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UniProtKB - O95071 (UBR5_HUMAN)

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Protein

E3 ubiquitin-protein ligase UBR5

Gene

UBR5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Miscellaneous

A cysteine residue is required for ubiquitin-thioester formation.

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-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 sitei2768Glycyl thioester intermediatePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1177 – 1245UBR-typePROSITE-ProRule annotationAdd BLAST69

GO - Molecular functioni

  • RNA binding Source: InterPro
  • ubiquitin binding Source: InterPro
  • ubiquitin protein ligase activity Source: FlyBase
  • ubiquitin-protein transferase activity Source: ProtInc
  • ubiquitin-ubiquitin ligase activity Source: BHF-UCL
  • zinc ion binding Source: InterPro
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cell proliferation Source: ProtInc
  • cellular response to DNA damage stimulus Source: HGNC
  • 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 gene expression Source: MGI
  • positive regulation of protein import into nucleus, translocation Source: BHF-UCL
  • progesterone receptor signaling pathway Source: HGNC
  • protein K48-linked ubiquitination Source: FlyBase
  • protein polyubiquitination Source: BHF-UCL
  • ubiquitin-dependent protein catabolic process Source: ProtInc
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionTransferase
Biological processDNA damage, DNA repair, Ubl conjugation pathway
LigandMetal-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: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
Short name:
hHYD
Progestin-induced protein
Gene namesi
Name:UBR5
Synonyms:EDD, EDD1, HYD, KIAA0896
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiHostDB:ENSG00000104517.12
HGNCiHGNC:16806 UBR5
MIMi608413 gene
neXtProtiNX_O95071

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2768C → A: Loss of ubiquitin binding. 1 Publication1

Organism-specific databases

DisGeNETi51366
OpenTargetsiENSG00000104517
PharmGKBiPA162408175

Polymorphism and mutation databases

BioMutaiUBR5

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000869312 – 2799E3 ubiquitin-protein ligase UBR5Add BLAST2798

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1
Modified residuei110PhosphoserineCombined sources1 Publication1
Modified residuei327PhosphoserineCombined sources1 Publication1
Modified residuei352Phosphoserine1 Publication1
Modified residuei578PhosphoserineCombined sources1 Publication1
Modified residuei612PhosphoserineCombined sources1 Publication1
Modified residuei637Phosphothreonine1 Publication1
Modified residuei808PhosphoserineCombined sources1 Publication1
Modified residuei928Phosphoserine1 Publication1
Modified residuei1018Phosphoserine1 Publication1
Modified residuei1115Phosphothreonine1 Publication1
Modified residuei1135Phosphothreonine1 Publication1
Modified residuei1227Phosphoserine1 Publication1
Modified residuei1308PhosphoserineCombined sources1 Publication1
Modified residuei1355Phosphoserine1 Publication1
Modified residuei1375Phosphoserine1 Publication1
Modified residuei1481Phosphoserine1 Publication1
Modified residuei1549PhosphoserineCombined sources1
Modified residuei1736Phosphothreonine1 Publication1
Modified residuei1741Phosphoserine1 Publication1
Modified residuei1746PhosphotyrosineCombined sources1
Modified residuei1780Phosphoserine1 Publication1
Modified residuei1969PhosphothreonineCombined sources1 Publication1
Modified residuei1990PhosphoserineCombined sources1
Modified residuei2026Phosphoserine1 Publication1
Modified residuei2028Phosphoserine1 Publication1
Modified residuei2030Phosphothreonine1 Publication1
Modified residuei2076Phosphoserine1 Publication1
Modified residuei2213Phosphothreonine1 Publication1
Modified residuei2241PhosphoserineCombined sources1
Modified residuei2289Phosphoserine1 Publication1
Modified residuei2469PhosphoserineCombined sources1
Modified residuei2484Phosphoserine1 Publication1
Modified residuei2486PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO95071
MaxQBiO95071
PaxDbiO95071
PeptideAtlasiO95071
PRIDEiO95071
ProteomicsDBi50641

PTM databases

iPTMnetiO95071
PhosphoSitePlusiO95071

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

HPAiHPA053688

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 DCAF1 proteins (EDVP complex). Interacts directly with DYRK2. Interacts with PIH1D1 (PubMed:24656813).4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi119501, 166 interactors
CORUMiO95071
DIPiDIP-32930N
ELMiO95071
IntActiO95071, 72 interactors
MINTiO95071
STRINGi9606.ENSP00000429084

