P01133 (EGF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1207 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.9
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.10
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed in kidney, salivary gland, cerebrum and prostate. Ref.9
Involvement in disease	Defects in EGF are the cause of hypomagnesemia type 4 (HOMG4) [MIM:611718]; also known as renal hypomagnesemia normocalciuric. HOMG4 is a disorder characterized by massive renal hypomagnesemia and normal levels of serum calcium and calcium excretion. Clinical features include seizures, mild-to mederate psychomotor retardation, and brisk tendon reflexes. Ref.9
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 component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Primary hypomagnesemia
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Growth factor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA replication Traceable author statement. Source: ProtInc ERK1 and ERK2 cascade Inferred from direct assay. Source: UniProtKB STAT protein import into nucleus Inferred from sequence or structural similarity. Source: UniProtKB angiogenesis Inferred from direct assay. Source: HGNC epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome negative regulation of epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome negative regulation of secretion Inferred from direct assay. Source: BHF-UCL 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. Source: HGNC positive regulation of catenin import into nucleus Inferred from direct assay. Source: BHF-UCL positive regulation of epidermal growth factor-activated receptor activity Traceable author statement. Source: UniProtKB positive regulation of mitosis Inferred from direct assay. Source: HGNC positive regulation of peptidyl-threonine phosphorylation Inferred from direct assay. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay. Source: UniProtKB regulation of calcium ion import Inferred from direct assay. Source: BHF-UCL regulation of protein localization at cell surface Inferred from direct assay. Source: BHF-UCL
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement. Source: ProtInc platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro epidermal growth factor receptor binding Traceable author statement. Source: UniProtKB growth factor activity Inferred from direct assay. Source: MGI transmembrane receptor protein tyrosine kinase activator activity Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EGFR	P00533	3	EBI-640857,EBI-297353

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Potential

Chain

23 – 1207

1185

Pro-epidermal growth factor

PRO_0000007540

Chain

971 – 1023

53

Epidermal growth factor

PRO_0000007541

Regions

Topological domain

23 – 1032

1010

Extracellular Potential

Transmembrane

1033 – 1053

21

Helical; Potential

Topological domain

1054 – 1207

154

Cytoplasmic Potential

Repeat

86 – 127

42

LDL-receptor class B 1

Repeat

128 – 169

42

LDL-receptor class B 2

Repeat

170 – 211

42

LDL-receptor class B 3

Repeat

212 – 258

47

LDL-receptor class B 4

Domain

314 – 355

42

EGF-like 1

Domain

356 – 396

41

EGF-like 2; calcium-binding Potential

Domain

397 – 437

41

EGF-like 3

Domain

435 – 477

43

EGF-like 4

Repeat

483 – 523

41

LDL-receptor class B 5

Repeat

524 – 566

43

LDL-receptor class B 6

Repeat

567 – 609

43

LDL-receptor class B 7

Repeat

610 – 653

44

LDL-receptor class B 8

Repeat

654 – 696

43

LDL-receptor class B 9

Domain

741 – 781

41

EGF-like 5

Domain

831 – 869

39

EGF-like 6

Domain

870 – 911

42

EGF-like 7; calcium-binding Potential

Domain

912 – 952

41

EGF-like 8; calcium-binding Potential

Domain

972 – 1013

42

EGF-like 9

Amino acid modifications

Glycosylation

38

1

N-linked (GlcNAc...) Potential

Glycosylation

104

1

N-linked (GlcNAc...) Potential

Glycosylation

117

1

N-linked (GlcNAc...) Potential

Glycosylation

148

1

N-linked (GlcNAc...) Potential

Glycosylation

324

1

N-linked (GlcNAc...) Potential

Glycosylation

404

1

N-linked (GlcNAc...) Potential

Glycosylation

596

1

N-linked (GlcNAc...) Potential

Glycosylation

815

1

N-linked (GlcNAc...) Potential

Glycosylation

926

1

N-linked (GlcNAc...) Potential

Disulfide bond

318 ↔ 330

By similarity

Disulfide bond

325 ↔ 339

By similarity

Disulfide bond

341 ↔ 354

By similarity

Disulfide bond

360 ↔ 371

By similarity

Disulfide bond

367 ↔ 380

By similarity

Disulfide bond

382 ↔ 395

By similarity

Disulfide bond

401 ↔ 412

By similarity

Disulfide bond

408 ↔ 421

By similarity

Disulfide bond

423 ↔ 436

By similarity

Disulfide bond

439 ↔ 451

By similarity

Disulfide bond

447 ↔ 461

By similarity

Disulfide bond

463 ↔ 476

By similarity

Disulfide bond

745 ↔ 756

By similarity

Disulfide bond

752 ↔ 765

By similarity

Disulfide bond

767 ↔ 780

By similarity

Disulfide bond

835 ↔ 846

By similarity

Disulfide bond

840 ↔ 855

By similarity

Disulfide bond

857 ↔ 868

By similarity

Disulfide bond

874 ↔ 888

By similarity

Disulfide bond

881 ↔ 897

By similarity

Disulfide bond

899 ↔ 910

By similarity

Disulfide bond

916 ↔ 929

By similarity

Disulfide bond

923 ↔ 938

By similarity

Disulfide bond

940 ↔ 951

By similarity

Disulfide bond

976 ↔ 990

Ref.11 Ref.12 Ref.13 Ref.15

Disulfide bond

984 ↔ 1001

Ref.11 Ref.12 Ref.13 Ref.15

Disulfide bond

1003 ↔ 1012

Ref.11 Ref.12 Ref.13 Ref.15

Natural variations

Alternative sequence

314 – 355

42

Missing in isoform 2.

