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Epithelial membrane protein 2 (EMP-2) (Protein XMP)

 EMP2_HUMAN              Reviewed;         167 AA.
P54851; B2R7V6; D3DUF8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
13-FEB-2019, entry version 150.
RecName: Full=Epithelial membrane protein 2;
Short=EMP-2;
AltName: Full=Protein XMP;
Name=EMP2; Synonyms=XMP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
PubMed=8917086; DOI=10.1016/0378-1119(96)00134-5;
Taylor V., Suter U.;
"Epithelial membrane protein-2 and epithelial membrane protein-3: two
novel members of the peripheral myelin protein 22 gene family.";
Gene 175:115-120(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8996089; DOI=10.1016/S0378-1119(96)00475-1;
Ben-Porath I., Benvenisty N.;
"Characterization of a tumor-associated gene, a member of a novel
family of genes encoding membrane glycoproteins.";
Gene 183:69-75(1996).
[3]
SEQUENCE REVISION.
Ben-Porath I., Benvenisty N.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Kim Y.-S., Ueda E., Borok Z., Kim S.-Y., Jetten A.M.;
"Genomic structure of the human epithelial membrane protein 2 (EMP2)
gene; regulation by two alternative promoters.";
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, INTERACTION WITH P2RX7, AND SUBCELLULAR LOCATION.
PubMed=12107182; DOI=10.1074/jbc.M205120200;
Wilson H.L., Wilson S.A., Surprenant A., North R.A.;
"Epithelial membrane proteins induce membrane blebbing and interact
with the P2X7 receptor C terminus.";
J. Biol. Chem. 277:34017-34023(2002).
[9]
TISSUE SPECIFICITY.
PubMed=12710941; DOI=10.1016/S0014-4800(03)00009-1;
Wadehra M., Sulur G.G., Braun J., Gordon L.K., Goodglick L.;
"Epithelial membrane protein-2 is expressed in discrete anatomical
regions of the eye.";
Exp. Mol. Pathol. 74:106-112(2003).
[10]
FUNCTION, AND INTERACTION WITH ITGB3.
PubMed=16216233; DOI=10.1016/j.ydbio.2005.09.003;
Wadehra M., Forbes A., Pushkarna N., Goodglick L., Gordon L.K.,
Williams C.J., Braun J.;
"Epithelial membrane protein-2 regulates surface expression of
alphavbeta3 integrin in the endometrium.";
Dev. Biol. 287:336-345(2005).
[11]
FUNCTION.
PubMed=16487956; DOI=10.1016/j.ydbio.2006.01.015;
Wadehra M., Dayal M., Mainigi M., Ord T., Iyer R., Braun J.,
Williams C.J.;
"Knockdown of the tetraspan protein epithelial membrane protein-2
inhibits implantation in the mouse.";
Dev. Biol. 292:430-441(2006).
[12]
INDUCTION.
PubMed=18400107; DOI=10.1186/1477-7827-6-15;
Wadehra M., Mainigi M., Morales S.A., Rao R.G., Gordon L.K.,
Williams C.J., Braun J.;
"Steroid hormone regulation of EMP2 expression and localization in the
endometrium.";
Reprod. Biol. Endocrinol. 6:15-15(2008).
[13]
INTERACTION WITH PTK2, AND FUNCTION.
PubMed=19494199; DOI=10.1167/iovs.08-3315;
Morales S.A., Mareninov S., Coulam P., Wadehra M., Goodglick L.,
Braun J., Gordon L.K.;
"Functional consequences of interactions between FAK and epithelial
membrane protein 2 (EMP2).";
Invest. Ophthalmol. Vis. Sci. 50:4949-4956(2009).
[14]
FUNCTION, INTERACTION WITH PTK2, AND SUBCELLULAR LOCATION.
PubMed=21637765; DOI=10.1371/journal.pone.0019945;
Fu M., Rao R., Sudhakar D., Hogue C.P., Rutta Z., Morales S.,
Gordon L.K., Braun J., Goodglick L., Wadehra M.;
"Epithelial membrane protein-2 promotes endometrial tumor formation
through activation of FAK and Src.";
PLoS ONE 6:E19945-E19945(2011).
