GGYNCTCAGR 950
    PSSPGLSCPD STAPSLLGED GHHLDRNSYP GCPSSYDGYC LNGGVCMHIE 1000
    SLDSYTCNCV IGYSGDRCQT RDLRWWELRH AGYGQKHDIM VVAVCMVALV 1050
    LLLVLGMWGT YYYRTRKQLS NPPKNPCDEP SGSVSSSGPN SSSGAAVASC 1100
    PQPWFVVLEK HQDPKNGSLP ADGTNGAVVD AGLSPSLQLG SVHLTSWRQK 1150
    PHIDGMGTGQ SCWIPPSSDR GPQEIEGNSH LPSYRPVGPE KLHSLQSANG 1200
    SCHERAPDLP RQTEPVQ 1217
    Length:1,217
    Mass (Da):133,072
    Last modified:July 27, 2011 - v2
    Checksum:i28F35C928280D31B
    GO

    Sequence cautioni

    The sequence CAA24115.1 differs from that shown. Reason: Frameshift at positions 1134 and 1168.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti790 – 7901D → Y in CAA24115. (PubMed:6304537)Curated
    Sequence conflicti931 – 9311G → A in AAA37539. (PubMed:6602382)Curated
    Sequence conflicti931 – 9311G → A in CAA24115. (PubMed:6304537)Curated
    Sequence conflicti931 – 9311G → A in AAH60741. (PubMed:15489334)Curated
    Sequence conflicti931 – 9311G → A in AAH92277. (PubMed:15489334)Curated
    Sequence conflicti956 – 9561L → R in AAA37539. (PubMed:6602382)Curated
    Sequence conflicti956 – 9561L → R in CAA24115. (PubMed:6304537)Curated
    Sequence conflicti956 – 9561L → R in AAH60741. (PubMed:15489334)Curated
    Sequence conflicti956 – 9561L → R in AAH92277. (PubMed:15489334)Curated
    Sequence conflicti1048 – 10481A → S in CAA24115. (PubMed:6304537)Curated
    Sequence conflicti1054 – 10541V → L in AAA37539. (PubMed:6602382)Curated
    Sequence conflicti1054 – 10541V → L in CAA24115. (PubMed:6304537)Curated
    Sequence conflicti1054 – 10541V → L in AAH60741. (PubMed:15489334)Curated
    Sequence conflicti1054 – 10541V → L in AAH92277. (PubMed:15489334)Curated
    Sequence conflicti1090 – 10901N → D in AAA37539. (PubMed:6602382)Curated
    Sequence conflicti1090 – 10901N → D in CAA24115. (PubMed:6304537)Curated
    Sequence conflicti1090 – 10901N → D in AAH60741. (PubMed:15489334)Curated
    Sequence conflicti1090 – 10901N → D in AAH92277. (PubMed:15489334)Curated
    Sequence conflicti1217 – 12171Q → K in AAA37539. (PubMed:6602382)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00380 mRNA. Translation: AAA37539.1.
    V00741 mRNA. Translation: CAA24115.1. Frameshift.
    V00741 mRNA. Translation: CAA24116.1.
    AC098732 Genomic DNA. No translation available.
    BC060741 mRNA. Translation: AAH60741.1.
    BC092277 mRNA. Translation: AAH92277.1.
    CCDSiCCDS17833.1.
    RefSeqiNP_034243.2. NM_010113.3.
    UniGeneiMm.252481.

    Genome annotation databases

    EnsembliENSMUST00000029653; ENSMUSP00000029653; ENSMUSG00000028017.
    GeneIDi13645.
    KEGGimmu:13645.
    UCSCiuc008rig.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00380 mRNA. Translation: AAA37539.1 .
    V00741 mRNA. Translation: CAA24115.1 . Frameshift.
    V00741 mRNA. Translation: CAA24116.1 .
    AC098732 Genomic DNA. No translation available.
    BC060741 mRNA. Translation: AAH60741.1 .
    BC092277 mRNA. Translation: AAH92277.1 .
    CCDSi CCDS17833.1.
    RefSeqi NP_034243.2. NM_010113.3.
    UniGenei Mm.252481.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A3P NMR - A 980-1024 [» ]
    1EGF NMR - A 977-1029 [» ]
    1EPG NMR - A 977-1029 [» ]
    1EPH NMR - A 977-1029 [» ]
    1EPI NMR - A 977-1029 [» ]
    1EPJ NMR - A 977-1029 [» ]
    1GK5 NMR - A 977-1018 [» ]
    3EGF NMR - A 977-1029 [» ]
    ProteinModelPortali P01132.
    SMRi P01132. Positions 977-1029.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-5762N.
    IntActi P01132. 5 interactions.

