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E3 ubiquitin-protein ligase ARIH1 (EC 2.3.2.-) (H7-AP2) (HHARI) (Monocyte protein 6) (MOP-6) (Protein ariadne-1 homolog) (ARI-1) (UbcH7-binding protein) (UbcM4-interacting protein) (Ubiquitin-conjugating enzyme E2-binding protein 1)

 ARI1_HUMAN              Reviewed;         557 AA.
Q9Y4X5; B2R6U3; O76026; Q9H3T6; Q9UEN0; Q9UP39;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
10-MAY-2002, sequence version 2.
20-JUN-2018, entry version 170.
RecName: Full=E3 ubiquitin-protein ligase ARIH1;
EC=2.3.2.31 {ECO:0000269|PubMed:15236971, ECO:0000269|PubMed:21532592, ECO:0000269|PubMed:27565346};
AltName: Full=H7-AP2 {ECO:0000303|PubMed:10521492};
AltName: Full=HHARI {ECO:0000303|PubMed:11278816};
AltName: Full=Monocyte protein 6 {ECO:0000303|Ref.10};
Short=MOP-6 {ECO:0000303|Ref.10};
AltName: Full=Protein ariadne-1 homolog {ECO:0000303|Ref.3};
Short=ARI-1 {ECO:0000303|Ref.3};
AltName: Full=UbcH7-binding protein {ECO:0000303|PubMed:11278816};
AltName: Full=UbcM4-interacting protein;
AltName: Full=Ubiquitin-conjugating enzyme E2-binding protein 1 {ECO:0000303|PubMed:10521492};
Name=ARIH1 {ECO:0000312|HGNC:HGNC:689};
Synonyms=ARI, MOP6 {ECO:0000303|Ref.10},
UBCH7BP {ECO:0000303|PubMed:11278816};
ORFNames=HUSSY-27 {ECO:0000303|PubMed:11124703};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=10521492; DOI=10.1074/jbc.274.43.30963;
Moynihan T.P., Ardley H.C., Nuber U., Rose S.A., Jones P.F.,
Markham A.F., Scheffner M., Robinson P.A.;
"The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING
finger/IBR motif-containing domains of HHARI and H7-AP1.";
J. Biol. Chem. 274:30963-30968(1999).
[2]
SEQUENCE REVISION TO 227.
Ardley H.C.;
Submitted (MAY-2002) to UniProtKB.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Trockenbacher A., Marksteiner R., Schneider R.;
"Human ariadne homolog.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[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 [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 95-557.
PubMed=10880484;
Aguilera M., Oliveros M., Martinez-Padron M., Barbas J.A., Ferrus A.;
"Ariadne-1: a vital Drosophila gene is required in development and
defines a new conserved family of ring-finger proteins.";
Genetics 155:1231-1244(2000).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 298-557.
TISSUE=Brain;
PubMed=11124703;
DOI=10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.0.CO;2-H;
Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B.,
Cannata N., Zimbello R., Lanfranchi G., Valle G.;
"Characterization of 16 novel human genes showing high similarity to
yeast sequences.";
Yeast 18:69-80(2001).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 377-557.
TISSUE=Monocyte;
Fujii Y., Takayama K., Ukai Y., Yoshimoto M.;
"Molecular and biological characterization of a new ring finger
protein, MOP-6 which is highly expressed in activated human
monocytes.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[11]
IDENTIFICATION.
PubMed=11124525;
Tan N.G., Ardley H.C., Rose S.A., Leek J.P., Markham A.F.,
Robinson P.A.;
"Characterisation of the human and mouse orthologues of the Drosophila
ariadne gene.";
Cytogenet. Cell Genet. 90:242-245(2000).
[12]
INTERACTION WITH UBE2L3, MUTAGENESIS OF 187-GLN-ILE-188; ILE-188;
CYS-208 AND TYR-258, AND SUBCELLULAR LOCATION.
PubMed=11278816; DOI=10.1074/jbc.M011028200;
Ardley H.C., Tan N.G.S., Rose S.A., Markham A.F., Robinson P.A.;
"Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that
regulate its interaction with the ubiquitin-conjugating enzyme,
Ubch7.";
J. Biol. Chem. 276:19640-19647(2001).
[13]
FUNCTION.
PubMed=14623119; DOI=10.1016/S0014-5793(03)01235-3;
Tan N.G., Ardley H.C., Scott G.B., Rose S.A., Markham A.F.,
Robinson P.A.;
"Human homologue of ariadne promotes the ubiquitylation of translation
initiation factor 4E homologous protein, 4EHP.";
FEBS Lett. 554:501-504(2003).
