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P01133

- EGF_HUMAN

UniProt

P01133 - EGF_HUMAN

Protein

Pro-epidermal growth factor

Gene

EGF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 2 (07 Jul 2009)
      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 TRPM6.1 Publication

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. epidermal growth factor receptor binding Source: UniProtKB
    3. growth factor activity Source: HGNC
    4. protein binding Source: IntAct
    5. transmembrane receptor protein tyrosine kinase activator activity Source: UniProtKB

    GO - Biological processi

    1. activation of MAPKK activity Source: Ensembl
    2. activation of transmembrane receptor protein tyrosine kinase activity Source: GOC
    3. angiogenesis Source: HGNC
    4. blood coagulation Source: Reactome
    5. branching morphogenesis of an epithelial tube Source: Ensembl
    6. DNA replication Source: ProtInc
    7. epidermal growth factor receptor signaling pathway Source: Reactome
    8. ERK1 and ERK2 cascade Source: UniProtKB
    9. Fc-epsilon receptor signaling pathway Source: Reactome
    10. fibroblast growth factor receptor signaling pathway Source: Reactome
    11. innate immune response Source: Reactome
    12. mammary gland alveolus development Source: Ensembl
    13. negative regulation of cholesterol efflux Source: Ensembl
    14. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
    15. negative regulation of secretion Source: BHF-UCL
    16. neurotrophin TRK receptor signaling pathway Source: Reactome
    17. peptidyl-tyrosine phosphorylation Source: Ensembl
    18. phosphatidylinositol-mediated signaling Source: Reactome
    19. platelet activation Source: Reactome
    20. platelet degranulation Source: Reactome
    21. positive regulation of catenin import into nucleus Source: BHF-UCL
    22. positive regulation of cell proliferation Source: BHF-UCL
    23. positive regulation of cerebellar granule cell precursor proliferation Source: Ensembl
    24. positive regulation of DNA binding Source: UniProtKB
    25. positive regulation of epidermal growth factor-activated receptor activity Source: UniProtKB
    26. positive regulation of hyaluronan biosynthetic process Source: UniProtKB
    27. positive regulation of MAP kinase activity Source: HGNC
    28. positive regulation of mitosis Source: HGNC
    29. positive regulation of peptidyl-threonine phosphorylation Source: UniProtKB
    30. positive regulation of phosphorylation Source: HGNC
    31. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: Ensembl
    32. positive regulation of transcription, DNA-templated Source: UniProtKB
    33. regulation of calcium ion import Source: BHF-UCL
    34. regulation of protein localization to cell surface Source: BHF-UCL
    35. signal transduction Source: Reactome
    36. STAT protein import into nucleus Source: UniProtKB

    Keywords - Molecular functioni

    Growth factor

    Enzyme and pathway databases

    ReactomeiREACT_115596. Signaling by ERBB4.
    REACT_115720. PLCG1 events in ERBB2 signaling.
    REACT_115755. Signaling by ERBB2.
    REACT_115852. Signaling by constitutively active EGFR.
    REACT_115854. GRB2 events in ERBB2 signaling.
    REACT_115993. SHC1 events in ERBB2 signaling.
    REACT_116008. PI3K events in ERBB2 signaling.
    REACT_12478. EGFR interacts with phospholipase C-gamma.
    REACT_12484. EGFR downregulation.
    REACT_12578. GAB1 signalosome.
    REACT_12579. SHC1 events in EGFR signaling.
    REACT_12606. GRB2 events in EGFR signaling.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_9417. Signaling by EGFR.
    SignaLinkiP01133.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pro-epidermal growth factor
    Short name:
    EGF
    Cleaved into the following chain:
    Alternative name(s):
    Urogastrone
    Gene namesi
    Name:EGF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:3229. EGF.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. extracellular space Source: UniProt
    3. extracellular vesicular exosome Source: UniProtKB
    4. integral component of membrane Source: UniProtKB-KW
    5. lysosomal membrane Source: UniProtKB
    6. plasma membrane Source: ProtInc
    7. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Hypomagnesemia 4 (HOMG4) [MIM:611718]: A disorder characterized by massive renal hypomagnesemia and normal levels of serum calcium and calcium excretion. Clinical features include seizures, mild-to moderate psychomotor retardation, and brisk tendon reflexes.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1070 – 10701P → L in HOMG4; affects basolateral sorting of pro-EGF preventing the hormone to stimulate EGFR; lack of TRPM6 activation. 1 Publication
    VAR_039474

