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P01132

- EGF_MOUSE

UniProt

P01132 - EGF_MOUSE

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Protein

Pro-epidermal growth factor

Gene

Egf

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

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

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
Complete GO annotation...

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. extracellular vesicular exosome Source: Ensembl
  4. integral component of membrane Source: UniProtKB-KW
  5. lysosomal membrane Source: Ensembl
  6. 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 ↔ 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.
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.

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 ENSGT00760000118968.
HOGENOMi HOG000112345.
HOVERGENi HBG003858.
InParanoidi P01132.
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

« 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: October 29, 2014
This is version 170 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