Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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) (hHYD) (Progestin-induced protein)

 UBR5_HUMAN              Reviewed;        2799 AA.
O95071; B2RP24; J3KMW7; O94970; Q9NPL3;
05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2001, sequence version 2.
18-JUL-2018, entry version 193.
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;
Short=hHYD;
AltName: Full=Progestin-induced protein;
Name=UBR5; Synonyms=EDD, EDD1, HYD, KIAA0896;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart, and Placenta;
PubMed=10030672; DOI=10.1038/sj.onc.1202249;
Callaghan M.J., Russell A.J., Woollatt E., Sutherland G.R.,
Sutherland R.L., Watts C.K.W.;
"Identification of a human HECT family protein with homology to the
Drosophila tumor suppressor gene hyperplastic discs.";
Oncogene 17:3479-3491(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH TOPBP1.
TISSUE=Fetal brain;
PubMed=11714696; DOI=10.1074/jbc.M104347200;
Honda Y., Tojo M., Matsuzaki K., Anan T., Matsumoto M., Ando M.,
Saya H., Nakao M.;
"Cooperation of HECT-domain ubiquitin ligase hHYD and DNA
topoisomerase II-binding protein for DNA damage response.";
J. Biol. Chem. 277:3599-3605(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=10048485; DOI=10.1093/dnares/5.6.355;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:355-364(1998).
[4]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[5]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1746, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1969, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1308; SER-1549; THR-1969
AND SER-2486, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[14]
INTERACTION WITH EDVP COMPLEX.
PubMed=19287380; DOI=10.1038/ncb1848;
Maddika S., Chen J.;
"Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3
ligase.";
Nat. Cell Biol. 11:409-419(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2486, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1549 AND THR-1969, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
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).
[18]
FUNCTION AS CDK9 UBIQUITIN LIGASE, AND INTERACTION WITH CDK9 AND
TFIIS/TCEA1.
PubMed=21127351; DOI=10.1074/jbc.M110.176628;
Cojocaru M., Bouchard A., Cloutier P., Cooper J.J., Varzavand K.,
Price D.H., Coulombe B.;
"Transcription factor IIS cooperates with the E3 ligase UBR5 to
ubiquitinate the CDK9 subunit of the positive transcription elongation
factor B.";
J. Biol. Chem. 286:5012-5022(2011).
[19]
PHOSPHORYLATION AT SER-110; SER-327; SER-352; SER-578; SER-612;
THR-637; SER-808; SER-928; SER-1018; THR-1115; THR-1135; SER-1227;
SER-1308; SER-1355; SER-1375; SER-1481; THR-1736; SER-1741; SER-1780;
THR-1969; SER-2026; SER-2028; THR-2030; SER-2076; THR-2213; SER-2289
AND SER-2484.
PubMed=21924388; DOI=10.1016/j.jprot.2011.08.023;
Bethard J.R., Zheng H., Roberts L., Eblen S.T.;
"Identification of phosphorylation sites on the E3 ubiquitin ligase
UBR5/EDD.";
J. Proteomics 75:603-609(2011).
[20]
FUNCTION IN UBIQUITINATION OF PCK1.
PubMed=21726808; DOI=10.1016/j.molcel.2011.04.028;
Jiang W., Wang S., Xiao M., Lin Y., Zhou L., Lei Q., Xiong Y.,
Guan K.L., Zhao S.;
"Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation
via recruiting the UBR5 ubiquitin ligase.";
Mol. Cell 43:33-44(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327; SER-1549 AND
SER-2486, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
FUNCTION.
PubMed=22884692; DOI=10.1016/j.cell.2012.06.039;
Gudjonsson T., Altmeyer M., Savic V., Toledo L., Dinant C., Grofte M.,
Bartkova J., Poulsen M., Oka Y., Bekker-Jensen S., Mailand N.,
Neumann B., Heriche J.K., Shearer R., Saunders D., Bartek J.,
Lukas J., Lukas C.;
"TRIP12 and UBR5 Suppress Spreading of Chromatin Ubiquitylation at
Damaged Chromosomes.";
Cell 150:697-709(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-327; SER-578;
SER-612; SER-808; SER-1308; SER-1549; THR-1969; SER-2241; SER-2469 AND
SER-2486, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
INTERACTION WITH PIH1D1.