    Keywords - Diseasei

    Disease mutation, Primary hypomagnesemia

    Organism-specific databases

    MIMi611718. phenotype.
    Orphaneti210159. Adult hepatocellular carcinoma.
    34527. Familial primary hypomagnesemia with normocalcuria and normocalcemia.
    PharmGKBiPA27664.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 12071185Pro-epidermal growth factorPRO_0000007540Add
    BLAST
    Chaini971 – 102353Epidermal growth factorPRO_0000007541Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi148 – 1481N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi318 ↔ 330PROSITE-ProRule annotation
    Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi325 ↔ 339PROSITE-ProRule annotation
    Disulfide bondi341 ↔ 354PROSITE-ProRule annotation
    Disulfide bondi360 ↔ 371PROSITE-ProRule annotation
    Disulfide bondi367 ↔ 380PROSITE-ProRule annotation
    Disulfide bondi382 ↔ 395PROSITE-ProRule annotation
    Disulfide bondi401 ↔ 412PROSITE-ProRule annotation
    Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi408 ↔ 421PROSITE-ProRule annotation
    Disulfide bondi423 ↔ 436PROSITE-ProRule annotation
    Disulfide bondi439 ↔ 451PROSITE-ProRule annotation
    Disulfide bondi447 ↔ 461PROSITE-ProRule annotation
    Disulfide bondi463 ↔ 476PROSITE-ProRule annotation
    Glycosylationi596 – 5961N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi745 ↔ 756PROSITE-ProRule annotation
    Disulfide bondi752 ↔ 765PROSITE-ProRule annotation
    Disulfide bondi767 ↔ 780PROSITE-ProRule annotation
    Glycosylationi815 – 8151N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi835 ↔ 846PROSITE-ProRule annotation
    Disulfide bondi840 ↔ 855PROSITE-ProRule annotation
    Disulfide bondi857 ↔ 868PROSITE-ProRule annotation
    Disulfide bondi874 ↔ 888PROSITE-ProRule annotation
    Disulfide bondi881 ↔ 897PROSITE-ProRule annotation
    Disulfide bondi899 ↔ 910PROSITE-ProRule annotation
    Disulfide bondi916 ↔ 929PROSITE-ProRule annotation
    Disulfide bondi923 ↔ 938PROSITE-ProRule annotation
    Glycosylationi926 – 9261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi940 ↔ 951PROSITE-ProRule annotation
    Glycosylationi954 – 9541O-linked (GalNAc...); or Thr-9551 Publication
    Glycosylationi955 – 9551O-linked (GalNAc...); or Ser-9541 Publication
    Disulfide bondi976 ↔ 990
    Disulfide bondi984 ↔ 1001
    Disulfide bondi1003 ↔ 1012

    Post-translational modificationi

    O-glycosylated with core 1-like and core 2-like glycans. It is uncertain if Ser-954 or Thr-955 is O-glycosylated. The modification here shows glycan heterogeneity: HexHexNAc (major) and Hex2HexNAc2 (minor).1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP01133.
    PRIDEiP01133.

    PTM databases

    PhosphoSiteiP01133.

    Miscellaneous databases

    PMAP-CutDBP01133.

    Expressioni

    Tissue specificityi

    Expressed in kidney, salivary gland, cerebrum and prostate.1 Publication

    Gene expression databases

    ArrayExpressiP01133.
    BgeeiP01133.
    CleanExiHS_EGF.
    GenevestigatoriP01133.

    Organism-specific databases

    HPAiCAB017843.

