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Ubiquitin-conjugating enzyme E2 S (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme S) (E2-EPF) (Ubiquitin carrier protein S) (Ubiquitin-conjugating enzyme E2-24 kDa) (Ubiquitin-conjugating enzyme E2-EPF5) (Ubiquitin-protein ligase S)

 UBE2S_HUMAN             Reviewed;         222 AA.
Q16763; Q9BTC1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
10-OCT-2002, sequence version 2.
20-JUN-2018, entry version 175.
RecName: Full=Ubiquitin-conjugating enzyme E2 S;
EC=2.3.2.23 {ECO:0000269|PubMed:19820702, ECO:0000269|PubMed:19822757, ECO:0000269|PubMed:20061386};
AltName: Full=E2 ubiquitin-conjugating enzyme S;
AltName: Full=E2-EPF;
AltName: Full=Ubiquitin carrier protein S;
AltName: Full=Ubiquitin-conjugating enzyme E2-24 kDa;
AltName: Full=Ubiquitin-conjugating enzyme E2-EPF5;
AltName: Full=Ubiquitin-protein ligase S;
Name=UBE2S; Synonyms=E2EPF; ORFNames=OK/SW-cl.73;
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=Foreskin;
PubMed=1379239;
Liu Z., Diaz L.A., Haas A.L., Giudice G.J.;
"cDNA cloning of a novel human ubiquitin carrier protein. An antigenic
domain specifically recognized by endemic pemphigus foliaceus
autoantibodies is encoded in a secondary reading frame of this human
epidermal transcript.";
J. Biol. Chem. 267:15829-15835(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, and Skin;
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]
FUNCTION, AND INTERACTION WITH VHL.
PubMed=16819549; DOI=10.1038/nm1440;
Jung C.R., Hwang K.S., Yoo J., Cho W.K., Kim J.M., Kim W.H., Im D.S.;
"E2-EPF UCP targets pVHL for degradation and associates with tumor
growth and metastasis.";
Nat. Med. 12:809-816(2006).
[6]
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).
[7]
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).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=19820702; DOI=10.1038/ncb1983;
Garnett M.J., Mansfeld J., Godwin C., Matsusaka T., Wu J., Russell P.,
Pines J., Venkitaraman A.R.;
"UBE2S elongates ubiquitin chains on APC/C substrates to promote
mitotic exit.";
Nat. Cell Biol. 11:1363-1369(2009).
[9]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH CDC20 AND FZR,
UBIQUITINATION, AND MUTAGENESIS OF CYS-95.
PubMed=19822757; DOI=10.1073/pnas.0907887106;
Williamson A., Wickliffe K.E., Mellone B.G., Song L., Karpen G.H.,
Rape M.;
"Identification of a physiological E2 module for the human anaphase-
promoting complex.";
Proc. Natl. Acad. Sci. U.S.A. 106:18213-18218(2009).
[10]
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).
[11]
FUNCTION, AND MUTAGENESIS OF CYS-95.
PubMed=20622874; DOI=10.1038/nsmb.1873;
Bremm A., Freund S.M., Komander D.;
"Lys11-linked ubiquitin chains adopt compact conformations and are
preferentially hydrolyzed by the deubiquitinase Cezanne.";
Nat. Struct. Mol. Biol. 17:939-947(2010).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, 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).
[14]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 1-156.
Structural genomics consortium (SGC);
"Crystal structure of human ubiquitin-conjugating enzyme E2S.";
Submitted (FEB-2009) to the PDB data bank.
[15] {ECO:0000244|PDB:1ZDN}
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 1-156, FUNCTION, 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).
[16] {ECO:0000244|PDB:5L9T}
STRUCTURE BY ELECTRON MICROSCOPY (6.40 ANGSTROMS) IN COMPLEX WITH
APC/C, FUNCTION, INTERACTION WITH ANAPC2 AND ANAPC4, AND MUTAGENESIS
OF LEU-222.
PubMed=27259151; DOI=10.1016/j.cell.2016.05.037;
Brown N.G., VanderLinden R., Watson E.R., Weissmann F., Ordureau A.,
Wu K.P., Zhang W., Yu S., Mercredi P.Y., Harrison J.S., Davidson I.F.,
Qiao R., Lu Y., Dube P., Brunner M.R., Grace C.R., Miller D.J.,
Haselbach D., Jarvis M.A., Yamaguchi M., Yanishevski D., Petzold G.,
Sidhu S.S., Kuhlman B., Kirschner M.W., Harper J.W., Peters J.M.,
Stark H., Schulman B.A.;
"Dual RING E3 architectures regulate multiubiquitination and ubiquitin
chain elongation by APC/C.";
Cell 165:1440-1453(2016).
[17] {ECO:0000244|PDB:5BNB}
X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1-156 IN COMPLEX WITH
UBIQUITIN, AND MUTAGENESIS OF LYS-117.
PubMed=26828794; DOI=10.1371/journal.pone.0147550;
Lorenz S., Bhattacharyya M., Feiler C., Rape M., Kuriyan J.;
"Crystal structure of a Ube2S-ubiquitin conjugate.";
PLoS ONE 11:E0147550-E0147550(2016).
-!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
covalent attachment to other proteins (PubMed:22496338). Catalyzes
'Lys-11'-linked polyubiquitination. Acts as an essential factor of
the anaphase promoting complex/cyclosome (APC/C), a cell cycle-
regulated ubiquitin ligase that controls progression through
mitosis. Acts by specifically elongating 'Lys-11'-linked
polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on
APC/C substrates, enhancing the degradation of APC/C substrates by
the proteasome and promoting mitotic exit (PubMed:19820702,
PubMed:19822757, PubMed:27259151). Also acts by elongating
ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro;
it is however unclear whether UBE2D1/UBCH5 acts as an E2 enzyme
for the APC/C in vivo. Also involved in ubiquitination and
subsequent degradation of VHL, resulting in an accumulation of
HIF1A (PubMed:16819549). In vitro able to promote
polyubiquitination using all 7 ubiquitin Lys residues, except
'Lys-48'-linked polyubiquitination (PubMed:20061386,
PubMed:20622874). {ECO:0000269|PubMed:16819549,
ECO:0000269|PubMed:19820702, ECO:0000269|PubMed:19822757,
ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20622874,
ECO:0000269|PubMed:22496338, ECO:0000269|PubMed:27259151}.
-!- 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:19820702, ECO:0000269|PubMed:19822757,
ECO:0000269|PubMed:20061386}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000269|PubMed:19820702, ECO:0000269|PubMed:19822757}.
-!- SUBUNIT: Component of the APC/C complex, composed of at least 14
distinct subunits that assemble into a complex of at least 19
chains with a combined molecular mass of around 1.2 MDa. Within
this complex, directly interacts with ANAPC2 and ANAPC4
(PubMed:27259151). Interacts with CDC20, FZR1/CDH1 and VHL
(PubMed:16819549, PubMed:19822757). {ECO:0000269|PubMed:16819549,
ECO:0000269|PubMed:19822757, ECO:0000269|PubMed:27259151}.
-!- INTERACTION:
Q9UJX6:ANAPC2; NbExp=4; IntAct=EBI-2339823, EBI-396211;
-!- PTM: Autoubiquitinated by the APC/C complex during G1, leading to
its degradation by the proteasome. {ECO:0000269|PubMed:19822757}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
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EMBL; M91670; AAA58446.1; -; mRNA.
EMBL; AB062397; BAB93484.1; -; mRNA.
EMBL; AC020922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004236; AAH04236.1; -; mRNA.
EMBL; BC007554; AAH07554.1; -; mRNA.
EMBL; BC065364; AAH65364.1; -; mRNA.
CCDS; CCDS33114.1; -.
RefSeq; NP_055316.2; NM_014501.2.
UniGene; Hs.396393; -.
PDB; 1ZDN; X-ray; 1.93 A; A/B=1-156.
PDB; 5BNB; X-ray; 2.49 A; A/B/C/D=1-156.
PDB; 5L9T; EM; 6.40 A; T=1-222.
PDBsum; 1ZDN; -.
PDBsum; 5BNB; -.
PDBsum; 5L9T; -.
ProteinModelPortal; Q16763; -.
SMR; Q16763; -.
BioGrid; 118150; 86.
DIP; DIP-52784N; -.
IntAct; Q16763; 15.
MINT; Q16763; -.
STRING; 9606.ENSP00000264552; -.
iPTMnet; Q16763; -.
PhosphoSitePlus; Q16763; -.
BioMuta; UBE2S; -.
DMDM; 23829978; -.
EPD; Q16763; -.
MaxQB; Q16763; -.
PaxDb; Q16763; -.
PeptideAtlas; Q16763; -.
PRIDE; Q16763; -.
ProteomicsDB; 61055; -.
DNASU; 27338; -.
Ensembl; ENST00000264552; ENSP00000264552; ENSG00000108106.
GeneID; 27338; -.
KEGG; hsa:27338; -.
UCSC; uc002qkx.2; human.
CTD; 27338; -.
DisGeNET; 27338; -.
EuPathDB; HostDB:ENSG00000108106.13; -.
GeneCards; UBE2S; -.
H-InvDB; HIX0039201; -.
HGNC; HGNC:17895; UBE2S.
HPA; CAB015228; -.
HPA; HPA057150; -.
MIM; 610309; gene.
neXtProt; NX_Q16763; -.
OpenTargets; ENSG00000108106; -.
PharmGKB; PA134904441; -.
eggNOG; KOG0423; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00910000143990; -.
HOGENOM; HOG000233455; -.
HOVERGEN; HBG063308; -.
InParanoid; Q16763; -.
KO; K10583; -.
OrthoDB; EOG091G0USF; -.
PhylomeDB; Q16763; -.
TreeFam; TF101120; -.
BRENDA; 2.3.2.B6; 2681.
Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q16763; -.
UniPathway; UPA00143; -.
ChiTaRS; UBE2S; human.
EvolutionaryTrace; Q16763; -.
GenomeRNAi; 27338; -.
PRO; PR:Q16763; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000108106; -.
CleanEx; HS_UBE2S; -.
ExpressionAtlas; Q16763; baseline and differential.
Genevisible; Q16763; HS.
GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0010458; P:exit from mitosis; IDA:UniProtKB.
GO; GO:0010994; P:free ubiquitin chain polymerization; IDA:UniProtKB.
GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IDA:UniProtKB.
GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
GO; GO:0044314; P:protein K27-linked ubiquitination; IDA:UniProtKB.
GO; GO:0035519; P:protein K29-linked ubiquitination; IDA:UniProtKB.
GO; GO:0085020; P:protein K6-linked ubiquitination; IDA:UniProtKB.
GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
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; Acetylation; ATP-binding; Cell cycle; Cell division;
Complete proteome; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 222 Ubiquitin-conjugating enzyme E2 S.
/FTId=PRO_0000082507.
ACT_SITE 95 95 Glycyl thioester intermediate.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 173 173 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MUTAGEN 95 95 C->S: Loss of function.
{ECO:0000269|PubMed:19822757,
ECO:0000269|PubMed:20622874}.
MUTAGEN 117 117 K->A: Reduced ubiquitination activity.
{ECO:0000269|PubMed:26828794}.
MUTAGEN 222 222 L->A: Impairs polyubiquitination in the
presence of APC/C complex, decreasing
affinity for substrate.
{ECO:0000269|PubMed:27259151}.
CONFLICT 216 216 K -> KRAL (in Ref. 1; AAA58446).
{ECO:0000305}.
HELIX 10 25 {ECO:0000244|PDB:1ZDN}.
STRAND 31 35 {ECO:0000244|PDB:1ZDN}.
STRAND 42 48 {ECO:0000244|PDB:1ZDN}.
TURN 54 57 {ECO:0000244|PDB:1ZDN}.
STRAND 59 65 {ECO:0000244|PDB:1ZDN}.
TURN 68 72 {ECO:0000244|PDB:1ZDN}.
STRAND 76 81 {ECO:0000244|PDB:1ZDN}.
STRAND 92 94 {ECO:0000244|PDB:1ZDN}.
HELIX 96 99 {ECO:0000244|PDB:1ZDN}.
TURN 100 102 {ECO:0000244|PDB:1ZDN}.
HELIX 109 121 {ECO:0000244|PDB:1ZDN}.
HELIX 125 127 {ECO:0000244|PDB:1ZDN}.
HELIX 131 139 {ECO:0000244|PDB:1ZDN}.
HELIX 141 155 {ECO:0000244|PDB:1ZDN}.
SEQUENCE 222 AA; 23845 MW; 2842DC3DCD2AFCB5 CRC64;
MNSNVENLPP HIIRLVYKEV TTLTADPPDG IKVFPNEEDL TDLQVTIEGP EGTPYAGGLF
RMKLLLGKDF PASPPKGYFL TKIFHPNVGA NGEICVNVLK RDWTAELGIR HVLLTIKCLL
IHPNPESALN EEAGRLLLEN YEEYAARARL LTEIHGGAGG PSGRAEAGRA LASGTEASST
DPGAPGGPGG AEGPMAKKHA GERDKKLAAK KKTDKKRALR RL


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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
EIAAB44895 HIP2,HIP-2,Homo sapiens,Human,Huntingtin-interacting protein 2,LIG,UBE2K,Ubiquitin carrier protein,Ubiquitin-conjugating enzyme E2 K,Ubiquitin-conjugating enzyme E2(25K),Ubiquitin-conjugating enzyme E
EIAAB44896 Hip2,HIP-2,Huntingtin-interacting protein 2,Mouse,Mus musculus,Ube2k,Ubiquitin carrier protein,Ubiquitin-conjugating enzyme E2 K,Ubiquitin-conjugating enzyme E2(25K),Ubiquitin-conjugating enzyme E2-25
EIAAB44894 Bos taurus,Bovine,HIP2,HIP-2,Huntingtin-interacting protein 2,UBE2K,Ubiquitin carrier protein,Ubiquitin-conjugating enzyme E2 K,Ubiquitin-conjugating enzyme E2(25K),Ubiquitin-conjugating enzyme E2-25
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
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
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
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
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
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 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


 

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