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Ubiquitin-conjugating enzyme E2 Q1 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme Q1) (Protein NICE-5) (Ubiquitin carrier protein Q1) (Ubiquitin-protein ligase Q1)

 UB2Q1_HUMAN             Reviewed;         422 AA.
Q7Z7E8; B4DF92; Q29SN7; Q3B841; Q5I0X2; Q6IS04; Q6P7P2; Q96MV4;
Q9BVX5; Q9UGL6;
21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
20-JUN-2018, entry version 139.
RecName: Full=Ubiquitin-conjugating enzyme E2 Q1;
EC=2.3.2.23;
AltName: Full=E2 ubiquitin-conjugating enzyme Q1;
AltName: Full=Protein NICE-5;
AltName: Full=Ubiquitin carrier protein Q1;
AltName: Full=Ubiquitin-protein ligase Q1;
Name=UBE2Q1; Synonyms=NICE5, UBE2Q; ORFNames=PRO3094;
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).
Altmann M.E., Schulze E., Adham I.M., Koehler M., Engel W.;
"Isolation and characterization of the human UBE2Q gene and its murine
ortholog.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Wassler M., Sagar B., Geng Y.-J.;
"Cloning and characterization of galactosyl transferase-associated
protein (GTAP), a human ubiquitin-conjugating enzyme that regulate
stem cell adhesion, growth and differentiation.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 204-422.
TISSUE=Cerebellum;
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=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[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), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 163-422 (ISOFORM 1).
TISSUE=Cervix, and Uterus;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 282-422, AND TISSUE SPECIFICITY.
TISSUE=Keratinocyte;
PubMed=11230159; DOI=10.1101/gr.114801;
Marenholz I., Zirra M., Fischer D.F., Backendorf C., Ziegler A.,
Mischke D.;
"Identification of human epidermal differentiation complex (EDC)-
encoded genes by subtractive hybridization of entire YACs to a gridded
keratinocyte cDNA library.";
Genome Res. 11:341-355(2001).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 312-386.
TISSUE=Fetal liver;
Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
Liu M., He F.;
"Functional prediction of the coding sequences of 121 new genes
deduced by analysis of cDNA clones from human fetal liver.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 352-422.
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND 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).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[13] {ECO:0000244|PDB:2QGX}
X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 247-414, AND
AUTOUBIQUITINATION.
PubMed=22496338; DOI=10.1074/mcp.O111.013706;
Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J.,
Avvakumov G.V., Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K.,
Arrowsmith C.H., Raught B., Dhe-Paganon S.;
"A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
function screen.";
Mol. Cell. Proteomics 11:329-341(2012).
-!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
proteins (PubMed:22496338). May be involved in hormonal
homeostasis in females. Involved in regulation of B4GALT1 cell
surface expression, B4GALT1-mediated cell adhesion to laminin and
embryoid body formation (By similarity).
{ECO:0000250|UniProtKB:Q7TSS2, ECO:0000269|PubMed:22496338}.
-!- 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}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: Monomer and homodimer. Only the homodimer is linked to
ubiquitin through thiolester activation. Interacts (via N-
terminus) with B4GALT1 (via N-terminal cytoplasmic domain). The
interaction is direct. {ECO:0000250|UniProtKB:Q7TSS2}.
-!- INTERACTION:
Q13643:FHL3; NbExp=3; IntAct=EBI-10258181, EBI-741101;
Q9UNE7:STUB1; NbExp=3; IntAct=EBI-1783287, EBI-357085;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7TSS2}. Cell
projection, filopodium {ECO:0000250|UniProtKB:Q7TSS2}. Cytoplasm,
cytosol {ECO:0000250|UniProtKB:Q7TSS2}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q7Z7E8-1; Sequence=Displayed;
Name=2;
IsoId=Q7Z7E8-2; Sequence=VSP_017296;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:11230159}.
-!- PTM: Autoubiquitinated in vitro in the presence of NEDD4L.
{ECO:0000269|PubMed:22496338}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SEQUENCE CAUTION:
Sequence=AAF71141.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH61583.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH87836.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAI07058.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB71173.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAB65097.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AY112698; AAM60814.1; -; mRNA.
EMBL; AY948200; AAY23342.1; -; mRNA.
EMBL; AK056388; BAB71173.1; ALT_INIT; mRNA.
EMBL; AK293986; BAG57353.1; -; mRNA.
EMBL; AL592078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53193.1; -; Genomic_DNA.
EMBL; BC000848; AAH00848.1; -; mRNA.
EMBL; BC015316; AAH15316.2; -; mRNA.
EMBL; BC061583; AAH61583.1; ALT_INIT; mRNA.
EMBL; BC070158; AAH70158.1; -; mRNA.
EMBL; BC087836; AAH87836.1; ALT_INIT; mRNA.
EMBL; BC107057; AAI07058.1; ALT_INIT; mRNA.
EMBL; AJ243666; CAB65097.1; ALT_INIT; mRNA.
EMBL; AF116721; AAF71141.1; ALT_INIT; mRNA.
EMBL; CR457219; CAG33500.1; -; mRNA.
CCDS; CCDS1069.1; -. [Q7Z7E8-1]
RefSeq; NP_060052.3; NM_017582.6. [Q7Z7E8-1]
UniGene; Hs.607928; -.
PDB; 2QGX; X-ray; 2.56 A; A/B/C/D=247-414.
PDBsum; 2QGX; -.
ProteinModelPortal; Q7Z7E8; -.
SMR; Q7Z7E8; -.
BioGrid; 120732; 24.
IntAct; Q7Z7E8; 8.
MINT; Q7Z7E8; -.
STRING; 9606.ENSP00000292211; -.
iPTMnet; Q7Z7E8; -.
PhosphoSitePlus; Q7Z7E8; -.
BioMuta; UBE2Q1; -.
DMDM; 74750234; -.
EPD; Q7Z7E8; -.
MaxQB; Q7Z7E8; -.
PaxDb; Q7Z7E8; -.
PeptideAtlas; Q7Z7E8; -.
PRIDE; Q7Z7E8; -.
ProteomicsDB; 69523; -.
ProteomicsDB; 69524; -. [Q7Z7E8-2]
DNASU; 55585; -.
Ensembl; ENST00000292211; ENSP00000292211; ENSG00000160714. [Q7Z7E8-1]
GeneID; 55585; -.
KEGG; hsa:55585; -.
UCSC; uc001fff.2; human. [Q7Z7E8-1]
CTD; 55585; -.
EuPathDB; HostDB:ENSG00000160714.9; -.
GeneCards; UBE2Q1; -.
H-InvDB; HIX0001106; -.
HGNC; HGNC:15698; UBE2Q1.
HPA; HPA063368; -.
MIM; 617429; gene.
neXtProt; NX_Q7Z7E8; -.
OpenTargets; ENSG00000160714; -.
PharmGKB; PA38029; -.
eggNOG; KOG0897; Eukaryota.
eggNOG; ENOG410XRET; LUCA.
GeneTree; ENSGT00390000018573; -.
HOVERGEN; HBG061368; -.
InParanoid; Q7Z7E8; -.
KO; K10582; -.
OMA; DSPLHND; -.
OrthoDB; EOG091G0LGG; -.
PhylomeDB; Q7Z7E8; -.
TreeFam; TF313338; -.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q7Z7E8; -.
UniPathway; UPA00143; -.
ChiTaRS; UBE2Q1; human.
EvolutionaryTrace; Q7Z7E8; -.
GenomeRNAi; 55585; -.
PRO; PR:Q7Z7E8; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000160714; -.
CleanEx; HS_UBE2Q1; -.
Genevisible; Q7Z7E8; HS.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:Ensembl.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0009566; P:fertilization; IEA:Ensembl.