[14]
FUNCTION.
PubMed=17289916; DOI=10.1101/gad.1521607;
Okumura F., Zou W., Zhang D.E.;
"ISG15 modification of the eIF4E cognate 4EHP enhances cap structure-
binding activity of 4EHP.";
Genes Dev. 21:255-260(2007).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
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).
[17]
FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, INTERACTION WITH
UBE2L3, ACTIVE SITE, DOMAIN, AND MUTAGENESIS OF CYS-357.
PubMed=21532592; DOI=10.1038/nature09966;
Wenzel D.M., Lissounov A., Brzovic P.S., Klevit R.E.;
"UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT
hybrids.";
Nature 474:105-108(2011).
[18]
SUBCELLULAR LOCATION.
PubMed=21590270; DOI=10.1007/s12031-011-9535-1;
Parelkar S.S., Cadena J.G., Kim C., Wang Z., Sugal R., Bentley B.,
Moral L., Ardley H.C., Schwartz L.M.;
"The parkin-like human homolog of Drosophila ariadne-1 (HHARI) can
induce aggresome formation in mammalian cells and is immunologically
detectable in Lewy bodies.";
J. Mol. Neurosci. 46:109-121(2012).
[19]
FUNCTION, INTERACTION WITH UBE2L3, INTERACTION WITH CULLIN-RING
COMPLEXES, ENZYME REGULATION, AND MUTAGENESIS OF HIS-205.
PubMed=24076655; DOI=10.1038/emboj.2013.209;
Kelsall I.R., Duda D.M., Olszewski J.L., Hofmann K., Knebel A.,
Langevin F., Wood N., Wightman M., Schulman B.A., Alpi A.F.;
"TRIAD1 and HHARI bind to and are activated by distinct neddylated
Cullin-RING ligase complexes.";
EMBO J. 32:2848-2860(2013).
[20]
SUBCELLULAR LOCATION.
PubMed=23059369; DOI=10.1016/j.yexcr.2012.10.002;
Elmehdawi F., Wheway G., Szymanska K., Adams M., High A.S.,
Johnson C.A., Robinson P.A.;
"Human homolog of drosophila ariadne (HHARI) is a marker of cellular
proliferation associated with nuclear bodies.";
Exp. Cell Res. 319:161-172(2013).
[21]
FUNCTION, AND INDUCTION.
PubMed=25624349; DOI=10.1128/MCB.01152-14;
von Stechow L., Typas D., Carreras Puigvert J., Oort L., Siddappa R.,
Pines A., Vrieling H., van de Water B., Mullenders L.H., Danen E.H.;
"The E3 ubiquitin ligase ARIH1 protects against genotoxic stress by
initiating a 4EHP-mediated mRNA translation arrest.";
Mol. Cell. Biol. 35:1254-1268(2015).
[22]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3, INTERACTION
WITH CULLIN-RING COMPLEXES, ENZYME REGULATION, AND MUTAGENESIS OF
VAL-123; PHE-150; 156-LYS--PHE-158; ILE-188; 257-LYS-TYR-258;
265-SER--VAL-267; 340-ASN-THR-341; 342-LYS-GLU-343; 531-ILE-GLU-352;
ASN-358; HIS-359; 378-PRO-TRP-379; 383-GLY--ALA-385; TRP-386; TYR-417;
420-ARG--ASN-423; 430-PHE-GLU-431; TYR-476; GLU-492; ASN-493; GLN-495;
GLU-499; GLU-503 AND TYR-531.
PubMed=27565346; DOI=10.1016/j.cell.2016.07.027;
Scott D.C., Rhee D.Y., Duda D.M., Kelsall I.R., Olszewski J.L.,
Paulo J.A., de Jong A., Ovaa H., Alpi A.F., Harper J.W.,
Schulman B.A.;
"Two distinct types of E3 ligases work in unison to regulate substrate
ubiquitylation.";
Cell 166:1198-1214(2016).
[23]
STRUCTURE BY NMR OF 336-394 IN COMPLEX WITH ZINC, FUNCTION, CATALYTIC
ACTIVITY, AND MUTAGENESIS OF CYS-347; ILE-351; CYS-357; HIS-359;
CYS-367; PHE-371; CYS-372; TRP-373; TRP-379 AND TRP-386.
