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Protein

E3 ubiquitin-protein ligase UBR5

Gene

Ubr5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity2 Publications

Catalytic activityi

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.

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei2761Glycyl thioester intermediatePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1171 – 1239UBR-typePROSITE-ProRule annotationAdd BLAST69

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase UBR5 (EC:2.3.2.26)
Alternative name(s):
E3 ubiquitin-protein ligase, HECT domain-containing 1
HECT-type E3 ubiquitin transferase UBR5
Hyperplastic discs protein homolog
Gene namesi
Name:Ubr5
Synonyms:Edd, Edd1, Kiaa0896
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1918040. Ubr5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000869322 – 2792E3 ubiquitin-protein ligase UBR5Add BLAST2791

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineBy similarity1
Modified residuei110PhosphoserineBy similarity1
Modified residuei321PhosphoserineCombined sources1
Modified residuei346PhosphoserineBy similarity1
Modified residuei572PhosphoserineBy similarity1
Modified residuei606PhosphoserineBy similarity1
Modified residuei631PhosphothreonineBy similarity1
Modified residuei802PhosphoserineBy similarity1
Modified residuei922PhosphoserineBy similarity1
Modified residuei1012PhosphoserineBy similarity1
Modified residuei1109PhosphothreonineBy similarity1
Modified residuei1129PhosphothreonineBy similarity1
Modified residuei1221PhosphoserineBy similarity1
Modified residuei1302PhosphoserineBy similarity1
Modified residuei1349PhosphoserineBy similarity1
Modified residuei1369PhosphoserineBy similarity1
Modified residuei1475PhosphoserineBy similarity1
Modified residuei1543PhosphoserineBy similarity1
Modified residuei1730PhosphothreonineBy similarity1
Modified residuei1735PhosphoserineBy similarity1
Modified residuei1740PhosphotyrosineBy similarity1
Modified residuei1774PhosphoserineBy similarity1
Modified residuei1963PhosphothreonineBy similarity1
Modified residuei1984PhosphoserineBy similarity1
Modified residuei2020PhosphoserineBy similarity1
Modified residuei2022PhosphoserineBy similarity1
Modified residuei2024PhosphothreonineBy similarity1
Modified residuei2070PhosphoserineBy similarity1
Modified residuei2207PhosphothreonineBy similarity1
Modified residuei2235PhosphoserineBy similarity1
Modified residuei2283PhosphoserineBy similarity1
Modified residuei2463PhosphoserineBy similarity1
Modified residuei2477PhosphoserineBy similarity1
Modified residuei2479PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ80TP3.
MaxQBiQ80TP3.
PaxDbiQ80TP3.
PeptideAtlasiQ80TP3.
PRIDEiQ80TP3.

PTM databases

iPTMnetiQ80TP3.
PhosphoSitePlusiQ80TP3.

Interactioni

Subunit structurei

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 VPRBP proteins (EDVP complex). Interacts directly with DYRK2. Interacts with PIH1D1.By similarity

Protein-protein interaction databases

BioGridi214255. 29 interactors.
DIPiDIP-56890N.
IntActiQ80TP3. 8 interactors.
STRINGi10090.ENSMUSP00000105965.

Structurei

3D structure databases

ProteinModelPortaliQ80TP3.
SMRiQ80TP3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2371 – 2448PABCPROSITE-ProRule annotationAdd BLAST78
Domaini2455 – 2792HECTPROSITE-ProRule annotationAdd BLAST338

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi934 – 939Poly-Glu6
Compositional biasi1523 – 1531Poly-Ser9
Compositional biasi1618 – 1675Ser-richAdd BLAST58
Compositional biasi1665 – 1675Poly-SerAdd BLAST11
Compositional biasi1756 – 1762Poly-Ala7
Compositional biasi1980 – 1991Asp/Glu-rich (acidic)Add BLAST12
Compositional biasi2030 – 2053Pro-richAdd BLAST24
Compositional biasi2323 – 2342Arg/Glu-rich (mixed charge)Add BLAST20
Compositional biasi2351 – 2360Arg/Asp-rich (mixed charge)10
Compositional biasi2422 – 2426Poly-Leu5
Compositional biasi2482 – 2493Asp/Glu-rich (acidic)Add BLAST12
Compositional biasi2730 – 2750Pro-richAdd BLAST21

Sequence similaritiesi

Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
Contains 1 PABC domain.PROSITE-ProRule annotation
Contains 1 UBR-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1171 – 1239UBR-typePROSITE-ProRule annotationAdd BLAST69

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0943. Eukaryota.
COG5021. LUCA.
HOVERGENiHBG096012.
InParanoidiQ80TP3.
KOiK10593.
PhylomeDBiQ80TP3.

