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Ubiquitin-like-conjugating enzyme ATG3 (EC 6.3.2.-) (Autophagy-related protein 3) (APG3-like) (hApg3) (Protein PC3-96)

 ATG3_HUMAN              Reviewed;         314 AA.
Q9NT62; Q6PKC5; Q9H6L9;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 140.
RecName: Full=Ubiquitin-like-conjugating enzyme ATG3;
EC=6.3.2.-;
AltName: Full=Autophagy-related protein 3;
Short=APG3-like;
Short=hApg3;
AltName: Full=Protein PC3-96;
Name=ATG3; Synonyms=APG3, APG3L;
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), TISSUE SPECIFICITY,
MUTAGENESIS OF CYS-264, SUBCELLULAR LOCATION, FUNCTION, ACTIVE SITE,
AND INTERACTION WITH ATG7 AND ATG12.
TISSUE=Brain;
PubMed=11825910; DOI=10.1074/jbc.M200385200;
Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.;
"Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple
substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the
conjugation of hApg12p to hApg5p.";
J. Biol. Chem. 277:13739-13744(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Retina;
Wu B.X., Li Y., Laser M., Crosson C.E., Hazard E.S. III, Ma J.X.;
"Cloning and characterization of human PC3-96 gene.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung, and Lymph;
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 118-314 (ISOFORM 2).
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).
[6]
FUNCTION, AND INTERACTION WITH THE ATG12-ATG5 CONJUGATE.
PubMed=12207896; DOI=10.1016/S0006-291X(02)02057-0;
Tanida I., Nishitani T., Nemoto T., Ueno T., Kominami E.;
"Mammalian Apg12p, but not the Apg12p.Apg5p conjugate, facilitates LC3
processing.";
Biochem. Biophys. Res. Commun. 296:1164-1170(2002).
[7]
FUNCTION.
PubMed=12890687; DOI=10.1074/jbc.M300550200;
Nemoto T., Tanida I., Tanida-Miyake E., Minematsu-Ikeguchi N.,
Yokota M., Ohsumi M., Ueno T., Kominami E.;
"The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation,
facilitates MAP-LC3 modification.";
J. Biol. Chem. 278:39517-39526(2003).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[10]
FUNCTION.
PubMed=16704426; DOI=10.1111/j.1742-4658.2006.05260.x;
Tanida I., Sou Y.S., Minematsu-Ikeguchi N., Ueno T., Kominami E.;
"Atg8L/Apg8L is the fourth mammalian modifier of mammalian Atg8
conjugation mediated by human Atg4B, Atg7 and Atg3.";
FEBS J. 273:2553-2562(2006).
[11]
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).
[12]
INTERACTION WITH FNBP1L.
PubMed=19342671; DOI=10.4049/jimmunol.0803050;
Huett A., Ng A., Cao Z., Kuballa P., Komatsu M., Daly M.J.,
Podolsky D.K., Xavier R.J.;
"A novel hybrid yeast-human network analysis reveals an essential role
for FNBP1L in antibacterial autophagy.";
J. Immunol. 182:4917-4930(2009).
[13]
FUNCTION, AND INTERACTION WITH ATG12.
PubMed=20723759; DOI=10.1016/j.cell.2010.07.018;
Radoshevich L., Murrow L., Chen N., Fernandez E., Roy S., Fung C.,
Debnath J.;
"ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and
cell death.";
Cell 142:590-600(2010).
[14]
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).
[15]
DOMAIN, AND CLEAVAGE BY CASP8.
PubMed=22644571; DOI=10.1007/s10495-012-0735-0;
Oral O., Oz-Arslan D., Itah Z., Naghavi A., Deveci R., Karacali S.,
Gozuacik D.;
"Cleavage of Atg3 protein by caspase-8 regulates autophagy during
receptor-activated cell death.";
Apoptosis 17:810-820(2012).
[16]
INTERACTION WITH ATG3 AND ATG12.
PubMed=22170151; DOI=10.4161/auto.8.1.18339;
Tanida I., Yamasaki M., Komatsu M., Ueno T.;
"The FAP motif within human ATG7, an autophagy-related E1-like enzyme,
is essential for the E2-substrate reaction of LC3 lipidation.";
Autophagy 8:88-97(2012).
[17]
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).
-!- FUNCTION: E2 conjugating enzyme required for the cytoplasm to
vacuole transport (Cvt), autophagy, and mitochondrial homeostasis.
Responsible for the E2-like covalent binding of
phosphatidylethanolamine to the C-terminal Gly of ATG8-like
proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-
ATG5 conjugate plays a role of an E3 and promotes the transfer of
ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE).