PubMed=15236971; DOI=10.1016/j.jmb.2004.05.035;
Capili A.D., Edghill E.L., Wu K., Borden K.L.;
"Structure of the C-terminal RING finger from a RING-IBR-RING/TRIAD
motif reveals a novel zinc-binding domain distinct from a RING.";
J. Mol. Biol. 340:1117-1129(2004).
[24]
STRUCTURE BY NMR OF 325-396 OF MUTANT CYS-357 IN COMPLEX WITH ZINC,
AND MUTAGENESIS OF CYS-357.
PubMed=24058416; DOI=10.1371/journal.pone.0074047;
Spratt D.E., Mercier P., Shaw G.S.;
"Structure of the HHARI catalytic domain shows glimpses of a HECT E3
ligase.";
PLoS ONE 8:E74047-E74047(2013).
[25]
X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) IN COMPLEX WITH ZINC, ACTIVE
SITE, DOMAIN, ENZYME REGULATION, INTERACTION WITH UBE2L3, FUNCTION,
AND MUTAGENESIS OF ILE-188; PHE-416; 420-ARG--ASN-423; SER-427;
430-PHE-GLU-431 AND GLU-503.
PubMed=23707686; DOI=10.1016/j.str.2013.04.019;
Duda D.M., Olszewski J.L., Schuermann J.P., Kurinov I., Miller D.J.,
Nourse A., Alpi A.F., Schulman B.A.;
"Structure of HHARI, a RING-IBR-RING ubiquitin ligase: autoinhibition
of an Ariadne-family E3 and insights into ligation mechanism.";
Structure 21:1030-1041(2013).
-!- FUNCTION: E3 ubiquitin-protein ligase, which catalyzes
ubiquitination of target proteins together with ubiquitin-
conjugating enzyme E2 UBE2L3 (PubMed:15236971, PubMed:21532592,
PubMed:24076655, PubMed:27565346, PubMed:23707686). Acts as an
atypical E3 ubiquitin-protein ligase by working together with
cullin-RING ubiquitin ligase (CRL) complexes and initiating
ubiquitination of CRL substrates: associates with CRL complexes
and specifically mediates addition of the first ubiquitin on CRLs
targets (PubMed:27565346). The initial ubiquitin is then elongated
by CDC34/UBE2R1 and UBE2R2 (PubMed:27565346). E3 ubiquitin-protein
ligase activity is activated upon binding to neddylated cullin-
RING ubiquitin ligase complexes (PubMed:24076655,
PubMed:27565346). Plays a role in protein translation in response
to DNA damage by mediating ubiquitination of EIF4E2, the
consequences of EIF4E2 ubiquitination are however unclear
(PubMed:25624349). According to a report, EIF4E2 ubiquitination
leads to promote EIF4E2 cap-binding and protein translation arrest
(PubMed:25624349). According to another report EIF4E2
ubiquitination leads to its subsequent degradation
(PubMed:14623119). Acts as the ligase involved in ISGylation of
EIF4E2 (PubMed:17289916). {ECO:0000269|PubMed:14623119,
ECO:0000269|PubMed:15236971, ECO:0000269|PubMed:17289916,
ECO:0000269|PubMed:21532592, ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:24076655, ECO:0000269|PubMed:25624349,
ECO:0000269|PubMed:27565346}.
-!- CATALYTIC ACTIVITY: [E2 ubiquitin-conjugating enzyme]-S-
ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2
ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-
N(6)-ubiquitinyl-L-lysine. {ECO:0000269|PubMed:15236971,
ECO:0000269|PubMed:21532592, ECO:0000269|PubMed:27565346}.
-!- ENZYME REGULATION: Autoinhibited by the ariadne domain, which
masks the second RING-type zinc finger that contains the active
site and inhibits the E3 activity (PubMed:23707686). Inhibition is
relieved upon binding to neddylated cullin-RING ubiquitin ligase
complexes, which activate the E3 ligase activity of ARIH1
(PubMed:24076655, PubMed:27565346). {ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:24076655, ECO:0000269|PubMed:27565346}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts (via the first RING-type zinc finger) with
UBE2L3 (PubMed:11278816, PubMed:21532592, PubMed:24076655,
PubMed:23707686). Associates with cullin-RING ubiquitin ligase
(CRL) complexes containing CUL1, CUL2 and CUL3 (PubMed:24076655,
PubMed:27565346). Interacts with neddylated CUL1 (PubMed:24076655,
PubMed:27565346). Interacts with neddylated CUL2 (PubMed:24076655,
PubMed:27565346). Interacts with neddylated CUL3 (PubMed:24076655,
PubMed:27565346). Interacts with neddylated CUL4A
(PubMed:24076655). {ECO:0000269|PubMed:11278816,
ECO:0000269|PubMed:21532592, ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:24076655, ECO:0000269|PubMed:27565346}.