    Interactioni

    Subunit structurei

    Interacts with EGFR and promotes EGFR dimerization. Interacts with RHBDF2 By similarity. Interacts with RHBDF1; may retain EGF in the endoplasmic reticulum and regulates its degradation through the endoplasmic reticulum-associated degradation (ERAD).By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EGFRP0053316EBI-640857,EBI-297353
    EgfrQ012793EBI-640857,EBI-6296235From a different organism.

    Protein-protein interaction databases

    BioGridi108270. 16 interactions.
    DIPiDIP-5767N.
    IntActiP01133. 7 interactions.
    MINTiMINT-260489.
    STRINGi9606.ENSP00000265171.

    Structurei

    Secondary structure

    1
    1207
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi979 – 9813
    Beta strandi982 – 9843
    Turni985 – 9873
    Beta strandi989 – 9935
    Turni994 – 9974
    Beta strandi998 – 10036
    Beta strandi1007 – 10093
    Turni1018 – 10214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IVOX-ray3.30C/D971-1023[»]
    1JL9X-ray3.00A/B971-1021[»]
    1NQLX-ray2.80B971-1023[»]
    1P9JNMR-A976-1022[»]
    2KV4NMR-A971-1023[»]
    3NJPX-ray3.30C/D975-1021[»]
    ProteinModelPortaliP01133.
    SMRiP01133. Positions 42-773, 839-1020.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01133.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 10321010ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1054 – 1207154CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1033 – 105321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati86 – 12742LDL-receptor class B 1Add
    BLAST
    Repeati128 – 16942LDL-receptor class B 2Add
    BLAST
    Repeati170 – 21142LDL-receptor class B 3Add
    BLAST
    Repeati212 – 25847LDL-receptor class B 4Add
    BLAST
    Domaini314 – 35542EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini356 – 39641EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini397 – 43741EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini435 – 47743EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Repeati483 – 52341LDL-receptor class B 5Add
    BLAST
    Repeati524 – 56643LDL-receptor class B 6Add
    BLAST
    Repeati567 – 60943LDL-receptor class B 7Add
    BLAST
    Repeati610 – 65344LDL-receptor class B 8Add
    BLAST
    Repeati654 – 69643LDL-receptor class B 9Add
    BLAST
    Domaini741 – 78141EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini831 – 86939EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini870 – 91142EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini912 – 95241EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini972 – 101342EGF-like 9PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni801 – 8077O-glycosylated at one site

    Sequence similaritiesi

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

    Keywords - Domaini

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

    Phylogenomic databases

    eggNOGiNOG325841.
    HOGENOMiHOG000112345.
    HOVERGENiHBG003858.
    InParanoidiP01133.
    KOiK04357.
    OMAiKIYFAHT.
    OrthoDBiEOG7Q2N4J.
    PhylomeDBiP01133.
    TreeFamiTF315253.

