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Protein

Pro-epidermal growth factor

Gene

EGF

Organism
Homo sapiens (Human)
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. Can induce neurite outgrowth in motoneurons of the pond snail Lymnaea stagnalis in vitro (PubMed:10964941).2 Publications

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • epidermal growth factor receptor binding Source: UniProtKB
  • growth factor activity Source: HGNC
  • transmembrane receptor protein tyrosine kinase activator activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

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. Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
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 Signaling by Aberrant PI3K in Cancer.
REACT_267817. Constitutive Signaling by EGFRvIII.
REACT_268595. Inhibition of Signaling by Overexpressed EGFR.
REACT_318. Platelet degranulation.
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 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:3229. EGF.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 10321010ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1033 – 105321HelicalSequence AnalysisAdd
BLAST
Topological domaini1054 – 1207154CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • lysosomal membrane Source: UniProtKB
  • plasma membrane Source: ProtInc
  • platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Hypomagnesemia 4 (HOMG4)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:611718
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 normocalciuria and normocalcemia.
PharmGKBiPA27664.

Chemistry

DrugBankiDB00364. Sucralfate.

Polymorphism and mutation databases

BioMutaiEGF.
DMDMi251757262.

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

BgeeiP01133.
CleanExiHS_EGF.
GenevisibleiP01133. HS.

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 – 9813Combined sources
Beta strandi982 – 9843Combined sources
Turni985 – 9873Combined sources
Beta strandi989 – 9935Combined sources
Turni994 – 9974Combined sources
Beta strandi998 – 10036Combined sources
Beta strandi1007 – 10093Combined sources
Turni1018 – 10214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 973-1020.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01133.

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.
GeneTreeiENSGT00760000118968.
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. AlignAdd to basket

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

        10         20         30         40         50
MLLTLIILLP VVSKFSFVSL SAPQHWSCPE GTLAGNGNST CVGPAPFLIF
60 70 80 90 100
SHGNSIFRID TEGTNYEQLV VDAGVSVIMD FHYNEKRIYW VDLERQLLQR
110 120 130 140 150
VFLNGSRQER VCNIEKNVSG MAINWINEEV IWSNQQEGII TVTDMKGNNS
160 170 180 190 200
HILLSALKYP ANVAVDPVER FIFWSSEVAG SLYRADLDGV GVKALLETSE
210 220 230 240 250
KITAVSLDVL DKRLFWIQYN REGSNSLICS CDYDGGSVHI SKHPTQHNLF
260 270 280 290 300
AMSLFGDRIF YSTWKMKTIW IANKHTGKDM VRINLHSSFV PLGELKVVHP
310 320 330 340 350
LAQPKAEDDT WEPEQKLCKL RKGNCSSTVC GQDLQSHLCM CAEGYALSRD
360 370 380 390 400
RKYCEDVNEC AFWNHGCTLG CKNTPGSYYC TCPVGFVLLP DGKRCHQLVS
410 420 430 440 450
CPRNVSECSH DCVLTSEGPL CFCPEGSVLE RDGKTCSGCS SPDNGGCSQL
460 470 480 490 500
CVPLSPVSWE CDCFPGYDLQ LDEKSCAASG PQPFLLFANS QDIRHMHFDG
510 520 530 540 550
TDYGTLLSQQ MGMVYALDHD PVENKIYFAH TALKWIERAN MDGSQRERLI
560 570 580 590 600
EEGVDVPEGL AVDWIGRRFY WTDRGKSLIG RSDLNGKRSK IITKENISQP
610 620 630 640 650
RGIAVHPMAK RLFWTDTGIN PRIESSSLQG LGRLVIASSD LIWPSGITID
660 670 680 690 700
FLTDKLYWCD AKQSVIEMAN LDGSKRRRLT QNDVGHPFAV AVFEDYVWFS
710 720 730 740 750
DWAMPSVMRV NKRTGKDRVR LQGSMLKPSS LVVVHPLAKP GADPCLYQNG
760 770 780 790 800
GCEHICKKRL GTAWCSCREG FMKASDGKTC LALDGHQLLA GGEVDLKNQV
810 820 830 840 850
TPLDILSKTR VSEDNITESQ HMLVAEIMVS DQDDCAPVGC SMYARCISEG
860 870 880 890 900
EDATCQCLKG FAGDGKLCSD IDECEMGVPV CPPASSKCIN TEGGYVCRCS
910 920 930 940 950
EGYQGDGIHC LDIDECQLGE HSCGENASCT NTEGGYTCMC AGRLSEPGLI
960 970 980 990 1000
CPDSTPPPHL REDDHHYSVR NSDSECPLSH DGYCLHDGVC MYIEALDKYA
1010 1020 1030 1040 1050
CNCVVGYIGE RCQYRDLKWW ELRHAGHGQQ QKVIVVAVCV VVLVMLLLLS
1060 1070 1080 1090 1100
LWGAHYYRTQ KLLSKNPKNP YEESSRDVRS RRPADTEDGM SSCPQPWFVV
1110 1120 1130 1140 1150
IKEHQDLKNG GQPVAGEDGQ AADGSMQPTS WRQEPQLCGM GTEQGCWIPV
1160 1170 1180 1190 1200
SSDKGSCPQV MERSFHMPSY GTQTLEGGVE KPHSLLSANP LWQQRALDPP

