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Recombinant Human E3 ubiquitin-protein ligase UBR5 (UBR5), partial

Recombinant Human E3 ubiquitin-protein ligase UBR5 (UBR5), partial

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

UBR5

Uniprot NO.

O95071

Alternative Names

4432411E13Rik; AW549941; C77315; D030042K14; DD5; E3 identified by differential display; E3 ubiquitin protein ligase, HECT domain containing, 1; E3 ubiquitin-protein ligase; E3 ubiquitin-protein ligase UBR5; EDD 1; EDD; EDD1; FLJ11310; HECT domain-containing 1; hHYD; HYD; Hyperplastic discs protein homolog; Hyperplastic discs, Drosophila, homolog of; KIAA0896; MGC57263; mKIAA0896; Progestin induced protein; Progestin-induced protein; Rat100; Ubiquitin protein ligase; Ubiquitin protein ligase E3 component n recognin 5; UBR5; UBR5_HUMAN

Species

Homo sapiens (Human)

Source

Yeast

Expression Region

2-2799

Target Protein Sequence

TSIHFVVHP LPGTEDQLND RLREVSEKLN KYNLNSHPPL NVLEQATIKQ CVVGPNHAAF LLEDGRVCRI GFSVQPDRLE LGKPDNNDGS KLNSNSGAGR TSRPGRTSDS PWFLSGSETL GRLAGNTLGS RWSSGVGGSG GGSSGRSSAG ARDSRRQTRV IRTGRDRGSG LLGSQPQPVI PASVIPEELI SQAQVVLQGK SRSVIIRELQ RTNLDVNLAV NNLLSRDDED GDDGDDTASE SYLPGEDLMS LLDADIHSAH PSVIIDADAM FSEDISYFGY PSFRRSSLSR LGSSRVLLLP LERDSELLRE RESVLRLRER RWLDGASFDN ERGSTSKEGE PNLDKKNTPV QSPVSLGEDL QWWPDKDGTK FICIGALYSE LLAVSSKGEL YQWKWSESEP YRNAQNPSLH HPRATFLGLT NEKIVLLSAN SIRATVATEN NKVATWVDET LSSVASKLEH TAQTYSELQG ERIVSLHCCA LYTCAQLENS LYWWGVVPFS QRKKMLEKAR AKNKKPKSSA GISSMPNITV GTQVCLRNNP LYHAGAVAFS ISAGIPKVGV LMESVWNMND SCRFQLRSPE SLKNMEKASK TTEAKPESKQ EPVKTEMGPP PSPASTCSDA SSIASSASMP YKRRRSTPAP KEEEKVNEEQ WSLREVVFVE DVKNVPVGKV LKVDGAYVAV KFPGTSSNTN CQNSSGPDAD PSSLLQDCRL LRIDELQVVK TGGTPKVPDC FQRTPKKLCI PEKTEILAVN VDSKGVHAVL KTGNWVRYCI FDLATGKAEQ ENNFPTSSIA FLGQNERNVA IFTAGQESPI ILRDGNGTIY PMAKDCMGGI RDPDWLDLPP ISSLGMGVHS LINLPANSTI KKKAAVIIMA VEKQTLMQHI LRCDYEACRQ YLMNLEQAVV LEQNLQMLQT FISHRCDGNR NILHACVSVC FPTSNKETKE EEEAERSERN TFAERLSAVE AIANAISVVS SNGPGNRAGS SSSRSLRLRE MMRRSLRAAG LGRHEAGASS