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Ubiquitin-protein ligase E3A (EC 2.3.2.26) (E6AP ubiquitin-protein ligase) (HECT-type ubiquitin transferase E3A) (Human papillomavirus E6-associated protein) (Oncogenic protein-associated protein E6-AP) (Renal carcinoma antigen NY-REN-54)

 UBE3A_HUMAN             Reviewed;         875 AA.
Q05086; A8K8Z9; P78355; Q93066; Q9UEP4; Q9UEP5; Q9UEP6; Q9UEP7;
Q9UEP8; Q9UEP9;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 4.
22-NOV-2017, entry version 183.
RecName: Full=Ubiquitin-protein ligase E3A;
EC=2.3.2.26;
AltName: Full=E6AP ubiquitin-protein ligase;
AltName: Full=HECT-type ubiquitin transferase E3A;
AltName: Full=Human papillomavirus E6-associated protein;
AltName: Full=Oncogenic protein-associated protein E6-AP;
AltName: Full=Renal carcinoma antigen NY-REN-54;
Name=UBE3A; Synonyms=E6AP, EPVE6AP, HPVE6A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS I; II AND III), AND
VARIANT GLY-290.
TISSUE=Keratinocyte;
PubMed=9143503; DOI=10.1006/geno.1997.4617;
Yamamoto Y., Huibregtse J.M., Howley P.M.;
"The human E6-AP gene (UBE3A) encodes three potential protein isoforms
generated by differential splicing.";
Genomics 41:263-266(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I).
TISSUE=Fetal brain;
PubMed=8988171; DOI=10.1038/ng0197-70;
Kishino T., Lalande M., Wagstaff J.;
"UBE3A/E6-AP mutations cause Angelman syndrome.";
Nat. Genet. 15:70-73(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM I), AND VARIANTS TYR-44 AND
THR-201.
PubMed=8988172; DOI=10.1038/ng0197-74;
Matsuura T., Sutcliffe J.S., Fang P., Galjaard R.-J., Jiang Y.-H.,
Benton C.S., Rommens J.M., Beaudet A.L.;
"De novo truncating mutations in E6-AP ubiquitin-protein ligase gene
(UBE3A) in Angelman syndrome.";
Nat. Genet. 15:74-77(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM III).
TISSUE=Testis;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 11-875, PARTIAL PROTEIN SEQUENCE,
CHARACTERIZATION, AND VARIANT GLY-290.
TISSUE=Keratinocyte;
PubMed=8380895; DOI=10.1128/MCB.13.2.775;
Huibregtse J.M., Scheffner M., Howley P.M.;
"Cloning and expression of the cDNA for E6-AP, a protein that mediates
the interaction of the human papillomavirus E6 oncoprotein with p53.";
Mol. Cell. Biol. 13:775-784(1993).
[8]
CHARACTERIZATION.
PubMed=9688277; DOI=10.1046/j.1432-1327.1998.2540643.x;
Nuber U., Schwarz S.E., Scheffner M.;
"The ubiquitin-protein ligase E6-associated protein (E6-AP) serves as
its own substrate.";
Eur. J. Biochem. 254:643-649(1998).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-787, AND VARIANT GLY-290.
Hennies H.C., Buerger J., Sperling K., Reis A.;
"Mutations in the E6-AP gene (UBE3A) in patients with Angelman
syndrome.";
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[10]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[11]
FUNCTION.
PubMed=10373495; DOI=10.1074/jbc.274.26.18785;
Kumar S., Talis A.L., Howley P.M.;
"Identification of HHR23A as a substrate for E6-associated protein-
mediated ubiquitination.";
J. Biol. Chem. 274:18785-18792(1999).
[12]
INTERACTION WITH UBQLN1 AND UBQLN2.
PubMed=10983987; DOI=10.1016/S1097-2765(00)00040-X;
Kleijnen M.F., Shih A.H., Zhou P., Kumar S., Soccio R.E.,
Kedersha N.L., Gill G., Howley P.M.;
"The hPLIC proteins may provide a link between the ubiquitination
machinery and the proteasome.";
Mol. Cell 6:409-419(2000).
[13]
INTERACTION WITH BPY2.
PubMed=12207887; DOI=10.1016/S0006-291X(02)02040-5;
Wong E.Y., Tse J.Y., Yao K.M., Tam P.C., Yeung W.S.;
"VCY2 protein interacts with the HECT domain of ubiquitin-protein
ligase E3A.";
Biochem. Biophys. Res. Commun. 296:1104-1111(2002).
[14]
FUNCTION, AND INTERACTION WITH ESR1 AND WBP2.
PubMed=16772533; DOI=10.1210/me.2005-0533;
Dhananjayan S.C., Ramamoorthy S., Khan O.Y., Ismail A., Sun J.,
Slingerland J., O'Malley B.W., Nawaz Z.;
"WW domain binding protein-2, an E6-associated protein interacting
protein, acts as a coactivator of estrogen and progesterone
receptors.";
Mol. Endocrinol. 20:2343-2354(2006).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human
26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[16]
INTERACTION WITH HCV CORE PROTEIN.
PubMed=17108031; DOI=10.1128/JVI.01684-06;
Shirakura M., Murakami K., Ichimura T., Suzuki R., Shimoji T.,
Fukuda K., Abe K., Sato S., Fukasawa M., Yamakawa Y., Nishijima M.,
Moriishi K., Matsuura Y., Wakita T., Suzuki T., Howley P.M.,
Miyamura T., Shoji I.;
"E6AP ubiquitin ligase mediates ubiquitylation and degradation of
hepatitis C virus core protein.";
J. Virol. 81:1174-1185(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[18]
FUNCTION.
PubMed=19325566; DOI=10.1038/cdd.2009.31;
Louria-Hayon I., Alsheich-Bartok O., Levav-Cohen Y., Silberman I.,
Berger M., Grossman T., Matentzoglu K., Jiang Y.H., Muller S.,
Scheffner M., Haupt S., Haupt Y.;
"E6AP promotes the degradation of the PML tumor suppressor.";
Cell Death Differ. 16:1156-1166(2009).
[19]
FUNCTION.
PubMed=19233847; DOI=10.1074/jbc.M806804200;
Mishra A., Godavarthi S.K., Maheshwari M., Goswami A., Jana N.R.;
"The ubiquitin ligase E6-AP is induced and recruited to aggresomes in
response to proteasome inhibition and may be involved in the
ubiquitination of Hsp70-bound misfolded proteins.";
J. Biol. Chem. 284:10537-10545(2009).
[20]
FUNCTION.
PubMed=19204938; DOI=10.1002/jcb.22096;
Shimoji T., Murakami K., Sugiyama Y., Matsuda M., Inubushi S.,
Nasu J., Shirakura M., Suzuki T., Wakita T., Kishino T., Hotta H.,
Miyamura T., Shoji I.;
"Identification of annexin A1 as a novel substrate for E6AP-mediated
ubiquitylation.";
J. Cell. Biochem. 106:1123-1135(2009).
[21]
FUNCTION.
PubMed=19591933; DOI=10.1016/j.nbd.2009.06.010;
Mishra A., Godavarthi S.K., Jana N.R.;
"UBE3A/E6-AP regulates cell proliferation by promoting proteasomal
degrADation of p27.";
Neurobiol. Dis. 36:26-34(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[23]
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).
[24]
INTERACTION WITH WBP2.
PubMed=21642474; DOI=10.1096/fj.10-169136;
Lim S.K., Orhant-Prioux M., Toy W., Tan K.Y., Lim Y.P.;
"Tyrosine phosphorylation of transcriptional coactivator WW-domain
binding protein 2 regulates estrogen receptor alpha function in breast
cancer via the Wnt pathway.";
FASEB J. 25:3004-3018(2011).
[25]
FUNCTION, AND INTERACTION WITH HIF1AN; MAPK6; NEURL4 AND PSMD4.
PubMed=22645313; DOI=10.1128/MCB.00201-12;
Martinez-Noel G., Galligan J.T., Sowa M.E., Arndt V., Overton T.M.,
Harper J.W., Howley P.M.;
"Identification and proteomic analysis of distinct UBE3A/E6AP protein
complexes.";
Mol. Cell. Biol. 32:3095-3106(2012).
[26]
PHOSPHORYLATION AT TYR-659.
PubMed=23581475; DOI=10.1021/bi301710c;
Chan A.L., Grossman T., Zuckerman V., Campigli Di Giammartino D.,
Moshel O., Scheffner M., Monahan B., Pilling P., Jiang Y.H., Haupt S.,
Schueler-Furman O., Haupt Y.;
"c-Abl phosphorylates E6AP and regulates its E3 ubiquitin ligase
activity.";
Biochemistry 52:3119-3129(2013).
[27]
SUBUNIT, AND MUTAGENESIS OF PHE-750.
PubMed=24273172; DOI=10.1074/jbc.M113.517805;
Ronchi V.P., Klein J.M., Edwards D.J., Haas A.L.;
"The active form of E6-associated protein (E6AP)/UBE3A ubiquitin
ligase is an oligomer.";
J. Biol. Chem. 289:1033-1048(2014).
[28]
FUNCTION, AND INTERACTION WITH ARNTL.
PubMed=24728990; DOI=10.1093/nar/gku225;
Gossan N.C., Zhang F., Guo B., Jin D., Yoshitane H., Yao A.,
Glossop N., Zhang Y.Q., Fukada Y., Meng Q.J.;
"The E3 ubiquitin ligase UBE3A is an integral component of the
molecular circadian clock through regulating the BMAL1 transcription
factor.";
Nucleic Acids Res. 42:5765-5775(2014).
[29]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 495-852 IN COMPLEX WITH
UBE2L3.
PubMed=10558980; DOI=10.1126/science.286.5443.1321;
Huang L., Kinnucan E., Wang G., Beaudenon S., Howley P.M.,
Huibregtse J.M., Pavletich N.P.;
"Structure of an E6AP-UbcH7 complex: insights into ubiquitination by
the E2-E3 enzyme cascade.";
Science 286:1321-1326(1999).
[30]
STRUCTURE BY NMR OF 401-418.
PubMed=11170455; DOI=10.1021/bi0019592;
Be X., Hong Y., Wei J., Androphy E.J., Chen J.J., Baleja J.D.;
"Solution structure determination and mutational analysis of the
papillomavirus E6 interacting peptide of E6AP.";
Biochemistry 40:1293-1299(2001).
[31]
STRUCTURE BY NMR OF 24-87, AND ZINC-FINGER.
PubMed=21947926; DOI=10.1007/s10858-011-9552-y;
Lemak A., Yee A., Bezsonova I., Dhe-Paganon S., Arrowsmith C.H.;
"Zn-binding AZUL domain of human ubiquitin protein ligase Ube3A.";
J. Biomol. NMR 51:185-190(2011).
[32]
VARIANT AS ILE-826 INS, VARIANTS HIS-62; THR-201 AND PRO-372, AND
INVOLVEMENT IN AS.
PubMed=9585605; DOI=10.1086/301877;
Malzac P., Webber H., Moncla A., Graham J.M. Jr., Kukolich M.,
Williams C., Pagon R.A., Ramsdell L.A., Kishino T., Wagstaff J.;
"Mutation analysis of UBE3A in Angelman syndrome patients.";
Am. J. Hum. Genet. 62:1353-1360(1998).
[33]
VARIANTS AS LYS-129; VAL-235; GLN-260; HIS-260; TRP-286; PRO-458;
LEU-481; PRO-500; ARG-568; LYS-589; GLN-607; ILE-679; CYS-713 AND
LEU-850, AND VARIANTS ARG-140; GLY-156; THR-293; THR-358; ILE-501;
GLU-611; PRO-611; ARG-696 AND ILE-785.
PubMed=25212744; DOI=10.1002/humu.22687;
Sadikovic B., Fernandes P., Zhang V.W., Ward P.A., Miloslavskaya I.,
Rhead W., Rosenbaum R., Gin R., Roa B., Fang P.;
"Mutation update for UBE3A variants in Angelman syndrome.";
Hum. Mutat. 35:1407-1417(2014).
-!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
an E2 ubiquitin-conjugating enzyme in the form of a thioester and
transfers it to its substrates. Several substrates have been
identified including the RAD23A and RAD23B, MCM7 (which is
involved in DNA replication), annexin A1, the PML tumor
suppressor, and the cell cycle regulator CDKN1B. Catalyzes the
high-risk human papilloma virus E6-mediated ubiquitination of
p53/TP53, contributing to the neoplastic progression of cells
infected by these viruses. Additionally, may function as a
cellular quality control ubiquitin ligase by helping the
degradation of the cytoplasmic misfolded proteins. Finally, UBE3A
also promotes its own degradation in vivo. Plays an important role
in the regulation of the circadian clock: involved in the
ubiquitination of the core clock component ARNTL/BMAL1, leading to
its proteasomal degradation (PubMed:24728990). Acts as
transcriptional coactivator of progesterone receptor PGR upon
progesterone hormone activation (PubMed:16772533). Synergizes with
WBP2 in enhancing PGR activity (PubMed:16772533).
{ECO:0000269|PubMed:10373495, ECO:0000269|PubMed:16772533,
ECO:0000269|PubMed:19204938, ECO:0000269|PubMed:19233847,
ECO:0000269|PubMed:19325566, ECO:0000269|PubMed:19591933,
ECO:0000269|PubMed:22645313, ECO:0000269|PubMed:24728990}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: The active form is probably a homotrimer. Binds UBQLN1
and UBQLN2. Interacts with the 26S proteasome. Interacts with HCV
core protein and targets it to degradation. Interacts with the E6
protein of the cancer-associated human papillomavirus types 16 and
18. The E6/E6-AP complex binds to and targets the p53/TP53 tumor-
suppressor protein for ubiquitin-mediated proteolysis. Interacts
with BPY2. Interacts with HIF1AN, MAPK6 AND NEURL4; interaction
with MAPK6 may be mediated by NEURL4. Interacts with the
proteasomal subunit PSMD4. Interacts with ARNTL/BMAL1. Interacts
with ESR1 and WBP2 (PubMed:16772533, PubMed:21642474).
{ECO:0000269|PubMed:10558980, ECO:0000269|PubMed:10983987,
ECO:0000269|PubMed:12207887, ECO:0000269|PubMed:16772533,
ECO:0000269|PubMed:17108031, ECO:0000269|PubMed:21642474,
ECO:0000269|PubMed:22645313, ECO:0000269|PubMed:24273172,
ECO:0000269|PubMed:24728990}.
-!- INTERACTION:
B3KPL7:-; NbExp=3; IntAct=EBI-10175863, EBI-10175860;
Q9NZD4:AHSP; NbExp=3; IntAct=EBI-10175863, EBI-720250;
Q8TDY4:ASAP3; NbExp=3; IntAct=EBI-10175863, EBI-2609717;
Q7Z3C6:ATG9A; NbExp=3; IntAct=EBI-10175863, EBI-727146;
P03126:E6 (xeno); NbExp=9; IntAct=EBI-954357, EBI-1177242;
P04019:E6 (xeno); NbExp=5; IntAct=EBI-954357, EBI-1177232;
P06462:E6 (xeno); NbExp=2; IntAct=EBI-954357, EBI-7069993;
P06463:E6 (xeno); NbExp=6; IntAct=EBI-954357, EBI-1186926;
P06931:E6 (xeno); NbExp=2; IntAct=EBI-954357, EBI-7281937;
Q77E16:E6 (xeno); NbExp=3; IntAct=EBI-954357, EBI-7011359;
Q2WGJ6:KLHL38; NbExp=3; IntAct=EBI-10175863, EBI-6426443;
A1L4G7:TAT; NbExp=3; IntAct=EBI-10175863, EBI-10223561;
P17735:TAT; NbExp=8; IntAct=EBI-11026619, EBI-12046643;
P04637:TP53; NbExp=6; IntAct=EBI-954357, EBI-366083;
Q5U5U6:UBB; NbExp=3; IntAct=EBI-10175863, EBI-1642104;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O08759}.
Cytoplasm {ECO:0000250|UniProtKB:O08759}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=II;
IsoId=Q05086-1; Sequence=Displayed;
Name=I;
IsoId=Q05086-2; Sequence=VSP_006705;
Name=III;
IsoId=Q05086-3; Sequence=VSP_006706;
-!- PTM: Phosphorylation at Tyr-659 by ABL1 impairs E3 ligase activity
and protects p53/TP53 from degradation in (HPV)-infected cells.
{ECO:0000269|PubMed:23581475}.
-!- DISEASE: Angelman syndrome (AS) [MIM:105830]: A neurodevelopmental
disorder characterized by severe motor and intellectual
retardation, ataxia, frequent jerky limb movements and flapping of
the arms and hands, hypotonia, seizures, absence of speech,
frequent smiling and episodes of paroxysmal laughter, open-mouthed
expression revealing the tongue. {ECO:0000269|PubMed:25212744,
ECO:0000269|PubMed:9585605}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-
thioester formation.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/UBE3AID42756ch15q11.html";
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EMBL; X98021; CAA66653.1; -; Genomic_DNA.
EMBL; X98027; CAA66653.1; JOINED; Genomic_DNA.
EMBL; X98022; CAA66653.1; JOINED; Genomic_DNA.
EMBL; X98023; CAA66653.1; JOINED; Genomic_DNA.
EMBL; X98024; CAA66653.1; JOINED; Genomic_DNA.
EMBL; X98025; CAA66653.1; JOINED; Genomic_DNA.
EMBL; X98026; CAA66653.1; JOINED; Genomic_DNA.
EMBL; X98028; CAA66653.1; JOINED; Genomic_DNA.
EMBL; X98029; CAA66653.1; JOINED; Genomic_DNA.
EMBL; X98030; CAA66653.1; JOINED; Genomic_DNA.
EMBL; X98031; CAA66654.1; -; mRNA.
EMBL; X98032; CAA66655.1; -; mRNA.
EMBL; X98033; CAA66656.1; -; mRNA.
EMBL; AC100774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK292514; BAF85203.1; -; mRNA.
EMBL; AC124997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471151; EAW57645.1; -; Genomic_DNA.
EMBL; L07557; AAA35542.1; -; mRNA.
EMBL; AF016708; AAB69154.1; -; Genomic_DNA.
EMBL; AF016703; AAB69154.1; JOINED; Genomic_DNA.
EMBL; AF016704; AAB69154.1; JOINED; Genomic_DNA.
EMBL; AF016705; AAB69154.1; JOINED; Genomic_DNA.
EMBL; AF016706; AAB69154.1; JOINED; Genomic_DNA.
EMBL; AF016707; AAB69154.1; JOINED; Genomic_DNA.
EMBL; U84404; AAB49301.1; -; mRNA.
EMBL; AJ001107; CAA04534.1; -; Genomic_DNA.
EMBL; AJ001108; CAA04535.1; -; Genomic_DNA.
EMBL; AJ001109; CAA04536.1; -; Genomic_DNA.
EMBL; AJ001110; CAA04537.1; -; Genomic_DNA.
EMBL; AJ001111; CAA04538.1; -; Genomic_DNA.
EMBL; AJ001112; CAA04539.1; -; Genomic_DNA.
CCDS; CCDS32177.1; -. [Q05086-2]
CCDS; CCDS45191.1; -. [Q05086-3]
CCDS; CCDS45192.1; -. [Q05086-1]
RefSeq; NP_000453.2; NM_000462.3. [Q05086-1]
RefSeq; NP_570853.1; NM_130838.1. [Q05086-2]
RefSeq; NP_570854.1; NM_130839.2. [Q05086-3]
RefSeq; XP_005268324.1; XM_005268267.4. [Q05086-2]
RefSeq; XP_005268325.1; XM_005268268.4. [Q05086-2]
RefSeq; XP_005268326.1; XM_005268269.4. [Q05086-2]
RefSeq; XP_005268327.1; XM_005268270.4. [Q05086-2]
RefSeq; XP_005268328.1; XM_005268271.4. [Q05086-2]
RefSeq; XP_006720738.1; XM_006720675.3. [Q05086-2]
RefSeq; XP_006720739.1; XM_006720676.3. [Q05086-2]
RefSeq; XP_011520296.1; XM_011521994.2. [Q05086-1]
RefSeq; XP_011520297.1; XM_011521995.2. [Q05086-1]
RefSeq; XP_016878033.1; XM_017022544.1. [Q05086-1]
RefSeq; XP_016878034.1; XM_017022545.1. [Q05086-1]
RefSeq; XP_016878035.1; XM_017022546.1. [Q05086-1]
RefSeq; XP_016878036.1; XM_017022547.1. [Q05086-3]
RefSeq; XP_016878037.1; XM_017022548.1. [Q05086-3]
RefSeq; XP_016878038.1; XM_017022549.1. [Q05086-3]
RefSeq; XP_016878039.1; XM_017022550.1. [Q05086-3]
RefSeq; XP_016878040.1; XM_017022551.1. [Q05086-2]
RefSeq; XP_016878041.1; XM_017022552.1. [Q05086-2]
RefSeq; XP_016878042.1; XM_017022553.1. [Q05086-2]
RefSeq; XP_016878043.1; XM_017022554.1. [Q05086-2]
RefSeq; XP_016878044.1; XM_017022555.1. [Q05086-2]
UniGene; Hs.598862; -.
PDB; 1C4Z; X-ray; 2.60 A; A/B/C=518-875.
PDB; 1D5F; X-ray; 2.80 A; A/B/C=518-875.
PDB; 1EQX; NMR; -; A=401-418.
PDB; 2KR1; NMR; -; A=24-87.
PDB; 4GIZ; X-ray; 2.55 A; A/B=403-414.
PDB; 4XR8; X-ray; 2.25 A; A/B=406-417.
PDBsum; 1C4Z; -.
PDBsum; 1D5F; -.
PDBsum; 1EQX; -.
PDBsum; 2KR1; -.
PDBsum; 4GIZ; -.
PDBsum; 4XR8; -.
ProteinModelPortal; Q05086; -.
SMR; Q05086; -.
BioGrid; 113185; 189.
CORUM; Q05086; -.
DIP; DIP-6002N; -.
IntAct; Q05086; 59.
MINT; MINT-147444; -.
STRING; 9606.ENSP00000381045; -.
iPTMnet; Q05086; -.
PhosphoSitePlus; Q05086; -.
BioMuta; UBE3A; -.
DMDM; 215274240; -.
EPD; Q05086; -.
MaxQB; Q05086; -.
PaxDb; Q05086; -.
PeptideAtlas; Q05086; -.
PRIDE; Q05086; -.
DNASU; 7337; -.
Ensembl; ENST00000232165; ENSP00000232165; ENSG00000114062. [Q05086-2]
Ensembl; ENST00000397954; ENSP00000381045; ENSG00000114062. [Q05086-1]
Ensembl; ENST00000428984; ENSP00000401265; ENSG00000114062. [Q05086-2]
Ensembl; ENST00000438097; ENSP00000411258; ENSG00000114062. [Q05086-2]
Ensembl; ENST00000566215; ENSP00000457771; ENSG00000114062. [Q05086-2]
Ensembl; ENST00000614096; ENSP00000481796; ENSG00000114062. [Q05086-3]
Ensembl; ENST00000630424; ENSP00000486349; ENSG00000114062. [Q05086-2]
Ensembl; ENST00000637886; ENSP00000490258; ENSG00000114062. [Q05086-3]
Ensembl; ENST00000638011; ENSP00000490111; ENSG00000114062. [Q05086-2]
Ensembl; ENST00000638155; ENSP00000490557; ENSG00000114062. [Q05086-2]
GeneID; 7337; -.
KEGG; hsa:7337; -.
UCSC; uc001zaq.4; human. [Q05086-1]
CTD; 7337; -.
DisGeNET; 7337; -.
EuPathDB; HostDB:ENSG00000114062.17; -.
GeneCards; UBE3A; -.
GeneReviews; UBE3A; -.
HGNC; HGNC:12496; UBE3A.
HPA; CAB009723; -.
HPA; HPA039410; -.
HPA; HPA040380; -.
MalaCards; UBE3A; -.
MIM; 105830; phenotype.
MIM; 601623; gene.
neXtProt; NX_Q05086; -.
OpenTargets; ENSG00000114062; -.
Orphanet; 72; Angelman syndrome.
PharmGKB; PA37144; -.
eggNOG; KOG0941; Eukaryota.
eggNOG; COG5021; LUCA.
GeneTree; ENSGT00900000140848; -.
HOVERGEN; HBG059326; -.
InParanoid; Q05086; -.
KO; K10587; -.
OMA; DTDHNEE; -.
OrthoDB; EOG091G01LV; -.
PhylomeDB; Q05086; -.
TreeFam; TF315189; -.
BRENDA; 2.3.2.B9; 2681.
BRENDA; 6.3.2.19; 2681.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; Q05086; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q05086; -.
GeneWiki; UBE3A; -.
GenomeRNAi; 7337; -.
PRO; PR:Q05086; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000114062; -.
ExpressionAtlas; Q05086; baseline and differential.
Genevisible; Q05086; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:CACAO.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0030521; P:androgen receptor signaling pathway; IEA:Ensembl.
GO; GO:0007420; P:brain development; TAS:ProtInc.
GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IEA:Ensembl.
GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:CACAO.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0060736; P:prostate gland growth; IEA:Ensembl.
GO; GO:0051865; P:protein autoubiquitination; IDA:FlyBase.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:2000058; P:regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0035037; P:sperm entry; IEA:Ensembl.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00078; HECTc; 1.
InterPro; IPR032353; AZUL.
InterPro; IPR000569; HECT_dom.
InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
InterPro; IPR017134; UBE3A.
Pfam; PF16558; AZUL; 1.
Pfam; PF00632; HECT; 1.
PIRSF; PIRSF037201; Ubiquitin-protein_ligase_E6-AP; 1.
SMART; SM00119; HECTc; 1.
SUPFAM; SSF56204; SSF56204; 1.
PROSITE; PS50237; HECT; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Biological rhythms;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Host-virus interaction; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Proteasome; Reference proteome;
Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 875 Ubiquitin-protein ligase E3A.
/FTId=PRO_0000194980.
DOMAIN 776 875 HECT. {ECO:0000255|PROSITE-
ProRule:PRU00104}.
ZN_FING 44 83 C4-type; atypical.
{ECO:0000269|PubMed:21947926}.
REGION 401 418 E6-binding.
REGION 418 517 Interaction with HCV core protein.
COMPBIAS 394 399 Asp/Glu-rich (acidic).
ACT_SITE 843 843 Glycyl thioester intermediate.
MOD_RES 218 218 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:19690332}.
MOD_RES 659 659 Phosphotyrosine; by ABL1.
{ECO:0000269|PubMed:23581475}.
VAR_SEQ 1 23 Missing (in isoform I).
{ECO:0000303|PubMed:8988171,
ECO:0000303|PubMed:9143503}.
/FTId=VSP_006705.
VAR_SEQ 1 10 MEKLHQCYWK -> MATACKR (in isoform III).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:9143503}.
/FTId=VSP_006706.
VARIANT 44 44 C -> Y (probable polymorphism).
{ECO:0000269|PubMed:8988172}.
/FTId=VAR_007852.
VARIANT 62 62 R -> H (in dbSNP:rs587784511).
{ECO:0000269|PubMed:9585605}.
/FTId=VAR_008142.
VARIANT 129 129 T -> K (in AS; unknown pathological
significance; dbSNP:rs587781241).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073196.
VARIANT 140 140 C -> R (common polymorphism; may be
associated with AS; dbSNP:rs587782907).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073197.
VARIANT 156 156 V -> G (common polymorphism; may be
associated with AS; dbSNP:rs587782915).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073198.
VARIANT 201 201 A -> T (in dbSNP:rs147145506).
{ECO:0000269|PubMed:8988172,
ECO:0000269|PubMed:9585605}.
/FTId=VAR_007853.
VARIANT 235 235 D -> V (in AS; unknown pathological
significance; dbSNP:rs587780581).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073199.
VARIANT 260 260 L -> H (in AS; unknown pathological
significance; dbSNP:rs587780582).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073200.
VARIANT 260 260 L -> Q (in AS; unknown pathological
significance).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073201.
VARIANT 286 286 L -> W (in AS; unknown pathological
significance; dbSNP:rs587780583).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073202.
VARIANT 290 290 V -> G (in dbSNP:rs1059383).
{ECO:0000269|PubMed:8380895,
ECO:0000269|PubMed:9143503,
ECO:0000269|Ref.9}.
/FTId=VAR_047516.
VARIANT 293 293 N -> T (common polymorphism; may be
associated with AS; dbSNP:rs587782908).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073203.
VARIANT 358 358 S -> T (common polymorphism; may be
associated with AS; dbSNP:rs141984760).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073204.
VARIANT 372 372 S -> P. {ECO:0000269|PubMed:9585605}.
/FTId=VAR_008143.
VARIANT 458 458 L -> P (in AS; unknown pathological
significance; dbSNP:rs587781242).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073205.
VARIANT 481 481 P -> L (in AS; unknown pathological
significance; dbSNP:rs587780584).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073206.
VARIANT 500 500 R -> P (in AS; unknown pathological
significance; dbSNP:rs587781243).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073207.
VARIANT 501 501 M -> I (common polymorphism; may be
associated with AS; dbSNP:rs587782916).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073208.
VARIANT 568 568 G -> R (in AS; unknown pathological
significance; dbSNP:rs587781233).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073209.
VARIANT 589 589 M -> K (in AS; unknown pathological
significance; dbSNP:rs587781244).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073210.
VARIANT 607 607 E -> Q (in AS; unknown pathological
significance; dbSNP:rs587781235).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073211.
VARIANT 611 611 Q -> E (common polymorphism; may be
associated with AS; dbSNP:rs587782918).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073212.
VARIANT 611 611 Q -> P (common polymorphism; may be
associated with AS; dbSNP:rs587782919).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073213.
VARIANT 679 679 T -> I (in AS; unknown pathological
significance; dbSNP:rs587781236).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073214.
VARIANT 696 696 L -> R (common polymorphism; may be
associated with AS; dbSNP:rs587782920).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073215.
VARIANT 713 713 F -> C (in AS; unknown pathological
significance; dbSNP:rs587781237).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073216.
VARIANT 785 785 V -> I (common polymorphism; may be
associated with AS; dbSNP:rs587782910).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073217.
VARIANT 826 826 I -> II (in AS).
{ECO:0000269|PubMed:9585605}.
/FTId=VAR_008144.
VARIANT 850 850 P -> L (in AS; unknown pathological
significance; dbSNP:rs587781239).
{ECO:0000269|PubMed:25212744}.
/FTId=VAR_073218.
MUTAGEN 750 750 F->D: Disrupt trimer formation, 50-fold
reduction in E3 ligase activity.
{ECO:0000269|PubMed:24273172}.
CONFLICT 359 359 R -> RNLVNEFNSR (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 423 423 P -> L (in Ref. 7; AAA35542).
{ECO:0000305}.
CONFLICT 647 649 TFR -> LFV (in Ref. 7; AAA35542).
{ECO:0000305}.
CONFLICT 669 669 E -> V (in Ref. 7; AAA35542).
{ECO:0000305}.
CONFLICT 686 686 D -> N (in Ref. 7; AAA35542).
{ECO:0000305}.
HELIX 27 41 {ECO:0000244|PDB:2KR1}.
HELIX 65 78 {ECO:0000244|PDB:2KR1}.
HELIX 407 413 {ECO:0000244|PDB:4XR8}.
STRAND 525 527 {ECO:0000244|PDB:1C4Z}.
STRAND 529 531 {ECO:0000244|PDB:1C4Z}.
HELIX 532 545 {ECO:0000244|PDB:1C4Z}.
HELIX 548 552 {ECO:0000244|PDB:1C4Z}.
STRAND 557 559 {ECO:0000244|PDB:1C4Z}.
HELIX 569 582 {ECO:0000244|PDB:1C4Z}.
HELIX 585 587 {ECO:0000244|PDB:1C4Z}.
STRAND 589 592 {ECO:0000244|PDB:1C4Z}.
TURN 594 596 {ECO:0000244|PDB:1C4Z}.
STRAND 599 601 {ECO:0000244|PDB:1C4Z}.
HELIX 609 624 {ECO:0000244|PDB:1C4Z}.
HELIX 635 641 {ECO:0000244|PDB:1C4Z}.
HELIX 648 654 {ECO:0000244|PDB:1C4Z}.
HELIX 656 667 {ECO:0000244|PDB:1C4Z}.
HELIX 672 675 {ECO:0000244|PDB:1C4Z}.
STRAND 679 684 {ECO:0000244|PDB:1C4Z}.
TURN 687 689 {ECO:0000244|PDB:1C4Z}.
STRAND 692 697 {ECO:0000244|PDB:1C4Z}.
TURN 698 702 {ECO:0000244|PDB:1C4Z}.
TURN 707 709 {ECO:0000244|PDB:1C4Z}.
HELIX 710 722 {ECO:0000244|PDB:1C4Z}.
HELIX 727 741 {ECO:0000244|PDB:1C4Z}.
STRAND 742 744 {ECO:0000244|PDB:1C4Z}.
HELIX 753 760 {ECO:0000244|PDB:1C4Z}.
TURN 768 770 {ECO:0000244|PDB:1C4Z}.
STRAND 775 779 {ECO:0000244|PDB:1C4Z}.
HELIX 785 795 {ECO:0000244|PDB:1C4Z}.
HELIX 799 809 {ECO:0000244|PDB:1C4Z}.
STRAND 810 815 {ECO:0000244|PDB:1C4Z}.
HELIX 820 823 {ECO:0000244|PDB:1C4Z}.
STRAND 826 833 {ECO:0000244|PDB:1C4Z}.
STRAND 839 841 {ECO:0000244|PDB:1C4Z}.
HELIX 842 844 {ECO:0000244|PDB:1C4Z}.
STRAND 846 851 {ECO:0000244|PDB:1C4Z}.
HELIX 855 868 {ECO:0000244|PDB:1C4Z}.
SEQUENCE 875 AA; 100688 MW; F80F0502B3B3838A CRC64;
MEKLHQCYWK SGEPQSDDIE ASRMKRAAAK HLIERYYHQL TEGCGNEACT NEFCASCPTF
LRMDNNAAAI KALELYKINA KLCDPHPSKK GASSAYLENS KGAPNNSCSE IKMNKKGARI
DFKDVTYLTE EKVYEILELC REREDYSPLI RVIGRVFSSA EALVQSFRKV KQHTKEELKS
LQAKDEDKDE DEKEKAACSA AAMEEDSEAS SSRIGDSSQG DNNLQKLGPD DVSVDIDAIR
RVYTRLLSNE KIETAFLNAL VYLSPNVECD LTYHNVYSRD PNYLNLFIIV MENRNLHSPE
YLEMALPLFC KAMSKLPLAA QGKLIRLWSK YNADQIRRMM ETFQQLITYK VISNEFNSRN
LVNDDDAIVA ASKCLKMVYY ANVVGGEVDT NHNEEDDEEP IPESSELTLQ ELLGEERRNK
KGPRVDPLET ELGVKTLDCR KPLIPFEEFI NEPLNEVLEM DKDYTFFKVE TENKFSFMTC
PFILNAVTKN LGLYYDNRIR MYSERRITVL YSLVQGQQLN PYLRLKVRRD HIIDDALVRL
EMIAMENPAD LKKQLYVEFE GEQGVDEGGV SKEFFQLVVE EIFNPDIGMF TYDESTKLFW
FNPSSFETEG QFTLIGIVLG LAIYNNCILD VHFPMVVYRK LMGKKGTFRD LGDSHPVLYQ
SLKDLLEYEG NVEDDMMITF QISQTDLFGN PMMYDLKENG DKIPITNENR KEFVNLYSDY
ILNKSVEKQF KAFRRGFHMV TNESPLKYLF RPEEIELLIC GSRNLDFQAL EETTEYDGGY
TRDSVLIREF WEIVHSFTDE QKRLFLQFTT GTDRAPVGGL GKLKMIIAKN GPDTERLPTS
HTCFNVLLLP EYSSKEKLKE RLLKAITYAK GFGML


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EIAAB45117 E3 ubiquitin-protein ligase UBR3,Kiaa2024,Mouse,Mus musculus,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,Ubr3,Zfp650,Zinc finger protein 650,Znf650
EIAAB25831 C1orf166,E3 ubiquitin-protein ligase MUL1,GIDE,Growth inhibition and death E3 ligase,Homo sapiens,Human,MAPL,Mitochondrial ubiquitin ligase activator of NFKB 1,Mitochondrial-anchored protein ligase,MU
EIAAB45115 C6orf133,E3 ubiquitin-protein ligase UBR2,Homo sapiens,Human,KIAA0349,N-recognin-2,Ubiquitin-protein ligase E3-alpha-2,Ubiquitin-protein ligase E3-alpha-II,UBR2
EIAAB44818 Homo sapiens,Human,NICE5,PRO3094,Protein NICE-5,UBE2Q,UBE2Q1,Ubiquitin carrier protein Q1,Ubiquitin-conjugating enzyme E2 Q1,Ubiquitin-protein ligase Q1
EIAAB44908 Cell proliferation-inducing gene 50 protein,Homo sapiens,HSPC150,Human,PIG50,UBE2T,Ubiquitin carrier protein T,Ubiquitin-conjugating enzyme E2 T,Ubiquitin-protein ligase T
10-663-45300 ubiquitin-conjugating enzyme (UBC9) Human - EC 6.3.2.19; SUMO-1-protein ligase; Ubiquitin-conjugating enzyme E2 I; Ubiquitin-protein ligase I; Ubiquitin carrier protein I; Ubiquitin carrier protein 9; 1 mg
10-663-45300 ubiquitin-conjugating enzyme (UBC9) Human - EC 6.3.2.19; SUMO-1-protein ligase; Ubiquitin-conjugating enzyme E2 I; Ubiquitin-protein ligase I; Ubiquitin carrier protein I; Ubiquitin carrier protein 9; 0.05 mg
10-663-45300 ubiquitin-conjugating enzyme (UBC9) Human - EC 6.3.2.19; SUMO-1-protein ligase; Ubiquitin-conjugating enzyme E2 I; Ubiquitin-protein ligase I; Ubiquitin carrier protein I; Ubiquitin carrier protein 9; 0.01 mg
EIAAB45296 Ac2-121,E3 ubiquitin-protein ligase UHRF1,Liver regeneration-related protein LRRG126,Rat,Rattus norvegicus,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing PHD
EIAAB45112 E3 ubiquitin-protein ligase UBR1,Homo sapiens,Human,N-recognin-1,Ubiquitin-protein ligase E3-alpha-1,Ubiquitin-protein ligase E3-alpha-I,UBR1
26-019 KIAA0317 contains 1 filamin repeat and 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain. The exact function of KIAA0317 remains unknown. 0.05 mg
18-003-44311 Ubiquitin-conjugating enzyme E2-25 kDa - EC 6.3.2.19; Ubiquitin-protein ligase; Ubiquitin carrier protein; E2(25K); Huntingtin-interacting protein 2; HIP-2 Polyclonal 0.1 mg Protein A
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
10-002-38076 Ubiquitin Conjugating enzyme 9 human - hUbc9 (E2); EC 6.3.2.19; SUMO-1-protein ligase; Ubiquitin-conjugating enzyme E2 I; Ubiquitin-protein ligase I; Ubiquitin carrier protein I; Ubiquitin carrier pro 0.5 mg
EIAAB44911 Homo sapiens,Human,Probable ubiquitin-conjugating enzyme E2 W,UBE2W,Ubiquitin carrier protein W,Ubiquitin-protein ligase W
EIAAB44790 HBUCE1,Homo sapiens,Human,UBCH5D,UBE2D4,Ubiquitin carrier protein D4,Ubiquitin-conjugating enzyme E2 D4,Ubiquitin-protein ligase D4
EIAAB44801 E217K,Homo sapiens,Human,UBC7,UBE2G,UBE2G1,Ubiquitin carrier protein G1,Ubiquitin-conjugating enzyme E2 G1,Ubiquitin-protein ligase G1


 

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