HQMELTQ
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. Curated

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Epidermal growth factor entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 973-1020.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL5734.
DrugBankiDB00364. Sucralfate.

PTM databases

PhosphoSiteiP01133.

Polymorphism and mutation databases

BioMutaiEGF.
DMDMi251757262.

Proteomic databases

PaxDbiP01133.
PRIDEiP01133.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1950.
GeneCardsiGC04P110834.
HGNCiHGNC:3229. EGF.
HPAiCAB017843.
MIMi131530. gene.
611718. phenotype.
neXtProtiNX_P01133.
Orphaneti210159. Adult hepatocellular carcinoma.
34527. Familial primary hypomagnesemia with normocalciuria and normocalcemia.
PharmGKBiPA27664.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG325841.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000112345.
HOVERGENiHBG003858.
InParanoidiP01133.
KOiK04357.
OMAiKIYFAHT.
OrthoDBiEOG7Q2N4J.
PhylomeDBiP01133.
TreeFamiTF315253.

Enzyme and pathway databases

ReactomeiREACT_115596. Signaling by ERBB4.
REACT_115720. PLCG1 events in ERBB2 signaling.
REACT_115755. Signaling by ERBB2.
REACT_115852. Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
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 Signaling by Aberrant PI3K in Cancer.
REACT_267817. Constitutive Signaling by EGFRvIII.
REACT_268595. Inhibition of Signaling by Overexpressed EGFR.
REACT_318. Platelet degranulation.
REACT_75829. PIP3 activates AKT signaling.
REACT_9417. Signaling by EGFR.
SignaLinkiP01133.

Miscellaneous databases

ChiTaRSiEGF. human.
EvolutionaryTraceiP01133.
GeneWikiiEpidermal_growth_factor.
GenomeRNAii1950.
NextBioi7903.
PMAP-CutDBP01133.
PROiP01133.
SOURCEiSearch...

Gene expression databases

BgeeiP01133.
CleanExiHS_EGF.
GenevisibleiP01133. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "Neurotrophic actions of a novel molluscan epidermal growth factor."
    Hermann P.M., van Kesteren R.E., Wildering W.C., Painter S.D., Reno J.M., Smith J.S., Kumar S.B., Geraerts W.P., Ericsson L.H., Smit A.B., Bulloch A.G., Nagle G.T.
    J. Neurosci. 20:6355-6364(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. Cited for: FUNCTION, TISSUE SPECIFICITY, VARIANT HOMG4 LEU-1070, CHARACTERIZATION OF VARIANT HOMG4 LEU-1070.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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: July 22, 2015
This is version 180 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

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.