Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

E3 ubiquitin-protein ligase UBR5

Gene

UBR5

Organism
Homo sapiens (Human)
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. 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.By similarity3 Publications

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2768 – 27681Glycyl thioester intermediatePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1177 – 124569UBR-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • RNA binding Source: InterPro
  • ubiquitin-protein transferase activity Source: ProtInc
  • ubiquitin-ubiquitin ligase activity Source: BHF-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell proliferation Source: ProtInc
  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA repair Source: UniProtKB-KW
  • negative regulation of double-strand break repair Source: UniProtKB
  • negative regulation of histone H2A K63-linked ubiquitination Source: UniProtKB
  • positive regulation of canonical Wnt signaling pathway Source: BHF-UCL
  • positive regulation of catenin import into nucleus Source: BHF-UCL
  • positive regulation of protein import into nucleus, translocation Source: BHF-UCL
  • progesterone receptor signaling pathway Source: HGNC
  • protein polyubiquitination Source: BHF-UCL
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: GO_Central
  • ubiquitin-dependent protein catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi6.3.2.19. 2681.
SignaLinkiO95071.
SIGNORiO95071.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase UBR5 (EC:6.3.2.-)
Alternative name(s):
E3 ubiquitin-protein ligase, HECT domain-containing 1
Hyperplastic discs protein homolog
Short name:
hHYD
Progestin-induced protein
Gene namesi
Name:UBR5
Synonyms:EDD, EDD1, HYD, KIAA0896
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:16806. UBR5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2768 – 27681C → A: Loss of ubiquitin binding. 1 Publication

Organism-specific databases

PharmGKBiPA162408175.

Polymorphism and mutation databases

BioMutaiUBR5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 27992798E3 ubiquitin-protein ligase UBR5PRO_0000086931Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineCombined sources
Modified residuei110 – 1101PhosphoserineCombined sources1 Publication
Modified residuei327 – 3271PhosphoserineCombined sources1 Publication
Modified residuei352 – 3521Phosphoserine1 Publication
Modified residuei578 – 5781PhosphoserineCombined sources1 Publication
Modified residuei612 – 6121PhosphoserineCombined sources1 Publication
Modified residuei637 – 6371Phosphothreonine1 Publication
Modified residuei808 – 8081PhosphoserineCombined sources1 Publication
Modified residuei928 – 9281Phosphoserine1 Publication
Modified residuei1018 – 10181Phosphoserine1 Publication
Modified residuei1115 – 11151Phosphothreonine1 Publication
Modified residuei1135 – 11351Phosphothreonine1 Publication
Modified residuei1227 – 12271Phosphoserine1 Publication
Modified residuei1308 – 13081PhosphoserineCombined sources1 Publication
Modified residuei1355 – 13551Phosphoserine1 Publication
Modified residuei1375 – 13751Phosphoserine1 Publication
Modified residuei1481 – 14811Phosphoserine1 Publication
Modified residuei1549 – 15491PhosphoserineCombined sources
Modified residuei1736 – 17361Phosphothreonine1 Publication
Modified residuei1741 – 17411Phosphoserine1 Publication
Modified residuei1746 – 17461PhosphotyrosineCombined sources
Modified residuei1780 – 17801Phosphoserine1 Publication
Modified residuei1969 – 19691PhosphothreonineCombined sources1 Publication
Modified residuei1990 – 19901PhosphoserineCombined sources
Modified residuei2026 – 20261Phosphoserine1 Publication
Modified residuei2028 – 20281Phosphoserine1 Publication
Modified residuei2030 – 20301Phosphothreonine1 Publication
Modified residuei2076 – 20761Phosphoserine1 Publication
Modified residuei2213 – 22131Phosphothreonine1 Publication
Modified residuei2241 – 22411PhosphoserineCombined sources
Modified residuei2289 – 22891Phosphoserine1 Publication
Modified residuei2469 – 24691PhosphoserineCombined sources
Modified residuei2484 – 24841Phosphoserine1 Publication
Modified residuei2486 – 24861PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO95071.
MaxQBiO95071.
PaxDbiO95071.
PeptideAtlasiO95071.
PRIDEiO95071.

