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Enhancer of polycomb homolog 1

 EPC1_HUMAN              Reviewed;         836 AA.
Q9H2F5; B4DSC3; D3DRX7; Q5VW54; Q5VW56; Q5VW58; Q8NAQ4; Q8NE21;
Q96LF4; Q96RR6; Q9H7T7;
15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
27-SEP-2017, entry version 139.
RecName: Full=Enhancer of polycomb homolog 1;
Name=EPC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
INTERACTION WITH TRIM27.
PubMed=10976108; DOI=10.1074/jbc.M006585200;
Shimono Y., Murakami H., Hasegawa Y., Takahashi M.;
"RET finger protein is a transcriptional repressor and interacts with
enhancer of polycomb that has dual transcriptional functions.";
J. Biol. Chem. 275:39411-39419(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Nunes D.N., Dias-Neto E., Brentani R.R., Camargo A.A.;
"Cloning and characterization of two human homologs of the enhancer of
polycomb gene (EPC1) from Drosophila.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Brain, and Placenta;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
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).
[7]
PROTEIN SEQUENCE OF 58-68 AND 802-813, IDENTIFICATION IN NUA4 COMPLEX,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12963728; DOI=10.1074/jbc.C300389200;
Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
Conaway R.C., Conaway J.W.;
"Identification of new subunits of the multiprotein mammalian
TRRAP/TIP60-containing histone acetyltransferase complex.";
J. Biol. Chem. 278:42733-42736(2003).
[8]
REVIEW ON NUA4 COMPLEX.
PubMed=15196461; DOI=10.1016/j.gde.2004.02.009;
Doyon Y., Cote J.;
"The highly conserved and multifunctional NuA4 HAT complex.";
Curr. Opin. Genet. Dev. 14:147-154(2004).
[9]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4
COMPLEX, AND IDENTIFICATION IN A NUA4-RELATED SRCAP-CONTAINING
COMPLEX.
PubMed=14966270; DOI=10.1128/MCB.24.5.1884-1896.2004;
Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
"Structural and functional conservation of the NuA4 histone
acetyltransferase complex from yeast to humans.";
Mol. Cell. Biol. 24:1884-1896(2004).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-319 AND LYS-673, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[14]
VARIANT LEU-123.
PubMed=25787250; DOI=10.1073/pnas.1503696112;
Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D.,
Stalberg P., Akerstroem G., Westin G., Hellman P., Carling T.,
Bjoerklund P., Lifton R.P.;
"Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
insulin-producing adenomas.";
Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
-!- FUNCTION: Component of the NuA4 histone acetyltransferase (HAT)
complex which is involved in transcriptional activation of select
genes principally by acetylation of nucleosomal histones H4 and
H2A. This modification may both alter nucleosome - DNA
interactions and promote interaction of the modified histones with
other proteins which positively regulate transcription. This
complex may be required for the activation of transcriptional
programs associated with oncogene and proto-oncogene mediated
growth induction, tumor suppressor mediated growth arrest and
replicative senescence, apoptosis, and DNA repair. NuA4 may also
play a direct role in DNA repair when directly recruited to sites
of DNA damage. {ECO:0000269|PubMed:14966270}.
-!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
which contains the catalytic subunit KAT5/TIP60 and the subunits
EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49,
RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX,
MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. HTATTIP/TIP60, EPC1, and
ING3 together constitute a minimal HAT complex termed Piccolo
NuA4. Component of a NuA4-related complex which contains EP400,
TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49,
RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. The NuA4
complex interacts with MYC and the adenovirus E1A protein. EPC1
interacts with TRIM27. {ECO:0000269|PubMed:10976108,
ECO:0000269|PubMed:12963728, ECO:0000269|PubMed:14966270}.
-!- INTERACTION:
P19012:KRT15; NbExp=3; IntAct=EBI-769270, EBI-739566;
Q6NUQ1:RINT1; NbExp=4; IntAct=EBI-769270, EBI-726876;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10976108}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9H2F5-1; Sequence=Displayed;
Name=2;
IsoId=Q9H2F5-2; Sequence=VSP_012877;
Name=3;
IsoId=Q9H2F5-3; Sequence=VSP_012875, VSP_012877;
-!- SIMILARITY: Belongs to the enhancer of polycomb family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB14888.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC03857.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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EMBL; AF277374; AAG41402.1; -; mRNA.
EMBL; AF286905; AAK60501.1; -; mRNA.
EMBL; AK024329; BAB14888.1; ALT_INIT; mRNA.
EMBL; AK092304; BAC03857.1; ALT_SEQ; mRNA.
EMBL; AK299676; BAG61585.1; -; mRNA.
EMBL; AL158834; CAH70821.1; -; Genomic_DNA.
EMBL; AL391839; CAH70821.1; JOINED; Genomic_DNA.
EMBL; AL158834; CAH70822.1; -; Genomic_DNA.
EMBL; AL391839; CAH70822.1; JOINED; Genomic_DNA.
EMBL; AL158834; CAH70823.1; -; Genomic_DNA.
EMBL; AL391839; CAH70823.1; JOINED; Genomic_DNA.
EMBL; AL391839; CAH70453.1; -; Genomic_DNA.
EMBL; AL158834; CAH70453.1; JOINED; Genomic_DNA.
EMBL; AL391839; CAH70454.1; -; Genomic_DNA.
EMBL; AL158834; CAH70454.1; JOINED; Genomic_DNA.
EMBL; AL391839; CAH70455.1; -; Genomic_DNA.
EMBL; AL158834; CAH70455.1; JOINED; Genomic_DNA.
EMBL; CH471072; EAW85972.1; -; Genomic_DNA.
EMBL; CH471072; EAW85973.1; -; Genomic_DNA.
EMBL; BC036529; AAH36529.1; -; mRNA.
CCDS; CCDS60511.1; -. [Q9H2F5-2]
CCDS; CCDS7172.1; -. [Q9H2F5-1]
CCDS; CCDS73083.1; -. [Q9H2F5-3]
RefSeq; NP_001258933.1; NM_001272004.1. [Q9H2F5-2]
RefSeq; NP_001258948.1; NM_001272019.2.
RefSeq; NP_001269320.1; NM_001282391.1. [Q9H2F5-3]
RefSeq; NP_079485.1; NM_025209.3. [Q9H2F5-1]
UniGene; Hs.167805; -.
ProteinModelPortal; Q9H2F5; -.
BioGrid; 123227; 37.
CORUM; Q9H2F5; -.
IntAct; Q9H2F5; 16.
STRING; 9606.ENSP00000263062; -.
iPTMnet; Q9H2F5; -.
PhosphoSitePlus; Q9H2F5; -.
SwissPalm; Q9H2F5; -.
DMDM; 59797889; -.
EPD; Q9H2F5; -.
MaxQB; Q9H2F5; -.
PaxDb; Q9H2F5; -.
PeptideAtlas; Q9H2F5; -.
PRIDE; Q9H2F5; -.
Ensembl; ENST00000263062; ENSP00000263062; ENSG00000120616. [Q9H2F5-1]
Ensembl; ENST00000319778; ENSP00000318559; ENSG00000120616. [Q9H2F5-2]
Ensembl; ENST00000375110; ENSP00000364251; ENSG00000120616. [Q9H2F5-3]
GeneID; 80314; -.
KEGG; hsa:80314; -.
UCSC; uc001iwg.3; human. [Q9H2F5-1]
CTD; 80314; -.
DisGeNET; 80314; -.
EuPathDB; HostDB:ENSG00000120616.15; -.
GeneCards; EPC1; -.
HGNC; HGNC:19876; EPC1.
MIM; 610999; gene.
neXtProt; NX_Q9H2F5; -.
OpenTargets; ENSG00000120616; -.
PharmGKB; PA134981141; -.
eggNOG; KOG2261; Eukaryota.
eggNOG; ENOG410XSSX; LUCA.
GeneTree; ENSGT00390000013262; -.
HOVERGEN; HBG051489; -.
InParanoid; Q9H2F5; -.
KO; K11322; -.
OMA; ALSHQVT; -.
OrthoDB; EOG091G0252; -.
PhylomeDB; Q9H2F5; -.
TreeFam; TF106438; -.
Reactome; R-HSA-3214847; HATs acetylate histones.
ChiTaRS; EPC1; human.
GeneWiki; EPC1; -.
GenomeRNAi; 80314; -.
PRO; PR:Q9H2F5; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000120616; -.
Genevisible; Q9H2F5; HS.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:UniProtKB.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; TAS:UniProtKB.
GO; GO:0035886; P:vascular smooth muscle cell differentiation; IEA:Ensembl.
InterPro; IPR024943; Enhancer_polycomb.
InterPro; IPR019542; Enhancer_polycomb-like_N.
InterPro; IPR009607; Enhancer_polycomb_C.
PANTHER; PTHR14898; PTHR14898; 1.
Pfam; PF06752; E_Pc_C; 1.
Pfam; PF10513; EPL1; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Chromatin regulator;
Complete proteome; Direct protein sequencing; Growth regulation;
Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 836 Enhancer of polycomb homolog 1.
/FTId=PRO_0000214153.
MOD_RES 539 539 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 319 319 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 673 673 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 51 MSKLSFRARALDASKPLPVFRCEDLPDLHEYASINRAVPQM
PTGMEKEEES -> M (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.2}.
/FTId=VSP_012875.
VAR_SEQ 621 643 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_012877.
VARIANT 123 123 V -> L. {ECO:0000269|PubMed:25787250}.
/FTId=VAR_074181.
CONFLICT 156 156 S -> G (in Ref. 2; AAK60501).
{ECO:0000305}.
CONFLICT 256 256 K -> R (in Ref. 2; AAK60501).
{ECO:0000305}.
CONFLICT 783 783 A -> V (in Ref. 6; AAH36529).
{ECO:0000305}.
CONFLICT 825 825 N -> S (in Ref. 3; BAC03857).
{ECO:0000305}.
SEQUENCE 836 AA; 93463 MW; E9E89699E73336B5 CRC64;
MSKLSFRARA LDASKPLPVF RCEDLPDLHE YASINRAVPQ MPTGMEKEEE SEHHLQRAIS
AQQVYGEKRD NMVIPVPEAE SNIAYYESIY PGEFKMPKQL IHIQPFSLDA EQPDYDLDSE
DEVFVNKLKK KMDICPLQFE EMIDRLEKGS GQQPVSLQEA KLLLKEDDEL IREVYEYWIK
KRKNCRGPSL IPSVKQEKRD GSSTNDPYVA FRRRTEKMQT RKNRKNDEAS YEKMLKLRRD
LSRAVTILEM IKRREKSKRE LLHLTLEIME KRYNLGDYNG EIMSEVMAQR QPMKPTYAIP
IIPITNSSQF KHQEAMDVKE FKVNKQDKAD LIRPKRKYEK KPKVLPSSAA ATPQQTSPAA
LPVFNAKDLN QYDFPSSDEE PLSQVLSGSS EAEEDNDPDG PFAFRRKAGC QYYAPHLDQT
GNWPWTSPKD GGLGDVRYRY CLTTLTVPQR CIGFARRRVG RGGRVLLDRA HSDYDSVFHH
LDLEMLSSPQ HSPVNQFANT SETNTSDKSF SKDLSQILVN IKSCRWRHFR PRTPSLHDSD
NDELSCRKLY RSINRTGTAQ PGTQTCSTST QSKSSSGSAH FAFTAEQYQQ HQQQLALMQK
QQLAQIQQQQ ANSNSSTNTS QNLASNQQKS GFRLNIQGLE RTLQGFVSKT LDSASAQFAA
SALVTSEQLM GFKMKDDVVL GIGVNGVLPA SGVYKGLHLS STTPTALVHT SPSTAGSALL
QPSNITQTSS SHSALSHQVT AANSATTQVL IGNNIRLTVP SSVATVNSIA PINARHIPRT
LSAVPSSALK LAAAANCQVS KVPSSSSVDS VPRENHESEK PALNNIADNT VAMEVT


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EPC1_MOUSE ELISA Kit FOR Enhancer of polycomb homolog 1; organism: Mouse; gene name: Epc1 96T
EPC2_MOUSE ELISA Kit FOR Enhancer of polycomb homolog 2; organism: Mouse; gene name: Epc2 96T
CSB-EL007715MO Mouse enhancer of polycomb homolog 1 (Drosophila) (EPC1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL007716HU Human enhancer of polycomb homolog 2 (Drosophila) (EPC2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL007715HU Human enhancer of polycomb homolog 1 (Drosophila) (EPC1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL007716MO Mouse enhancer of polycomb homolog 2 (Drosophila) (EPC2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
18-003-42562 Chromobox protein homolog 8 - Polycomb 3 homolog; Pc3; hPc3; Rectachrome 1 Polyclonal 0.05 mg Aff Pur


 

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