Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

(E3-independent) E2 ubiquitin-conjugating enzyme UBE2O (EC 2.3.2.24) (E2/E3 hybrid ubiquitin-protein ligase UBE2O) (Ubiquitin carrier protein O) (Ubiquitin-conjugating enzyme E2 O) (Ubiquitin-conjugating enzyme E2 of 230 kDa) (Ubiquitin-conjugating enzyme E2-230K) (Ubiquitin-protein ligase O)

 UBE2O_MOUSE             Reviewed;        1288 AA.
Q6ZPJ3; A2A7X3; Q60800; Q6PCR9; Q7TPN2; Q8BLE8;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
28-MAR-2018, entry version 119.
RecName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme UBE2O;
EC=2.3.2.24;
AltName: Full=E2/E3 hybrid ubiquitin-protein ligase UBE2O;
AltName: Full=Ubiquitin carrier protein O;
AltName: Full=Ubiquitin-conjugating enzyme E2 O;
AltName: Full=Ubiquitin-conjugating enzyme E2 of 230 kDa;
Short=Ubiquitin-conjugating enzyme E2-230K;
AltName: Full=Ubiquitin-protein ligase O;
Name=Ube2o; Synonyms=Kiaa1734;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 103-628, TISSUE SPECIFICITY, AND
INDUCTION.
TISSUE=Reticulocyte;
PubMed=7761435; DOI=10.1073/pnas.92.11.4982;
Wefes I., Mastrandrea L.D., Haldeman M., Koury S.T., Tamburlin J.,
Pickart C.M., Finley D.;
"Induction of ubiquitin-conjugating enzymes during terminal erythroid
differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 92:4982-4986(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-1288.
STRAIN=FVB/N; TISSUE=Liver;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 867-1288.
STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
ENZYME REGULATION.
PubMed=8634298; DOI=10.1021/bi952105y;
Berleth E.S., Pickart C.M.;
"Mechanism of ubiquitin conjugating enzyme E2-230K: catalysis
involving a thiol relay?";
Biochemistry 35:1664-1671(1996).
[7]
INTERACTION WITH CPNE1 AND CPNE4.
PubMed=12522145; DOI=10.1074/jbc.M212632200;
Tomsig J.L., Snyder S.L., Creutz C.E.;
"Identification of targets for calcium signaling through the copine
family of proteins. Characterization of a coiled-coil copine-binding
motif.";
J. Biol. Chem. 278:10048-10054(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84; SER-833 AND
SER-836, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84; SER-394;
SER-436; SER-833; THR-835 AND SER-836, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: E2/E3 hybrid ubiquitin-protein ligase that displays both
E2 and E3 ligase activities and mediates monoubiquitination of
target proteins. Negatively regulates TRAF6-mediated NF-kappa-B
activation independently of its E2 activity. Acts as a positive
regulator of BMP7 signaling by mediating monoubiquitination of
SMAD6, thereby regulating adipogenesis. Mediates
monoubiquitination at different sites of the nuclear localization
signal (NLS) of BAP1, leading to cytoplasmic retention of BAP1.
Also able to monoubiquitinate the NLS of other chromatin-
associated proteins, such as INO80 and CXXC1, affecting their
subcellular location. Acts as a regulator of retrograde transport
by assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to
mediate 'Lys-63'-linked ubiquitination of WASHC1, leading to
promote endosomal F-actin assembly.
{ECO:0000250|UniProtKB:Q9C0C9}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-
activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000250|UniProtKB:Q9C0C9,
ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- ENZYME REGULATION: Inhibited by inorganic arsenite such as
phenylarsenoxides. {ECO:0000269|PubMed:8634298}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: Interacts with CPNE1 (via VWFA domain) and CPNE4 (via
VWFA domain) (PubMed:12522145). {ECO:0000269|PubMed:12522145}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C0C9}.
Nucleus {ECO:0000250|UniProtKB:Q9C0C9}. Note=Mainly localizes to
the cytoplasm. {ECO:0000250|UniProtKB:Q9C0C9}.
-!- TISSUE SPECIFICITY: Highly expressed in reticulocytes.
{ECO:0000269|PubMed:7761435}.
-!- INDUCTION: By EPO/Erythropoietin which induces erythroid
differentiation. {ECO:0000269|PubMed:7761435}.
-!- PTM: Phosphorylated. Phosphorylation affects subcellular location.
{ECO:0000250|UniProtKB:Q9C0C9}.
