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E3 ubiquitin-protein ligase UBR5 (EC 2.3.2.26) (E3 ubiquitin-protein ligase, HECT domain-containing 1) (HECT-type E3 ubiquitin transferase UBR5) (Hyperplastic discs protein homolog)

 UBR5_MOUSE              Reviewed;        2792 AA.
Q80TP3; Q698K9; Q6PEQ8; Q6PFQ9; Q80VL4; Q810V6; Q9CXE9;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
27-SEP-2005, sequence version 2.
23-MAY-2018, entry version 142.
RecName: Full=E3 ubiquitin-protein ligase UBR5;
EC=2.3.2.26;
AltName: Full=E3 ubiquitin-protein ligase, HECT domain-containing 1;
AltName: Full=HECT-type E3 ubiquitin transferase UBR5;
AltName: Full=Hyperplastic discs protein homolog;
Name=Ubr5; Synonyms=Edd, Edd1, Kiaa0896;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=C57BL/6J;
PubMed=15282321; DOI=10.1128/MCB.24.16.7225-7234.2004;
Saunders D.N., Hird S.L., Withington S.L., Dunwoodie S.L.,
Henderson M.J., Biben C., Sutherland R.L., Ormandy C.J., Watts C.K.W.;
"Edd, the murine hyperplastic disc gene, is essential for yolk sac
vascularization and chorioallantoic fusion.";
Mol. Cell. Biol. 24:7225-7234(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1028-2792.
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1292-2792.
STRAIN=FVB/N-3; TISSUE=Eye, Liver, and Mammary gland;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2483-2792.
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
FUNCTION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16055722; DOI=10.1128/MCB.25.16.7120-7136.2005;
Tasaki T., Mulder L.C.F., Iwamatsu A., Lee M.J., Davydov I.V.,
Varshavsky A., Muesing M., Kwon Y.T.;
"A family of mammalian E3 ubiquitin ligases that contain the UBR box
motif and recognize N-degrons.";
Mol. Cell. Biol. 25:7120-7136(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the
N-end rule pathway. Ubiquitinates acetylated PCK1. Also acts as a
regulator of DNA damage response by acting as a suppressor of
RNF168, an E3 ubiquitin-protein ligase that promotes accumulation
of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites,
thereby acting as a guard against excessive spreading of
ubiquitinated chromatin at damaged chromosomes (By similarity).
Recognizes and binds to proteins bearing specific N-terminal
residues that are destabilizing according to the N-end rule,
leading to their ubiquitination and subsequent degradation.
Involved in maturation and/or transcriptional regulation of mRNA
by activating CDK9 by polyubiquitination. May play a role in
control of cell cycle progression. May have tumor suppressor
function. Plays an essential role in extraembryonic development.
Regulates DNA topoisomerase II binding protein (TopBP1) for the
DNA damage response. {ECO:0000250, ECO:0000269|PubMed:15282321,
ECO:0000269|PubMed:16055722}.
-!- 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: Binds TOPBP1. Associates with CDK9 and TFIIS/TCEA1 and
forms a transcription regulatory complex made of CDK9, RNAP II,
UBR5 and TFIIS/TCEA1 that can stimulate target gene transcription
by recruiting their promoters. Associates with the E3 ligase
complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 proteins (EDVP
complex). Interacts directly with DYRK2. Interacts with PIH1D1.
{ECO:0000250|UniProtKB:O95071}.
-!- INTERACTION:
Q3U2S4-1:Otud5; NbExp=2; IntAct=EBI-2553642, EBI-16131219;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-
thioester formation.
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EMBL; AY550908; AAT28194.1; -; mRNA.
EMBL; AK122398; BAC65680.1; -; mRNA.
EMBL; BC049162; AAH49162.1; -; mRNA.
EMBL; BC049224; AAH49224.1; -; mRNA.
EMBL; BC057458; AAH57458.1; -; mRNA.
EMBL; BC057923; AAH57923.1; -; mRNA.
EMBL; AK014485; BAB29387.1; -; mRNA.
RefSeq; NP_001074828.2; NM_001081359.3.
RefSeq; NP_001106192.1; NM_001112721.2.
UniGene; Mm.476840; -.
ProteinModelPortal; Q80TP3; -.
SMR; Q80TP3; -.
BioGrid; 214255; 32.
DIP; DIP-56890N; -.
IntAct; Q80TP3; 12.
STRING; 10090.ENSMUSP00000105965; -.
iPTMnet; Q80TP3; -.
PhosphoSitePlus; Q80TP3; -.
EPD; Q80TP3; -.
MaxQB; Q80TP3; -.
PaxDb; Q80TP3; -.
PeptideAtlas; Q80TP3; -.
PRIDE; Q80TP3; -.
GeneID; 70790; -.
KEGG; mmu:70790; -.