    Family and domain databases

    Gene3Di2.120.10.30. 2 hits.
    2.40.155.10. 1 hit.
    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.
    IPR023413. GFP_like.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR000033. LDLR_classB_rpt.
    IPR016317. Pro-epidermal_GF.
    [Graphical view]
    PfamiPF00008. EGF. 1 hit.
    PF07645. EGF_CA. 3 hits.
    PF00058. Ldl_recept_b. 4 hits.
    [Graphical view]
    PIRSFiPIRSF001778. Pro-epidermal_growth_factor. 1 hit.
    SMARTiSM00181. EGF. 6 hits.
    SM00179. EGF_CA. 2 hits.
    SM00135. LY. 9 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 4 hits.
    PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 7 hits.
    PS50026. EGF_3. 5 hits.
    PS01187. EGF_CA. 3 hits.
    PS51120. LDLRB. 9 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P01133-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLLTLIILLP VVSKFSFVSL SAPQHWSCPE GTLAGNGNST CVGPAPFLIF     50
    SHGNSIFRID TEGTNYEQLV VDAGVSVIMD FHYNEKRIYW VDLERQLLQR 100
    VFLNGSRQER VCNIEKNVSG MAINWINEEV IWSNQQEGII TVTDMKGNNS 150
    HILLSALKYP ANVAVDPVER FIFWSSEVAG SLYRADLDGV GVKALLETSE 200
    KITAVSLDVL DKRLFWIQYN REGSNSLICS CDYDGGSVHI SKHPTQHNLF 250
    AMSLFGDRIF YSTWKMKTIW IANKHTGKDM VRINLHSSFV PLGELKVVHP 300
    LAQPKAEDDT WEPEQKLCKL RKGNCSSTVC GQDLQSHLCM CAEGYALSRD 350
    RKYCEDVNEC AFWNHGCTLG CKNTPGSYYC TCPVGFVLLP DGKRCHQLVS 400
    CPRNVSECSH DCVLTSEGPL CFCPEGSVLE RDGKTCSGCS SPDNGGCSQL 450
    CVPLSPVSWE CDCFPGYDLQ LDEKSCAASG PQPFLLFANS QDIRHMHFDG 500
    TDYGTLLSQQ MGMVYALDHD PVENKIYFAH TALKWIERAN MDGSQRERLI 550
    EEGVDVPEGL AVDWIGRRFY WTDRGKSLIG RSDLNGKRSK IITKENISQP 600
    RGIAVHPMAK RLFWTDTGIN PRIESSSLQG LGRLVIASSD LIWPSGITID 650
    FLTDKLYWCD AKQSVIEMAN LDGSKRRRLT QNDVGHPFAV AVFEDYVWFS 700
    DWAMPSVMRV NKRTGKDRVR LQGSMLKPSS LVVVHPLAKP GADPCLYQNG 750
    GCEHICKKRL GTAWCSCREG FMKASDGKTC LALDGHQLLA GGEVDLKNQV 800
    TPLDILSKTR VSEDNITESQ HMLVAEIMVS DQDDCAPVGC SMYARCISEG 850
    EDATCQCLKG FAGDGKLCSD IDECEMGVPV CPPASSKCIN TEGGYVCRCS 900
    EGYQGDGIHC LDIDECQLGE HSCGENASCT NTEGGYTCMC AGRLSEPGLI 950
    CPDSTPPPHL REDDHHYSVR NSDSECPLSH DGYCLHDGVC MYIEALDKYA 1000
    CNCVVGYIGE RCQYRDLKWW ELRHAGHGQQ QKVIVVAVCV VVLVMLLLLS 1050
    LWGAHYYRTQ KLLSKNPKNP YEESSRDVRS RRPADTEDGM SSCPQPWFVV 1100
    IKEHQDLKNG GQPVAGEDGQ AADGSMQPTS WRQEPQLCGM GTEQGCWIPV 1150
    SSDKGSCPQV MERSFHMPSY GTQTLEGGVE KPHSLLSANP LWQQRALDPP 1200
    HQMELTQ 1207
    Length:1,207
    Mass (Da):133,994
    Last modified:July 7, 2009 - v2
    Checksum:i3C787F1D405CFAF1
    GO
    Isoform 2 (identifier: P01133-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         314-355: Missing.

    Show »
    Length:1,165
    Mass (Da):129,256
    Checksum:i5449AE11FA9276B5
    GO
    Isoform 3 (identifier: P01133-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         912-952: Missing.

    Note: No experimental confirmation available. Gene prediction based on cDNA data.

    Show »
    Length:1,166
    Mass (Da):129,746
    Checksum:i4872256969C28678
    GO