-!- PTM: Ubiquitinated: autoubiquitinates, possibly affecting its
subcellular location. {ECO:0000250|UniProtKB:Q9C0C9}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SEQUENCE CAUTION:
Sequence=AAA69916.1; Type=Frameshift; Positions=344, 367, 374, 411; Evidence={ECO:0000305};
Sequence=AAH59193.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC32345.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC98241.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK129431; BAC98241.1; ALT_INIT; mRNA.
EMBL; AL645851; CAM17106.1; -; Genomic_DNA.
EMBL; AL607039; CAM17106.1; JOINED; Genomic_DNA.
EMBL; AL607039; CAM20507.1; -; Genomic_DNA.
EMBL; AL645851; CAM20507.1; JOINED; Genomic_DNA.
EMBL; U20780; AAA69916.1; ALT_FRAME; mRNA.
EMBL; BC059193; AAH59193.1; ALT_INIT; mRNA.
EMBL; AK045398; BAC32345.1; ALT_INIT; mRNA.
CCDS; CCDS25670.1; -.
PIR; I49264; I49264.
RefSeq; NP_776116.2; NM_173755.3.
UniGene; Mm.243950; -.
ProteinModelPortal; Q6ZPJ3; -.
SMR; Q6ZPJ3; -.
BioGrid; 229895; 7.
IntAct; Q6ZPJ3; 5.
MINT; Q6ZPJ3; -.
STRING; 10090.ENSMUSP00000080791; -.
iPTMnet; Q6ZPJ3; -.
PhosphoSitePlus; Q6ZPJ3; -.
EPD; Q6ZPJ3; -.
MaxQB; Q6ZPJ3; -.
PaxDb; Q6ZPJ3; -.
PeptideAtlas; Q6ZPJ3; -.
PRIDE; Q6ZPJ3; -.
Ensembl; ENSMUST00000082152; ENSMUSP00000080791; ENSMUSG00000020802.
GeneID; 217342; -.
KEGG; mmu:217342; -.
UCSC; uc007mlm.1; mouse.
CTD; 63893; -.
MGI; MGI:2444266; Ube2o.
eggNOG; KOG0895; Eukaryota.
eggNOG; ENOG410XQ7W; LUCA.
GeneTree; ENSGT00730000110680; -.
HOGENOM; HOG000231096; -.
HOVERGEN; HBG080116; -.
InParanoid; Q6ZPJ3; -.
KO; K10581; -.
OMA; ERWTSKS; -.
OrthoDB; EOG091G04SX; -.
TreeFam; TF325556; -.
UniPathway; UPA00143; -.
ChiTaRS; Ube2o; mouse.
PRO; PR:Q6ZPJ3; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020802; -.
CleanEx; MM_UBE2O; -.
Genevisible; Q6ZPJ3; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
ATP-binding; Coiled coil; Complete proteome; Cytoplasm;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Transferase; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 1288 (E3-independent) E2 ubiquitin-conjugating
enzyme UBE2O.
/FTId=PRO_0000280638.
COILED 809 879 {ECO:0000255}.
COMPBIAS 2 38 Ala-rich.
ACT_SITE 1037 1037 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000250|UniProtKB:Q9C0C9}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 84 84 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 436 436 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 483 483 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9C0C9}.
MOD_RES 486 486 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9C0C9}.
MOD_RES 510 510 Phosphoserine.
{ECO:0000250|UniProtKB:Q9C0C9}.
MOD_RES 833 833 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 835 835 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 836 836 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 893 893 Phosphoserine.
{ECO:0000250|UniProtKB:Q9C0C9}.
CONFLICT 309 309 C -> S (in Ref. 3; AAA69916).
{ECO:0000305}.
CONFLICT 317 319 SPP -> CPR (in Ref. 3; AAA69916).
{ECO:0000305}.
CONFLICT 343 343 Q -> H (in Ref. 3; AAA69916).
{ECO:0000305}.
CONFLICT 871 871 A -> G (in Ref. 4; BAC32345).
{ECO:0000305}.
CONFLICT 1160 1160 L -> P (in Ref. 1; BAC98241 and 4;
AAH59193). {ECO:0000305}.
SEQUENCE 1288 AA; 140834 MW; D2BCE5F36A687CE1 CRC64;
MADPAAPAPA QAQAAAAPTP AAAPAAAAPP PAPATDSASG PSSDSGPEAG SQRLLFSHDL
VSGRYRGSVH FGLVRLIHGE DSDSEGDDDG RGSSGCSEAG GAGHEEGRAS PLRRGYVRVQ
WYPEGVKQHV KETKLKLEDR SVVPRDVVRH MRSTDSQCGT VIDVNIDCAV KLIGTNCIIY
PVNSKDLQHI WPFMYGDYIA YDCWLGKVYD LKNQIILKLS NGARCSMNTE DGAKLYDVCP
HVSDSGLFFD DSYGFYPGQV LIGPAKIFSS VQWLSGVKPV LSTKSKFRVV VEEVQVVELK
VTWITKSFCP GGTDSVSPPP SIITQENLGR VKRLGCFDHA QRQLGERCLY VFPAKVEPAK
IAWECPEKNC AQGEGSMAKK VKRLLKKQVV RIMSCTPDTQ CPRDHSMEDP DKKGEARAGS
EIGSASPEEQ PDGSASPVEM QDEGSEELQE TCEPLPPFLL KEGGDDGLHS AEQDADDEAA
DDTDDTSSVT SSASSTTSSQ SGSGTGRKKS IPLSIKNLKR KHKRKKNKVT RDFKPGDRVA
VEVVTTMTSA DVMWQDGSVE CNIRSNDLFP VHHLDNNEFC PGDFVVDKRV QSCPDPAVYG
VVQSGDHVGR TCMVKWFKLR PSGDDVELIG EEEDVSVYDI ADHPDFRFRT TDIVIRIGNT
EDGALPKEDE PSVGQVARVD VSSKVEVVWA DNSKTIILPQ HLYNIESEIE ESDYDSVEGS
SSGASSDEWE DDSDSWETDN GLVDDEHPKI EELAAILPAE QPTAPEEDKG VVISEEAATA
AIQGAVAMAA PVAGLMEKAG KDGPPKSFRE LKEAIKILES LKNMTVEQLL TGSPTSPTVE
PEKPTREKKF LDDIKKLQEN LKKTLDNVAI AEEEKMEAVP DTERKEEKPE VQSPVKAEWP
SETPVLCQQC GGRPGVTFTS AKGEVFSVLE FAPSNHSFKK IEFQPPEAKK FFSTVRKEMA
LLATSLPDGI MVKTFEDRMD LFSALIKGPT RTPYEDGLYL FDIQLPNIYP AVPPHFCYLS
QCSGRLNPNL YDNGKVCVSL LGTWIGKGTE RWTSKSSLLQ VLISIQGLIL VNEPYYNEAG
FDSDRGLQEG YENSRCYNEM ALIRVVQSMT QLVRRPPEVF EQEIRQHFSV GGWRLVNRIE
SWLETHAMQE RAQVMPNGAL KDSSSLEPMA AAELSDSGRE EPEDVGMAPG EASQGSDSEG
GAQGPASASR DHTEQTETAP DASAPPSVRP KRRRKSYRSF LPEKSGYPDI GFPLFPLSKG
FIKSIRGVLT QFRAALLEAG MPESTEDK


Related products :

Catalog number Product name Quantity
EIAAB44901 Homo sapiens,Human,KIAA1734,UBE2O,Ubiquitin carrier protein O,Ubiquitin-conjugating enzyme E2 O,Ubiquitin-conjugating enzyme E2 of 230 kDa,Ubiquitin-conjugating enzyme E2-230K,Ubiquitin-protein ligase
EIAAB44902 Kiaa1734,Mouse,Mus musculus,Ube2o,Ubiquitin carrier protein O,Ubiquitin-conjugating enzyme E2 O,Ubiquitin-conjugating enzyme E2 of 230 kDa,Ubiquitin-conjugating enzyme E2-230K,Ubiquitin-protein ligase
EIAAB44905 E2epf,Mouse,Mus musculus,Ube2s,Ubiquitin carrier protein S,Ubiquitin-conjugating enzyme E2 S,Ubiquitin-conjugating enzyme E2-24 kDa,Ubiquitin-conjugating enzyme E2-EPF5,Ubiquitin-protein ligase S
EIAAB44789 Homo sapiens,Human,UBC5C,UBCH5C,UBE2D3,Ubiquitin carrier protein D3,Ubiquitin-conjugating enzyme E2 D3,Ubiquitin-conjugating enzyme E2(17)KB 3,Ubiquitin-conjugating enzyme E2-17 kDa 3,Ubiquitin-protei
EIAAB44903 E2EPF,E2-EPF,Homo sapiens,Human,OK_SW-cl.73,UBE2S,Ubiquitin carrier protein S,Ubiquitin-conjugating enzyme E2 S,Ubiquitin-conjugating enzyme E2-24 kDa,Ubiquitin-conjugating enzyme E2-EPF5,Ubiquitin-pr
EIAAB44779 Rat,Rattus norvegicus,Ube2d1,Ubiquitin carrier protein D1,Ubiquitin-conjugating enzyme E2 D1,Ubiquitin-conjugating enzyme E2(17)KB 1,Ubiquitin-conjugating enzyme E2-17 kDa 1,Ubiquitin-protein ligase D
EIAAB44778 Mouse,Mus musculus,Ube2d1,Ubiquitin carrier protein D1,Ubiquitin-conjugating enzyme E2 D1,Ubiquitin-conjugating enzyme E2(17)KB 1,Ubiquitin-conjugating enzyme E2-17 kDa 1,Ubiquitin-protein ligase D1
EIAAB44788 Mouse,Mus musculus,Ube2d3,Ubiquitin carrier protein D3,Ubiquitin-conjugating enzyme E2 D3,Ubiquitin-conjugating enzyme E2(17)KB 3,Ubiquitin-conjugating enzyme E2-17 kDa 3,Ubiquitin-protein ligase D3
EIAAB44783 Mouse,Mus musculus,Ubc4,Ubch4,Ubch5b,Ube2d2,Ubiquitin carrier protein D2,Ubiquitin-conjugating enzyme E2 D2,Ubiquitin-conjugating enzyme E2(17)KB 2,Ubiquitin-conjugating enzyme E2-17 kDa 2,Ubiquitin-p
EIAAB44784 Homo sapiens,Human,UBC4,UBC5B,UBCH4,UBCH5B,UBE2D2,Ubiquitin carrier protein D2,Ubiquitin-conjugating enzyme E2 D2,Ubiquitin-conjugating enzyme E2(17)KB 2,Ubiquitin-conjugating enzyme E2-17 kDa 2,Ubiqu
EIAAB44752 Rat,Rattus norvegicus,Ube2d2,Ube2d2b,Ubiquitin carrier protein D2B,Ubiquitin-conjugating enzyme E2 D2B,Ubiquitin-conjugating enzyme E2(17)KB 2B,Ubiquitin-conjugating enzyme E2-17 kDa 2B,Ubiquitin-prot
E1063h ELISA kit hHR6B,Homo sapiens,HR6B,Human,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2-17 kDa,Ubiquitin-protein ligase B 96T
E1063h ELISA hHR6B,Homo sapiens,HR6B,Human,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2-17 kDa,Ubiquitin-protein ligase B 96T
U1063h CLIA hHR6B,Homo sapiens,HR6B,Human,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2-17 kDa,Ubiquitin-protein ligase B 96T
U1063Rb CLIA HR6B,Oryctolagus cuniculus,Rabbit,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
E1063Rb ELISA HR6B,Oryctolagus cuniculus,Rabbit,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
E1063Rb ELISA kit HR6B,Oryctolagus cuniculus,Rabbit,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
E1063r ELISA kit HR6B,RAD6 homolog B,Rad6b,Rat,Rattus norvegicus,Ube2b,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
U1063r CLIA HR6B,RAD6 homolog B,Rad6b,Rat,Rattus norvegicus,Ube2b,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
E1063r ELISA HR6B,RAD6 homolog B,Rad6b,Rat,Rattus norvegicus,Ube2b,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
EIAAB44782 Rat,Rattus norvegicus,Ubc4,Ubch4,Ubch5b,Ube2d2,Ubiquitin carrier protein D2,Ubiquitin-conjugating enzyme E2 D2,Ubiquitin-conjugating enzyme E2(17)KB 2,Ubiquitin-conjugating enzyme E2-17 kDa 2,Ubiquiti
EIAAB44898 Bendless-like ubiquitin-conjugating enzyme,BLU,Homo sapiens,Human,Ubc13,UBE2N,Ubiquitin carrier protein N,Ubiquitin-conjugating enzyme E2 N,Ubiquitin-protein ligase N
EIAAB44786 PAPase,Phosphoarginine phosphatase,Rat,Rattus norvegicus,Ube2d3,Ubiquitin carrier protein D3,Ubiquitin-conjugating enzyme E2 D3,Ubiquitin-conjugating enzyme E2(17)KB 3,Ubiquitin-conjugating enzyme E2-
EIAAB44825 CDC34,Homo sapiens,Human,UBCH3,UBE2R1,Ubiquitin-conjugating enzyme E2 R1,Ubiquitin-conjugating enzyme E2-32 kDa complementing,Ubiquitin-conjugating enzyme E2-CDC34,Ubiquitin-protein ligase R1
EIAAB44754 Homo sapiens,Human,Putative ubiquitin-conjugating enzyme E2 D2-like protein,UBE2D2L,UBE2DNL,Ubiquitin carrier protein D2-like,Ubiquitin-conjugating enzyme E2D N-terminal-like,Ubiquitin-protein ligase


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur