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P01133

- EGF_HUMAN

UniProt

P01133 - EGF_HUMAN

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Protein

Pro-epidermal growth factor

Gene
EGF
Organism
Homo sapiens (Human)
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 TRPM6.1 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
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. 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 10321010Extracellular Reviewed predictionAdd
BLAST
Transmembranei1033 – 105321Helical; Reviewed predictionAdd
BLAST
Topological domaini1054 – 1207154Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: UniProt
  3. extracellular vesicular exosome Source: UniProt
  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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 – 2222 Reviewed predictionAdd
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...) Reviewed prediction
Glycosylationi104 – 1041N-linked (GlcNAc...) Reviewed prediction
Glycosylationi117 – 1171N-linked (GlcNAc...) Reviewed prediction
Glycosylationi148 – 1481N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi318 ↔ 330 By similarity
Glycosylationi324 – 3241N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi325 ↔ 339 By similarity
Disulfide bondi341 ↔ 354 By similarity
Disulfide bondi360 ↔ 371 By similarity
Disulfide bondi367 ↔ 380 By similarity
Disulfide bondi382 ↔ 395 By similarity
Disulfide bondi401 ↔ 412 By similarity
Glycosylationi404 – 4041N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi408 ↔ 421 By similarity
Disulfide bondi423 ↔ 436 By similarity
Disulfide bondi439 ↔ 451 By similarity
Disulfide bondi447 ↔ 461 By similarity
Disulfide bondi463 ↔ 476 By similarity
Glycosylationi596 – 5961N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi745 ↔ 756 By similarity
Disulfide bondi752 ↔ 765 By similarity
Disulfide bondi767 ↔ 780 By similarity
Glycosylationi815 – 8151N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi835 ↔ 846 By similarity
Disulfide bondi840 ↔ 855 By similarity
Disulfide bondi857 ↔ 868 By similarity
Disulfide bondi874 ↔ 888 By similarity
Disulfide bondi881 ↔ 897 By similarity
Disulfide bondi899 ↔ 910 By similarity
Disulfide bondi916 ↔ 929 By similarity
Disulfide bondi923 ↔ 938 By similarity
Glycosylationi926 – 9261N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi940 ↔ 951 By similarity
Glycosylationi954 – 9541O-linked (GalNAc...); or Thr-9551 Publication
Glycosylationi955 – 9551O-linked (GalNAc...); or Ser-9541 Publication
Disulfide bondi976 ↔ 9904 Publications
Disulfide bondi984 ↔ 10014 Publications
Disulfide bondi1003 ↔ 10124 Publications

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).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EGFRP0053315EBI-640857,EBI-297353
EgfrQ012793EBI-640857,EBI-6296235From a different organism.

Protein-protein interaction databases

BioGridi108270. 16 interactions.
DIPiDIP-5767N.
IntActiP01133. 5 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.

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 1Add
BLAST
Domaini356 – 39641EGF-like 2; calcium-binding Reviewed predictionAdd
BLAST
Domaini397 – 43741EGF-like 3Add
BLAST
Domaini435 – 47743EGF-like 4Add
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 5Add
BLAST
Domaini831 – 86939EGF-like 6Add
BLAST
Domaini870 – 91142EGF-like 7; calcium-binding Reviewed predictionAdd
BLAST
Domaini912 – 95241EGF-like 8; calcium-binding Reviewed predictionAdd
BLAST
Domaini972 – 101342EGF-like 9Add
BLAST

Region

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

Sequence similaritiesi

Contains 9 EGF-like domains.

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.

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. VSP_041586Add
BLAST
Alternative sequencei912 – 95241Missing in isoform 3. VSP_047190Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti302 – 3021A → T in BAG61319. 1 Publication

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. 5 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

« 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. 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: September 3, 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
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

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