    Sequence cautioni

    The sequence AAR84237.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti302 – 3021A → T in BAG61319. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161S → R.1 Publication
    Corresponds to variant rs11568849 [ dbSNP | Ensembl ].
    VAR_020161
    Natural varianti151 – 1511H → Y.
    Corresponds to variant rs9991664 [ dbSNP | Ensembl ].
    VAR_033825
    Natural varianti257 – 2571D → H.1 Publication
    Corresponds to variant rs11568911 [ dbSNP | Ensembl ].
    VAR_020968
    Natural varianti292 – 2921L → H.
    Corresponds to variant rs35191533 [ dbSNP | Ensembl ].
    VAR_033826
    Natural varianti431 – 4311R → K.1 Publication
    Corresponds to variant rs11568943 [ dbSNP | Ensembl ].
    VAR_020162
    Natural varianti638 – 6381S → R.1 Publication
    Corresponds to variant rs11568992 [ dbSNP | Ensembl ].
    VAR_020969
    Natural varianti708 – 7081M → I.1 Publication
    Corresponds to variant rs2237051 [ dbSNP | Ensembl ].
    VAR_002275
    Natural varianti723 – 7231G → R.
    Corresponds to variant rs6413481 [ dbSNP | Ensembl ].
    VAR_020163
    Natural varianti784 – 7841D → V.1 Publication
    Corresponds to variant rs11569017 [ dbSNP | Ensembl ].
    VAR_020164
    Natural varianti842 – 8421M → T.1 Publication
    Corresponds to variant rs11569046 [ dbSNP | Ensembl ].
    VAR_020165
    Natural varianti920 – 9201E → V.2 Publications
    Corresponds to variant rs4698803 [ dbSNP | Ensembl ].
    VAR_020970
    Natural varianti981 – 9811D → E.1 Publication
    Corresponds to variant rs11569086 [ dbSNP | Ensembl ].
    VAR_020971
    Natural varianti1043 – 10431L → F.1 Publication
    Corresponds to variant rs11569098 [ dbSNP | Ensembl ].
    VAR_020166
    Natural varianti1070 – 10701P → L in HOMG4; affects basolateral sorting of pro-EGF preventing the hormone to stimulate EGFR; lack of TRPM6 activation. 1 Publication
    VAR_039474
    Natural varianti1084 – 10841A → G.1 Publication
    Corresponds to variant rs11569111 [ dbSNP | Ensembl ].
    VAR_020972

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei314 – 35542Missing in isoform 2. 1 PublicationVSP_041586Add
    BLAST
    Alternative sequencei912 – 95241Missing in isoform 3. CuratedVSP_047190Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04571 mRNA. Translation: CAA28240.1.
    AY506357 Genomic DNA. Translation: AAR84237.1. Sequence problems.
    AK299306 mRNA. Translation: BAG61319.1.
    AC004050 Genomic DNA. No translation available.
    AC005509 Genomic DNA. No translation available.
    BC093731 mRNA. Translation: AAH93731.1.
    BC113461 mRNA. Translation: AAI13462.1.
    CCDSiCCDS3689.1. [P01133-1]
    CCDS54794.1. [P01133-3]
    CCDS54795.1. [P01133-2]
    PIRiA25531. EGHU.
    RefSeqiNP_001171601.1. NM_001178130.1. [P01133-3]
    NP_001171602.1. NM_001178131.1. [P01133-2]
    NP_001954.2. NM_001963.4. [P01133-1]
    UniGeneiHs.419815.

    Genome annotation databases

    EnsembliENST00000265171; ENSP00000265171; ENSG00000138798. [P01133-1]
    ENST00000503392; ENSP00000421384; ENSG00000138798. [P01133-3]
    ENST00000509793; ENSP00000424316; ENSG00000138798. [P01133-2]
    GeneIDi1950.
    KEGGihsa:1950.
    UCSCiuc003hzy.4. human. [P01133-1]
    uc011cfu.2. human. [P01133-2]