Family and domain databases

CDDicd14423. CUE_UBR5. 1 hit.
Gene3Di1.10.1900.10. 1 hit.
2.130.10.30. 3 hits.
InterProiIPR024725. E3_UbLigase_EDD_UBA.
IPR000569. HECT_dom.
IPR002004. PABP_HYD.
IPR009091. RCC1/BLIP-II.
IPR003126. Znf_UBR.
[Graphical view]
PfamiPF11547. E3_UbLigase_EDD. 1 hit.
PF00632. HECT. 1 hit.
PF00658. PABP. 1 hit.
[Graphical view]
SMARTiSM00119. HECTc. 1 hit.
SM00517. PolyA. 1 hit.
SM00396. ZnF_UBR1. 1 hit.
[Graphical view]
SUPFAMiSSF50985. SSF50985. 1 hit.
SSF56204. SSF56204. 2 hits.
SSF63570. SSF63570. 1 hit.
PROSITEiPS50237. HECT. 1 hit.
PS51309. PABC. 1 hit.
PS51157. ZF_UBR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q80TP3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSIHFVVHP LPGTEDQLND RLREVSEKLN KYNLNSHPPL NVLEQATIKQ
60 70 80 90 100
CVVGPNHAAF LLEDGRICRI GFSVQPDRLE LGKPDNNDGS KLNSSSGTGR
110 120 130 140 150
TSRPGRTSDS PWFLSGSETL GRLAGNTLGS RWSSGVGGSG GGSSGRSSAG
160 170 180 190 200
ARDSRRQTRV IRTGRDRGSG LLGSQPQPVI PASVIPEELI SQAQVVLQGK
210 220 230 240 250
SRSVIIRELQ RTNLDVNLAV NNLLSRDDED GDDGDDTASE SYLPGEDLMS
260 270 280 290 300
LLDADIHSAH PSVIIDADAM FSEDISYFGY PSFRRSSLSR LGSSRERDSE
310 320 330 340 350
LLRERESVLR LRERRWLDGA SFDNERGSTS KEGESNPDKK NTPVQSPVSL
360 370 380 390 400
GEDLQWWPDK DGTKFTCIGA LYSELLAVSS KGELYQWKWS ESEPYRNAQN
410 420 430 440 450
PSLHHPRATF LGLTNEKIVL LSANSIRATV ATENNKVATW VDETLSSVAS
460 470 480 490 500
KLEHTAQTYS ELQGERIVSL HCCALYTCAQ LENNLYWWGV VPFSQRKKML
510 520 530 540 550
EKARAKNKKP KSSAGISSMP NITVGTQVCL RNNPLYHAGA VAFSISAGIP
560 570 580 590 600
KVGVLMESVW NMNDSCRFQL RSPESLKSME KASKTLETKP ESKQEPVKTE
610 620 630 640 650
MGPPPSPAST CSDASSIASS ASMPYKRRRS TPAPREEEKV NEEQWPLREV
660 670 680 690 700
VFVEDVKNVP VGKVLKVDGA YVAVKFPGTS TNTTCQNSSG PDADPSSLLQ
710 720 730 740 750
DCRLLRIDEL QVVKTGGTPK VPDCFQRTPK KLCIPEKTEI LAVNVDSKGV
760 770 780 790 800
HAVLKTGSWV RYCVFDLATG KAEQENNFPT SSVAFLGQDE RSVAIFTAGQ
810 820 830 840 850
ESPIVLRDGN GTIYPMAKDC MGGIRDPDWL DLPPISSLGM GVHSLINLPA
860 870 880 890 900
NSTIKKKAAI IIMAVEKQTL MQHILRCDYE ACRQYLVNLE QAVVLEQNRQ
910 920 930 940 950
MLQTFISHRC DGNRNILHAC VSVCFPTSNK ETKEEEEAER SERNTFAERL
960 970 980 990 1000
SAVEAIANAI SVVSSNGPGN RAGSSNSRSL RLREMMRRSL RAAGLGRHEA
1010 1020 1030 1040 1050
GASSSDHQDP VSPPIAPPSW VPDPPSMDPD GDIDFILAPA VGSLTTAATG
1060 1070 1080 1090 1100
SGQGPSTSTI PGPSTEPSVV ESKDRKANAH FILKLLCDSA VLQPYLRELL
1110 1120 1130 1140 1150
SAKDARGMTP FMSAVSGRAY SAAITILETA QKIAKAEVSA SEKEEDVFMG
1160 1170 1180 1190 1200
MVCPSGTNPD DSPLYVLCCN DTCSFTWTGA EHINQDIFEC RTCGLLESLC
1210 1220 1230 1240 1250
CCTECARVCH KGHDCKLKRT SPTAYCDCWE KCKCKTLIAG QKSARLDLLY
1260 1270 1280 1290 1300
RLLTATNLVT LPNSRGEHLL LFLVQTVARQ TVEHCQYRPP RIREDRNRKT
1310 1320 1330 1340 1350
ASPEDSDMPD HDLEPPRFAQ LALERVLQDW NALRSMIMFG SQENKDPLSA
1360 1370 1380 1390 1400
SSRIGHLLPE EQVYLNQQSG TIRLDCFTHC LIVKCTADIL LLDTLLGTLV