[15]
FUNCTION.
PubMed=22728127; DOI=10.1016/j.exer.2012.06.002;
Morales S.A., Telander D.G., Mareninov S., Nagy A., Wadehra M.,
Braun J., Gordon L.K.;
"Anti-EMP2 diabody blocks epithelial membrane protein 2 (EMP2) and FAK
mediated collagen gel contraction in ARPE-19 cells.";
Exp. Eye Res. 102:10-16(2012).
[16]
FUNCTION.
PubMed=23439602; DOI=10.1167/iovs.12-11013;
Morales S.A., Telander D.G., Leon D., Forward K., Braun J.,
Wadehra M., Gordon L.K.;
"Epithelial membrane protein 2 controls VEGF expression in ARPE-19
cells.";
Invest. Ophthalmol. Vis. Sci. 54:2367-2372(2013).
[17]
FUNCTION.
PubMed=23334331; DOI=10.1038/onc.2012.622;
Gordon L.K., Kiyohara M., Fu M., Braun J., Dhawan P., Chan A.,
Goodglick L., Wadehra M.;
"EMP2 regulates angiogenesis in endometrial cancer cells through
induction of VEGF.";
Oncogene 32:5369-5376(2013).
[18]
FUNCTION, INVOLVEMENT IN NPHS10, VARIANTS NPHS10 LEU-7 AND THR-10, AND
CHARACTERIZATION OF VARIANTS NPHS10 LEU-7 AND THR-10.
PubMed=24814193; DOI=10.1016/j.ajhg.2014.04.010;
Gee H.Y., Ashraf S., Wan X., Vega-Warner V., Esteve-Rudd J.,
Lovric S., Fang H., Hurd T.W., Sadowski C.E., Allen S.J., Otto E.A.,
Korkmaz E., Washburn J., Levy S., Williams D.S., Bakkaloglu S.A.,
Zolotnitskaya A., Ozaltin F., Zhou W., Hildebrandt F.;
"Mutations in EMP2 cause childhood-onset nephrotic syndrome.";
Am. J. Hum. Genet. 94:884-890(2014).
-!- FUNCTION: Functions as a key regulator of cell membrane
composition by regulating proteins surface expression. Also, plays
a role in regulation of processes including cell migration, cell
proliferation, cell contraction and cell adhesion. Negatively
regulates caveolae formation by reducing CAV1 expression and CAV1
amount by increasing lysosomal degradation (PubMed:24814193).
Facilitates surface trafficking and formation of lipid rafts
bearing GPI-anchor proteins (By similarity). Regulates surface
expression of MHC1 and ICAM1 proteins increasing susceptibility to
T-cell mediated cytotoxicity (By similarity). Regulates the plasma
membrane expression of the integrin heterodimers ITGA6-ITGB1,
ITGA5-ITGB3 and ITGA5-ITGB1 resulting in modulation of cell-matrix
adhesion (PubMed:16216233). Also regulates many processes through
PTK2. Regulates blood vessel endothelial cell migration and
angiogenesis by regulating VEGF protein expression through PTK2
activation (PubMed:23439602). Regulates cell migration and cell
contraction through PTK2 and SRC activation (PubMed:21637765,
PubMed:22728127). Regulates focal adhesion density, F-actin
conformation and cell adhesion capacity through interaction with
PTK2 (PubMed:19494199). Positively regulates cell proliferation
(PubMed:24814193). Plays a role during cell death and cell
blebbing (PubMed:12107182). Promotes angiogenesis and
vasculogenesis through induction of VEGFA via a HIF1A-dependent
pathway (PubMed:23334331). Also plays a role in embryo
implantation by regulating surface trafficking of integrin
heterodimer ITGA5-ITGB3 (PubMed:16487956). May play a role in
glomerular filtration (By similarity).
{ECO:0000250|UniProtKB:F1QIK8, ECO:0000250|UniProtKB:O88662,
ECO:0000269|PubMed:12107182, ECO:0000269|PubMed:16216233,
ECO:0000269|PubMed:16487956, ECO:0000269|PubMed:19494199,
ECO:0000269|PubMed:21637765, ECO:0000269|PubMed:22728127,
ECO:0000269|PubMed:23334331, ECO:0000269|PubMed:23439602,
ECO:0000269|PubMed:24814193}.