GO; GO:0007617; P:mating behavior; IEA:Ensembl.
GO; GO:0070459; P:prolactin secretion; IEA:Ensembl.
GO; GO:0061458; P:reproductive system development; IEA:Ensembl.
GO; GO:0001967; P:suckling behavior; IEA:Ensembl.
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; 2.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Cell projection; Complete proteome; Cytoplasm; Nucleotide-binding;
Nucleus; Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 422 Ubiquitin-conjugating enzyme E2 Q1.
/FTId=PRO_0000223876.
COMPBIAS 8 38 Gly-rich.
ACT_SITE 351 351 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
VAR_SEQ 1 169 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_017296.
CONFLICT 287 287 N -> Y (in Ref. 7; CAB65097).
{ECO:0000305}.
HELIX 250 264 {ECO:0000244|PDB:2QGX}.
HELIX 267 270 {ECO:0000244|PDB:2QGX}.
STRAND 273 278 {ECO:0000244|PDB:2QGX}.
HELIX 279 281 {ECO:0000244|PDB:2QGX}.
STRAND 285 291 {ECO:0000244|PDB:2QGX}.
HELIX 298 309 {ECO:0000244|PDB:2QGX}.
STRAND 315 320 {ECO:0000244|PDB:2QGX}.
TURN 325 327 {ECO:0000244|PDB:2QGX}.
STRAND 331 337 {ECO:0000244|PDB:2QGX}.
STRAND 339 341 {ECO:0000244|PDB:2QGX}.
STRAND 348 350 {ECO:0000244|PDB:2QGX}.
TURN 357 359 {ECO:0000244|PDB:2QGX}.
HELIX 366 379 {ECO:0000244|PDB:2QGX}.
STRAND 386 388 {ECO:0000244|PDB:2QGX}.
HELIX 390 392 {ECO:0000244|PDB:2QGX}.
HELIX 395 405 {ECO:0000244|PDB:2QGX}.
SEQUENCE 422 AA; 46127 MW; 106FF7E59DF65555 CRC64;
MQQPQPQGQQ QPGPGQQLGG QGAAPGAGGG PGGGPGPGPC LRRELKLLES IFHRGHERFR
IASACLDELS CEFLLAGAGG AGAGAAPGPH LPPRGSVPGD PVRIHCNITE SYPAVPPIWS
VESDDPNLAA VLERLVDIKK GNTLLLQHLK RIISDLCKLY NLPQHPDVEM LDQPLPAEQC
TQEDVSSEDE DEEMPEDTED LDHYEMKEEE PAEGKKSEDD GIGKENLAIL EKIKKNQRQD
YLNGAVSGSV QATDRLMKEL RDIYRSQSFK GGNYAVELVN DSLYDWNVKL LKVDQDSALH
NDLQILKEKE GADFILLNFS FKDNFPFDPP FVRVVSPVLS GGYVLGGGAI CMELLTKQGW
SSAYSIESVI MQISATLVKG KARVQFGANK SQYSLTRAQQ SYKSLVQIHE KNGWYTPPKE
DG


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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
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
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
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
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
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
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
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
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
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
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
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
EIAAB44818 Homo sapiens,Human,NICE5,PRO3094,Protein NICE-5,UBE2Q,UBE2Q1,Ubiquitin carrier protein Q1,Ubiquitin-conjugating enzyme E2 Q1,Ubiquitin-protein ligase Q1
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
EIAAB44899 Bendless-like ubiquitin-conjugating enzyme,Blu,Mouse,Mus musculus,Ubc13,Ube2n,Ubiquitin carrier protein N,Ubiquitin-conjugating enzyme E2 N,Ubiquitin-protein ligase N
EIAAB44891 Homo sapiens,Human,UbcH2,UBE2H,Ubiquitin carrier protein H,Ubiquitin-conjugating enzyme E2 H,Ubiquitin-conjugating enzyme E2-20K,Ubiquitin-protein ligase H


 

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