    PTM databases

    PhosphoSitei P01132.

    Proteomic databases

    MaxQBi P01132.
    PaxDbi P01132.
    PRIDEi P01132.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029653 ; ENSMUSP00000029653 ; ENSMUSG00000028017 .
    GeneIDi 13645.
    KEGGi mmu:13645.
    UCSCi uc008rig.2. mouse.

    Organism-specific databases

    CTDi 1950.
    MGIi MGI:95290. Egf.

    Phylogenomic databases

    eggNOGi NOG325841.
    GeneTreei ENSGT00750000117524.
    HOGENOMi HOG000112345.
    HOVERGENi HBG003858.
    InParanoidi Q569W5.
    KOi K04357.
    OMAi KIYFAHT.
    OrthoDBi EOG7Q2N4J.
    TreeFami TF315253.

    Enzyme and pathway databases

    Reactomei REACT_188190. PLCG1 events in ERBB2 signaling.
    REACT_188191. Signaling by ERBB2.
    REACT_188528. GRB2 events in ERBB2 signaling.
    REACT_188574. SHC1 events in ERBB2 signaling.
    REACT_188579. Signaling by ERBB4.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_199123. Signaling by constitutively active EGFR.
    REACT_203917. EGFR downregulation.
    REACT_206286. GAB1 signalosome.
    REACT_215348. PI3K events in ERBB2 signaling.
    REACT_226341. PIP3 activates AKT signaling.

    Miscellaneous databases

    ChiTaRSi EGF. mouse.
    EvolutionaryTracei P01132.
    NextBioi 284358.
    PMAP-CutDB P01132.
    PROi P01132.
    SOURCEi Search...

    Gene expression databases

    Bgeei P01132.
    CleanExi MM_EGF.
    Genevestigatori P01132.

    Family and domain databases

    Gene3Di 2.120.10.30. 2 hits.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR000033. LDLR_classB_rpt.
    IPR016317. Pro-epidermal_GF.
    [Graphical view ]
    Pfami PF00008. EGF. 1 hit.
    PF07645. EGF_CA. 2 hits.
    PF00058. Ldl_recept_b. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF001778. Pro-epidermal_growth_factor. 1 hit.
    SMARTi SM00181. EGF. 5 hits.
    SM00179. EGF_CA. 2 hits.
    SM00135. LY. 9 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 2 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 3 hits.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 6 hits.
    PS50026. EGF_3. 5 hits.
    PS01187. EGF_CA. 3 hits.
    PS51120. LDLRB. 8 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of a mouse submaxillary messenger RNA encoding epidermal growth factor and seven related proteins."
      Scott J., Urdea M., Quiroga M., Sanchez-Pescador R., Fong N.M., Selby M., Rutter W.J., Bell G.I.
      Science 221:236-240(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Nucleotide sequence of epidermal growth factor cDNA predicts a 128,000-molecular weight protein precursor."
      Gray A., Dull T.J., Ullrich A.
      Nature 303:722-725(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Kidney and Salivary gland.
    5. "The primary structure of epidermal growth factor."
      Savage C.R. Jr., Inagami T., Cohen S.
      J. Biol. Chem. 247:7612-7621(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 977-1029.
    6. "Epidermal growth factor. Location of disulfide bonds."
      Savage C.R. Jr., Hash J.H., Cohen S.
      J. Biol. Chem. 248:7669-7672(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    7. "Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling."
      Zettl M., Adrain C., Strisovsky K., Lastun V., Freeman M.
      Cell 145:79-91(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RHBDF1 AND RHBDF2.
    8. "Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints."
      Montelione G.T., Wuethrich K., Burgess A.W., Nice E.C., Wagner G., Gibson K.D., Scheraga H.A.
      Biochemistry 31:236-249(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 977-1029.
    9. "Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions."
      Kohda D., Inagaki F.
      Biochemistry 31:11928-11939(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 977-1029.
    10. "Role of the 6-20 disulfide bridge in the structure and activity of epidermal growth factor."
      Barnham K.J., Torres A.M., Alewood D., Alewood P.F., Domagala T., Nice E.C., Norton R.S.
      Protein Sci. 7:1738-1749(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 980-1024.

    Entry informationi

    Entry nameiEGF_MOUSE
    AccessioniPrimary (citable) accession number: P01132
    Secondary accession number(s): E9QNX6, Q569W5, Q6P9J2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 169 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3