PTM databases

iPTMnetiO95071.
PhosphoSiteiO95071.

Expressioni

Tissue specificityi

Widely expressed. Most abundant in testis and expressed at high levels in brain, pituitary and kidney.

Gene expression databases

BgeeiENSG00000104517.
CleanExiHS_UBR5.
ExpressionAtlasiO95071. baseline and differential.
GenevisibleiO95071. HS.

Organism-specific databases

HPAiHPA024728.
HPA053688.

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 (e.g. gamma fibrinogen/FGG) 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 (PubMed:24656813).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P352226EBI-358329,EBI-491549
GSK3BP498418EBI-358329,EBI-373586
PAIP2Q9BPZ35EBI-358329,EBI-2957445

Protein-protein interaction databases

BioGridi119501. 134 interactions.
DIPiDIP-32930N.
IntActiO95071. 56 interactions.
MINTiMINT-196086.
STRINGi9606.ENSP00000429084.

Structurei

Secondary structure

1
2799
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi182 – 1843Combined sources
Helixi187 – 19610Combined sources
Helixi202 – 21110Combined sources
Turni212 – 2143Combined sources
Helixi216 – 2249Combined sources
Helixi2394 – 240815Combined sources
Helixi2410 – 24123Combined sources
Helixi2413 – 24208Combined sources
Helixi2425 – 24339Combined sources
Helixi2435 – 245218Combined sources
Helixi2687 – 26926Combined sources
Beta strandi2695 – 26984Combined sources
Helixi2704 – 272017Combined sources
Helixi2723 – 273412Combined sources
Beta strandi2751 – 27566Combined sources
Beta strandi2764 – 27663Combined sources
Turni2767 – 27704Combined sources
Beta strandi2771 – 27755Combined sources
Helixi2780 – 279112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I2TX-ray1.04A2393-2453[»]
2QHOX-ray1.85B/D/F/H180-230[»]
3PT3X-ray1.97A/B2687-2799[»]
ProteinModelPortaliO95071.
SMRiO95071. Positions 180-228, 2393-2453, 2686-2792.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95071.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2377 – 245478PABCPROSITE-ProRule annotationAdd
BLAST
Domaini2462 – 2799338HECTPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi940 – 9456Poly-Glu
Compositional biasi980 – 9856Poly-Ser
Compositional biasi1528 – 153710Poly-Ser
Compositional biasi1671 – 168111Poly-SerAdd
BLAST
Compositional biasi1762 – 17687Poly-Ala
Compositional biasi1986 – 199712Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi2036 – 205924Pro-richAdd
BLAST
Compositional biasi2329 – 234820Arg/Glu-rich (mixed charge)Add
BLAST
Compositional biasi2357 – 236610Arg/Asp-rich (mixed charge)
Compositional biasi2489 – 250012Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi2737 – 275721Pro-richAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1177 – 124569UBR-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0943. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00840000129735.
HOGENOMiHOG000046848.
HOVERGENiHBG096012.
InParanoidiO95071.
KOiK10593.
OMAiENSLYWW.
OrthoDBiEOG091G005O.
PhylomeDBiO95071.
TreeFamiTF314406.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O95071-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTSIHFVVHP LPGTEDQLND RLREVSEKLN KYNLNSHPPL NVLEQATIKQ
60 70 80 90 100
CVVGPNHAAF LLEDGRVCRI GFSVQPDRLE LGKPDNNDGS KLNSNSGAGR
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 LGSSRVLLLP
310 320 330 340 350
LERDSELLRE RESVLRLRER RWLDGASFDN ERGSTSKEGE PNLDKKNTPV
360 370 380 390 400
QSPVSLGEDL QWWPDKDGTK FICIGALYSE LLAVSSKGEL YQWKWSESEP
410 420 430 440 450
YRNAQNPSLH HPRATFLGLT NEKIVLLSAN SIRATVATEN NKVATWVDET
460 470 480 490 500
LSSVASKLEH TAQTYSELQG ERIVSLHCCA LYTCAQLENS LYWWGVVPFS
510 520 530 540 550
QRKKMLEKAR AKNKKPKSSA GISSMPNITV GTQVCLRNNP LYHAGAVAFS
560 570 580 590 600
ISAGIPKVGV LMESVWNMND SCRFQLRSPE SLKNMEKASK TTEAKPESKQ