-!- SUBUNIT: Interacts with PTK2; regulates PTK2 activation and
localization (PubMed:19494199, PubMed:21637765). Interacts with
ITGB3; regulates the levels of the heterodimer ITGA5-ITGB3
integrin surface expression (PubMed:16216233). Interacts with
P2RX7 (via C-terminus) (PubMed:12107182). Interacts with ITGB1;
the interaction may be direct or indirect and ITGB1 has a
heterodimer form (By similarity). {ECO:0000250|UniProtKB:O88662,
ECO:0000269|PubMed:12107182, ECO:0000269|PubMed:16216233,
ECO:0000269|PubMed:19494199, ECO:0000269|PubMed:21637765}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000250|UniProtKB:O88662}; Multi-pass membrane protein
{ECO:0000255}. Cell membrane {ECO:0000269|PubMed:12107182,
ECO:0000269|PubMed:21637765}. Apical cell membrane
{ECO:0000250|UniProtKB:O88662}. Membrane raft
{ECO:0000269|PubMed:21637765}. Cytoplasm
{ECO:0000269|PubMed:21637765}. Nucleus
{ECO:0000250|UniProtKB:Q66HH2}. Note=Localizes in cytoplasm, foot
processes and cell bodies of podocytes and nucleus of endothelial
cells of kidney. Localizes to the apical cell surface in the
luminal epithelium and glandular epithelium. Colocalized with
ITGB1 and GPI-anchor proteins on plasma membrane.
{ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:Q66HH2}.
-!- TISSUE SPECIFICITY: Expressed in ciliary body epithelia, sclera,
cornea, and retinal pigment epithelium (at protein level)
(PubMed:12710941). {ECO:0000269|PubMed:12710941}.
-!- INDUCTION: Up-regulated by progesterone, increasing plasma
membrane expression. {ECO:0000269|PubMed:18400107}.
-!- DISEASE: Nephrotic syndrome 10 (NPHS10) [MIM:615861]: A form of
nephrotic syndrome, a renal disease clinically characterized by
focal segmental glomerulosclerosis, progressive renal failure,
severe proteinuria, hypoalbuminemia, hyperlipidemia and edema.
NPHS10 is a steroid-sensitive form characterized by onset in
childhood and remission without end-stage kidney disease.
{ECO:0000269|PubMed:24814193}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U52100; AAC51779.1; -; mRNA.
EMBL; X94770; CAA64393.1; -; mRNA.
EMBL; AY057060; AAL27085.1; -; Genomic_DNA.
EMBL; AK313134; BAG35953.1; -; mRNA.
EMBL; CH471112; EAW85180.1; -; Genomic_DNA.
EMBL; CH471112; EAW85181.1; -; Genomic_DNA.
EMBL; CH471112; EAW85182.1; -; Genomic_DNA.
EMBL; BC009687; AAH09687.1; -; mRNA.
CCDS; CCDS10541.1; -.
PIR; JC5044; JC5044.
PIR; JC5732; JC5732.
RefSeq; NP_001415.1; NM_001424.5.
RefSeq; XP_006720927.1; XM_006720864.3.
UniGene; Hs.531561; -.
ProteinModelPortal; P54851; -.
SMR; P54851; -.
BioGrid; 108328; 2.
IntAct; P54851; 2.
STRING; 9606.ENSP00000352540; -.
iPTMnet; P54851; -.
PhosphoSitePlus; P54851; -.
BioMuta; EMP2; -.
DMDM; 1706643; -.
jPOST; P54851; -.
PaxDb; P54851; -.
PeptideAtlas; P54851; -.
PRIDE; P54851; -.
ProteomicsDB; 56740; -.
DNASU; 2013; -.
Ensembl; ENST00000359543; ENSP00000352540; ENSG00000213853.
Ensembl; ENST00000536829; ENSP00000445712; ENSG00000213853.
GeneID; 2013; -.
KEGG; hsa:2013; -.
