GenomeNet

Database: UniProt
Entry: Q6UW88
LinkDB: Q6UW88
Original site: Q6UW88 
ID   EPGN_HUMAN              Reviewed;         154 AA.
AC   Q6UW88; A1BMM3; A1BMM4; A1BMM5; A1BMM6; A1BMM7; A1BMM8; A8K090;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   10-APR-2019, entry version 129.
DE   RecName: Full=Epigen;
DE   AltName: Full=Epithelial mitogen;
DE            Short=EPG;
DE   Flags: Precursor;
GN   Name=EPGN; ORFNames=UNQ3072/PRO9904;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4; 5; 6 AND 7).
RA   Johnstone L.S., Abumaree M., Martin J., Webster G., Murison G.;
RT   "Human keratinocytes express several alternatively spliced forms of
RT   EPIGEN, encoding directly secreted and intracellular proteins.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 23-37.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally
RT   verified cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=15611079; DOI=10.1074/jbc.M413919200;
RA   Kochupurakkal B.S., Harari D., Di-Segni A., Maik-Rachline G.,
RA   Lyass L., Gur G., Kerber G., Citri A., Lavi S., Eilam R.,
RA   Chalifa-Caspi V., Eshhar Z., Pikarsky E., Pinkas-Kramarski R.,
RA   Bacus S.S., Yarden Y.;
RT   "Epigen, the last ligand of ErbB receptors, reveals intricate
RT   relationships between affinity and mitogenicity.";
RL   J. Biol. Chem. 280:8503-8512(2005).
CC   -!- FUNCTION: Promotes the growth of epithelial cells. May stimulate
CC       the phosphorylation of EGFR and mitogen-activated protein kinases.
CC       {ECO:0000269|PubMed:15611079}.
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Membrane {ECO:0000305}; Single-
CC       pass type I membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Membrane {ECO:0000305}; Single-
CC       pass type I membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Isoform 4: Secreted {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Isoform 5: Secreted {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Isoform 6: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1;
CC         IsoId=Q6UW88-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6UW88-2; Sequence=VSP_036655, VSP_036658;
CC       Name=3; Synonyms=B;
CC         IsoId=Q6UW88-3; Sequence=VSP_036657;
CC       Name=4; Synonyms=E;
CC         IsoId=Q6UW88-4; Sequence=VSP_036656;
CC       Name=5; Synonyms=F;
CC         IsoId=Q6UW88-5; Sequence=VSP_036655, VSP_036657;
CC       Name=6; Synonyms=G;
CC         IsoId=Q6UW88-6; Sequence=VSP_036655, VSP_036656;
CC       Name=7; Synonyms=D;
CC         IsoId=Q6UW88-7; Sequence=VSP_036654, VSP_036656;
DR   EMBL; DQ235264; ABB60043.1; -; mRNA.
DR   EMBL; DQ235265; ABB60044.1; -; mRNA.
DR   EMBL; DQ235266; ABB60045.1; -; mRNA.
DR   EMBL; DQ235267; ABB60046.1; -; mRNA.
DR   EMBL; DQ235268; ABB60047.1; -; mRNA.
DR   EMBL; DQ235269; ABB60048.1; -; mRNA.
DR   EMBL; AY358920; AAQ89279.1; -; mRNA.
DR   EMBL; AK289455; BAF82144.1; -; mRNA.
DR   CCDS; CCDS59475.1; -. [Q6UW88-5]
DR   CCDS; CCDS59476.1; -. [Q6UW88-6]
DR   CCDS; CCDS59477.1; -. [Q6UW88-3]
DR   CCDS; CCDS59478.1; -. [Q6UW88-1]
DR   CCDS; CCDS59479.1; -. [Q6UW88-4]
DR   RefSeq; NP_001257918.1; NM_001270989.1. [Q6UW88-1]
DR   RefSeq; NP_001257919.1; NM_001270990.1. [Q6UW88-3]
DR   RefSeq; NP_001257920.1; NM_001270991.1. [Q6UW88-5]
DR   RefSeq; NP_001257921.1; NM_001270992.1. [Q6UW88-4]
DR   RefSeq; NP_001257922.1; NM_001270993.1. [Q6UW88-6]
DR   RefSeq; XP_005265723.1; XM_005265666.4.
DR   UniGene; Hs.401237; -.
DR   PDB; 5WB8; X-ray; 3.00 A; B/C=49-108.
DR   PDBsum; 5WB8; -.
DR   ProteinModelPortal; Q6UW88; -.
DR   SMR; Q6UW88; -.
DR   IntAct; Q6UW88; 4.
DR   STRING; 9606.ENSP00000411898; -.
DR   PhosphoSitePlus; Q6UW88; -.
DR   BioMuta; EPGN; -.
DR   DMDM; 229464464; -.
DR   PeptideAtlas; Q6UW88; -.
DR   PRIDE; Q6UW88; -.
DR   ProteomicsDB; 67455; -.
DR   ProteomicsDB; 67456; -. [Q6UW88-2]
DR   ProteomicsDB; 67457; -. [Q6UW88-3]
DR   ProteomicsDB; 67458; -. [Q6UW88-4]
DR   ProteomicsDB; 67459; -. [Q6UW88-5]
DR   ProteomicsDB; 67460; -. [Q6UW88-6]
DR   ProteomicsDB; 67461; -. [Q6UW88-7]
DR   TopDownProteomics; Q6UW88-2; -. [Q6UW88-2]
DR   DNASU; 255324; -.