    Polymorphism databases

    DMDMi251757262.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Epidermal growth factor entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04571 mRNA. Translation: CAA28240.1 .
    AY506357 Genomic DNA. Translation: AAR84237.1 . Sequence problems.
    AK299306 mRNA. Translation: BAG61319.1 .
    AC004050 Genomic DNA. No translation available.
    AC005509 Genomic DNA. No translation available.
    BC093731 mRNA. Translation: AAH93731.1 .
    BC113461 mRNA. Translation: AAI13462.1 .
    CCDSi CCDS3689.1. [P01133-1 ]
    CCDS54794.1. [P01133-3 ]
    CCDS54795.1. [P01133-2 ]
    PIRi A25531. EGHU.
    RefSeqi NP_001171601.1. NM_001178130.1. [P01133-3 ]
    NP_001171602.1. NM_001178131.1. [P01133-2 ]
    NP_001954.2. NM_001963.4. [P01133-1 ]
    UniGenei Hs.419815.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IVO X-ray 3.30 C/D 971-1023 [» ]
    1JL9 X-ray 3.00 A/B 971-1021 [» ]
    1NQL X-ray 2.80 B 971-1023 [» ]
    1P9J NMR - A 976-1022 [» ]
    2KV4 NMR - A 971-1023 [» ]
    3NJP X-ray 3.30 C/D 975-1021 [» ]
    ProteinModelPortali P01133.
    SMRi P01133. Positions 42-773, 839-1020.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108270. 16 interactions.
    DIPi DIP-5767N.
    IntActi P01133. 7 interactions.
    MINTi MINT-260489.
    STRINGi 9606.ENSP00000265171.

    Chemistry

    BindingDBi P01133.
    ChEMBLi CHEMBL5734.
    DrugBanki DB00605. Sulindac.

    PTM databases

    PhosphoSitei P01133.

    Polymorphism databases

    DMDMi 251757262.

    Proteomic databases

    PaxDbi P01133.
    PRIDEi P01133.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265171 ; ENSP00000265171 ; ENSG00000138798 . [P01133-1 ]
    ENST00000503392 ; ENSP00000421384 ; ENSG00000138798 . [P01133-3 ]
    ENST00000509793 ; ENSP00000424316 ; ENSG00000138798 . [P01133-2 ]
    GeneIDi 1950.
    KEGGi hsa:1950.
    UCSCi uc003hzy.4. human. [P01133-1 ]
    uc011cfu.2. human. [P01133-2 ]

    Organism-specific databases

    CTDi 1950.
    GeneCardsi GC04P110834.
    HGNCi HGNC:3229. EGF.
    HPAi CAB017843.
    MIMi 131530. gene.
    611718. phenotype.
    neXtProti NX_P01133.
    Orphaneti 210159. Adult hepatocellular carcinoma.
    34527. Familial primary hypomagnesemia with normocalcuria and normocalcemia.
    PharmGKBi PA27664.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG325841.
    HOGENOMi HOG000112345.
    HOVERGENi HBG003858.
    InParanoidi P01133.
    KOi K04357.
    OMAi KIYFAHT.
    OrthoDBi EOG7Q2N4J.
    PhylomeDBi P01133.
    TreeFami TF315253.

    Enzyme and pathway databases

    Reactomei REACT_115596. Signaling by ERBB4.
    REACT_115720. PLCG1 events in ERBB2 signaling.
    REACT_115755. Signaling by ERBB2.
    REACT_115852. Signaling by constitutively active EGFR.
    REACT_115854. GRB2 events in ERBB2 signaling.
    REACT_115993. SHC1 events in ERBB2 signaling.
    REACT_116008. PI3K events in ERBB2 signaling.
    REACT_12478. EGFR interacts with phospholipase C-gamma.
    REACT_12484. EGFR downregulation.
    REACT_12578. GAB1 signalosome.
    REACT_12579. SHC1 events in EGFR signaling.
    REACT_12606. GRB2 events in EGFR signaling.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_9417. Signaling by EGFR.
    SignaLinki P01133.

    Miscellaneous databases

    ChiTaRSi EGF. human.
    EvolutionaryTracei P01133.
    GeneWikii Epidermal_growth_factor.
    GenomeRNAii 1950.
    NextBioi 7903.
    PMAP-CutDB P01133.
    PROi P01133.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01133.
    Bgeei P01133.
    CleanExi HS_EGF.
    Genevestigatori P01133.

    Family and domain databases

    Gene3Di 2.120.10.30. 2 hits.
    2.40.155.10. 1 hit.
    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.
    IPR023413. GFP_like.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR000033. LDLR_classB_rpt.
    IPR016317. Pro-epidermal_GF.
    [Graphical view ]
    Pfami PF00008. EGF. 1 hit.
    PF07645. EGF_CA. 3 hits.
    PF00058. Ldl_recept_b. 4 hits.
    [Graphical view ]
    PIRSFi PIRSF001778. Pro-epidermal_growth_factor. 1 hit.
    SMARTi SM00181. EGF. 6 hits.
    SM00179. EGF_CA. 2 hits.
    SM00135. LY. 9 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 4 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 3 hits.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 7 hits.
    PS50026. EGF_3. 5 hits.
    PS01187. EGF_CA. 3 hits.
    PS51120. LDLRB. 9 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human epidermal growth factor precursor: cDNA sequence, expression in vitro and gene organization."
      Bell G.I., Fong N.M., Stempien M.M., Wormsted M.A., Caput D., Ku L., Urdea M.S., Rall L.B., Sanchez-Pescador R.
      Nucleic Acids Res. 14:8427-8446(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Kidney.
    2. NIEHS SNPs program
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16; HIS-257; LYS-431; ARG-638; ILE-708; VAL-784; THR-842; VAL-920; GLU-981; PHE-1043 AND GLY-1084.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT VAL-920.
      Tissue: Teratocarcinoma.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Colon.
    6. "The primary structure of human urogastrone."
      Gregory H., Preston B.M.
      Int. J. Pept. Protein Res. 9:107-118(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 971-1023.
    7. "The primary structure of human EGF produced by genetic engineering, studied by high-performance tandem mass spectrometry."
      Furuya M., Akashi S., Hirayama K.
      Biochem. Biophys. Res. Commun. 163:1100-1106(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 971-1023.
    8. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
      Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-954 AND THR-955, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "Human epidermal growth factor. High resolution solution structure and comparison with human transforming growth factor alpha."
      Hommel U., Harvey T.S., Driscoll P.C., Campbell I.D.
      J. Mol. Biol. 227:271-282(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF EGF.
    10. Cited for: FUNCTION, TISSUE SPECIFICITY, VARIANT HOMG4 LEU-1070, CHARACTERIZATION OF VARIANT HOMG4 LEU-1070.
    11. "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.
    12. "Crystal structure of human epidermal growth factor and its dimerization."
      Lu H.S., Chai J.J., Li M., Huang B.R., He C.H., Bi R.C.
      J. Biol. Chem. 276:34913-34917(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 971-1021, DISULFIDE BONDS.
    13. "Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains."
      Ogiso H., Ishitani R., Nureki O., Fukai S., Yamanaka M., Kim J.H., Saito K., Sakamoto A., Inoue M., Shirouzu M., Yokoyama S.
      Cell 110:775-787(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 971-1023 IN COMPLEX WITH EGFR, DISULFIDE BONDS.
    14. "EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization."
      Ferguson K.M., Berger M.B., Mendrola J.M., Cho H.S., Leahy D.J., Lemmon M.A.
      Mol. Cell 11:507-517(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 971-1023 IN COMPLEX WITH EGFR, DISULFIDE BONDS.
    15. "The NMR solution structure of human epidermal growth factor (hEGF) at physiological pH and its interactions with suramin."
      Huang H.W., Mohan S.K., Yu C.
      Biochem. Biophys. Res. Commun. 402:705-710(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 971-1023 IN COMPLEX WITH SURAMIN.
    16. "Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor."
      Lu C., Mi L.Z., Grey M.J., Zhu J., Graef E., Yokoyama S., Springer T.A.
      Mol. Cell. Biol. 30:5432-5443(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 975-1021 IN COMPLEX WITH EGFR, DISULFIDE BONDS.

    Entry informationi

    Entry nameiEGF_HUMAN
    AccessioniPrimary (citable) accession number: P01133
    Secondary accession number(s): B4DRK7
    , E7EVD2, E9PBF0, Q52LZ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 171 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3