SDHQDPVSPP IAPPSWVPDP PAMDPDGDID FILAPAVGSL TTAATGTGQG PSTSTIPGPS TEPSVVESKD RKANAHFILK LLCDSVVLQP YLRELLSAKD ARGMTPFMSA VSGRAYPAAI TILETAQKIA KAEISSSEKE EDVFMGMVCP SGTNPDDSPL YVLCCNDTCS FTWTGAEHIN QDIFECRTCG LLESLCCCTE CARVCHKGHD CKLKRTSPTA YCDCWEKCKC KTLIAGQKSA RLDLLYRLLT ATNLVTLPNS RGEHLLLFLV QTVARQTVEH CQYRPPRIRE DRNRKTASPE DSDMPDHDLE PPRFAQLALE RVLQDWNALK SMIMFGSQEN KDPLSASSRI GHLLPEEQVY LNQQSGTIRL DCFTHCLIVK CTADILLLDT LLGTLVKELQ NKYTPGRREE AIAVTMRFLR SVARVFVILS VEMASSKKKN NFIPQPIGKC KRVFQALLPY AVEELCNVAE SLIVPVRMGI ARPTAPFTLA STSIDAMQGS EELFSVEPLP PRPSSDQSSS SSQSQSSYII RNPQQRRISQ SQPVRGRDEE QDDIVSADVE EVEVVEGVAG EEDHHDEQEE HGEENAEAEG QHDEHDEDGS DMELDLLAAA ETESDSESNH SNQDNASGRR SVVTAATAGS EAGASSVPAF FSEDDSQSND SSDSDSSSSQ SDDIEQETFM LDEPLERTTN SSHANGAAQA PRSMQWAVRN TQHQRAASTA PSSTSTPAAS SAGLIYIDPS NLRRSGTIST SAAAAAAALE ASNASSYLTS ASSLARAYSI VIRQISDLMG LIPKYNHLVY SQIPAAVKLT YQDAVNLQNY VEEKLIPTWN WMVSIMDSTE AQLRYGSALA SAGDPGHPNH PLHASQNSAR RERMTAREEA SLRTLEGRRR ATLLSARQGM MSARGDFLNY ALSLMRSHND EHSDVLPVLD VCSLKHVAYV FQALIYWIKA MNQQTTLDTP QLERKRTREL LELGIDNEDS EHENDDDTNQ SATLNDKDDD SLPAETGQNH PFFRRSDSMT FLGCIPPNPF EVPLAEAIPL ADQPHLLQPN ARKEDLFGRP SQGLYSSSAS SGKCLMEVTV DRNCLEVLPT KMSYAANLKN VMNMQNRQKK EGEEQPVLPE ETESSKPGPS AHDLAAQLKS SLLAEIGLTE SEGPPLTSFR PQCSFMGMVI SHDMLLGRWR LSLELFGRVF MEDVGAEPGS ILTELGGFEV KESKFRREME KLRNQQSRDL SLEVDRDRDL LIQQTMRQLN NHFGRRCATT PMAVHRVKVT FKDEPGEGSG VARSFYTAIA QAFLSNEKLP NLECIQNANK GTHTSLMQRL RNRGERDRER EREREMRRSS GLRAGSRRDR DRDFRRQLSI DTRPFRPASE GNPSDDPEPL PAHRQALGER LYPRVQAMQP AFASKITGML LELSPAQLLL LLASEDSLRA RVDEAMELII AHGRENGADS ILDLGLVDSS EKVQQENRKR HGSSRSVVDM DLDDTDDGDD NAPLFYQPGK RGFYTPRPGK NTEARLNCFR NIGRILGLCL LQNELCPITL NRHVIKVLLG RKVNWHDFAF FDPVMYESLR QLILASQSSD ADAVFSAMDL AFAIDLCKEE GGGQVELIPN GVNIPVTPQN VYEYVRKYAE HRMLVVAEQP LHAMRKGLLD VLPKNSLEDL TAEDFRLLVN GCGEVNVQML ISFTSFNDES GENAEKLLQF KRWFWSIVEK MSMTERQDLV YFWTSSPSLP ASEEGFQPMP SITIRPPDDQ HLPTANTCIS RLYVPLYSSK QILKQKLLLA IKTKNFGFV
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage Condition

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Customer Reviews and Q&A

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■ Q&A

Is this protein expressed in mammalian cells? It requires post-translation modification to be activated.

Thanks for your inquiry.
Yes. This protein is expressed in mammalian cells, and we usually use the HEK293. The expressed protein is with post-translation modification. It's much closer to the natural protein.

Target Background

Function(From Uniprot)

E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. 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. Regulates DNA topoisomerase II binding protein (TopBP1) in the DNA damage response. Plays an essential role in extraembryonic development. 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.

Gene References into Functions

UBR5 is a modulator of super-vigilant proteostasis of induced pluripotent stem cells from Huntington's disease patients PMID:30038412
UBR5 was highly expressed in colon cancer not only at mRNA level but also at protein level; UBR5 promoted the growth of colon cancer cells, and inhibited apoptosis. PMID:29441938
BMI1 and UBR5 repress the polymerase II (Pol II)-mediated transcription at damaged sites PMID:27647897
Results found that EDD was consistent with GOLPH3 expression and also promoted the EMT process and activated Wnt/beta-catenin signaling in epithelial ovarian cancer. PMID:28332316
UBR5 directly binds to the tumor suppressor esophageal cancer-related gene 4, increasing its ubiquitination to reducing the protein stability of ECRG4 to promote colorectal cancer progression. PMID:28856538
Wnt-dependent inactivation of the Groucho/TLE co-repressor by the HECT E3 ubiquitin ligase Hyd/UBR5 is a key prerequisite that enables Armadillo/beta-catenin to activate transcription. PMID:28689657
UBR5 downregulates proapoptotic MOAP-1 and suggest that UBR5 can confer cisplatin resistance in ovarian cancer. PMID:27721409
Data suggest that UBR5 down-regulates levels of TRAF3, a key component of Toll-like receptor signaling, via the miRNA pathway; p90RSK is an upstream regulator of UBR5; p90RSK phosphorylates UBR5 as required for translational repression of TRAF3 mRNA. (UBR5 = ubiquitin protein ligase E3 component n-recognin 5 protein; TRAF3 = TNF receptor-associated factor 3; p90RSK = 90 kDa ribosomal protein S6 kinase) PMID:28559278
Data show that ubiquitin protein ligase E3 component n-recognin 5 protein (UBR5) bound the tumor suppressor gastrokine 1 (GKN1) and increased its ubiquitination to reduce the protein stability of GKN1. PMID:27590582
Findings unveil UBR5 as a novel and critical regulator of tumor growth, metastasis, and immune response in triple negative breast cancer. PMID:28330927
Study highlights many functional biological role of UBR5 especially in cancer where it seems to be a key regulator of cell signaling. [review] PMID:26464214
Human herpesvirus-6 U14 induces cell cycle arrest in G2/M phase by associating with a cellular protein, EDD. PMID:26340541
Elevated metaphase RanGTP levels use Ubr5 to couple overall chromosome congression to SAC silencing. PMID:26438829
results confirm the role of the MLLE domain of UBR5 in substrate recruitment and suggest a potential role in regulating UBR5 ligase activity. PMID:26224628
these observations highlight the potential role of EDD in regulating mitotic progression and the cellular response to perturbed mitosis. PMID:25833949
Utilizing a high throughput RNAi screening approach author identified UBR5, a protein commonly amplified in breast cancer, as a novel regulator of ERalpha protein levels and transcriptional activity. PMID:24441042
the alpha4 N-terminus binding to endogenous PP2Ac and PABP, and the C-terminus to EDD, is reported. PMID:24145130
These results identify EDD as a dual regulator of cell survival and cisplatin resistance and suggest that EDD is a therapeutic target for ovarian cancer. PMID:24379240
UBR5 knockdown results in accumulation of cellular pregnane X receptor and an increase in its activity. PMID:24438055
As a molecular adaptor, Vpr enhanced the interaction between TERT and the VPRBP substrate receptor of the DYRK2-associated EDD-DDB1-VPRBP E3 ligase complex, resulting in increased ubiquitination of TERT. PMID:23612978
The recurrence and clustering of deleterious mutations implicate UBR5 mutations as a critical pathogenic event in a subgroup of mantle cell lymphoma. PMID:23407552
Data indicate that Dyrk2 phosphorylates TERT protein, which is then associated with the EDD-DDB1-VprBP E3 ligase complex for subsequent ubiquitin-mediated TERT protein degradation. PMID:23362280
Ubiquitination assays showed that the C-lobe of UBR5 is able to form a thioester-linked E3-ubiquitin complex, although it does not physically interact with UBCH4 in NMR experiments PMID:23027739
Study shows that TRIP12 and UBR5, two HECT domain ubiquitin E3 ligases, control accumulation of RNF168, a rate-limiting component of a pathway that ubiquitylates histones after DNA breakage. PMID:22884692
Increased p53 levels upon EDD depletion cause a G(1) arrest, as co-depletion of EDD and p53 completely rescues this effect on cell cycle progression. PMID:22374670
EDD1 suppresses death-receptor expression, and its expression is elevated in breast, pancreas, and lung cancer cell lines resistant to death receptor-mediated apoptosis. PMID:21949371
through binding to p53, EDD actively inhibits p53 phosphorylation by ATM and plays a role in ensuring smooth G(1)/S progression. PMID:21383020
EDD ubiquitinates beta-catenin through Lys29- or Lys11-linked ubiquitin chains, leading to enhanced stability of beta-catenin. PMID:21118991
The authors show that human EDD can interact independently with both human papillomavirus type 18 E6 and human E6AP. PMID:21228227
identify UBR5 as a novel E3 ligase that regulates transcription and define an additional function of TFIIS in the regulation of CDK9. PMID:21127351
study confirmed the presence of UBR5 mutation in exon 45 in high microsatellite instability cacarcinomas; could not identify exon 42 mutations in colorectal cancers and exon 51 mutations in breast cancers PMID:20025491
ubiquitin-protein ligase EDD interacts with importin alpha 5 through consensus basic nuclear localization signals and is localized in cell nuclei. EDD also binds progesterone receptor (PR) and potentiates progestin-mediated gene transactivation. PMID:12011095
EDD is a novel mediator in DNA damage signal transduction via CHK2 and emphasize the potential importance of EDD in cancer. PMID:17074762
EDD plays the role in the maintenance of genomic stability, emphasising the potential importance of dysregulated EDD expression and/or function in the evolution of cancer. PMID:18073532
These results identify EDD as a new independent prognostic marker for outcome in serous ovarian cancer PMID:18349819