UCSC; uc002czx.4; human.
CTD; 2013; -.
DisGeNET; 2013; -.
EuPathDB; HostDB:ENSG00000213853.9; -.
GeneCards; EMP2; -.
HGNC; HGNC:3334; EMP2.
HPA; HPA014711; -.
MalaCards; EMP2; -.
MIM; 602334; gene.
MIM; 615861; phenotype.
neXtProt; NX_P54851; -.
OpenTargets; ENSG00000213853; -.
Orphanet; 93216; Familial idiopathic steroid-resistant nephrotic syndrome with minimal changes.
Orphanet; 93209; Idiopathic steroid-sensitive nephrotic syndrome with diffuse mesangial proliferation.
Orphanet; 93206; Idiopathic steroid-sensitive nephrotic syndrome with focal segmental hyalinosis.
Orphanet; 93207; Idiopathic steroid-sensitive nephrotic syndrome with minimal change.
PharmGKB; PA27771; -.
eggNOG; ENOG410IH06; Eukaryota.
eggNOG; ENOG4111QXD; LUCA.
GeneTree; ENSGT00940000153917; -.
HOGENOM; HOG000059542; -.
HOVERGEN; HBG001690; -.
InParanoid; P54851; -.
OMA; NNTNCTE; -.
OrthoDB; 1345659at2759; -.
PhylomeDB; P54851; -.
TreeFam; TF330414; -.
ChiTaRS; EMP2; human.
GeneWiki; EMP2; -.
GenomeRNAi; 2013; -.
PRO; PR:P54851; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000213853; Expressed in 213 organ(s), highest expression level in visceral pleura.
Genevisible; P54851; HS.
GO; GO:0045177; C:apical part of cell; ISS:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005178; F:integrin binding; IPI:MGI.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0007015; P:actin filament organization; IDA:UniProtKB.
GO; GO:0070252; P:actin-mediated cell contraction; IDA:UniProtKB.
GO; GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB.
GO; GO:0032060; P:bleb assembly; IDA:UniProtKB.
GO; GO:0043534; P:blood vessel endothelial cell migration; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
GO; GO:0008219; P:cell death; IDA:UniProtKB.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0008283; P:cell population proliferation; TAS:ProtInc.
GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
GO; GO:0007566; P:embryo implantation; IMP:UniProtKB.
GO; GO:0001765; P:membrane raft assembly; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IDA:MGI.
GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IDA:MGI.
GO; GO:0034394; P:protein localization to cell surface; IMP:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0045765; P:regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0001952; P:regulation of cell-matrix adhesion; IBA:GO_Central.
GO; GO:0010594; P:regulation of endothelial cell migration; IDA:UniProtKB.
GO; GO:0003093; P:regulation of glomerular filtration; IDA:UniProtKB.
GO; GO:0043549; P:regulation of kinase activity; IDA:UniProtKB.
GO; GO:2001212; P:regulation of vasculogenesis; IDA:UniProtKB.
GO; GO:0001913; P:T cell mediated cytotoxicity; ISS:UniProtKB.
InterPro; IPR003933; EMP-2.
InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
InterPro; IPR004032; PMP22_EMP_MP20.
PANTHER; PTHR10671:SF32; PTHR10671:SF32; 1.
Pfam; PF00822; PMP22_Claudin; 1.
PRINTS; PR01453; EPMEMFAMILY.
PRINTS; PR01455; EPMEMPROT2.
PROSITE; PS01221; PMP22_1; 1.
PROSITE; PS01222; PMP22_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasm; Disease mutation;
Glycoprotein; Golgi apparatus; Membrane; Nucleus; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 167 Epithelial membrane protein 2.
/FTId=PRO_0000164658.
TRANSMEM 1 21 Helical. {ECO:0000255}.
TRANSMEM 67 87 Helical. {ECO:0000255}.
TRANSMEM 95 115 Helical. {ECO:0000255}.
TRANSMEM 143 163 Helical. {ECO:0000255}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 47 47 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 52 52 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 7 7 F -> L (in NPHS10; decreased amount of
CAV1; dbSNP:rs730882194).
{ECO:0000269|PubMed:24814193}.
/FTId=VAR_071478.
VARIANT 10 10 A -> T (in NPHS10; decreased amount of
CAV1; dbSNP:rs587777482).
{ECO:0000269|PubMed:24814193}.
/FTId=VAR_071479.
CONFLICT 20 20 F -> L (in Ref. 3; CAA64393).
{ECO:0000305}.
CONFLICT 64 64 V -> F (in Ref. 3; CAA64393).
{ECO:0000305}.
SEQUENCE 167 AA; 19199 MW; 3E341DF3581EBCBF CRC64;
MLVLLAFIIA FHITSAALLF IATVDNAWWV GDEFFADVWR ICTNNTNCTV INDSFQEYST
LQAVQATMIL STILCCIAFF IFVLQLFRLK QGERFVLTSI IQLMSCLCVM IAASIYTDRR
EDIHDKNAKF YPVTREGSYG YSYILAWVAF ACTFISGMMY LILRKRK


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SDHF1_HUMAN Rat ELISA Kit FOR Epithelial membrane protein 1 96T
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SP-88512-1 EMP-1 (Epithelial Membrane Protein) (AA: Gly-Gly-Thr-Tyr-Ser-Cys-His-Phe-Gly-Pro-Leu-Thr-Trp-Val-Cys-Lys-Pro-Gln-Gly-Gly) (MW: 2093.39) 1 mg
EB07249 Epithelial membrane protein 3 (EMP3) 0.1 mg
EB07249 Epithelial membrane protein 3 (EMP3) 0.1 mg
CENPS_MOUSE Rat ELISA Kit FOR Epithelial membrane protein 1 96T

Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1502: Mitochondrial biogenesis
WP1624: Bacterial secretion system
WP1665: Limonene and pinene degradation
WP1689: Porphyrin and chlorophyll metabolism
WP1692: Protein export
WP1713: Two-component system
WP1714: Tyrosine metabolism
WP2199: Seed Development
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination

Related Genes :
[Emp2 Xmp] Epithelial membrane protein 2 (EMP-2) (Protein XMP)
[EMP2 XMP] Epithelial membrane protein 2 (EMP-2) (Protein XMP)
[Emp2] Epithelial membrane protein 2 (EMP-2)
[EMP2] Epithelial membrane protein 2 (EMP-2)
[EMP2] Epithelial membrane protein 2 (EMP-2)
[EPCAM GA733-2 M1S2 M4S1 MIC18 TACSTD1 TROP1] Epithelial cell adhesion molecule (Ep-CAM) (Adenocarcinoma-associated antigen) (Cell surface glycoprotein Trop-1) (Epithelial cell surface antigen) (Epithelial glycoprotein) (EGP) (Epithelial glycoprotein 314) (EGP314) (hEGP314) (KS 1/4 antigen) (KSA) (Major gastrointestinal tumor-associated protein GA733-2) (Tumor-associated calcium signal transducer 1) (CD antigen CD326)
[Tmed2 Rnp24] Transmembrane emp24 domain-containing protein 2 (COPI-coated vesicle membrane protein p24) (Membrane protein p24A) (RNP21.4) (p24 family protein beta-1) (p24beta1)
[Tmed2 Rnp24 Sid394] Transmembrane emp24 domain-containing protein 2 (COPI-coated vesicle membrane protein p24) (Membrane protein p24A) (Sid 394) (p24 family protein beta-1) (p24beta1)
[TMED2 RNP24] Transmembrane emp24 domain-containing protein 2 (Membrane protein p24A) (p24) (p24 family protein beta-1) (p24beta1)
[DDR1 CAK EDDR1 NEP NTRK4 PTK3A RTK6 TRKE] Epithelial discoidin domain-containing receptor 1 (Epithelial discoidin domain receptor 1) (EC 2.7.10.1) (CD167 antigen-like family member A) (Cell adhesion kinase) (Discoidin receptor tyrosine kinase) (HGK2) (Mammary carcinoma kinase 10) (MCK-10) (Protein-tyrosine kinase 3A) (Protein-tyrosine kinase RTK-6) (TRK E) (Tyrosine kinase DDR) (Tyrosine-protein kinase CAK) (CD antigen CD167a)
[MUC1 PUM] Mucin-1 (MUC-1) (Breast carcinoma-associated antigen DF3) (Cancer antigen 15-3) (CA 15-3) (Carcinoma-associated mucin) (Episialin) (H23AG) (Krebs von den Lungen-6) (KL-6) (PEMT) (Peanut-reactive urinary mucin) (PUM) (Polymorphic epithelial mucin) (PEM) (Tumor-associated epithelial membrane antigen) (EMA) (Tumor-associated mucin) (CD antigen CD227) [Cleaved into: Mucin-1 subunit alpha (MUC1-NT) (MUC1-alpha); Mucin-1 subunit beta (MUC1-beta) (MUC1-CT)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[EPHA2 ECK] Ephrin type-A receptor 2 (EC 2.7.10.1) (Epithelial cell kinase) (Tyrosine-protein kinase receptor ECK)
[Epha2 Eck Myk2 Sek2] Ephrin type-A receptor 2 (EC 2.7.10.1) (Epithelial cell kinase) (Tyrosine-protein kinase receptor ECK) (Tyrosine-protein kinase receptor MPK-5) (Tyrosine-protein kinase receptor SEK-2)
[Maea Emp] E3 ubiquitin-protein transferase MAEA (EC 2.3.2.27) (Erythroblast macrophage protein) (Macrophage erythroblast attacher)
[Tnf Tnfa Tnfsf2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[Tmed10 Tmp21] Transmembrane emp24 domain-containing protein 10 (21 kDa transmembrane-trafficking protein) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)
[MAEA EMP HLC10 PIG5] E3 ubiquitin-protein transferase MAEA (EC 2.3.2.27) (Cell proliferation-inducing gene 5 protein) (Erythroblast macrophage protein) (Human lung cancer oncogene 10 protein) (HLC-10) (Macrophage erythroblast attacher) (P44EMLP)
[ECT2] Protein ECT2 (Epithelial cell-transforming sequence 2 oncogene)
[Ptpro GLEPP1 Ptpn15 PTPU2] Receptor-type tyrosine-protein phosphatase O (R-PTP-O) (EC 3.1.3.48) (Glomerular epithelial protein 1) (Protein tyrosine phosphatase U2) (PTP-U2) (PTPase U2)
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[CDH1 CDHE UVO] Cadherin-1 (CAM 120/80) (Epithelial cadherin) (E-cadherin) (Uvomorulin) (CD antigen CD324) [Cleaved into: E-Cad/CTF1; E-Cad/CTF2; E-Cad/CTF3]
[Ptk2 Fadk Fak Fak1 Kiaa4203] Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK)
[botA atx bna bonT CLM_0897] Botulinum neurotoxin type A2 (BoNT/A) (Bontoxilysin-A) (BOTOX) [Cleaved into: Botulinum neurotoxin A2 light chain (LC) (EC 3.4.24.69); Botulinum neurotoxin A2 heavy chain (HC)]
[Cdh1] Cadherin-1 (ARC-1) (Epithelial cadherin) (E-cadherin) (Uvomorulin) (CD antigen CD324) [Cleaved into: E-Cad/CTF1; E-Cad/CTF2; E-Cad/CTF3]
[DDR1 EDDR1] Epithelial discoidin domain-containing receptor 1 (Epithelial discoidin domain receptor 1) (EC 2.7.10.1) (CD167 antigen-like family member A) (Discoidin receptor tyrosine kinase) (Tyrosine kinase DDR) (CD antigen CD167a)
[STEAP2 PCANAP1 STAMP1 UNQ6507/PRO23203] Metalloreductase STEAP2 (EC 1.16.1.-) (Prostate cancer-associated protein 1) (Protein up-regulated in metastatic prostate cancer) (PUMPCn) (Six-transmembrane epithelial antigen of prostate 2) (SixTransMembrane protein of prostate 1)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[Trpv6] Transient receptor potential cation channel subfamily V member 6 (TrpV6) (Calcium transport protein 1) (CaT1) (Epithelial calcium channel 2) (ECaC2)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.47) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

Bibliography :
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