610 620 630 640 650
EPVKTEMGPP PSPASTCSDA SSIASSASMP YKRRRSTPAP KEEEKVNEEQ
660 670 680 690 700
WSLREVVFVE DVKNVPVGKV LKVDGAYVAV KFPGTSSNTN CQNSSGPDAD
710 720 730 740 750
PSSLLQDCRL LRIDELQVVK TGGTPKVPDC FQRTPKKLCI PEKTEILAVN
760 770 780 790 800
VDSKGVHAVL KTGNWVRYCI FDLATGKAEQ ENNFPTSSIA FLGQNERNVA
810 820 830 840 850
IFTAGQESPI ILRDGNGTIY PMAKDCMGGI RDPDWLDLPP ISSLGMGVHS
860 870 880 890 900
LINLPANSTI KKKAAVIIMA VEKQTLMQHI LRCDYEACRQ YLMNLEQAVV
910 920 930 940 950
LEQNLQMLQT FISHRCDGNR NILHACVSVC FPTSNKETKE EEEAERSERN
960 970 980 990 1000
TFAERLSAVE AIANAISVVS SNGPGNRAGS SSSRSLRLRE MMRRSLRAAG
1010 1020 1030 1040 1050
LGRHEAGASS SDHQDPVSPP IAPPSWVPDP PAMDPDGDID FILAPAVGSL
1060 1070 1080 1090 1100
TTAATGTGQG PSTSTIPGPS TEPSVVESKD RKANAHFILK LLCDSVVLQP
1110 1120 1130 1140 1150
YLRELLSAKD ARGMTPFMSA VSGRAYPAAI TILETAQKIA KAEISSSEKE
1160 1170 1180 1190 1200
EDVFMGMVCP SGTNPDDSPL YVLCCNDTCS FTWTGAEHIN QDIFECRTCG
1210 1220 1230 1240 1250
LLESLCCCTE CARVCHKGHD CKLKRTSPTA YCDCWEKCKC KTLIAGQKSA
1260 1270 1280 1290 1300
RLDLLYRLLT ATNLVTLPNS RGEHLLLFLV QTVARQTVEH CQYRPPRIRE
1310 1320 1330 1340 1350
DRNRKTASPE DSDMPDHDLE PPRFAQLALE RVLQDWNALK SMIMFGSQEN
1360 1370 1380 1390 1400
KDPLSASSRI GHLLPEEQVY LNQQSGTIRL DCFTHCLIVK CTADILLLDT
1410 1420 1430 1440 1450
LLGTLVKELQ NKYTPGRREE AIAVTMRFLR SVARVFVILS VEMASSKKKN
1460 1470 1480 1490 1500
NFIPQPIGKC KRVFQALLPY AVEELCNVAE SLIVPVRMGI ARPTAPFTLA
1510 1520 1530 1540 1550
STSIDAMQGS EELFSVEPLP PRPSSDQSSS SSQSQSSYII RNPQQRRISQ
1560 1570 1580 1590 1600
SQPVRGRDEE QDDIVSADVE EVEVVEGVAG EEDHHDEQEE HGEENAEAEG
1610 1620 1630 1640 1650
QHDEHDEDGS DMELDLLAAA ETESDSESNH SNQDNASGRR SVVTAATAGS
1660 1670 1680 1690 1700
EAGASSVPAF FSEDDSQSND SSDSDSSSSQ SDDIEQETFM LDEPLERTTN
1710 1720 1730 1740 1750
SSHANGAAQA PRSMQWAVRN TQHQRAASTA PSSTSTPAAS SAGLIYIDPS
1760 1770 1780 1790 1800
NLRRSGTIST SAAAAAAALE ASNASSYLTS ASSLARAYSI VIRQISDLMG
1810 1820 1830 1840 1850
LIPKYNHLVY SQIPAAVKLT YQDAVNLQNY VEEKLIPTWN WMVSIMDSTE
1860 1870 1880 1890 1900
AQLRYGSALA SAGDPGHPNH PLHASQNSAR RERMTAREEA SLRTLEGRRR
1910 1920 1930 1940 1950
ATLLSARQGM MSARGDFLNY ALSLMRSHND EHSDVLPVLD VCSLKHVAYV
1960 1970 1980 1990 2000
FQALIYWIKA MNQQTTLDTP QLERKRTREL LELGIDNEDS EHENDDDTNQ
2010 2020 2030 2040 2050
SATLNDKDDD SLPAETGQNH PFFRRSDSMT FLGCIPPNPF EVPLAEAIPL
2060 2070 2080 2090 2100
ADQPHLLQPN ARKEDLFGRP SQGLYSSSAS SGKCLMEVTV DRNCLEVLPT
2110 2120 2130 2140 2150
KMSYAANLKN VMNMQNRQKK EGEEQPVLPE ETESSKPGPS AHDLAAQLKS
2160 2170 2180 2190 2200
SLLAEIGLTE SEGPPLTSFR PQCSFMGMVI SHDMLLGRWR LSLELFGRVF
2210 2220 2230 2240 2250
MEDVGAEPGS ILTELGGFEV KESKFRREME KLRNQQSRDL SLEVDRDRDL
2260 2270 2280 2290 2300
LIQQTMRQLN NHFGRRCATT PMAVHRVKVT FKDEPGEGSG VARSFYTAIA
2310 2320 2330 2340 2350
QAFLSNEKLP NLECIQNANK GTHTSLMQRL RNRGERDRER EREREMRRSS
2360 2370 2380 2390 2400
GLRAGSRRDR DRDFRRQLSI DTRPFRPASE GNPSDDPEPL PAHRQALGER
2410 2420 2430 2440 2450
LYPRVQAMQP AFASKITGML LELSPAQLLL LLASEDSLRA RVDEAMELII
2460 2470 2480 2490 2500
AHGRENGADS ILDLGLVDSS EKVQQENRKR HGSSRSVVDM DLDDTDDGDD
2510 2520 2530 2540 2550
NAPLFYQPGK RGFYTPRPGK NTEARLNCFR NIGRILGLCL LQNELCPITL
2560 2570 2580 2590 2600
NRHVIKVLLG RKVNWHDFAF FDPVMYESLR QLILASQSSD ADAVFSAMDL
2610 2620 2630 2640 2650
AFAIDLCKEE GGGQVELIPN GVNIPVTPQN VYEYVRKYAE HRMLVVAEQP
2660 2670 2680 2690 2700
LHAMRKGLLD VLPKNSLEDL TAEDFRLLVN GCGEVNVQML ISFTSFNDES
2710 2720 2730 2740 2750
GENAEKLLQF KRWFWSIVEK MSMTERQDLV YFWTSSPSLP ASEEGFQPMP
2760 2770 2780 2790
SITIRPPDDQ HLPTANTCIS RLYVPLYSSK QILKQKLLLA IKTKNFGFV
Length:2,799
Mass (Da):309,352
Last modified:October 1, 2001 - v2
Checksum:i871300DB404FF561
GO
Isoform 2 (identifier: O95071-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2474-2474: Missing.

Note: No experimental confirmation available.
Show »
Length:2,798
Mass (Da):309,224
Checksum:iD0743129ECF82394
GO

Sequence cautioni

The sequence BAA74919 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1341S → P in AAF88143 (PubMed:11714696).Curated
Sequence conflicti229 – 2291E → K in AAF88143 (PubMed:11714696).Curated
Sequence conflicti258 – 2581S → Y in AAF88143 (PubMed:11714696).Curated
Sequence conflicti374 – 3752IG → M in AAF88143 (PubMed:11714696).Curated
Sequence conflicti772 – 7721D → H in AAF88143 (PubMed:11714696).Curated
Sequence conflicti780 – 7801Q → R in AAF88143 (PubMed:11714696).Curated
Sequence conflicti884 – 8841D → G in AAF88143 (PubMed:11714696).Curated
Sequence conflicti1811 – 18111S → P in AAF88143 (PubMed:11714696).Curated
Sequence conflicti2144 – 21441L → H in AAF88143 (PubMed:11714696).Curated
Sequence conflicti2282 – 22821K → R in AAF88143 (PubMed:11714696).Curated
Sequence conflicti2489 – 24891D → N in AAF88143 (PubMed:11714696).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2150 – 21501S → R.
Corresponds to variant rs1062822 [ dbSNP | Ensembl ].
VAR_051466