-!- INTERACTION:
Q13616:CUL1; NbExp=6; IntAct=EBI-2514233, EBI-359390;
P68036:UBE2L3; NbExp=5; IntAct=EBI-2514233, EBI-711173;
P68036-1:UBE2L3; NbExp=3; IntAct=EBI-2514233, EBI-15556257;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11278816,
ECO:0000269|PubMed:21590270, ECO:0000269|PubMed:23059369}. Nucleus
{ECO:0000269|PubMed:23059369}. Nucleus, Cajal body
{ECO:0000269|PubMed:23059369}. Note=Mainly cytoplasmic
(PubMed:11278816). Present in Lewy body (PubMed:21590270).
{ECO:0000269|PubMed:11278816, ECO:0000269|PubMed:21590270}.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:10521492}.
-!- INDUCTION: Up-regulated following DNA damage (PubMed:25624349).
{ECO:0000269|PubMed:25624349}.
-!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
interact with the E2 conjugating enzyme UBE2L3 and function like
HECT-type E3 enzymes: they bind E2s via the first RING-type zinc
finger, but require an obligate trans-thiolation step during the
ubiquitin transfer, requiring a conserved active site Cys residue
in the second RING-type zinc finger (PubMed:21532592,
PubMed:23707686). The active site probably forms a thioester
intermediate with ubiquitin taken from the active-site cysteine of
the E2 before ultimately transferring it to a Lys residue on the
substrate (PubMed:21532592, PubMed:23707686).
{ECO:0000269|PubMed:21532592, ECO:0000269|PubMed:23707686}.
-!- DOMAIN: The Ariadne domain inhibits activity by masking the second
RING-type zinc finger that contains the active site
(PubMed:23707686). {ECO:0000269|PubMed:23707686}.
-!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
{ECO:0000305}.
-!- CAUTION: The RING-type 2 zinc finger was initially reported to
only bind 1 zinc ion instead of 2 compared to classical RING-types
(PubMed:15236971). But it was later shown that it is not the case
and binds 2 zinc ions (PubMed:24058416, PubMed:23707686).
{ECO:0000269|PubMed:15236971, ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:24058416}.
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EMBL; AJ243190; CAB45870.1; -; mRNA.
EMBL; AF072832; AAD28088.1; -; mRNA.
EMBL; AK312715; BAG35590.1; -; mRNA.
EMBL; AC079322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC100827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471082; EAW77907.1; -; Genomic_DNA.
EMBL; BC051877; AAH51877.1; -; mRNA.
EMBL; AJ130976; CAA10274.1; -; mRNA.
EMBL; AJ009771; CAA08817.1; -; mRNA.
EMBL; AB014774; BAB19786.1; -; mRNA.
CCDS; CCDS10244.1; -.
RefSeq; NP_005735.2; NM_005744.3.
UniGene; Hs.268787; -.
PDB; 1WD2; NMR; -; A=336-394.
PDB; 2M9Y; NMR; -; A=325-396.
PDB; 4KBL; X-ray; 3.30 A; A/B=1-557.
PDB; 4KC9; X-ray; 3.60 A; A=1-557.
PDB; 5TTE; X-ray; 3.50 A; B=1-557.
PDB; 5UDH; X-ray; 3.24 A; A/B=90-557.
PDBsum; 1WD2; -.
PDBsum; 2M9Y; -.
PDBsum; 4KBL; -.
PDBsum; 4KC9; -.
PDBsum; 5TTE; -.
PDBsum; 5UDH; -.
ProteinModelPortal; Q9Y4X5; -.
SMR; Q9Y4X5; -.
BioGrid; 117348; 110.
DIP; DIP-53626N; -.
IntAct; Q9Y4X5; 12.
MINT; Q9Y4X5; -.
STRING; 9606.ENSP00000369217; -.
iPTMnet; Q9Y4X5; -.
PhosphoSitePlus; Q9Y4X5; -.
BioMuta; ARIH1; -.
DMDM; 20532376; -.
EPD; Q9Y4X5; -.
MaxQB; Q9Y4X5; -.
PaxDb; Q9Y4X5; -.
PeptideAtlas; Q9Y4X5; -.
PRIDE; Q9Y4X5; -.
ProteomicsDB; 86264; -.
Ensembl; ENST00000379887; ENSP00000369217; ENSG00000166233.
GeneID; 25820; -.
KEGG; hsa:25820; -.
UCSC; uc002aut.5; human.
CTD; 25820; -.
DisGeNET; 25820; -.
EuPathDB; HostDB:ENSG00000166233.12; -.
GeneCards; ARIH1; -.
H-InvDB; HIX0012409; -.
HGNC; HGNC:689; ARIH1.
HPA; HPA003295; -.
HPA; HPA073245; -.
MIM; 605624; gene.
neXtProt; NX_Q9Y4X5; -.
OpenTargets; ENSG00000166233; -.
PharmGKB; PA24982; -.
eggNOG; KOG1815; Eukaryota.
eggNOG; ENOG410XP9Y; LUCA.
GeneTree; ENSGT00890000139392; -.
HOGENOM; HOG000216612; -.
HOVERGEN; HBG018737; -.
InParanoid; Q9Y4X5; -.
KO; K11968; -.
OMA; LARYLHY; -.
OrthoDB; EOG091G01SC; -.
PhylomeDB; Q9Y4X5; -.
TreeFam; TF300805; -.
BRENDA; 2.3.2.B10; 2681.
BRENDA; 6.3.2.19; 2681.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
UniPathway; UPA00143; -.
ChiTaRS; ARIH1; human.
EvolutionaryTrace; Q9Y4X5; -.
GeneWiki; ARIH1; -.
GenomeRNAi; 25820; -.
PRO; PR:Q9Y4X5; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000166233; -.
CleanEx; HS_ARIH1; -.
ExpressionAtlas; Q9Y4X5; baseline and differential.
Genevisible; Q9Y4X5; HS.
GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0097413; C:Lewy body; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; TAS:UniProtKB.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0019787; F:ubiquitin-like protein transferase activity; TAS:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR031127; E3_UB_ligase_RBR.
InterPro; IPR002867; IBR_dom.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR11685; PTHR11685; 1.
Pfam; PF01485; IBR; 2.
SMART; SM00647; IBR; 2.
SMART; SM00184; RING; 2.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Metal-binding; Nucleus; Reference proteome; Repeat; Transferase;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 557 E3 ubiquitin-protein ligase ARIH1.
/FTId=PRO_0000055752.
ZN_FING 186 236 RING-type 1; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
ZN_FING 256 317 IBR-type.
ZN_FING 344 375 RING-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 105 153 UBA-like. {ECO:0000305|PubMed:23707686}.
REGION 408 557 Ariadne domain.
{ECO:0000305|PubMed:23707686}.
ACT_SITE 357 357 {ECO:0000269|PubMed:21532592,
ECO:0000269|PubMed:23707686}.
METAL 186 186 Zinc 1. {ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 189 189 Zinc 1. {ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 203 203 Zinc 2. {ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 205 205 Zinc 2; via pros nitrogen.
{ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 208 208 Zinc 1. {ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 211 211 Zinc 1. {ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 231 231 Zinc 2. {ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 236 236 Zinc 2. {ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 276 276 Zinc 3. {ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 281 281 Zinc 3. {ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 297 297 Zinc 3. {ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 299 299 Zinc 3. {ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 304 304 Zinc 4. {ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 307 307 Zinc 4. {ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 312 312 Zinc 4; via tele nitrogen.
{ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 317 317 Zinc 4. {ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686}.
METAL 344 344 Zinc 5. {ECO:0000244|PDB:1WD2,
ECO:0000244|PDB:2M9Y,
ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:15236971,
ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:24058416}.
METAL 347 347 Zinc 5. {ECO:0000244|PDB:1WD2,
ECO:0000244|PDB:2M9Y,
ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:15236971,
ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:24058416}.
METAL 362 362 Zinc 5. {ECO:0000244|PDB:1WD2,
ECO:0000244|PDB:2M9Y,
ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:15236971,
ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:24058416}.
METAL 367 367 Zinc 5. {ECO:0000244|PDB:1WD2,
ECO:0000244|PDB:2M9Y,
ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:15236971,
ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:24058416}.
METAL 372 372 Zinc 6. {ECO:0000244|PDB:2M9Y,
ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:24058416}.
METAL 375 375 Zinc 6. {ECO:0000244|PDB:2M9Y,
ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:24058416}.
METAL 382 382 Zinc 6; via tele nitrogen.
{ECO:0000244|PDB:2M9Y,
ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:24058416}.
METAL 389 389 Zinc 6. {ECO:0000244|PDB:2M9Y,
ECO:0000244|PDB:4KBL,
ECO:0000244|PDB:4KC9,
ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:24058416}.
MOD_RES 142 142 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Z1K5}.
MUTAGEN 123 123 V->A: Strongly decreased ability to
initiate ubiquitination of cullin-RING
complexes. {ECO:0000269|PubMed:27565346}.
MUTAGEN 150 150 F->A: Strongly decreased ability to
initiate ubiquitination of cullin-RING
complexes. {ECO:0000269|PubMed:27565346}.
MUTAGEN 156 158 KLF->AAA: Strongly decreased ability to
initiate ubiquitination of cullin-RING
complexes. {ECO:0000269|PubMed:27565346}.
MUTAGEN 187 188 QI->HV: No loss of interaction with
UBE2L3. {ECO:0000269|PubMed:11278816}.
MUTAGEN 188 188 I->A: Loss of interaction with UBE2L3.
Decreased E3 ligase activity. Strongly
decreased ability to initiate
ubiquitination of cullin-RING complexes.
{ECO:0000269|PubMed:11278816,
ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:27565346}.
MUTAGEN 205 205 H->A: Impaired interaction with UBE2L3
without affecting interaction with
neddylated cullin-RING complexes.
{ECO:0000269|PubMed:24076655}.
MUTAGEN 208 208 C->A,H: Loss of interaction with UBE2L3.
{ECO:0000269|PubMed:11278816}.
MUTAGEN 257 258 KY->AAA: Strongly decreased ability to
initiate ubiquitination of cullin-RING
complexes. {ECO:0000269|PubMed:27565346}.
MUTAGEN 258 258 Y->A: No loss of interaction with UBE2L3.
{ECO:0000269|PubMed:11278816}.
MUTAGEN 265 267 SFV->AAA: Strongly decreased ability to
initiate ubiquitination of cullin-RING
complexes. {ECO:0000269|PubMed:27565346}.
MUTAGEN 340 341 NT->AA: Strongly decreased ability to
initiate ubiquitination of cullin-RING
complexes. {ECO:0000269|PubMed:27565346}.
MUTAGEN 342 343 KE->AA: Strongly decreased ability to
initiate ubiquitination of cullin-RING
complexes. {ECO:0000269|PubMed:27565346}.
MUTAGEN 347 347 C->A: Impairs zinc-binding and folding.
Abolishes E3 ubiquitin-protein ligase
activity. {ECO:0000269|PubMed:15236971}.
MUTAGEN 351 352 IE->AA: Strongly decreased ability to
initiate ubiquitination of cullin-RING
complexes. {ECO:0000269|PubMed:27565346}.
MUTAGEN 351 351 I->A: Disrupts the hydrophobic network.
Abolishes E3 ubiquitin-protein ligase
activity. {ECO:0000269|PubMed:15236971}.
MUTAGEN 357 357 C->A,S: Does not affect zinc binding and
folding. Abolishes ability to transfer
ubiquitin and E3 ubiquitin-protein ligase
activity. {ECO:0000269|PubMed:15236971,
ECO:0000269|PubMed:21532592,
ECO:0000269|PubMed:24058416,
ECO:0000269|PubMed:24076655}.
MUTAGEN 358 358 N->A: Defects in ligation.
{ECO:0000269|PubMed:27565346}.
MUTAGEN 359 359 H->A: Defects in ligation. Does not
affect zinc binding, folding. Does not
impair E3 ubiquitin-protein ligase
activity. {ECO:0000269|PubMed:15236971,
ECO:0000269|PubMed:27565346}.
MUTAGEN 367 367 C->A: Impairs zinc-binding and folding.
Abolishes E3 ubiquitin-protein ligase
activity. {ECO:0000269|PubMed:15236971}.
MUTAGEN 371 371 F->A: Disrupts the hydrophobic network.
Abolishes E3 ubiquitin-protein ligase
activity. {ECO:0000269|PubMed:15236971}.
MUTAGEN 372 372 C->A: Impairs E3 ubiquitin-protein ligase
activity. {ECO:0000269|PubMed:15236971}.
MUTAGEN 373 373 W->A: Abolishes E3 ubiquitin-protein
ligase activity.
{ECO:0000269|PubMed:15236971}.
MUTAGEN 378 379 PW->AA: Defects in ligation.
{ECO:0000269|PubMed:27565346}.
MUTAGEN 379 379 W->A: Does not affect E3 ubiquitin-
protein ligase activity.
{ECO:0000269|PubMed:15236971}.
MUTAGEN 383 385 GSA->AAD: Defects in ligation.
{ECO:0000269|PubMed:27565346}.
MUTAGEN 386 386 W->A: Does not affect E3 ubiquitin-
protein ligase activity. Strongly
decreased ability to initiate
ubiquitination of cullin-RING complexes.
{ECO:0000269|PubMed:15236971,
ECO:0000269|PubMed:27565346}.
MUTAGEN 416 416 F->A: Slightly relieves autoinhibition of
the E3 ligase activity by the ariadne
domain. {ECO:0000269|PubMed:23707686}.
MUTAGEN 417 417 Y->A: Hyperactive 'open' mutant that
displays enhanced E3 ubiquitin-protein
ligase activity.
{ECO:0000269|PubMed:27565346}.
MUTAGEN 420 423 RYMN->AYMA: Slightly relieves
autoinhibition of the E3 ligase activity
by the ariadne domain. Hyperactive 'open'
mutant that displays enhanced E3
ubiquitin-protein ligase activity; when
associated with A-503.
{ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:27565346}.
MUTAGEN 427 427 S->A: Slightly relieves autoinhibition of
the E3 ligase activity by the ariadne
domain. {ECO:0000269|PubMed:23707686}.
MUTAGEN 430 431 FE->AA: Relieves autoinhibition of the E3
ligase activity by the ariadne domain;
when associated with A-503. Hyperactive
'open' mutant that displays enhanced E3
ubiquitin-protein ligase activity; when
associated with A-503.
{ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:24076655,
ECO:0000269|PubMed:27565346}.
MUTAGEN 476 476 Y->A: Hyperactive 'open' mutant that
displays enhanced E3 ubiquitin-protein
ligase activity.
{ECO:0000269|PubMed:27565346}.
MUTAGEN 492 492 E->A: Hyperactive 'open' mutant that
displays enhanced E3 ubiquitin-protein
ligase activity.
{ECO:0000269|PubMed:27565346}.
MUTAGEN 493 493 N->A: Hyperactive 'open' mutant that
displays enhanced E3 ubiquitin-protein
ligase activity.
{ECO:0000269|PubMed:27565346}.
MUTAGEN 495 495 Q->A: Hyperactive 'open' mutant that
displays enhanced E3 ubiquitin-protein
ligase activity.
{ECO:0000269|PubMed:27565346}.
MUTAGEN 499 499 E->A: Hyperactive 'open' mutant that
displays enhanced E3 ubiquitin-protein
ligase activity.
{ECO:0000269|PubMed:27565346}.
MUTAGEN 503 503 E->A: Relieves autoinhibition of the E3
ligase activity by the ariadne domain;
when associated with 430-A-A-431.
Hyperactive 'open' mutant that displays
enhanced E3 ubiquitin-protein ligase
activity; when associated with 430-A-A-
431. Hyperactive 'open' mutant that
displays enhanced E3 ubiquitin-protein
ligase activity; when associated with
420-A--A-423.
{ECO:0000269|PubMed:23707686,
ECO:0000269|PubMed:24076655,
ECO:0000269|PubMed:27565346}.
MUTAGEN 531 531 Y->A: Strongly decreased ability to
initiate ubiquitination of cullin-RING
complexes. {ECO:0000269|PubMed:27565346}.
CONFLICT 122 122 E -> D (in Ref. 3; AAD28088).
{ECO:0000305}.
CONFLICT 227 227 Q -> H (in Ref. 1; CAB45870).
{ECO:0000305}.
CONFLICT 237 237 D -> N (in Ref. 8; CAA10274).
{ECO:0000305}.
CONFLICT 303 303 F -> S (in Ref. 9; CAA08817).
{ECO:0000305}.
CONFLICT 309 316 ENWHDPVK -> AIGMILFQ (in Ref. 9;
CAA08817). {ECO:0000305}.
CONFLICT 322 322 K -> T (in Ref. 9; CAA08817).
{ECO:0000305}.
STRAND 101 105 {ECO:0000244|PDB:5UDH}.
HELIX 106 124 {ECO:0000244|PDB:5UDH}.
HELIX 128 137 {ECO:0000244|PDB:5UDH}.
TURN 138 140 {ECO:0000244|PDB:5UDH}.
HELIX 142 149 {ECO:0000244|PDB:5UDH}.
HELIX 154 161 {ECO:0000244|PDB:5UDH}.
TURN 187 189 {ECO:0000244|PDB:5UDH}.
HELIX 195 197 {ECO:0000244|PDB:5UDH}.
STRAND 198 200 {ECO:0000244|PDB:5UDH}.
STRAND 206 208 {ECO:0000244|PDB:5UDH}.
HELIX 209 219 {ECO:0000244|PDB:5UDH}.
STRAND 220 224 {ECO:0000244|PDB:4KBL}.
STRAND 232 235 {ECO:0000244|PDB:5UDH}.
HELIX 242 248 {ECO:0000244|PDB:5UDH}.
HELIX 252 268 {ECO:0000244|PDB:5UDH}.
STRAND 273 275 {ECO:0000244|PDB:5UDH}.
STRAND 283 289 {ECO:0000244|PDB:5UDH}.
STRAND 294 296 {ECO:0000244|PDB:5UDH}.
STRAND 298 300 {ECO:0000244|PDB:5UDH}.
STRAND 302 304 {ECO:0000244|PDB:5UDH}.
TURN 305 307 {ECO:0000244|PDB:5UDH}.
HELIX 317 325 {ECO:0000244|PDB:5UDH}.
TURN 326 328 {ECO:0000244|PDB:5UDH}.
TURN 331 333 {ECO:0000244|PDB:2M9Y}.
HELIX 337 340 {ECO:0000244|PDB:2M9Y}.
STRAND 341 343 {ECO:0000244|PDB:5UDH}.
TURN 345 347 {ECO:0000244|PDB:5UDH}.
STRAND 350 352 {ECO:0000244|PDB:5UDH}.
STRAND 359 361 {ECO:0000244|PDB:5UDH}.
STRAND 364 366 {ECO:0000244|PDB:5UDH}.
STRAND 370 372 {ECO:0000244|PDB:5UDH}.
TURN 373 375 {ECO:0000244|PDB:5UDH}.
STRAND 378 386 {ECO:0000244|PDB:5UDH}.
HELIX 411 432 {ECO:0000244|PDB:5UDH}.
HELIX 434 444 {ECO:0000244|PDB:5UDH}.
HELIX 452 480 {ECO:0000244|PDB:5UDH}.
HELIX 486 510 {ECO:0000244|PDB:5UDH}.
TURN 511 515 {ECO:0000244|PDB:5UDH}.
STRAND 518 520 {ECO:0000244|PDB:5UDH}.
HELIX 521 548 {ECO:0000244|PDB:5UDH}.
SEQUENCE 557 AA; 64118 MW; DFFF8965DAB41DC8 CRC64;
MDSDEGYNYE FDEDEECSEE DSGAEEEEDE DDDEPDDDTL DLGEVELVEP GLGVGGERDG
LLCGETGGGG GSALGPGGGG GGGGGGGGGG PGHEQEEDYR YEVLTAEQIL QHMVECIREV
NEVIQNPATI TRILLSHFNW DKEKLMERYF DGNLEKLFAE CHVINPSKKS RTRQMNTRSS
AQDMPCQICY LNYPNSYFTG LECGHKFCMQ CWSEYLTTKI MEEGMGQTIS CPAHGCDILV
DDNTVMRLIT DSKVKLKYQH LITNSFVECN RLLKWCPAPD CHHVVKVQYP DAKPVRCKCG
RQFCFNCGEN WHDPVKCKWL KKWIKKCDDD SETSNWIAAN TKECPKCHVT IEKDGGCNHM
VCRNQNCKAE FCWVCLGPWE PHGSAWYNCN RYNEDDAKAA RDAQERSRAA LQRYLFYCNR
YMNHMQSLRF EHKLYAQVKQ KMEEMQQHNM SWIEVQFLKK AVDVLCQCRA TLMYTYVFAF
YLKKNNQSII FENNQADLEN ATEVLSGYLE RDISQDSLQD IKQKVQDKYR YCESRRRVLL
QHVHEGYEKD LWEYIED


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18-003-43760 Ubiquitin-conjugating enzyme E2 L3 - EC 6.3.2.19; Ubiquitin-protein ligase L3; Ubiquitin carrier protein L3; UbcH7; E2-F1; L-UBC Polyclonal 0.1 mg Protein A
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
EIAAB44901 Homo sapiens,Human,KIAA1734,UBE2O,Ubiquitin carrier protein O,Ubiquitin-conjugating enzyme E2 O,Ubiquitin-conjugating enzyme E2 of 230 kDa,Ubiquitin-conjugating enzyme E2-230K,Ubiquitin-protein ligase


 

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