CTD; 51366; -.
MGI; MGI:1918040; Ubr5.
eggNOG; KOG0943; Eukaryota.
eggNOG; COG5021; LUCA.
HOVERGEN; HBG096012; -.
InParanoid; Q80TP3; -.
KO; K10593; -.
PhylomeDB; Q80TP3; -.
UniPathway; UPA00143; -.
ChiTaRS; Ubr5; mouse.
PRO; PR:Q80TP3; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:HGNC.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:2000780; P:negative regulation of double-strand break repair; ISS:UniProtKB.
GO; GO:1901315; P:negative regulation of histone H2A K63-linked ubiquitination; ISS:UniProtKB.
GO; GO:1905077; P:negative regulation of interleukin-17 secretion; IGI:MGI.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; ISO:MGI.
GO; GO:0050847; P:progesterone receptor signaling pathway; ISS:HGNC.
GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:MGI.
GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
CDD; cd14423; CUE_UBR5; 1.
InterPro; IPR024725; E3_UbLigase_EDD_UBA.
InterPro; IPR000569; HECT_dom.
InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
InterPro; IPR036053; PABP-dom.
InterPro; IPR002004; PABP_HYD.
InterPro; IPR009091; RCC1/BLIP-II.
InterPro; IPR003126; Znf_UBR.
Pfam; PF11547; E3_UbLigase_EDD; 1.
Pfam; PF00632; HECT; 1.
Pfam; PF00658; PABP; 1.
SMART; SM00119; HECTc; 1.
SMART; SM00517; PolyA; 1.
SMART; SM00396; ZnF_UBR1; 1.
SUPFAM; SSF50985; SSF50985; 1.
SUPFAM; SSF56204; SSF56204; 2.
SUPFAM; SSF63570; SSF63570; 1.
PROSITE; PS50237; HECT; 1.
PROSITE; PS51309; PABC; 1.
PROSITE; PS51157; ZF_UBR; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; DNA damage; DNA repair; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Transferase;
Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O95071}.
CHAIN 2 2792 E3 ubiquitin-protein ligase UBR5.
/FTId=PRO_0000086932.
DOMAIN 2371 2448 PABC. {ECO:0000255|PROSITE-
ProRule:PRU00641}.
DOMAIN 2455 2792 HECT. {ECO:0000255|PROSITE-
ProRule:PRU00104}.
ZN_FING 1171 1239 UBR-type. {ECO:0000255|PROSITE-
ProRule:PRU00508}.
COMPBIAS 934 939 Poly-Glu.
COMPBIAS 1523 1531 Poly-Ser.
COMPBIAS 1618 1675 Ser-rich.
COMPBIAS 1665 1675 Poly-Ser.
COMPBIAS 1756 1762 Poly-Ala.
COMPBIAS 1980 1991 Asp/Glu-rich (acidic).
COMPBIAS 2030 2053 Pro-rich.
COMPBIAS 2323 2342 Arg/Glu-rich (mixed charge).
COMPBIAS 2351 2360 Arg/Asp-rich (mixed charge).
COMPBIAS 2422 2426 Poly-Leu.
COMPBIAS 2482 2493 Asp/Glu-rich (acidic).
COMPBIAS 2730 2750 Pro-rich.
ACT_SITE 2761 2761 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00104}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 346 346 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 572 572 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 606 606 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 631 631 Phosphothreonine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 802 802 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 922 922 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 1012 1012 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 1109 1109 Phosphothreonine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 1129 1129 Phosphothreonine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 1221 1221 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 1302 1302 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 1349 1349 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 1369 1369 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 1475 1475 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 1543 1543 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 1730 1730 Phosphothreonine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 1735 1735 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 1740 1740 Phosphotyrosine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 1774 1774 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 1963 1963 Phosphothreonine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 1984 1984 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 2020 2020 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 2022 2022 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 2024 2024 Phosphothreonine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 2070 2070 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 2207 2207 Phosphothreonine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 2235 2235 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 2283 2283 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 2463 2463 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 2477 2477 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
MOD_RES 2479 2479 Phosphoserine.
{ECO:0000250|UniProtKB:O95071}.
CONFLICT 1121 1121 S -> P (in Ref. 1; AAT28194).
{ECO:0000305}.
SEQUENCE 2792 AA; 308352 MW; 19E5E56E5094F5B6 CRC64;
MTSIHFVVHP LPGTEDQLND RLREVSEKLN KYNLNSHPPL NVLEQATIKQ CVVGPNHAAF
LLEDGRICRI GFSVQPDRLE LGKPDNNDGS KLNSSSGTGR TSRPGRTSDS PWFLSGSETL
GRLAGNTLGS RWSSGVGGSG GGSSGRSSAG ARDSRRQTRV IRTGRDRGSG LLGSQPQPVI
PASVIPEELI SQAQVVLQGK SRSVIIRELQ RTNLDVNLAV NNLLSRDDED GDDGDDTASE
SYLPGEDLMS LLDADIHSAH PSVIIDADAM FSEDISYFGY PSFRRSSLSR LGSSRERDSE
LLRERESVLR LRERRWLDGA SFDNERGSTS KEGESNPDKK NTPVQSPVSL GEDLQWWPDK
DGTKFTCIGA LYSELLAVSS KGELYQWKWS ESEPYRNAQN PSLHHPRATF LGLTNEKIVL
LSANSIRATV ATENNKVATW VDETLSSVAS KLEHTAQTYS ELQGERIVSL HCCALYTCAQ
LENNLYWWGV VPFSQRKKML EKARAKNKKP KSSAGISSMP NITVGTQVCL RNNPLYHAGA
VAFSISAGIP KVGVLMESVW NMNDSCRFQL RSPESLKSME KASKTLETKP ESKQEPVKTE
MGPPPSPAST CSDASSIASS ASMPYKRRRS TPAPREEEKV NEEQWPLREV VFVEDVKNVP
VGKVLKVDGA YVAVKFPGTS TNTTCQNSSG PDADPSSLLQ DCRLLRIDEL QVVKTGGTPK
VPDCFQRTPK KLCIPEKTEI LAVNVDSKGV HAVLKTGSWV RYCVFDLATG KAEQENNFPT
SSVAFLGQDE RSVAIFTAGQ ESPIVLRDGN GTIYPMAKDC MGGIRDPDWL DLPPISSLGM
GVHSLINLPA NSTIKKKAAI IIMAVEKQTL MQHILRCDYE ACRQYLVNLE QAVVLEQNRQ
MLQTFISHRC DGNRNILHAC VSVCFPTSNK ETKEEEEAER SERNTFAERL SAVEAIANAI
SVVSSNGPGN RAGSSNSRSL RLREMMRRSL RAAGLGRHEA GASSSDHQDP VSPPIAPPSW
VPDPPSMDPD GDIDFILAPA VGSLTTAATG SGQGPSTSTI PGPSTEPSVV ESKDRKANAH
FILKLLCDSA VLQPYLRELL SAKDARGMTP FMSAVSGRAY SAAITILETA QKIAKAEVSA
SEKEEDVFMG MVCPSGTNPD DSPLYVLCCN DTCSFTWTGA EHINQDIFEC RTCGLLESLC
CCTECARVCH KGHDCKLKRT SPTAYCDCWE KCKCKTLIAG QKSARLDLLY RLLTATNLVT
LPNSRGEHLL LFLVQTVARQ TVEHCQYRPP RIREDRNRKT ASPEDSDMPD HDLEPPRFAQ
LALERVLQDW NALRSMIMFG SQENKDPLSA SSRIGHLLPE EQVYLNQQSG TIRLDCFTHC
LIVKCTADIL LLDTLLGTLV KELQNKYTPG RREEAIAVTM RFLRSVARVF VILSVEMASS
KKKNNFIPQP IGKCKRVFQA LLPYAVEELC NVAESLIVPV RMGIARPTAP FTLASTSIDA
MQGSEELFSV EPLPPRPSSD QASSSSQSQS SYIIRNPQQR RISQSQPVRG RDEEQDDIVS
ADVEEVEVVE GVAGEEDHHD EQEEHGEENA EAEGHHDEHD EDGSDMELDL LAAAETESDS
ESNHSNQDNA SGRRSVVTAA TAGSEAGASS VPAFFSEDDS QSNDSSDSDS SSSQSDDIEQ
ETFMLDEPLE RTTNSSHANG AAQAPRSMQW AVRNPQHQRA ASTAPSSTST PAASSAGLIY
IDPSNLRRSG TISTSAAAAA AALEASNASS YLTSASSLAR AYSIVIRQIS DLMGLIPKYN
HLVYSQIPAA VKLTYQDAVN LQNYVEEKLI PTWNWMVSVM DSTEAQLRYG SALASAGDPG
HPNHPLHASQ NSARRERMTA REEASLRTLE GRRRATLLSA RQGMMSARGD FLNYALSLMR
SHNDEHSDVL PVLDVCSLKH VAYVFQALIY WIKAMNQQTT LDTPQLERKR TRELLELGID
NEDSEHENDD DTSQSATLND KDDDSLPAET GQNHPFFRRS DSMTFLGCIP PNPFEVPLAE
AIPLADQPHL LQPNARKEDL FGRPSQGLYS SSAGSGKCIV EVTMDRNCLE VLPTKMSYAA
NLKNVMNMQN RQKKEGEEQS LLAEEADSSK PGPSAPDVAA QLKSSLLAEI GLTESEGPPL
TSFRPQCSFM GMVISHDMLL GRWRLSLELF GRVFMEDVGA EPGSILTELG GFEVKESKFR
REMEKLRNQQ SRDLSLEVDR DRDLLIQQTM RQLNNHFGRR CATTPMAVHR VKVTFKDEPG
EGSGVARSFY TAIAQAFLSN EKLPNLDCIQ NANKGTHTSL MQRLRNRGER DREREREREM
RRSSGLRAGS RRDRDRDFRR QLSIDTRPFR PASEGNPSDD PDPLPAHRQA LGERLYPRVQ
AMQPAFASKI TGMLLELSPA QLLLLLASED SLRARVDEAM ELIIAHGREN GADSILDLGL
LDSSEKVQEN RKRHGSSRSV VDMDLEDTDD GDDNAPLFYQ PGKRGFYTPR PGKNTEARLN
CFRNIGRILG LCLLQNELCP ITLNRHVIKV LLGRKVNWHD FAFFDPVMYE SLRQLILASQ
SSDADAVFSA MDLAFAIDLC KEEGGGQVEL IPNGVNIPVT PQNVYEYVRK YAEHRMLVVA
EQPLHAMRKG LLDVLPKNSL EDLTAEDFRL LVNGCGEVNV QMLISFTSFN DESGENAEKL