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2474 – 24741Missing in isoform 2. 1 PublicationVSP_054399

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006010 mRNA. Translation: AAD01259.2.
U95000 mRNA. Translation: AAF88143.1.
AB020703 mRNA. Translation: BAA74919.3. Different initiation.
AP002907 Genomic DNA. No translation available.
AP002981 Genomic DNA. No translation available.
BC137234 mRNA. Translation: AAI37235.1.
CCDSiCCDS34933.1. [O95071-1]
CCDS64946.1. [O95071-2]
RefSeqiNP_001269802.1. NM_001282873.1. [O95071-2]
NP_056986.2. NM_015902.5. [O95071-1]
UniGeneiHs.492445.

Genome annotation databases

EnsembliENST00000220959; ENSP00000220959; ENSG00000104517. [O95071-2]
ENST00000520539; ENSP00000429084; ENSG00000104517. [O95071-1]
GeneIDi51366.
KEGGihsa:51366.
UCSCiuc003ykr.3. human. [O95071-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006010 mRNA. Translation: AAD01259.2.
U95000 mRNA. Translation: AAF88143.1.
AB020703 mRNA. Translation: BAA74919.3. Different initiation.
AP002907 Genomic DNA. No translation available.
AP002981 Genomic DNA. No translation available.
BC137234 mRNA. Translation: AAI37235.1.
CCDSiCCDS34933.1. [O95071-1]
CCDS64946.1. [O95071-2]
RefSeqiNP_001269802.1. NM_001282873.1. [O95071-2]
NP_056986.2. NM_015902.5. [O95071-1]
UniGeneiHs.492445.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I2TX-ray1.04A2393-2453[»]
2QHOX-ray1.85B/D/F/H180-230[»]
3PT3X-ray1.97A/B2687-2799[»]
ProteinModelPortaliO95071.
SMRiO95071. Positions 180-228, 2393-2453, 2686-2792.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119501. 134 interactions.
DIPiDIP-32930N.
IntActiO95071. 56 interactions.
MINTiMINT-196086.
STRINGi9606.ENSP00000429084.

PTM databases

iPTMnetiO95071.
PhosphoSiteiO95071.

Polymorphism and mutation databases

BioMutaiUBR5.

Proteomic databases

EPDiO95071.
MaxQBiO95071.
PaxDbiO95071.
PeptideAtlasiO95071.
PRIDEiO95071.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000220959; ENSP00000220959; ENSG00000104517. [O95071-2]
ENST00000520539; ENSP00000429084; ENSG00000104517. [O95071-1]
GeneIDi51366.
KEGGihsa:51366.
UCSCiuc003ykr.3. human. [O95071-1]

Organism-specific databases

CTDi51366.
GeneCardsiUBR5.
H-InvDBHIX0025542.
HGNCiHGNC:16806. UBR5.
HPAiHPA024728.
HPA053688.
MIMi608413. gene.
neXtProtiNX_O95071.
PharmGKBiPA162408175.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0943. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00840000129735.
HOGENOMiHOG000046848.
HOVERGENiHBG096012.
InParanoidiO95071.
KOiK10593.
OMAiENSLYWW.
OrthoDBiEOG091G005O.
PhylomeDBiO95071.
TreeFamiTF314406.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 2681.
SignaLinkiO95071.
SIGNORiO95071.

Miscellaneous databases

ChiTaRSiUBR5. human.
EvolutionaryTraceiO95071.
GeneWikiiUBR5.
GenomeRNAii51366.
PROiO95071.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000104517.
CleanExiHS_UBR5.
ExpressionAtlasiO95071. baseline and differential.
GenevisibleiO95071. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: O95071
Secondary accession number(s): B2RP24
, J3KMW7, O94970, Q9NPL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: October 1, 2001
Last modified: September 7, 2016
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

A cysteine residue is required for ubiquitin-thioester formation.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.