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P01133 (EGF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pro-epidermal growth factor

Short name=EGF

Cleaved into the following chain:

  1. Epidermal growth factor
    Alternative name(s):
    Urogastrone
Gene names
Name:EGF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1207 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10

Subunit structure

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). Ref.11

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed in kidney, salivary gland, cerebrum and prostate. Ref.10

Post-translational modification

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). Ref.8

Involvement in disease

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. Ref.10

Sequence similarities

Contains 9 EGF-like domains.

Contains 9 LDL-receptor class B repeats.

Sequence caution

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

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Primary hypomagnesemia
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionGrowth factor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Traceable author statement PubMed 9482941. Source: ProtInc

ERK1 and ERK2 cascade

Inferred from direct assay PubMed 16314496. Source: UniProtKB

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

STAT protein import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

activation of MAPKK activity

Inferred from electronic annotation. Source: Ensembl

activation of transmembrane receptor protein tyrosine kinase activity

Traceable author statement PubMed 9712850. Source: GOC

angiogenesis

Inferred from direct assay PubMed 15611079. Source: HGNC

blood coagulation

Traceable author statement. Source: Reactome

branching morphogenesis of an epithelial tube

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

mammary gland alveolus development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cholesterol efflux

Inferred from electronic annotation. Source: Ensembl

negative regulation of epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

negative regulation of secretion

Inferred from direct assay PubMed 10559227. Source: BHF-UCL

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from direct assay PubMed 15611079. Source: HGNC

positive regulation of catenin import into nucleus

Inferred from direct assay PubMed 20302655. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from direct assay PubMed 20388803. Source: BHF-UCL

positive regulation of cerebellar granule cell precursor proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of epidermal growth factor-activated receptor activity

Traceable author statement PubMed 9712850. Source: UniProtKB

positive regulation of hyaluronan biosynthetic process

Inferred from direct assay PubMed 17324121. Source: UniProtKB

positive regulation of mitosis

Inferred from direct assay PubMed 15611079. Source: HGNC

positive regulation of peptidyl-threonine phosphorylation

Inferred from direct assay PubMed 16314496. Source: UniProtKB

positive regulation of phosphorylation

Inferred from direct assay PubMed 15611079. Source: HGNC

positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16314496. Source: UniProtKB

regulation of calcium ion import

Inferred from direct assay PubMed 19996314. Source: BHF-UCL

regulation of protein localization to cell surface

Inferred from direct assay PubMed 19996314. Source: BHF-UCL

signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentextracellular region

Inferred by curator PubMed 9712850. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

plasma membrane

Traceable author statement Ref.1. Source: ProtInc

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

epidermal growth factor receptor binding

Traceable author statement PubMed 9712850. Source: UniProtKB

growth factor activity

Inferred from direct assay PubMed 15611079. Source: HGNC

protein binding

Inferred from physical interaction Ref.13Ref.14PubMed 21439278PubMed 23597562PubMed 2790960. Source: IntAct

transmembrane receptor protein tyrosine kinase activator activity

Traceable author statement PubMed 9712850. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EGFRP0053315EBI-640857,EBI-297353
EgfrQ012793EBI-640857,EBI-6296235From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P01133-1)

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.
Isoform 2 (identifier: P01133-2)

The sequence of this isoform differs from the canonical sequence as follows:
     314-355: Missing.
Isoform 3 (identifier: P01133-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 12071185Pro-epidermal growth factor
PRO_0000007540
Chain971 – 102353Epidermal growth factor
PRO_0000007541

Regions

Topological domain23 – 10321010Extracellular Potential
Transmembrane1033 – 105321Helical; Potential
Topological domain1054 – 1207154Cytoplasmic Potential
Repeat86 – 12742LDL-receptor class B 1
Repeat128 – 16942LDL-receptor class B 2
Repeat170 – 21142LDL-receptor class B 3
Repeat212 – 25847LDL-receptor class B 4
Domain314 – 35542EGF-like 1
Domain356 – 39641EGF-like 2; calcium-binding Potential
Domain397 – 43741EGF-like 3
Domain435 – 47743EGF-like 4
Repeat483 – 52341LDL-receptor class B 5
Repeat524 – 56643LDL-receptor class B 6
Repeat567 – 60943LDL-receptor class B 7
Repeat610 – 65344LDL-receptor class B 8
Repeat654 – 69643LDL-receptor class B 9
Domain741 – 78141EGF-like 5
Domain831 – 86939EGF-like 6
Domain870 – 91142EGF-like 7; calcium-binding Potential
Domain912 – 95241EGF-like 8; calcium-binding Potential
Domain972 – 101342EGF-like 9
Region801 – 8077O-glycosylated at one site