This step is required for the membrane association of ATG8-like
proteins. The formation of the ATG8-phosphatidylethanolamine
conjugates is essential for autophagy and for the cytoplasm to
vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also
acts as an autocatalytic E2-like enzyme, catalyzing the
conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing
a role in mitochondrial homeostasis but not in autophagy. ATG7
(E1-like enzyme) facilitates this reaction by forming an E1-E2
complex with ATG3. Promotes primary ciliogenesis by removing OFD1
from centriolar satellites via the autophagic pathway.
{ECO:0000269|PubMed:11825910, ECO:0000269|PubMed:12207896,
ECO:0000269|PubMed:12890687, ECO:0000269|PubMed:16704426,
ECO:0000269|PubMed:20723759}.
-!- SUBUNIT: Interacts with ATG7 and ATG12. The complex, composed of
ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5.
Interacts with FNBP1L. {ECO:0000269|PubMed:11825910,
ECO:0000269|PubMed:12207896, ECO:0000269|PubMed:19342671,
ECO:0000269|PubMed:20723759, ECO:0000269|PubMed:22170151}.
-!- INTERACTION:
O94817:ATG12; NbExp=5; IntAct=EBI-988094, EBI-746742;
O95166:GABARAP; NbExp=5; IntAct=EBI-988094, EBI-712001;
Q9H0R8:GABARAPL1; NbExp=3; IntAct=EBI-988094, EBI-746969;
P60520:GABARAPL2; NbExp=5; IntAct=EBI-988094, EBI-720116;
Q9GZQ8:MAP1LC3B; NbExp=7; IntAct=EBI-988094, EBI-373144;
Q7Z6L1:TECPR1; NbExp=3; IntAct=EBI-988094, EBI-2946676;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11825910}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NT62-1; Sequence=Displayed;
Name=2;
IsoId=Q9NT62-2; Sequence=VSP_013037;
Note=No experimental confirmation available. Ref.4 (AAH02830)
sequence differs from that shown due to a frameshift in position
311. {ECO:0000305};
-!- TISSUE SPECIFICITY: Widely expressed, with a highest expression in
heart, skeletal muscle, kidney, liver and placenta.
{ECO:0000269|PubMed:11825910}.
-!- PTM: Conjugated to ATG12 at Lys-243. ATG12-conjugation plays a
role in regulation of mitochondrial homeostasis and cell death,
while it is not involved in PE-conjugation to ATG8-like proteins
and autophagy.
-!- PTM: Cleaved by CASP8 upon death ligand binding such as tumor
necrosis factor-alpha. CASP8 cleavage blocks survival-related
autophagy and favors apoptosis. {ECO:0000269|PubMed:22644571}.
-!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH02830.1; Type=Frameshift; Positions=290; Evidence={ECO:0000305};
Sequence=BAB15237.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB079384; BAB90843.1; -; mRNA.
EMBL; AF202092; AAG35611.1; -; mRNA.
EMBL; AL137515; CAB70781.1; -; mRNA.
EMBL; BC002830; AAH02830.1; ALT_FRAME; mRNA.
EMBL; BC024221; AAH24221.1; -; mRNA.
EMBL; AK025778; BAB15237.1; ALT_INIT; mRNA.
CCDS; CCDS2966.1; -. [Q9NT62-1]
CCDS; CCDS63721.1; -. [Q9NT62-2]
PIR; T46276; T46276.
RefSeq; NP_001265641.1; NM_001278712.1. [Q9NT62-2]
RefSeq; NP_071933.2; NM_022488.4. [Q9NT62-1]
UniGene; Hs.477126; -.
PDB; 4NAW; X-ray; 2.20 A; D/H/L/P=140-170.
PDBsum; 4NAW; -.
ProteinModelPortal; Q9NT62; -.
SMR; Q9NT62; -.
BioGrid; 122171; 46.
DIP; DIP-35052N; -.
IntAct; Q9NT62; 25.
STRING; 9606.ENSP00000283290; -.
iPTMnet; Q9NT62; -.
PhosphoSitePlus; Q9NT62; -.
SwissPalm; Q9NT62; -.
BioMuta; ATG3; -.
DMDM; 61212142; -.
EPD; Q9NT62; -.
MaxQB; Q9NT62; -.
PaxDb; Q9NT62; -.
PeptideAtlas; Q9NT62; -.
PRIDE; Q9NT62; -.
DNASU; 64422; -.
Ensembl; ENST00000283290; ENSP00000283290; ENSG00000144848. [Q9NT62-1]
Ensembl; ENST00000402314; ENSP00000385943; ENSG00000144848. [Q9NT62-2]
GeneID; 64422; -.
KEGG; hsa:64422; -.
UCSC; uc003dzc.5; human. [Q9NT62-1]
CTD; 64422; -.
DisGeNET; 64422; -.
EuPathDB; HostDB:ENSG00000144848.10; -.
GeneCards; ATG3; -.
HGNC; HGNC:20962; ATG3.
HPA; CAB037260; -.
HPA; HPA040471; -.
MIM; 609606; gene.
neXtProt; NX_Q9NT62; -.
OpenTargets; ENSG00000144848; -.
PharmGKB; PA134883444; -.
eggNOG; KOG2981; Eukaryota.
eggNOG; ENOG410Y3BC; LUCA.
GeneTree; ENSGT00390000010308; -.
HOGENOM; HOG000234613; -.
HOVERGEN; HBG080876; -.
InParanoid; Q9NT62; -.
KO; K08343; -.
OMA; YEDVSQD; -.
OrthoDB; EOG091G0H8F; -.
PhylomeDB; Q9NT62; -.
TreeFam; TF105903; -.
Reactome; R-HSA-1632852; Macroautophagy.
SIGNOR; Q9NT62; -.
ChiTaRS; ATG3; human.
GenomeRNAi; 64422; -.
PRO; PR:Q9NT62; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000144848; -.
CleanEx; HS_ATG3; -.
ExpressionAtlas; Q9NT62; baseline and differential.
Genevisible; Q9NT62; HS.
GO; GO:0000153; C:cytoplasmic ubiquitin ligase complex; IPI:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0019777; F:Atg12 transferase activity; ISS:UniProtKB.
GO; GO:0019776; F:Atg8 ligase activity; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
GO; GO:0019787; F:ubiquitin-like protein transferase activity; IDA:MGI.
GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
GO; GO:0006464; P:cellular protein modification process; IDA:MGI.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISS:UniProtKB.
GO; GO:0050765; P:negative regulation of phagocytosis; IEA:Ensembl.
GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB.
InterPro; IPR007135; Autophagy-rel_prot_3.
InterPro; IPR019461; Autophagy-rel_prot_3_C.
InterPro; IPR007134; Autophagy-rel_prot_3_N.
Pfam; PF03987; Autophagy_act_C; 1.
Pfam; PF10381; Autophagy_C; 1.
Pfam; PF03986; Autophagy_N; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Autophagy;
Complete proteome; Cytoplasm; Isopeptide bond; Ligase;
Protein transport; Reference proteome; Transport; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 314 Ubiquitin-like-conjugating enzyme ATG3.
/FTId=PRO_0000213569.
MOTIF 166 169 Caspase cleavage motif LETD.
ACT_SITE 264 264 Glycyl thioester intermediate.
{ECO:0000305|PubMed:11825910}.
SITE 169 170 Cleavage; by CASP8.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
CROSSLNK 243 243 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ATG12).
{ECO:0000250}.
VAR_SEQ 290 314 LLIFLKFVQAVIPTIEYDYTRHFTM -> PSLYVRLVAKWL
LTIFFLRNLV (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_013037.
MUTAGEN 264 264 C->S: Instead of the formation of an
intermediate complex with a thiol ester
bond between ATG3 (E2-like enzyme) and
GABARAPL1/APG8L (substrate), a stable
complex with an O-ester bond is formed.
{ECO:0000269|PubMed:11825910}.
HELIX 157 163 {ECO:0000244|PDB:4NAW}.
SEQUENCE 314 AA; 35864 MW; 40EFE88DB5FE3EAB CRC64;
MQNVINTVKG KALEVAEYLT PVLKESKFKE TGVITPEEFV AAGDHLVHHC PTWQWATGEE
LKVKAYLPTG KQFLVTKNVP CYKRCKQMEY SDELEAIIEE DDGDGGWVDT YHNTGITGIT
EAVKEITLEN KDNIRLQDCS ALCEEEEDED EGEAADMEEY EESGLLETDE ATLDTRKIVE
ACKAKTDAGG EDAILQTRTY DLYITYDKYY QTPRLWLFGY DEQRQPLTVE HMYEDISQDH
VKKTVTIENH PHLPPPPMCS VHPCRHAEVM KKIIETVAEG GGELGVHMYL LIFLKFVQAV
IPTIEYDYTR HFTM


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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
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
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-
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
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
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
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
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 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
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


 

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