Structurei

Secondary structure

12799
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi182 – 184Combined sources3
Helixi187 – 196Combined sources10
Helixi202 – 211Combined sources10
Turni212 – 214Combined sources3
Helixi216 – 224Combined sources9
Helixi2394 – 2408Combined sources15
Helixi2410 – 2412Combined sources3
Helixi2413 – 2420Combined sources8
Helixi2425 – 2433Combined sources9
Helixi2435 – 2452Combined sources18
Helixi2687 – 2692Combined sources6
Beta strandi2695 – 2698Combined sources4
Helixi2704 – 2720Combined sources17
Helixi2723 – 2734Combined sources12
Beta strandi2751 – 2756Combined sources6
Beta strandi2764 – 2766Combined sources3
Turni2767 – 2770Combined sources4
Beta strandi2771 – 2775Combined sources5
Helixi2780 – 2791Combined sources12

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO95071

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2377 – 2454PABCPROSITE-ProRule annotationAdd BLAST78
Domaini2462 – 2799HECTPROSITE-ProRule annotationAdd BLAST338

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi940 – 945Poly-Glu6
Compositional biasi980 – 985Poly-Ser6
Compositional biasi1528 – 1537Poly-Ser10
Compositional biasi1671 – 1681Poly-SerAdd BLAST11
Compositional biasi1762 – 1768Poly-Ala7
Compositional biasi1986 – 1997Asp/Glu-rich (acidic)Add BLAST12
Compositional biasi2036 – 2059Pro-richAdd BLAST24
Compositional biasi2329 – 2348Arg/Glu-rich (mixed charge)Add BLAST20
Compositional biasi2357 – 2366Arg/Asp-rich (mixed charge)10
Compositional biasi2489 – 2500Asp/Glu-rich (acidic)Add BLAST12
Compositional biasi2737 – 2757Pro-richAdd BLAST21

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1177 – 1245UBR-typePROSITE-ProRule annotationAdd BLAST69

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0943 Eukaryota
COG5021 LUCA
GeneTreeiENSGT00850000132302
HOGENOMiHOG000046848
HOVERGENiHBG096012
InParanoidiO95071
KOiK10593
OMAiCHRGHDC
OrthoDBiEOG091G005O
PhylomeDBiO95071
TreeFamiTF314406

Family and domain databases

CDDicd14423 CUE_UBR5, 1 hit
InterProiView protein in InterPro
IPR024725 E3_UbLigase_EDD_UBA
IPR000569 HECT_dom
IPR035983 Hect_E3_ubiquitin_ligase
IPR036053 PABP-dom
IPR002004 PABP_HYD
IPR009091 RCC1/BLIP-II
IPR003126 Znf_UBR
PfamiView protein in Pfam
PF11547 E3_UbLigase_EDD, 1 hit
PF00632 HECT, 1 hit
PF00658 PABP, 1 hit
SMARTiView protein in SMART
SM00119 HECTc, 1 hit
SM00517 PolyA, 1 hit
SM00396 ZnF_UBR1, 1 hit
SUPFAMiSSF50985 SSF50985, 1 hit
SSF56204 SSF56204, 2 hits
SSF63570 SSF63570, 1 hit
PROSITEiView protein in PROSITE
PS50237 HECT, 1 hit
PS51309 PABC, 1 hit
PS51157 ZF_UBR, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti134S → P in AAF88143 (PubMed:11714696).Curated1
Sequence conflicti229E → K in AAF88143 (PubMed:11714696).Curated1
Sequence conflicti258S → Y in AAF88143 (PubMed:11714696).Curated1
Sequence conflicti374 – 375IG → M in AAF88143 (PubMed:11714696).Curated2
Sequence conflicti772D → H in AAF88143 (PubMed:11714696).Curated1
Sequence conflicti780Q → R in AAF88143 (PubMed:11714696).Curated1
Sequence conflicti884D → G in AAF88143 (PubMed:11714696).Curated1
Sequence conflicti1811S → P in AAF88143 (PubMed:11714696).Curated1
Sequence conflicti2144L → H in AAF88143 (PubMed:11714696).Curated1
Sequence conflicti2282K → R in AAF88143 (PubMed:11714696).Curated1
Sequence conflicti2489D → N in AAF88143 (PubMed:11714696).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0514662150S → R. Corresponds to variant dbSNP:rs1062822Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0543992474Missing in isoform 2. 1 Publication1

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

Similar proteinsi

Entry informationi

Entry nameiUBR5_HUMAN
AccessioniPrimary (citable) accession number: O95071
Secondary accession number(s): B2RP24
, J3KMW7, O94970, Q9NPL3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: October 1, 2001
Last modified: June 20, 2018
This is version 192 of the entry and version 2 of the sequence. See 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

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

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