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Protein

Pro-epidermal growth factor

Gene

Egf

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Enzyme and pathway databases

ReactomeiREACT_284350. Signaling by EGFR.
REACT_285497. GRB2 events in EGFR signaling.
REACT_286571. SHC1 events in EGFR signaling.
REACT_306499. GAB1 signalosome.
REACT_307071. Platelet degranulation.
REACT_309124. EGFR interacts with phospholipase C-gamma.
REACT_321592. SHC1 events in ERBB2 signaling.
REACT_327089. GRB2 events in ERBB2 signaling.
REACT_333474. PIP3 activates AKT signaling.
REACT_336938. PLCG1 events in ERBB2 signaling.
REACT_346893. PI3K events in ERBB2 signaling.
REACT_348099. Signaling by ERBB2.
REACT_348853. Signaling by ERBB4.
REACT_350802. EGFR downregulation.

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 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:95290. Egf.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 10381010ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1039 – 105820HelicalSequence AnalysisAdd
BLAST
Topological domaini1059 – 1217159CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • extracellular region Source: Reactome
  • extracellular space Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • lysosomal membrane Source: MGI
  • plasma membrane Source: UniProtKB
Complete GO annotation...

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 ↔ 996PROSITE-ProRule annotation1 Publication
Disulfide bondi990 ↔ 1007PROSITE-ProRule annotation1 Publication
Disulfide bondi1009 ↔ 1018PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP01132.
PaxDbiP01132.
PRIDEiP01132.

PTM databases

PhosphoSiteiP01132.

Miscellaneous databases

PMAP-CutDBP01132.

Expressioni

Gene expression databases

BgeeiP01132.
CleanExiMM_EGF.
GenevisibleiP01132. MM.

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.
STRINGi10090.ENSMUSP00000029653.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000112345.
HOVERGENiHBG003858.
InParanoidiP01132.
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

        10         20         30         40         50
MPWGRRPTWL LLAFLLVFLK ISILSVTAWQ TGNCQPGPLE RSERSGTCAG
60 70 80 90 100
PAPFLVFSQG KSISRIDPDG TNHQQLVVDA GISADMDIHY KKERLYWVDV
110 120 130 140 150
ERQVLLRVFL NGTGLEKVCN VERKVSGLAI DWIDDEVLWV DQQNGVITVT
160 170 180 190 200
DMTGKNSRVL LSSLKHPSNI AVDPIERLMF WSSEVTGSLH RAHLKGVDVK
210 220 230 240 250
TLLETGGISV LTLDVLDKRL FWVQDSGEGS HAYIHSCDYE GGSVRLIRHQ
260 270 280 290 300
ARHSLSSMAF FGDRIFYSVL KSKAIWIANK HTGKDTVRIN LHPSFVTPGK
310 320 330 340 350
LMVVHPRAQP RTEDAAKDPD PELLKQRGRP CRFGLCERDP KSHSSACAEG
360 370 380 390 400
YTLSRDRKYC EDVNECATQN HGCTLGCENT PGSYHCTCPT GFVLLPDGKQ
410 420 430 440 450
CHELVSCPGN VSKCSHGCVL TSDGPRCICP AGSVLGRDGK TCTGCSSPDN
460 470 480 490 500
GGCSQICLPL RPGSWECDCF PGYDLQSDRK SCAASGPQPL LLFANSQDIR
510 520 530 540 550
HMHFDGTDYK VLLSRQMGMV FALDYDPVES KIYFAQTALK WIERANMDGS
560 570 580 590 600
QRERLITEGV DTLEGLALDW IGRRIYWTDS GKSVVGGSDL SGKHHRIIIQ
610 620 630 640 650
ERISRPRGIA VHPRARRLFW TDVGMSPRIE SASLQGSDRV LIASSNLLEP
660 670 680 690 700
SGITIDYLTD TLYWCDTKRS VIEMANLDGS KRRRLIQNDV GHPFSLAVFE
710 720 730 740 750
DHLWVSDWAI PSVIRVNKRT GQNRVRLQGS MLKPSSLVVV HPLAKPGADP
760 770 780 790 800
CLYRNGGCEH ICQESLGTAR CLCREGFVKA WDGKMCLPQD YPILSGENAD
810 820 830 840 850
LSKEVTSLSN STQAEVPDDD GTESSTLVAE IMVSGMNYED DCGPGGCGSH
860 870 880 890 900
ARCVSDGETA ECQCLKGFAR DGNLCSDIDE CVLARSDCPS TSSRCINTEG
910 920 930 940 950
GYVCRCSEGY EGDGISCFDI DECQRGAHNC GENAACTNTE GGYNCTCAGR
960 970 980 990 1000
PSSPGLSCPD STAPSLLGED GHHLDRNSYP GCPSSYDGYC LNGGVCMHIE
1010 1020 1030 1040 1050
SLDSYTCNCV IGYSGDRCQT RDLRWWELRH AGYGQKHDIM VVAVCMVALV
1060 1070 1080 1090 1100
LLLVLGMWGT YYYRTRKQLS NPPKNPCDEP SGSVSSSGPN SSSGAAVASC
1110 1120 1130 1140 1150
PQPWFVVLEK HQDPKNGSLP ADGTNGAVVD AGLSPSLQLG SVHLTSWRQK
1160 1170 1180 1190 1200
PHIDGMGTGQ SCWIPPSSDR GPQEIEGNSH LPSYRPVGPE KLHSLQSANG
1210
SCHERAPDLP RQTEPVQ
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

DIPiDIP-5762N.
IntActiP01132. 5 interactions.
STRINGi10090.ENSMUSP00000029653.

PTM databases

PhosphoSiteiP01132.

Proteomic databases

MaxQBiP01132.
PaxDbiP01132.
PRIDEiP01132.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1950.
MGIiMGI:95290. Egf.

Phylogenomic databases

eggNOGiNOG325841.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000112345.
HOVERGENiHBG003858.
InParanoidiP01132.
KOiK04357.
OMAiKIYFAHT.
OrthoDBiEOG7Q2N4J.
TreeFamiTF315253.

Enzyme and pathway databases

ReactomeiREACT_284350. Signaling by EGFR.
REACT_285497. GRB2 events in EGFR signaling.
REACT_286571. SHC1 events in EGFR signaling.
REACT_306499. GAB1 signalosome.
REACT_307071. Platelet degranulation.
REACT_309124. EGFR interacts with phospholipase C-gamma.
REACT_321592. SHC1 events in ERBB2 signaling.
REACT_327089. GRB2 events in ERBB2 signaling.
REACT_333474. PIP3 activates AKT signaling.
REACT_336938. PLCG1 events in ERBB2 signaling.
REACT_346893. PI3K events in ERBB2 signaling.
REACT_348099. Signaling by ERBB2.
REACT_348853. Signaling by ERBB4.
REACT_350802. EGFR downregulation.

Miscellaneous databases

ChiTaRSiEgf. mouse.
EvolutionaryTraceiP01132.
NextBioi284358.
PMAP-CutDBP01132.
PROiP01132.
SOURCEiSearch...

Gene expression databases

BgeeiP01132.
CleanExiMM_EGF.
GenevisibleiP01132. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 176 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.