PubMed=24656813; DOI=10.1016/j.celrep.2014.03.013;
Horejsi Z., Stach L., Flower T.G., Joshi D., Flynn H., Skehel J.M.,
O'Reilly N.J., Ogrodowicz R.W., Smerdon S.J., Boulton S.J.;
"Phosphorylation-dependent PIH1D1 interactions define substrate
specificity of the R2TP cochaperone complex.";
Cell Rep. 7:19-26(2014).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1549 AND SER-1990, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
X-RAY CRYSTALLOGRAPHY (1.04 ANGSTROMS) OF 2391-2455, AND MUTAGENESIS
OF CYS-2768.
PubMed=11287654; DOI=10.1073/pnas.071552198;
Deo R.C., Sonenberg N., Burley S.K.;
"X-ray structure of the human hyperplastic discs protein: an ortholog
of the C-terminal domain of poly(A)-binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 98:4414-4419(2001).
-!- FUNCTION: 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 (By similarity). 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. {ECO:0000250, ECO:0000269|PubMed:21127351,
ECO:0000269|PubMed:21726808, ECO:0000269|PubMed:22884692}.
-!- 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
(e.g. gamma fibrinogen/FGG) 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 (PubMed:24656813).
{ECO:0000269|PubMed:11714696, ECO:0000269|PubMed:19287380,
ECO:0000269|PubMed:21127351, ECO:0000269|PubMed:24656813}.
-!- INTERACTION:
P35222:CTNNB1; NbExp=6; IntAct=EBI-358329, EBI-491549;
P49841:GSK3B; NbExp=8; IntAct=EBI-358329, EBI-373586;
Q9BPZ3:PAIP2; NbExp=5; IntAct=EBI-358329, EBI-2957445;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O95071-1; Sequence=Displayed;
Name=2;
IsoId=O95071-2; Sequence=VSP_054399;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Most abundant in testis and
expressed at high levels in brain, pituitary and kidney.
-!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-
thioester formation.
-!- SEQUENCE CAUTION:
Sequence=BAA74919.3; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF006010; AAD01259.2; -; mRNA.
EMBL; U95000; AAF88143.1; -; mRNA.
EMBL; AB020703; BAA74919.3; ALT_INIT; mRNA.
EMBL; AP002907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC137234; AAI37235.1; -; mRNA.
CCDS; CCDS34933.1; -. [O95071-1]
CCDS; CCDS64946.1; -. [O95071-2]
RefSeq; NP_001269802.1; NM_001282873.1. [O95071-2]
RefSeq; NP_056986.2; NM_015902.5. [O95071-1]
UniGene; Hs.492445; -.
PDB; 1I2T; X-ray; 1.04 A; A=2393-2453.
PDB; 2QHO; X-ray; 1.85 A; B/D/F/H=180-230.
PDB; 3PT3; X-ray; 1.97 A; A/B=2687-2799.
PDBsum; 1I2T; -.
PDBsum; 2QHO; -.
PDBsum; 3PT3; -.
ProteinModelPortal; O95071; -.
SMR; O95071; -.
BioGrid; 119501; 166.
CORUM; O95071; -.
DIP; DIP-32930N; -.
ELM; O95071; -.
IntAct; O95071; 75.
MINT; O95071; -.
STRING; 9606.ENSP00000429084; -.
iPTMnet; O95071; -.
PhosphoSitePlus; O95071; -.
BioMuta; UBR5; -.
EPD; O95071; -.
MaxQB; O95071; -.
PaxDb; O95071; -.
PeptideAtlas; O95071; -.
PRIDE; O95071; -.
ProteomicsDB; 50641; -.
Ensembl; ENST00000220959; ENSP00000220959; ENSG00000104517. [O95071-2]
Ensembl; ENST00000520539; ENSP00000429084; ENSG00000104517. [O95071-1]
GeneID; 51366; -.
KEGG; hsa:51366; -.
UCSC; uc003ykr.3; human. [O95071-1]
CTD; 51366; -.
DisGeNET; 51366; -.
EuPathDB; HostDB:ENSG00000104517.12; -.
GeneCards; UBR5; -.
H-InvDB; HIX0025542; -.
HGNC; HGNC:16806; UBR5.
HPA; HPA053688; -.
MIM; 608413; gene.
neXtProt; NX_O95071; -.
OpenTargets; ENSG00000104517; -.