VSP_041586

Natural variant

16

1

S → R. Ref.2
Corresponds to variant rs11568849 [ dbSNP | Ensembl ].

VAR_020161

Natural variant

151

1

H → Y.
Corresponds to variant rs9991664 [ dbSNP | Ensembl ].

VAR_033825

Natural variant

257

1

D → H. Ref.2
Corresponds to variant rs11568911 [ dbSNP | Ensembl ].

VAR_020968

Natural variant

292

1

L → H.
Corresponds to variant rs35191533 [ dbSNP | Ensembl ].

VAR_033826

Natural variant

431

1

R → K. Ref.2
Corresponds to variant rs11568943 [ dbSNP | Ensembl ].

VAR_020162

Natural variant

638

1

S → R. Ref.2
Corresponds to variant rs11568992 [ dbSNP | Ensembl ].

VAR_020969

Natural variant

708

1

M → I. Ref.2
Corresponds to variant rs2237051 [ dbSNP | Ensembl ].

VAR_002275

Natural variant

723

1

G → R.
Corresponds to variant rs6413481 [ dbSNP | Ensembl ].

VAR_020163

Natural variant

784

1

D → V. Ref.2
Corresponds to variant rs11569017 [ dbSNP | Ensembl ].

VAR_020164

Natural variant

842

1

M → T. Ref.2
Corresponds to variant rs11569046 [ dbSNP | Ensembl ].

VAR_020165

Natural variant

920

1

E → V. Ref.2 Ref.3
Corresponds to variant rs4698803 [ dbSNP | Ensembl ].

VAR_020970

Natural variant

981

1

D → E. Ref.2
Corresponds to variant rs11569086 [ dbSNP | Ensembl ].

VAR_020971

Natural variant

1043

1

L → F. Ref.2
Corresponds to variant rs11569098 [ dbSNP | Ensembl ].

VAR_020166

Natural variant

1070

1

P → L in HOMG4; affects basolateral sorting of pro-EGF preventing the hormone to stimulate EGFR; lack of TRPM6 activation. Ref.9

VAR_039474

Natural variant

1084

1

A → G. Ref.2
Corresponds to variant rs11569111 [ dbSNP | Ensembl ].

VAR_020972

Experimental info

Sequence conflict

302

1

A → T in BAG61319. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

1207

Helix Strand Turn

Details...

Turn

979 – 982

4

Beta strand

989 – 992

4

Helix

994 – 996

3

Beta strand

999 – 1003

5

Beta strand

1007 – 1009

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 7, 2009. Version 2. Checksum: 3C787F1D405CFAF1	FASTA	1,207	133,994
	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
	Isoform 2 [UniParc]. Checksum: 5449AE11FA9276B5	FASTA	1,165	129,256
	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 WEPDVNECAF WNHGCTLGCK NTPGSYYCTC PVGFVLLPDG KRCHQLVSCP 370 380 390 400 410 420 RNVSECSHDC VLTSEGPLCF CPEGSVLERD GKTCSGCSSP DNGGCSQLCV PLSPVSWECD 430 440 450 460 470 480 CFPGYDLQLD EKSCAASGPQ PFLLFANSQD IRHMHFDGTD YGTLLSQQMG MVYALDHDPV 490 500 510 520 530 540 ENKIYFAHTA LKWIERANMD GSQRERLIEE GVDVPEGLAV DWIGRRFYWT DRGKSLIGRS 550 560 570 580 590 600 DLNGKRSKII TKENISQPRG IAVHPMAKRL FWTDTGINPR IESSSLQGLG RLVIASSDLI 610 620 630 640 650 660 WPSGITIDFL TDKLYWCDAK QSVIEMANLD GSKRRRLTQN DVGHPFAVAV FEDYVWFSDW 670 680 690 700 710 720 AMPSVMRVNK RTGKDRVRLQ GSMLKPSSLV VVHPLAKPGA DPCLYQNGGC EHICKKRLGT 730 740 750 760 770 780 AWCSCREGFM KASDGKTCLA LDGHQLLAGG EVDLKNQVTP LDILSKTRVS EDNITESQHM 790 800 810 820 830 840 LVAEIMVSDQ DDCAPVGCSM YARCISEGED ATCQCLKGFA GDGKLCSDID ECEMGVPVCP 850 860 870 880 890 900 PASSKCINTE GGYVCRCSEG YQGDGIHCLD IDECQLGEHS CGENASCTNT EGGYTCMCAG 910 920 930 940 950 960 RLSEPGLICP DSTPPPHLRE DDHHYSVRNS DSECPLSHDG YCLHDGVCMY IEALDKYACN 970 980 990 1000 1010 1020 CVVGYIGERC QYRDLKWWEL RHAGHGQQQK VIVVAVCVVV LVMLLLLSLW GAHYYRTQKL 1030 1040 1050 1060 1070 1080 LSKNPKNPYE ESSRDVRSRR PADTEDGMSS CPQPWFVVIK EHQDLKNGGQ PVAGEDGQAA 1090 1100 1110 1120 1130 1140 DGSMQPTSWR QEPQLCGMGT EQGCWIPVSS DKGSCPQVME RSFHMPSYGT QTLEGGVEKP 1150 1160 HSLLSANPLW QQRALDPPHQ MELTQ