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation1481N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation4041N-linked (GlcNAc...) Potential
Glycosylation5961N-linked (GlcNAc...) Potential
Glycosylation8151N-linked (GlcNAc...) Potential
Glycosylation9261N-linked (GlcNAc...) Potential
Glycosylation9541O-linked (GalNAc...); or Thr-955 Ref.8
Glycosylation9551O-linked (GalNAc...); or Ser-954 Ref.8
Disulfide bond318 ↔ 330 By similarity
Disulfide bond325 ↔ 339 By similarity
Disulfide bond341 ↔ 354 By similarity
Disulfide bond360 ↔ 371 By similarity
Disulfide bond367 ↔ 380 By similarity
Disulfide bond382 ↔ 395 By similarity
Disulfide bond401 ↔ 412 By similarity
Disulfide bond408 ↔ 421 By similarity
Disulfide bond423 ↔ 436 By similarity
Disulfide bond439 ↔ 451 By similarity
Disulfide bond447 ↔ 461 By similarity
Disulfide bond463 ↔ 476 By similarity
Disulfide bond745 ↔ 756 By similarity
Disulfide bond752 ↔ 765 By similarity
Disulfide bond767 ↔ 780 By similarity
Disulfide bond835 ↔ 846 By similarity
Disulfide bond840 ↔ 855 By similarity
Disulfide bond857 ↔ 868 By similarity
Disulfide bond874 ↔ 888 By similarity
Disulfide bond881 ↔ 897 By similarity
Disulfide bond899 ↔ 910 By similarity
Disulfide bond916 ↔ 929 By similarity
Disulfide bond923 ↔ 938 By similarity
Disulfide bond940 ↔ 951 By similarity
Disulfide bond976 ↔ 990 Ref.12 Ref.13 Ref.14 Ref.16
Disulfide bond984 ↔ 1001 Ref.12 Ref.13 Ref.14 Ref.16
Disulfide bond1003 ↔ 1012 Ref.12 Ref.13 Ref.14 Ref.16

Natural variations

Alternative sequence314 – 35542Missing in isoform 2.
VSP_041586
Alternative sequence912 – 95241Missing in isoform 3.
VSP_047190
Natural variant161S → R. Ref.2
Corresponds to variant rs11568849 [ dbSNP | Ensembl ].
VAR_020161
Natural variant1511H → Y.
Corresponds to variant rs9991664 [ dbSNP | Ensembl ].
VAR_033825
Natural variant2571D → H. Ref.2
Corresponds to variant rs11568911 [ dbSNP | Ensembl ].
VAR_020968
Natural variant2921L → H.
Corresponds to variant rs35191533 [ dbSNP | Ensembl ].
VAR_033826
Natural variant4311R → K. Ref.2
Corresponds to variant rs11568943 [ dbSNP | Ensembl ].
VAR_020162
Natural variant6381S → R. Ref.2
Corresponds to variant rs11568992 [ dbSNP | Ensembl ].
VAR_020969
Natural variant7081M → I. Ref.2
Corresponds to variant rs2237051 [ dbSNP | Ensembl ].
VAR_002275
Natural variant7231G → R.
Corresponds to variant rs6413481 [ dbSNP | Ensembl ].
VAR_020163
Natural variant7841D → V. Ref.2
Corresponds to variant rs11569017 [ dbSNP | Ensembl ].
VAR_020164
Natural variant8421M → T. Ref.2
Corresponds to variant rs11569046 [ dbSNP | Ensembl ].
VAR_020165
Natural variant9201E → V. Ref.2 Ref.3
Corresponds to variant rs4698803 [ dbSNP | Ensembl ].
VAR_020970
Natural variant9811D → E. Ref.2
Corresponds to variant rs11569086 [ dbSNP | Ensembl ].
VAR_020971
Natural variant10431L → F. Ref.2
Corresponds to variant rs11569098 [ dbSNP | Ensembl ].
VAR_020166
Natural variant10701P → L in HOMG4; affects basolateral sorting of pro-EGF preventing the hormone to stimulate EGFR; lack of TRPM6 activation. Ref.10
VAR_039474
Natural variant10841A → G. Ref.2
Corresponds to variant rs11569111 [ dbSNP | Ensembl ].
VAR_020972

Experimental info

Sequence conflict3021A → T in BAG61319. Ref.3

Secondary structure

............. 1207
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 7, 2009. Version 2.
Checksum: 3C787F1D405CFAF1

FASTA1,207133,994
        10         20         30         40         50         60 
MLLTLIILLP VVSKFSFVSL SAPQHWSCPE GTLAGNGNST CVGPAPFLIF SHGNSIFRID 

        70         80         90        100        110        120 
TEGTNYEQLV VDAGVSVIMD FHYNEKRIYW VDLERQLLQR VFLNGSRQER VCNIEKNVSG 

       130        140        150        160        170        180 
MAINWINEEV IWSNQQEGII TVTDMKGNNS HILLSALKYP ANVAVDPVER FIFWSSEVAG 

       190        200        210        220        230        240 
SLYRADLDGV GVKALLETSE KITAVSLDVL DKRLFWIQYN REGSNSLICS CDYDGGSVHI 

       250        260        270        280        290        300 
SKHPTQHNLF AMSLFGDRIF YSTWKMKTIW IANKHTGKDM VRINLHSSFV PLGELKVVHP 

       310        320        330        340        350        360 
LAQPKAEDDT WEPEQKLCKL RKGNCSSTVC GQDLQSHLCM CAEGYALSRD RKYCEDVNEC 

       370        380        390        400        410        420 
AFWNHGCTLG CKNTPGSYYC TCPVGFVLLP DGKRCHQLVS CPRNVSECSH DCVLTSEGPL 

       430        440        450        460        470        480 
CFCPEGSVLE RDGKTCSGCS SPDNGGCSQL CVPLSPVSWE CDCFPGYDLQ LDEKSCAASG 

       490        500        510        520        530        540 
PQPFLLFANS QDIRHMHFDG TDYGTLLSQQ MGMVYALDHD PVENKIYFAH TALKWIERAN 

       550        560        570        580        590        600 
MDGSQRERLI EEGVDVPEGL AVDWIGRRFY WTDRGKSLIG RSDLNGKRSK IITKENISQP 

       610        620        630        640        650        660 
RGIAVHPMAK RLFWTDTGIN PRIESSSLQG LGRLVIASSD LIWPSGITID FLTDKLYWCD 

       670        680        690        700        710        720 
AKQSVIEMAN LDGSKRRRLT QNDVGHPFAV AVFEDYVWFS DWAMPSVMRV NKRTGKDRVR 

       730        740        750        760        770        780 
LQGSMLKPSS LVVVHPLAKP GADPCLYQNG GCEHICKKRL GTAWCSCREG FMKASDGKTC 

       790        800        810        820        830        840 
LALDGHQLLA GGEVDLKNQV TPLDILSKTR VSEDNITESQ HMLVAEIMVS DQDDCAPVGC 

       850        860        870        880        890        900 
SMYARCISEG EDATCQCLKG FAGDGKLCSD IDECEMGVPV CPPASSKCIN TEGGYVCRCS 

       910        920        930        940        950        960 
EGYQGDGIHC LDIDECQLGE HSCGENASCT NTEGGYTCMC AGRLSEPGLI CPDSTPPPHL 

       970        980        990       1000       1010       1020 
REDDHHYSVR NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW 

      1030       1040       1050       1060       1070       1080 
ELRHAGHGQQ QKVIVVAVCV VVLVMLLLLS LWGAHYYRTQ KLLSKNPKNP YEESSRDVRS 

      1090       1100       1110       1120       1130       1140 
RRPADTEDGM SSCPQPWFVV IKEHQDLKNG GQPVAGEDGQ AADGSMQPTS WRQEPQLCGM 

      1150       1160       1170       1180       1190       1200 
GTEQGCWIPV SSDKGSCPQV MERSFHMPSY GTQTLEGGVE KPHSLLSANP LWQQRALDPP 


HQMELTQ 

« Hide

Isoform 2 [UniParc].

Checksum: 5449AE11FA9276B5
Show »

FASTA1,165129,256
Isoform 3 [UniParc].

Checksum: 4872256969C28678
Show »

FASTA1,166129,746

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Impaired basolateral sorting of pro-EGF causes isolated recessive renal hypomagnesemia."
Groenestege W.M.T., Thebault S., van der Wijst J., van den Berg D., Janssen R., Tejpar S., van den Heuvel L.P., van Cutsem E., Hoenderop J.G., Knoers N.V., Bindels R.J.
J. Clin. Invest. 117:2260-2267(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

Epidermal growth factor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3689.1. [P01133-1]
CCDS54794.1. [P01133-3]
CCDS54795.1. [P01133-2]
PIREGHU. A25531.
RefSeqNP_001171601.1. NM_001178130.1. [P01133-3]
NP_001171602.1. NM_001178131.1. [P01133-2]
NP_001954.2. NM_001963.4. [P01133-1]
UniGeneHs.419815.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP01133.
SMRP01133. Positions 42-773, 839-1020.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108270. 16 interactions.
DIPDIP-5767N.
IntActP01133. 5 interactions.
MINTMINT-260489.
STRING9606.ENSP00000265171.

Chemistry

BindingDBP01133.
ChEMBLCHEMBL5734.
DrugBankDB00605. Sulindac.

PTM databases

PhosphoSiteP01133.

Polymorphism databases

DMDM251757262.

Proteomic databases

PaxDbP01133.
PRIDEP01133.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265171; ENSP00000265171; ENSG00000138798. [P01133-1]
ENST00000503392; ENSP00000421384; ENSG00000138798. [P01133-3]
ENST00000509793; ENSP00000424316; ENSG00000138798. [P01133-2]
GeneID1950.
KEGGhsa:1950.
UCSCuc003hzy.4. human. [P01133-1]
uc011cfu.2. human. [P01133-2]

Organism-specific databases

CTD1950.
GeneCardsGC04P110834.
HGNCHGNC:3229. EGF.
HPACAB017843.
MIM131530. gene.
611718. phenotype.
neXtProtNX_P01133.
Orphanet210159. Adult hepatocellular carcinoma.
34527. Familial primary hypomagnesemia with normocalcuria and normocalcemia.
PharmGKBPA27664.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG325841.
HOGENOMHOG000112345.
HOVERGENHBG003858.
InParanoidP01133.
KOK04357.
OMAKIYFAHT.
OrthoDBEOG7Q2N4J.
PhylomeDBP01133.
TreeFamTF315253.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP01133.

Gene expression databases

ArrayExpressP01133.
BgeeP01133.
CleanExHS_EGF.
GenevestigatorP01133.

Family and domain databases

Gene3D2.120.10.30. 2 hits.
2.40.155.10. 1 hit.
InterProIPR011042. 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]
PfamPF00008. EGF. 1 hit.
PF07645. EGF_CA. 3 hits.
PF00058. Ldl_recept_b. 4 hits.
[Graphical view]
PIRSFPIRSF001778. Pro-epidermal_growth_factor. 1 hit.
SMARTSM00181. EGF. 6 hits.
SM00179. EGF_CA. 2 hits.
SM00135. LY. 9 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 4 hits.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

ChiTaRSEGF. human.
EvolutionaryTraceP01133.
GeneWikiEpidermal_growth_factor.
GenomeRNAi1950.
NextBio7903.
PMAP-CutDBP01133.
PROP01133.
SOURCESearch...

Entry information

Entry nameEGF_HUMAN
AccessionPrimary (citable) accession number: P01133
Secondary accession number(s): B4DRK7 expand/collapse secondary AC list , E7EVD2, E9PBF0, Q52LZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 7, 2009
Last modified: July 9, 2014
This is version 169 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM