Reviewed, UniProtKB/Swiss-Prot O95071 (UBR5_HUMAN)

Names and origin

Protein names

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 names

Name:	UBR5
Synonyms:	EDD, EDD1, HYD, KIAA0896

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2799 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific amino-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation By similarity. May be involved in maturation and/or transcriptional regulation of mRNA. 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.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Binds TOPBP1.
Subcellular location	Nucleus.
Tissue specificity	Widely expressed. Most abundant in testis and expressed at high levels in brain, pituitary and kidney.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Miscellaneous	A cysteine residue is required for ubiquitin-thioester formation.
Sequence similarities	Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain. Contains 1 PABC domain. Contains 1 UBR-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell proliferation Ref.1 Traceable author statement. Source: ProtInc progesterone receptor signaling pathway Inferred from direct assay. Source: HGNC protein modification process Inferred from electronic annotation. Source: InterPro response to DNA damage stimulus Inferred from direct assay. Source: HGNC ubiquitin-dependent protein catabolic process Ref.1 Traceable author statement. Source: ProtInc
Cellular component	nucleus Inferred from direct assay. Source: HGNC soluble fraction Ref.1 Traceable author statement. Source: ProtInc
Molecular function	RNA binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct ubiquitin-protein ligase activity Ref.1 Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAGED1	Q9Y5V3	1	EBI-358329,EBI-716006
MCRS1	Q96EZ8	1	EBI-358329,EBI-348259

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2799

2799

E3 ubiquitin-protein ligase UBR5

PRO_0000086931

Regions

Domain

2377 – 2454

78

PABC

Domain

2462 – 2799

338

HECT

Zinc finger

1177 – 1245

69

UBR-type

Compositional bias

940 – 945

6

Poly-Glu

Compositional bias

980 – 985

6

Poly-Ser

Compositional bias

1528 – 1537

10

Poly-Ser

Compositional bias

1671 – 1681

11

Poly-Ser

Compositional bias

1762 – 1768

7

Poly-Ala

Compositional bias

1986 – 1997

12

Asp/Glu-rich (acidic)

Compositional bias

2036 – 2059

24

Pro-rich

Compositional bias

2329 – 2348

20

Arg/Glu-rich (mixed charge)

Compositional bias

2357 – 2366

10

Arg/Asp-rich (mixed charge)

Compositional bias

2489 – 2500

12

Asp/Glu-rich (acidic)

Compositional bias

2737 – 2757

21

Pro-rich

Sites

Active site

2768

1

Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue

139

1

Phosphoserine Ref.14

Modified residue

287

1

Phosphoserine Ref.7

Modified residue

327

1

Phosphoserine Ref.10 Ref.15

Modified residue

598

1

Phosphoserine Ref.12

Modified residue

1308

1

Phosphoserine Ref.15

Modified residue

1549

1

Phosphoserine Ref.9 Ref.13 Ref.14 Ref.15

Modified residue

1746

1

Phosphotyrosine Ref.8

Modified residue

1969

1

Phosphothreonine Ref.14 Ref.15

Modified residue

2071

1

Phosphoserine Ref.11

Modified residue

2486

1

Phosphoserine Ref.15

Natural variations

Natural variant

2150

1

S → R: dbSNP rs1062822.

VAR_051466

Experimental info

Mutagenesis

2768

1

C → A: Loss of ubiquitin binding. Ref.17

Sequence conflict

134

1

S → P in AAF88143. Ref.2

Sequence conflict

229

1

E → K in AAF88143. Ref.2

Sequence conflict

258

1

S → Y in AAF88143. Ref.2

Sequence conflict

374 – 375

2

IG → M in AAF88143. Ref.2

Sequence conflict

772

1

D → H in AAF88143. Ref.2

Sequence conflict

780

1

Q → R in AAF88143. Ref.2

Sequence conflict

884

1

D → G in AAF88143. Ref.2

Sequence conflict

1811

1

S → P in AAF88143. Ref.2

Sequence conflict

2144

1

L → H in AAF88143. Ref.2

Sequence conflict

2282

1

K → R in AAF88143. Ref.2

Sequence conflict

2474

1

Missing in BAA74919. Ref.3

Sequence conflict

2489

1

D → N in AAF88143. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2799

Helix Strand Turn

Details...

Helix

182 – 184

3

Helix

187 – 196

10

Helix

202 – 211

10

Turn

212 – 214

3

Helix

216 – 224

9

Helix

2394 – 2408

15

Helix

2410 – 2412

3

Helix

2413 – 2420

8

Helix

2425 – 2433

9

Helix

2435 – 2452

18

Sequences

	Sequence		Length	Mass (Da)
	O95071-1 [UniParc]. Last modified October 1, 2001. Version 2. Checksum: 871300DB404FF561	FASTA	2,799	309,352
	10 20 30 40 50 60 MTSIHFVVHP LPGTEDQLND RLREVSEKLN KYNLNSHPPL NVLEQATIKQ CVVGPNHAAF 70 80 90 100 110 120 LLEDGRVCRI GFSVQPDRLE LGKPDNNDGS KLNSNSGAGR TSRPGRTSDS PWFLSGSETL 130 140 150 160 170 180 GRLAGNTLGS RWSSGVGGSG GGSSGRSSAG ARDSRRQTRV IRTGRDRGSG LLGSQPQPVI 190 200 210 220 230 240 PASVIPEELI SQAQVVLQGK SRSVIIRELQ RTNLDVNLAV NNLLSRDDED GDDGDDTASE 250 260 270 280 290 300 SYLPGEDLMS LLDADIHSAH PSVIIDADAM FSEDISYFGY PSFRRSSLSR LGSSRVLLLP 310 320 330 340 350 360 LERDSELLRE RESVLRLRER RWLDGASFDN ERGSTSKEGE PNLDKKNTPV QSPVSLGEDL 370 380 390 400 410 420 QWWPDKDGTK FICIGALYSE LLAVSSKGEL YQWKWSESEP YRNAQNPSLH HPRATFLGLT 430 440 450 460 470 480 NEKIVLLSAN SIRATVATEN NKVATWVDET LSSVASKLEH TAQTYSELQG ERIVSLHCCA 490 500 510 520 530 540 LYTCAQLENS LYWWGVVPFS QRKKMLEKAR AKNKKPKSSA GISSMPNITV GTQVCLRNNP 550 560 570 580 590 600 LYHAGAVAFS ISAGIPKVGV LMESVWNMND SCRFQLRSPE SLKNMEKASK TTEAKPESKQ 610 620 630 640 650 660 EPVKTEMGPP PSPASTCSDA SSIASSASMP YKRRRSTPAP KEEEKVNEEQ WSLREVVFVE 670 680 690 700 710 720 DVKNVPVGKV LKVDGAYVAV KFPGTSSNTN CQNSSGPDAD PSSLLQDCRL LRIDELQVVK 730 740 750 760 770 780 TGGTPKVPDC FQRTPKKLCI PEKTEILAVN VDSKGVHAVL KTGNWVRYCI FDLATGKAEQ 790 800 810 820 830 840 ENNFPTSSIA FLGQNERNVA IFTAGQESPI ILRDGNGTIY PMAKDCMGGI RDPDWLDLPP 850 860 870 880 890 900 ISSLGMGVHS LINLPANSTI KKKAAVIIMA VEKQTLMQHI LRCDYEACRQ YLMNLEQAVV 910 920 930 940 950 960 LEQNLQMLQT FISHRCDGNR NILHACVSVC FPTSNKETKE EEEAERSERN TFAERLSAVE 970 980 990 1000 1010 1020 AIANAISVVS SNGPGNRAGS SSSRSLRLRE MMRRSLRAAG LGRHEAGASS SDHQDPVSPP 1030 1040 1050 1060 1070 1080 IAPPSWVPDP PAMDPDGDID FILAPAVGSL TTAATGTGQG PSTSTIPGPS TEPSVVESKD 1090 1100 1110 1120 1130 1140 RKANAHFILK LLCDSVVLQP YLRELLSAKD ARGMTPFMSA VSGRAYPAAI TILETAQKIA 1150 1160 1170 1180 1190 1200 KAEISSSEKE EDVFMGMVCP SGTNPDDSPL YVLCCNDTCS FTWTGAEHIN QDIFECRTCG 1210 1220 1230 1240 1250 1260 LLESLCCCTE CARVCHKGHD CKLKRTSPTA YCDCWEKCKC KTLIAGQKSA RLDLLYRLLT 1270 1280 1290 1300 1310 1320 ATNLVTLPNS RGEHLLLFLV QTVARQTVEH CQYRPPRIRE DRNRKTASPE DSDMPDHDLE 1330 1340 1350 1360 1370 1380 PPRFAQLALE RVLQDWNALK SMIMFGSQEN KDPLSASSRI GHLLPEEQVY LNQQSGTIRL 1390 1400 1410 1420 1430 1440 DCFTHCLIVK CTADILLLDT LLGTLVKELQ NKYTPGRREE AIAVTMRFLR SVARVFVILS 1450 1460 1470 1480 1490 1500 VEMASSKKKN NFIPQPIGKC KRVFQALLPY AVEELCNVAE SLIVPVRMGI ARPTAPFTLA 1510 1520 1530 1540 1550 1560 STSIDAMQGS EELFSVEPLP PRPSSDQSSS SSQSQSSYII RNPQQRRISQ SQPVRGRDEE 1570 1580 1590 1600 1610 1620 QDDIVSADVE EVEVVEGVAG EEDHHDEQEE HGEENAEAEG QHDEHDEDGS DMELDLLAAA 1630 1640 1650 1660 1670 1680 ETESDSESNH SNQDNASGRR SVVTAATAGS EAGASSVPAF FSEDDSQSND SSDSDSSSSQ 1690 1700 1710 1720 1730 1740 SDDIEQETFM LDEPLERTTN SSHANGAAQA PRSMQWAVRN TQHQRAASTA PSSTSTPAAS 1750 1760 1770 1780 1790 1800 SAGLIYIDPS NLRRSGTIST SAAAAAAALE ASNASSYLTS ASSLARAYSI VIRQISDLMG 1810 1820 1830 1840 1850 1860 LIPKYNHLVY SQIPAAVKLT YQDAVNLQNY VEEKLIPTWN WMVSIMDSTE AQLRYGSALA 1870 1880 1890 1900 1910 1920 SAGDPGHPNH PLHASQNSAR RERMTAREEA SLRTLEGRRR ATLLSARQGM MSARGDFLNY 1930 1940 1950 1960 1970 1980 ALSLMRSHND EHSDVLPVLD VCSLKHVAYV FQALIYWIKA MNQQTTLDTP QLERKRTREL 1990 2000 2010 2020 2030 2040 LELGIDNEDS EHENDDDTNQ SATLNDKDDD SLPAETGQNH PFFRRSDSMT FLGCIPPNPF 2050 2060 2070 2080 2090 2100 EVPLAEAIPL ADQPHLLQPN ARKEDLFGRP SQGLYSSSAS SGKCLMEVTV DRNCLEVLPT 2110 2120 2130 2140 2150 2160 KMSYAANLKN VMNMQNRQKK EGEEQPVLPE ETESSKPGPS AHDLAAQLKS SLLAEIGLTE 2170 2180 2190 2200 2210 2220 SEGPPLTSFR PQCSFMGMVI SHDMLLGRWR LSLELFGRVF MEDVGAEPGS ILTELGGFEV 2230 2240 2250 2260 2270 2280 KESKFRREME KLRNQQSRDL SLEVDRDRDL LIQQTMRQLN NHFGRRCATT PMAVHRVKVT 2290 2300 2310 2320 2330 2340 FKDEPGEGSG VARSFYTAIA QAFLSNEKLP NLECIQNANK GTHTSLMQRL RNRGERDRER 2350 2360 2370 2380 2390 2400 EREREMRRSS GLRAGSRRDR DRDFRRQLSI DTRPFRPASE GNPSDDPEPL PAHRQALGER 2410 2420 2430 2440 2450 2460 LYPRVQAMQP AFASKITGML LELSPAQLLL LLASEDSLRA RVDEAMELII AHGRENGADS 2470 2480 2490 2500 2510 2520 ILDLGLVDSS EKVQQENRKR HGSSRSVVDM DLDDTDDGDD NAPLFYQPGK RGFYTPRPGK 2530 2540 2550 2560 2570 2580 NTEARLNCFR NIGRILGLCL LQNELCPITL NRHVIKVLLG RKVNWHDFAF FDPVMYESLR 2590 2600 2610 2620 2630 2640 QLILASQSSD ADAVFSAMDL AFAIDLCKEE GGGQVELIPN GVNIPVTPQN VYEYVRKYAE 2650 2660 2670 2680 2690 2700 HRMLVVAEQP LHAMRKGLLD VLPKNSLEDL TAEDFRLLVN GCGEVNVQML ISFTSFNDES 2710 2720 2730 2740 2750 2760 GENAEKLLQF KRWFWSIVEK MSMTERQDLV YFWTSSPSLP ASEEGFQPMP SITIRPPDDQ 2770 2780 2790 HLPTANTCIS RLYVPLYSSK QILKQKLLLA IKTKNFGFV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a human HECT family protein with homology to the Drosophila tumor suppressor gene hyperplastic discs." Callaghan M.J., Russell A.J., Woollatt E., Sutherland G.R., Sutherland R.L., Watts C.K.W. Oncogene 17:3479-3491(1998) [PubMed: 10030672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart and Placenta.
[2]	"Cooperation of HECT-domain ubiquitin ligase hHYD and DNA topoisomerase II-binding protein for DNA damage response." Honda Y., Tojo M., Matsuzaki K., Anan T., Matsumoto M., Ando M., Saya H., Nakao M. J. Biol. Chem. 277:3599-3605(2002) [PubMed: 11714696] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TOPBP1. Tissue: Fetal brain.
[3]	"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." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:355-364(1998) [PubMed: 10048485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed: 12168954] [Abstract] Cited for: SEQUENCE REVISION.
[5]	Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[7]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, MASS SPECTROMETRY.
[8]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." 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. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1746, MASS SPECTROMETRY.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1549, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2071, MASS SPECTROMETRY.
[12]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598, MASS SPECTROMETRY. Tissue: Platelet.
[13]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1549, MASS SPECTROMETRY.
[14]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139; SER-1549 AND THR-1969, MASS SPECTROMETRY.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327; SER-1308; SER-1549; THR-1969 AND SER-2486, MASS SPECTROMETRY.
[16]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]	"X-ray structure of the human hyperplastic discs protein: an ortholog of the C-terminal domain of poly(A)-binding protein." Deo R.C., Sonenberg N., Burley S.K. Proc. Natl. Acad. Sci. U.S.A. 98:4414-4419(2001) [PubMed: 11287654] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.04 ANGSTROMS) OF 2391-2455, MUTAGENESIS OF CYS-2768.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF006010 mRNA. Translation: AAD01259.2.
U95000 mRNA. Translation: AAF88143.1.
AB020703 mRNA. Translation: BAA74919.3. Different initiation.
BC137234 mRNA. Translation: AAI37235.1.

IPI

IPI00026320.

RefSeq

NP_056986.2.

UniGene

Hs.591856

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I2T	X-ray	1.04	A	2393-2453	[»]
2QHO	X-ray	1.85	B/D/F/H	180-230	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O95071. 10 interactions.

PTM databases

PhosphoSite

O95071.

Proteomic databases

PRIDE

O95071.

Genome annotation databases

Ensembl

ENSG00000104517. Homo sapiens. [Contig view]

GeneID

51366.

KEGG

hsa:51366.

Organism-specific databases

GeneCards

GC08M103336.
GC08M103338.

H-InvDB

HIX0007699.

HGNC

HGNC:16806. UBR5.

MIM

608413. gene.

PharmGKB

PA142671917.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O95071.

HOVERGEN

O95071.

OMA

O95071. MPYKRRR.

Gene expression databases

ArrayExpress

O95071.

Bgee

O95071.

CleanEx

HS_UBR5.

GermOnline

ENSG00000104517. Homo sapiens.

Family and domain databases

InterPro

IPR000569. HECT.
IPR002004. PABP_HYD.
IPR003126. Znf_N-recognin.
IPR013993. Znf_N-recognin_met.
[Graphical view]

Gene3D

G3DSA:1.10.1900.10. PABP_HYD. 1 hit.

Pfam

PF00632. HECT. 1 hit.
PF00658. PABP. 1 hit.
PF02207. zf-UBR. 1 hit.
[Graphical view]

SMART

SM00119. HECTc. 1 hit.
SM00517. PolyA. 1 hit.
SM00396. ZnF_UBR1. 1 hit.
[Graphical view]

PROSITE

PS50237. HECT. 1 hit.
PS51309. PABC. 1 hit.
PS51157. ZF_UBR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

54837.

SOURCE

Search...

Entry information

Entry name

UBR5_HUMAN

Accession

Primary (citable) accession number: O95071
Secondary accession number(s): B2RP24, O94970, Q9NPL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 5, 2002
Last sequence update:	October 1, 2001
Last modified:	June 16, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)