References

	« Hide 'large scale' referencesShow '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: 3491360] [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: 14702039] [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: 15815621] [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: 15489334] [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: 300079] [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: 2789514] [Abstract] Cited for: PROTEIN SEQUENCE OF 971-1023.
[8]	"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: 1522591] [Abstract] Cited for: STRUCTURE BY NMR OF EGF.
[9]	"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: 17671655] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, VARIANT HOMG4 LEU-1070, CHARACTERIZATION OF VARIANT HOMG4 LEU-1070.
[10]	"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: 21439629] [Abstract] Cited for: INTERACTION WITH RHBDF1.
[11]	"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: 11438527] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 971-1021, DISULFIDE BONDS.
[12]	"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: 12297050] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 971-1023 IN COMPLEX WITH EGFR, DISULFIDE BONDS.
[13]	"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: 12620237] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 971-1023 IN COMPLEX WITH EGFR, DISULFIDE BONDS.
[14]	"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: 21029725] [Abstract] Cited for: STRUCTURE BY NMR OF 971-1023 IN COMPLEX WITH SURAMIN.
[15]	"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: 20837704] [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.

IPI

IPI00000073.
IPI00966866.

PIR

EGHU. A25531.

RefSeq

NP_001171602.1. NM_001178131.1.
NP_001954.2. NM_001963.4.

UniGene

Hs.419815.

3D structure databases

PDBe
RCSB PDB
PDBj

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	974-1022	[»]
2KV4	NMR	-	A	971-1023	[»]
3NJP	X-ray	3.30	C/D	975-1021	[»]

ProteinModelPortal

P01133.

SMR

P01133. Positions 14-1020.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5767N.

IntAct

P01133. 2 interactions.

MINT

MINT-260489.

STRING

P01133.

PTM databases

PhosphoSite

P01133.

Polymorphism databases

DMDM

251757262.

Proteomic databases

PRIDE

P01133.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265171; ENSP00000265171; ENSG00000138798.
ENST00000509793; ENSP00000424316; ENSG00000138798.

GeneID

1950.

KEGG

hsa:1950.

UCSC

uc003hzy.2. human.

Organism-specific databases

CTD

1950.

GeneCards

GC04P110834.

H-InvDB

HIX0031420.

HGNC

HGNC:3229. EGF.

HPA

CAB017843.

MIM

131530. gene.
611718. phenotype.

neXtProt

NX_P01133.

Orphanet

210159. Adult hepatocellular carcinoma.
34527. Hypomagnesemia with normocalciuria.

PharmGKB

PA27664.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06050.

HOGENOM

HBG279909.

HOVERGEN

HBG003858.

InParanoid

P01133.

OMA

DHDPVEN.

PhylomeDB

P01133.

Enzyme and pathway databases

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
arf6cyclingpathway. Arf6 signaling events.
ceramidepathway. Ceramide signaling pathway.
endothelinpathway. Endothelins.
telomerasepathway. Regulation of Telomerase.
ptp1bpathway. Signaling events mediated by PTP1B.
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P01133.

Bgee

P01133.

CleanEx

HS_EGF.

Genevestigator

P01133.

Family and domain databases

InterPro

IPR011042. 6-blade_b-propeller_TolB-like.
IPR006209. EGF.
IPR006210. EGF-like.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR000742. EGF_3.
IPR018097. EGF_Ca-bd_CS.
IPR000033. LDLR_classB_rpt.
IPR016317. Pro-epidermal_GF.
[Graphical view]

Gene3D

G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 3 hits.

KO

K04357.

Pfam

PF00008. EGF. 1 hit.
PF07645. EGF_CA. 3 hits.
PF00058. Ldl_recept_b. 4 hits.
[Graphical view]

PIRSF

PIRSF001778. Pro-epidermal_growth_factor. 1 hit.

SMART

SM00181. EGF. 6 hits.
SM00179. EGF_CA. 2 hits.
SM00135. LY. 9 hits.
[Graphical view]

PROSITE

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]

ProtoNet

Search...

Other

DrugBank

DB00605. Sulindac.

NextBio

7903.

PMAP-CutDB

P01133.

SOURCE

Search...

Entry information

Entry name

EGF_HUMAN

Accession

Primary (citable) accession number: P01133
Secondary accession number(s): B4DRK7, E9PBF0, Q52LZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 7, 2009
Last modified:	January 25, 2012
This is version 141 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.