DR   Ensembl; ENST00000332112; ENSP00000330375; ENSG00000182585. [Q6UW88-2]
DR   Ensembl; ENST00000413830; ENSP00000411898; ENSG00000182585. [Q6UW88-1]
DR   Ensembl; ENST00000502358; ENSP00000426678; ENSG00000182585. [Q6UW88-4]
DR   Ensembl; ENST00000503098; ENSP00000425890; ENSG00000182585. [Q6UW88-3]
DR   Ensembl; ENST00000505212; ENSP00000424392; ENSG00000182585. [Q6UW88-6]
DR   Ensembl; ENST00000509145; ENSP00000426630; ENSG00000182585. [Q6UW88-7]
DR   Ensembl; ENST00000514968; ENSP00000426550; ENSG00000182585. [Q6UW88-5]
DR   GeneID; 255324; -.
DR   KEGG; hsa:255324; -.
DR   UCSC; uc003hhw.5; human. [Q6UW88-1]
DR   CTD; 255324; -.
DR   DisGeNET; 255324; -.
DR   EuPathDB; HostDB:ENSG00000182585.9; -.
DR   GeneCards; EPGN; -.
DR   HGNC; HGNC:17470; EPGN.
DR   HPA; HPA014369; -.
DR   neXtProt; NX_Q6UW88; -.
DR   OpenTargets; ENSG00000182585; -.
DR   PharmGKB; PA162385143; -.
DR   GeneTree; ENSGT00510000048556; -.
DR   HOVERGEN; HBG079616; -.
DR   InParanoid; Q6UW88; -.
DR   OMA; YCYVRKR; -.
DR   OrthoDB; 1425022at2759; -.
DR   PhylomeDB; Q6UW88; -.
DR   TreeFam; TF335931; -.
DR   Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-HSA-177929; Signaling by EGFR.
DR   Reactome; R-HSA-179812; GRB2 events in EGFR signaling.
DR   Reactome; R-HSA-180292; GAB1 signalosome.
DR   Reactome; R-HSA-180336; SHC1 events in EGFR signaling.
DR   Reactome; R-HSA-182971; EGFR downregulation.
DR   Reactome; R-HSA-212718; EGFR interacts with phospholipase C-gamma.
DR   Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR   Reactome; R-HSA-5638303; Inhibition of Signaling by Overexpressed EGFR.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR   SIGNOR; Q6UW88; -.
DR   GenomeRNAi; 255324; -.
DR   PRO; PR:Q6UW88; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000182585; Expressed in 71 organ(s), highest expression level in esophagus mucosa.
DR   ExpressionAtlas; Q6UW88; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:HGNC.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:HGNC.
DR   GO; GO:0008083; F:growth factor activity; IDA:HGNC.
DR   GO; GO:0000187; P:activation of MAPK activity; ISS:HGNC.
DR   GO; GO:0001525; P:angiogenesis; IDA:HGNC.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:HGNC.
DR   GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; IDA:HGNC.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:HGNC.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:HGNC.
DR   GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:HGNC.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR015497; EGF_rcpt_ligand.
DR   PANTHER; PTHR10740; PTHR10740; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Growth factor; Membrane; Reference proteome; Secreted;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     22       {ECO:0000269|PubMed:15340161}.
FT   CHAIN        23    154       Epigen.
FT                                /FTId=PRO_0000045462.
FT   TOPO_DOM     23    110       Extracellular. {ECO:0000255}.
FT   TRANSMEM    111    131       Helical. {ECO:0000255}.
FT   TOPO_DOM    132    154       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       56     96       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD     37     37       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     41     41       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     60     73       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     68     84       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     86     95       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ      15     44       Missing (in isoform 7).
FT                                {ECO:0000303|Ref.1}.
FT                                /FTId=VSP_036654.
FT   VAR_SEQ      36     44       Missing (in isoform 2, isoform 5 and
FT                                isoform 6). {ECO:0000303|PubMed:12975309,
FT                                ECO:0000303|Ref.1}.
FT                                /FTId=VSP_036655.
FT   VAR_SEQ      87    137       Missing (in isoform 4, isoform 6 and
FT                                isoform 7). {ECO:0000303|Ref.1}.
FT                                /FTId=VSP_036656.
FT   VAR_SEQ      96    137       Missing (in isoform 3 and isoform 5).
FT                                {ECO:0000303|Ref.1}.
FT                                /FTId=VSP_036657.
FT   VAR_SEQ     137    154       CLKLKSPYNVCSGERRPL -> YEKDKI (in isoform
FT                                2). {ECO:0000303|PubMed:12975309}.
FT                                /FTId=VSP_036658.
FT   CONFLICT      9      9       V -> A (in Ref. 1; ABB60048).
FT                                {ECO:0000305}.
FT   CONFLICT     62     62       E -> G (in Ref. 1; ABB60047).
FT                                {ECO:0000305}.
FT   STRAND       66     68       {ECO:0000244|PDB:5WB8}.
FT   STRAND       74     76       {ECO:0000244|PDB:5WB8}.
FT   TURN         77     80       {ECO:0000244|PDB:5WB8}.
FT   STRAND       81     83       {ECO:0000244|PDB:5WB8}.
FT   TURN         92     95       {ECO:0000244|PDB:5WB8}.
SQ   SEQUENCE   154 AA;  17091 MW;  BC78016BE3026474 CRC64;
     MALGVPISVY LLFNAMTALT EEAAVTVTPP ITAQQGNWTV NKTEADNIEG PIALKFSHLC
     LEDHNSYCIN GACAFHHELE KAICRCFTGY TGERCEHLTL TSYAVDSYEK YIAIGIGVGL
     LLSGFLVIFY CYIRKRCLKL KSPYNVCSGE RRPL
//
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