1410 1420 1430 1440 1450
KELQNKYTPG RREEAIAVTM RFLRSVARVF VILSVEMASS KKKNNFIPQP
1460 1470 1480 1490 1500
IGKCKRVFQA LLPYAVEELC NVAESLIVPV RMGIARPTAP FTLASTSIDA
1510 1520 1530 1540 1550
MQGSEELFSV EPLPPRPSSD QASSSSQSQS SYIIRNPQQR RISQSQPVRG
1560 1570 1580 1590 1600
RDEEQDDIVS ADVEEVEVVE GVAGEEDHHD EQEEHGEENA EAEGHHDEHD
1610 1620 1630 1640 1650
EDGSDMELDL LAAAETESDS ESNHSNQDNA SGRRSVVTAA TAGSEAGASS
1660 1670 1680 1690 1700
VPAFFSEDDS QSNDSSDSDS SSSQSDDIEQ ETFMLDEPLE RTTNSSHANG
1710 1720 1730 1740 1750
AAQAPRSMQW AVRNPQHQRA ASTAPSSTST PAASSAGLIY IDPSNLRRSG
1760 1770 1780 1790 1800
TISTSAAAAA AALEASNASS YLTSASSLAR AYSIVIRQIS DLMGLIPKYN
1810 1820 1830 1840 1850
HLVYSQIPAA VKLTYQDAVN LQNYVEEKLI PTWNWMVSVM DSTEAQLRYG
1860 1870 1880 1890 1900
SALASAGDPG HPNHPLHASQ NSARRERMTA REEASLRTLE GRRRATLLSA
1910 1920 1930 1940 1950
RQGMMSARGD FLNYALSLMR SHNDEHSDVL PVLDVCSLKH VAYVFQALIY
1960 1970 1980 1990 2000
WIKAMNQQTT LDTPQLERKR TRELLELGID NEDSEHENDD DTSQSATLND
2010 2020 2030 2040 2050
KDDDSLPAET GQNHPFFRRS DSMTFLGCIP PNPFEVPLAE AIPLADQPHL
2060 2070 2080 2090 2100
LQPNARKEDL FGRPSQGLYS SSAGSGKCIV EVTMDRNCLE VLPTKMSYAA
2110 2120 2130 2140 2150
NLKNVMNMQN RQKKEGEEQS LLAEEADSSK PGPSAPDVAA QLKSSLLAEI
2160 2170 2180 2190 2200
GLTESEGPPL TSFRPQCSFM GMVISHDMLL GRWRLSLELF GRVFMEDVGA
2210 2220 2230 2240 2250
EPGSILTELG GFEVKESKFR REMEKLRNQQ SRDLSLEVDR DRDLLIQQTM
2260 2270 2280 2290 2300
RQLNNHFGRR CATTPMAVHR VKVTFKDEPG EGSGVARSFY TAIAQAFLSN
2310 2320 2330 2340 2350
EKLPNLDCIQ NANKGTHTSL MQRLRNRGER DREREREREM RRSSGLRAGS
2360 2370 2380 2390 2400
RRDRDRDFRR QLSIDTRPFR PASEGNPSDD PDPLPAHRQA LGERLYPRVQ
2410 2420 2430 2440 2450
AMQPAFASKI TGMLLELSPA QLLLLLASED SLRARVDEAM ELIIAHGREN
2460 2470 2480 2490 2500
GADSILDLGL LDSSEKVQEN RKRHGSSRSV VDMDLEDTDD GDDNAPLFYQ
2510 2520 2530 2540 2550
PGKRGFYTPR PGKNTEARLN CFRNIGRILG LCLLQNELCP ITLNRHVIKV
2560 2570 2580 2590 2600
LLGRKVNWHD FAFFDPVMYE SLRQLILASQ SSDADAVFSA MDLAFAIDLC
2610 2620 2630 2640 2650
KEEGGGQVEL IPNGVNIPVT PQNVYEYVRK YAEHRMLVVA EQPLHAMRKG
2660 2670 2680 2690 2700
LLDVLPKNSL EDLTAEDFRL LVNGCGEVNV QMLISFTSFN DESGENAEKL
2710 2720 2730 2740 2750
LQFKRWFWSI VEKMSMTERQ DLVYFWTSSP SLPASEEGFQ PMPSITIRPP
2760 2770 2780 2790
DDQHLPTANT CISRLYVPLY SSKQILKQKL LLAIKTKNFG FV
Length:2,792
Mass (Da):308,352
Last modified:September 27, 2005 - v2
Checksum:i19E5E56E5094F5B6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1121S → P in AAT28194 (PubMed:15282321).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY550908 mRNA. Translation: AAT28194.1.
AK122398 mRNA. Translation: BAC65680.1.
BC049162 mRNA. Translation: AAH49162.1.
BC049224 mRNA. Translation: AAH49224.1.
BC057458 mRNA. Translation: AAH57458.1.
BC057923 mRNA. Translation: AAH57923.1.
AK014485 mRNA. Translation: BAB29387.1.
RefSeqiNP_001074828.2. NM_001081359.3.
NP_001106192.1. NM_001112721.2.
UniGeneiMm.476840.

Genome annotation databases

GeneIDi70790.
KEGGimmu:70790.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY550908 mRNA. Translation: AAT28194.1.
AK122398 mRNA. Translation: BAC65680.1.
BC049162 mRNA. Translation: AAH49162.1.
BC049224 mRNA. Translation: AAH49224.1.
BC057458 mRNA. Translation: AAH57458.1.
BC057923 mRNA. Translation: AAH57923.1.
AK014485 mRNA. Translation: BAB29387.1.
RefSeqiNP_001074828.2. NM_001081359.3.
NP_001106192.1. NM_001112721.2.
UniGeneiMm.476840.

3D structure databases

ProteinModelPortaliQ80TP3.
SMRiQ80TP3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214255. 29 interactors.
DIPiDIP-56890N.
IntActiQ80TP3. 8 interactors.
STRINGi10090.ENSMUSP00000105965.

PTM databases

iPTMnetiQ80TP3.
PhosphoSitePlusiQ80TP3.

Proteomic databases

EPDiQ80TP3.
MaxQBiQ80TP3.
PaxDbiQ80TP3.
PeptideAtlasiQ80TP3.
PRIDEiQ80TP3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi70790.
KEGGimmu:70790.

Organism-specific databases

CTDi51366.
MGIiMGI:1918040. Ubr5.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0943. Eukaryota.
COG5021. LUCA.
HOVERGENiHBG096012.
InParanoidiQ80TP3.
KOiK10593.
PhylomeDBiQ80TP3.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiUbr5. mouse.
PROiQ80TP3.
SOURCEiSearch...

Family and domain databases

CDDicd14423. CUE_UBR5. 1 hit.
Gene3Di1.10.1900.10. 1 hit.
2.130.10.30. 3 hits.
InterProiIPR024725. E3_UbLigase_EDD_UBA.
IPR000569. HECT_dom.
IPR002004. PABP_HYD.
IPR009091. RCC1/BLIP-II.
IPR003126. Znf_UBR.
[Graphical view]
PfamiPF11547. E3_UbLigase_EDD. 1 hit.
PF00632. HECT. 1 hit.
PF00658. PABP. 1 hit.
[Graphical view]
SMARTiSM00119. HECTc. 1 hit.
SM00517. PolyA. 1 hit.
SM00396. ZnF_UBR1. 1 hit.
[Graphical view]
SUPFAMiSSF50985. SSF50985. 1 hit.
SSF56204. SSF56204. 2 hits.
SSF63570. SSF63570. 1 hit.
PROSITEiPS50237. HECT. 1 hit.
PS51309. PABC. 1 hit.
PS51157. ZF_UBR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUBR5_MOUSE
AccessioniPrimary (citable) accession number: Q80TP3
Secondary accession number(s): Q698K9
, Q6PEQ8, Q6PFQ9, Q80VL4, Q810V6, Q9CXE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2005
Last modified: November 2, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

A cysteine residue is required for ubiquitin-thioester formation.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.