PharmGKB; PA162408175; -.
eggNOG; KOG0943; Eukaryota.
eggNOG; COG5021; LUCA.
GeneTree; ENSGT00850000132302; -.
HOGENOM; HOG000046848; -.
HOVERGEN; HBG096012; -.
InParanoid; O95071; -.
KO; K10593; -.
OMA; CHRGHDC; -.
OrthoDB; EOG091G005O; -.
PhylomeDB; O95071; -.
TreeFam; TF314406; -.
BRENDA; 6.3.2.19; 2681.
SignaLink; O95071; -.
SIGNOR; O95071; -.
UniPathway; UPA00143; -.
ChiTaRS; UBR5; human.
EvolutionaryTrace; O95071; -.
GeneWiki; UBR5; -.
GenomeRNAi; 51366; -.
PRO; PR:O95071; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000104517; -.
CleanEx; HS_UBR5; -.
ExpressionAtlas; O95071; baseline and differential.
Genevisible; O95071; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HGNC.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0032991; C:protein-containing complex; IDA: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; IDA:FlyBase.
GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:ProtInc.
GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:HGNC.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:2000780; P:negative regulation of double-strand break repair; IMP:UniProtKB.
GO; GO:1901315; P:negative regulation of histone H2A K63-linked ubiquitination; IMP:UniProtKB.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IMP:BHF-UCL.
GO; GO:0050847; P:progesterone receptor signaling pathway; IDA:HGNC.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:FlyBase.
GO; GO:0000209; P:protein polyubiquitination; IDA:BHF-UCL.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
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;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
DNA damage; DNA repair; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transferase;
Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 2799 E3 ubiquitin-protein ligase UBR5.
/FTId=PRO_0000086931.
DOMAIN 2377 2454 PABC. {ECO:0000255|PROSITE-
ProRule:PRU00641}.
DOMAIN 2462 2799 HECT. {ECO:0000255|PROSITE-
ProRule:PRU00104}.
ZN_FING 1177 1245 UBR-type. {ECO:0000255|PROSITE-
ProRule:PRU00508}.
COMPBIAS 940 945 Poly-Glu.
COMPBIAS 980 985 Poly-Ser.
COMPBIAS 1528 1537 Poly-Ser.
COMPBIAS 1671 1681 Poly-Ser.
COMPBIAS 1762 1768 Poly-Ala.
COMPBIAS 1986 1997 Asp/Glu-rich (acidic).
COMPBIAS 2036 2059 Pro-rich.
COMPBIAS 2329 2348 Arg/Glu-rich (mixed charge).
COMPBIAS 2357 2366 Arg/Asp-rich (mixed charge).
COMPBIAS 2489 2500 Asp/Glu-rich (acidic).
COMPBIAS 2737 2757 Pro-rich.
ACT_SITE 2768 2768 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00104}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21924388}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21924388}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 578 578 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21924388}.
MOD_RES 612 612 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21924388}.
MOD_RES 637 637 Phosphothreonine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 808 808 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21924388}.
MOD_RES 928 928 Phosphoserine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 1018 1018 Phosphoserine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 1115 1115 Phosphothreonine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 1135 1135 Phosphothreonine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 1227 1227 Phosphoserine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 1308 1308 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21924388}.
MOD_RES 1355 1355 Phosphoserine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 1375 1375 Phosphoserine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 1481 1481 Phosphoserine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 1549 1549 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1736 1736 Phosphothreonine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 1741 1741 Phosphoserine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 1746 1746 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 1780 1780 Phosphoserine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 1969 1969 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21924388}.
MOD_RES 1990 1990 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2026 2026 Phosphoserine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 2028 2028 Phosphoserine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 2030 2030 Phosphothreonine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 2076 2076 Phosphoserine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 2213 2213 Phosphothreonine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 2241 2241 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2289 2289 Phosphoserine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 2469 2469 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2484 2484 Phosphoserine.
{ECO:0000269|PubMed:21924388}.
MOD_RES 2486 2486 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 2474 2474 Missing (in isoform 2).
{ECO:0000303|PubMed:10048485}.
/FTId=VSP_054399.
VARIANT 2150 2150 S -> R (in dbSNP:rs1062822).
/FTId=VAR_051466.
MUTAGEN 2768 2768 C->A: Loss of ubiquitin binding.
{ECO:0000269|PubMed:11287654}.
CONFLICT 134 134 S -> P (in Ref. 2; AAF88143).
{ECO:0000305}.
CONFLICT 229 229 E -> K (in Ref. 2; AAF88143).
{ECO:0000305}.
CONFLICT 258 258 S -> Y (in Ref. 2; AAF88143).
{ECO:0000305}.
CONFLICT 374 375 IG -> M (in Ref. 2; AAF88143).
{ECO:0000305}.
CONFLICT 772 772 D -> H (in Ref. 2; AAF88143).
{ECO:0000305}.
CONFLICT 780 780 Q -> R (in Ref. 2; AAF88143).
{ECO:0000305}.
CONFLICT 884 884 D -> G (in Ref. 2; AAF88143).
{ECO:0000305}.
CONFLICT 1811 1811 S -> P (in Ref. 2; AAF88143).
{ECO:0000305}.
CONFLICT 2144 2144 L -> H (in Ref. 2; AAF88143).
{ECO:0000305}.
CONFLICT 2282 2282 K -> R (in Ref. 2; AAF88143).
{ECO:0000305}.
CONFLICT 2489 2489 D -> N (in Ref. 2; AAF88143).
{ECO:0000305}.
HELIX 182 184 {ECO:0000244|PDB:2QHO}.
HELIX 187 196 {ECO:0000244|PDB:2QHO}.
HELIX 202 211 {ECO:0000244|PDB:2QHO}.
TURN 212 214 {ECO:0000244|PDB:2QHO}.
HELIX 216 224 {ECO:0000244|PDB:2QHO}.
HELIX 2394 2408 {ECO:0000244|PDB:1I2T}.
HELIX 2410 2412 {ECO:0000244|PDB:1I2T}.
HELIX 2413 2420 {ECO:0000244|PDB:1I2T}.
HELIX 2425 2433 {ECO:0000244|PDB:1I2T}.
HELIX 2435 2452 {ECO:0000244|PDB:1I2T}.
HELIX 2687 2692 {ECO:0000244|PDB:3PT3}.
STRAND 2695 2698 {ECO:0000244|PDB:3PT3}.
HELIX 2704 2720 {ECO:0000244|PDB:3PT3}.
HELIX 2723 2734 {ECO:0000244|PDB:3PT3}.
STRAND 2751 2756 {ECO:0000244|PDB:3PT3}.
STRAND 2764 2766 {ECO:0000244|PDB:3PT3}.
TURN 2767 2770 {ECO:0000244|PDB:3PT3}.
STRAND 2771 2775 {ECO:0000244|PDB:3PT3}.
HELIX 2780 2791 {ECO:0000244|PDB:3PT3}.
SEQUENCE 2799 AA; 309352 MW; 871300DB404FF561 CRC64;
MTSIHFVVHP 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


Related products :

Catalog number Product name Quantity
EIAAB45118 E3 ubiquitin-protein ligase UBR5,E3 ubiquitin-protein ligase, HECT domain-containing 1,EDD,EDD1,hHYD,Homo sapiens,Human,HYD,Hyperplastic discs protein homolog,KIAA0896,Progestin-induced protein,UBR5
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-EL025520MO Mouse E3 ubiquitin-protein ligase UBR5(UBR5) ELISA kit SpeciesMouse 96T
CSB-EL025520HU Human E3 ubiquitin-protein ligase UBR5(UBR5) ELISA kit SpeciesHuman 96T
UBR5 UBR5 Gene ubiquitin protein ligase E3 component n-recognin 5
CSB-EL025520MO Mouse E3 ubiquitin-protein ligase UBR5(UBR5) ELISA kit 96T
CSB-EL025520RA Rat E3 ubiquitin-protein ligase UBR5(UBR5) ELISA kit SpeciesRat 96T
CSB-EL025520HU Human E3 ubiquitin-protein ligase UBR5(UBR5) ELISA kit 96T
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-EL010276HU Human HECT, C2 and WW domain containing E3 ubiquitin protein ligase 1 (HECW1) 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-EL010277HU Human HECT, C2 and WW domain containing E3 ubiquitin protein ligase 2 (HECW2) ELISA kit, Species Human, 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
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
CSB-EL025520RA Rat ubiquitin protein ligase E3 component n-recognin 5 (UBR5) ELISA kit, Species Rat, 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


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur