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Ubiquitin-conjugating enzyme E2 B (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme B) (RAD6 homolog B) (HR6B) (hHR6B) (Ubiquitin carrier protein B) (Ubiquitin-conjugating enzyme E2-17 kDa) (Ubiquitin-protein ligase B)

 UBE2B_HUMAN             Reviewed;         152 AA.
P63146; B2R503; D3DQA2; P23567; Q4PJ15; Q9D0J6;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
27-SEP-2004, sequence version 1.
10-OCT-2018, entry version 149.
RecName: Full=Ubiquitin-conjugating enzyme E2 B;
EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
AltName: Full=E2 ubiquitin-conjugating enzyme B;
AltName: Full=RAD6 homolog B;
Short=HR6B;
Short=hHR6B;
AltName: Full=Ubiquitin carrier protein B;
AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa;
AltName: Full=Ubiquitin-protein ligase B;
Name=UBE2B; Synonyms=RAD6B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Placenta;
PubMed=2158443;
Schneider R., Eckerskorn C., Lottspeich F., Schweiger M.;
"The human ubiquitin carrier protein E2(Mr = 17,000) is homologous to
the yeast DNA repair gene RAD6.";
EMBO J. 9:1431-1435(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=1883845; DOI=10.1016/0167-4781(91)90039-O;
Woffendin C., Chen Z.Y., Staskus K., Retzel E.F., Plagemann P.G.;
"Mammalian mRNAs encoding protein closely related to ubiquitin-
conjugating enzyme encoded by yeast DNA repair gene RAD6.";
Biochim. Biophys. Acta 1090:81-85(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=1717990; DOI=10.1073/pnas.88.20.8865;
Koken M.H.M., Reynolds P., Jaspers-Dekker I., Prakash L., Prakash S.,
Bootsma D., Hoeijmakers J.H.J.;
"Structural and functional conservation of two human homologs of the
yeast DNA repair gene RAD6.";
Proc. Natl. Acad. Sci. U.S.A. 88:8865-8869(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[8]
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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow, and Brain;
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).
[10]
INTERACTION WITH RAD18.
PubMed=10908344; DOI=10.1093/nar/28.14.2847;
Xin H., Lin W., Sumanasekera W., Zhang Y., Wu X., Wang Z.;
"The human RAD18 gene product interacts with HHR6A and HHR6B.";
Nucleic Acids Res. 28:2847-2854(2000).
[11]
FUNCTION.
PubMed=16337599; DOI=10.1016/j.molcel.2005.11.012;
Kim J., Hake S.B., Roeder R.G.;
"The human homolog of yeast BRE1 functions as a transcriptional
coactivator through direct activator interactions.";
Mol. Cell 20:759-770(2005).
[12]
FUNCTION.
PubMed=17130289; DOI=10.1083/jcb.200606145;
Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.;
"Human SHPRH suppresses genomic instability through proliferating cell
nuclear antigen polyubiquitination.";
J. Cell Biol. 175:703-708(2006).
[13]
FUNCTION.
PubMed=17108083; DOI=10.1073/pnas.0608595103;
Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V.,
Hurwitz J., Prakash L., Prakash S., Haracska L.;
"Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent
polyubiquitylation of proliferating cell nuclear antigen.";
Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006).
[14]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=20061386; DOI=10.1074/jbc.M109.089003;
David Y., Ziv T., Admon A., Navon A.;
"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
preferred lysines.";
J. Biol. Chem. 285:8595-8604(2010).
[15]
INTERACTION WITH WAC.
PubMed=21329877; DOI=10.1016/j.molcel.2011.01.024;
Zhang F., Yu X.;
"WAC, a functional partner of RNF20/40, regulates histone H2B
ubiquitination and gene transcription.";
Mol. Cell 41:384-397(2011).
[16]
STRUCTURE BY NMR.
PubMed=11885984; DOI=10.1023/A:1013807519703;
Miura T., Klaus W., Ross A., Guntert P., Senn H.;
"The NMR structure of the class I human ubiquitin-conjugating enzyme
2b.";
J. Biomol. NMR 22:89-92(2002).
-!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
covalent attachment to other proteins. In association with the E3
enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription
regulation by catalyzing the monoubiquitination of histone H2B at
'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for
epigenetic transcriptional activation, elongation by RNA
polymerase II, telomeric silencing, and is also a prerequisite for
H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11'-, as
well as 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Required
for postreplication repair of UV-damaged DNA. Associates to the E3
ligase RAD18 to form the UBE2B-RAD18 ubiquitin ligase complex
involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-
164'. May be involved in neurite outgrowth.
{ECO:0000269|PubMed:16337599, ECO:0000269|PubMed:17108083,
ECO:0000269|PubMed:17130289, ECO:0000269|PubMed:1717990,
ECO:0000269|PubMed:20061386}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133,
ECO:0000269|PubMed:20061386}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: Interacts with RAD18, UBR2 and WAC.
{ECO:0000269|PubMed:10908344, ECO:0000269|PubMed:21329877}.
-!- INTERACTION:
Q7L7L0:HIST3H2A; NbExp=2; IntAct=EBI-712629, EBI-5325551;
Q9NS91:RAD18; NbExp=5; IntAct=EBI-712629, EBI-2339393;
Q8IWV7:UBR1; NbExp=2; IntAct=EBI-712629, EBI-711736;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P63149}. Nucleus
{ECO:0000250|UniProtKB:P63149}. Note=In peripheral neurons,
expressed both at the plasma membrane and in nuclei.
{ECO:0000250|UniProtKB:P63149}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ube2b/";
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EMBL; M74525; AAA35982.1; -; mRNA.
EMBL; X53251; CAA37339.1; -; mRNA.
EMBL; BT007071; AAP35734.1; -; mRNA.
EMBL; CR407634; CAG28562.1; -; mRNA.
EMBL; DQ090910; AAY68224.1; -; Genomic_DNA.
EMBL; AK312012; BAG34950.1; -; mRNA.
EMBL; CH471062; EAW62257.1; -; Genomic_DNA.
EMBL; CH471062; EAW62258.1; -; Genomic_DNA.
EMBL; BC005979; AAH05979.1; -; mRNA.
EMBL; BC008404; AAH08404.1; -; mRNA.
EMBL; BC008470; AAH08470.1; -; mRNA.
CCDS; CCDS4174.1; -.
PIR; B41222; B41222.
RefSeq; NP_003328.1; NM_003337.3.
UniGene; Hs.612096; -.
UniGene; Hs.730071; -.
PDB; 1JAS; NMR; -; A=1-152.
PDB; 1NXA; Model; -; A=1-152.
PDB; 2Y4W; NMR; -; A=1-152.
PDB; 2YB6; X-ray; 1.50 A; A=1-152.
PDB; 2YBF; X-ray; 2.00 A; A=1-152.
PDBsum; 1JAS; -.
PDBsum; 1NXA; -.
PDBsum; 2Y4W; -.
PDBsum; 2YB6; -.
PDBsum; 2YBF; -.
ProteinModelPortal; P63146; -.
SMR; P63146; -.
BioGrid; 113168; 77.
DIP; DIP-29832N; -.
IntAct; P63146; 21.
MINT; P63146; -.
STRING; 9606.ENSP00000265339; -.
ChEMBL; CHEMBL3784907; -.
iPTMnet; P63146; -.
PhosphoSitePlus; P63146; -.
BioMuta; UBE2B; -.
DMDM; 52783814; -.
EPD; P63146; -.
MaxQB; P63146; -.
PaxDb; P63146; -.
PeptideAtlas; P63146; -.
PRIDE; P63146; -.
ProteomicsDB; 57496; -.
TopDownProteomics; P63146; -.
DNASU; 7320; -.
Ensembl; ENST00000265339; ENSP00000265339; ENSG00000119048.
GeneID; 7320; -.
KEGG; hsa:7320; -.
UCSC; uc003kzh.4; human.
CTD; 7320; -.
DisGeNET; 7320; -.
EuPathDB; HostDB:ENSG00000119048.7; -.
GeneCards; UBE2B; -.
HGNC; HGNC:12473; UBE2B.
HPA; HPA003875; -.
HPA; HPA051765; -.
HPA; HPA065898; -.
MIM; 179095; gene.
neXtProt; NX_P63146; -.
OpenTargets; ENSG00000119048; -.
PharmGKB; PA37123; -.
eggNOG; KOG0419; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00900000140930; -.
HOGENOM; HOG000233454; -.
HOVERGEN; HBG063308; -.
InParanoid; P63146; -.
KO; K10574; -.
OMA; CHAIING; -.
OrthoDB; EOG091G0UM8; -.
PhylomeDB; P63146; -.
TreeFam; TF101128; -.
BRENDA; 2.3.2.B6; 2681.
Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; P63146; -.
UniPathway; UPA00143; -.
ChiTaRS; UBE2B; human.
EvolutionaryTrace; P63146; -.
GeneWiki; UBE2B; -.
GenomeRNAi; 7320; -.
PRO; PR:P63146; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000119048; Expressed in 230 organ(s), highest expression level in caudate nucleus.
CleanEx; HS_UBE2B; -.
ExpressionAtlas; P63146; baseline and differential.
Genevisible; P63146; HS.
GO; GO:0000785; C:chromatin; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0033503; C:HULC complex; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005657; C:replication fork; IDA:UniProtKB.
GO; GO:0001741; C:XY body; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:Ensembl.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0051026; P:chiasma assembly; IEA:Ensembl.
GO; GO:0042769; P:DNA damage response, detection of DNA damage; TAS:Reactome.
GO; GO:0006281; P:DNA repair; IGI:UniProtKB.
GO; GO:0033522; P:histone H2A ubiquitination; IMP:UniProtKB.
GO; GO:0070076; P:histone lysine demethylation; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0006344; P:maintenance of chromatin silencing; IEA:Ensembl.
GO; GO:0045141; P:meiotic telomere clustering; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:0033128; P:negative regulation of histone phosphorylation; IEA:Ensembl.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0010845; P:positive regulation of reciprocal meiotic recombination; IEA:Ensembl.
GO; GO:0006301; P:postreplication repair; IDA:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; IMP:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IMP:UniProtKB.
GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IDA:UniProtKB.
GO; GO:0009411; P:response to UV; IGI:UniProtKB.
GO; GO:0007288; P:sperm axoneme assembly; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; TAS:UniProtKB.
GO; GO:0070193; P:synaptonemal complex organization; IEA:Ensembl.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell membrane; Complete proteome;
Direct protein sequencing; DNA damage; DNA repair; Membrane;
Nucleotide-binding; Nucleus; Reference proteome; Transferase;
Ubl conjugation pathway.
CHAIN 1 152 Ubiquitin-conjugating enzyme E2 B.
/FTId=PRO_0000082447.
ACT_SITE 88 88 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000255|PROSITE-ProRule:PRU10133}.
CONFLICT 22 23 VG -> C (in Ref. 2). {ECO:0000305}.
CONFLICT 41 41 F -> I (in Ref. 2). {ECO:0000305}.
CONFLICT 54 54 K -> R (in Ref. 2). {ECO:0000305}.
HELIX 4 18 {ECO:0000244|PDB:2YB6}.
STRAND 24 29 {ECO:0000244|PDB:2YB6}.
STRAND 32 41 {ECO:0000244|PDB:2YB6}.
TURN 47 50 {ECO:0000244|PDB:2YB6}.
STRAND 52 58 {ECO:0000244|PDB:2YB6}.
TURN 61 65 {ECO:0000244|PDB:2YB6}.
STRAND 69 74 {ECO:0000244|PDB:2YB6}.
STRAND 85 87 {ECO:0000244|PDB:2YBF}.
HELIX 90 92 {ECO:0000244|PDB:2YB6}.
TURN 93 95 {ECO:0000244|PDB:2YB6}.
HELIX 102 113 {ECO:0000244|PDB:2YB6}.
HELIX 124 132 {ECO:0000244|PDB:2YB6}.
HELIX 134 147 {ECO:0000244|PDB:2YB6}.
SEQUENCE 152 AA; 17312 MW; CFDEEEE7E06840BE CRC64;
MSTPARRRLM RDFKRLQEDP PVGVSGAPSE NNIMQWNAVI FGPEGTPFED GTFKLVIEFS
EEYPNKPPTV RFLSKMFHPN VYADGSICLD ILQNRWSPTY DVSSILTSIQ SLLDEPNPNS
PANSQAAQLY QENKREYEKR VSAIVEQSWN DS


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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
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
U1063m CLIA E214K,HR6B,mHR6B,Mouse,Mus musculus,RAD6 homolog B,Rad6b,Ube2b,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-protein ligase B 96T
E1063m ELISA kit E214K,HR6B,mHR6B,Mouse,Mus musculus,RAD6 homolog B,Rad6b,Ube2b,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-protein ligase B 96T
E1063m ELISA E214K,HR6B,mHR6B,Mouse,Mus musculus,RAD6 homolog B,Rad6b,Ube2b,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-protein ligase B 96T
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
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
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
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
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
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-


 

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