LQFKRWFWSI VEKMSMTERQ DLVYFWTSSP SLPASEEGFQ PMPSITIRPP DDQHLPTANT
CISRLYVPLY SSKQILKQKL LLAIKTKNFG FV


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EIAAB45119 E3 ubiquitin-protein ligase UBR5,E3 ubiquitin-protein ligase, HECT domain-containing 1,Edd,Edd1,Hyperplastic discs protein homolog,Kiaa0896,Mouse,Mus musculus,Ubr5
EIAAB45120 100 kDa protein,Dd5,E3 ubiquitin-protein ligase UBR5,E3 ubiquitin-protein ligase, HECT domain-containing 1,Edd,Edd1,Hyd,Hyperplastic discs protein homolog,Rat,Rattus norvegicus,Ubr5
25-845 HACE1 contains 6 ANK repeats and 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain. HACE1 is an E3 ubiquitin-protein ligase that may function in cellular proteins degradation. 0.05 mg
CSB-EL025520HU Human E3 ubiquitin-protein ligase UBR5(UBR5) ELISA kit SpeciesHuman 96T
CSB-EL025520MO Mouse E3 ubiquitin-protein ligase UBR5(UBR5) ELISA kit SpeciesMouse 96T
CSB-EL025520MO Mouse E3 ubiquitin-protein ligase UBR5(UBR5) ELISA kit 96T
CSB-EL025520HU Human E3 ubiquitin-protein ligase UBR5(UBR5) ELISA kit 96T
CSB-EL025520RA Rat E3 ubiquitin-protein ligase UBR5(UBR5) ELISA kit SpeciesRat 96T
UBR5 UBR5 Gene ubiquitin protein ligase E3 component n-recognin 5
UBR5_MOUSE ELISA Kit FOR E3 ubiquitin-protein ligase UBR5; organism: Mouse; gene name: Ubr5 96T
CSB-EL025520RA Rat E3 ubiquitin-protein ligase UBR5(UBR5) ELISA kit 96T
HELB HECW2 Gene HECT, C2 and WW domain containing E3 ubiquitin protein ligase 2
HEG1 HECW1 Gene HECT, C2 and WW domain containing E3 ubiquitin protein ligase 1
ARP43277_P050 HACE1(HECT domain and ankyrin repeat containing, E3 ubiquitin protein ligase 1) 50 µg
HADH HACE1 Gene HECT domain and ankyrin repeat containing, E3 ubiquitin protein ligase 1
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
CSB-EL010277HU Human HECT, C2 and WW domain containing E3 ubiquitin protein ligase 2 (HECW2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL010277MO Mouse HECT, C2 and WW domain containing E3 ubiquitin protein ligase 2 (HECW2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL010276MO Mouse HECT, C2 and WW domain containing E3 ubiquitin protein ligase 1 (HECW1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL010276HU Human HECT, C2 and WW domain containing E3 ubiquitin protein ligase 1 (HECW1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL010115HU Human HECT domain and ankyrin repeat containing, E3 ubiquitin protein ligase 1 (HACE1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL010115MO Mouse HECT domain and ankyrin repeat containing, E3 ubiquitin protein ligase 1 (HACE1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL025520RA Rat ubiquitin protein ligase E3 component n-recognin 5 (UBR5) ELISA kit, Species Rat, Sample Type serum, plasma 96T
EIAAB45116 E3 ubiquitin-protein ligase UBR3,Homo sapiens,Human,KIAA2024,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,UBR3,Zinc finger protein 650,ZNF650


 

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