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Protein

E3 ubiquitin-protein ligase UBR5

Gene

Ubr5

Organism
Rattus norvegicus (Rat)
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) for 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 similarity).By similarity

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 sitei2757 – 27571Glycyl thioester intermediatePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1166 – 123469UBR-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • protein domain specific binding Source: RGD
  • RNA binding Source: InterPro
  • ubiquitin protein ligase activity Source: CACAO
  • zinc ion binding Source: InterPro

GO - Biological processi

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

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase UBR5 (EC:6.3.2.-)
Alternative name(s):
100 kDa protein
E3 ubiquitin-protein ligase, HECT domain-containing 1
Hyperplastic discs protein homolog
Gene namesi
Name:Ubr5
Synonyms:Dd5, Edd, Edd1, Hyd
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621236. Ubr5.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27882788E3 ubiquitin-protein ligase UBR5PRO_0000086933Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001PhosphoserineBy similarity
Modified residuei317 – 3171PhosphoserineBy similarity
Modified residuei342 – 3421PhosphoserineBy similarity
Modified residuei567 – 5671PhosphoserineBy similarity
Modified residuei601 – 6011PhosphoserineBy similarity
Modified residuei626 – 6261PhosphothreonineBy similarity
Modified residuei797 – 7971PhosphoserineBy similarity
Modified residuei917 – 9171PhosphoserineBy similarity
Modified residuei1007 – 10071PhosphoserineBy similarity
Modified residuei1104 – 11041PhosphothreonineBy similarity
Modified residuei1124 – 11241PhosphothreonineBy similarity
Modified residuei1216 – 12161PhosphoserineBy similarity
Modified residuei1297 – 12971PhosphoserineBy similarity
Modified residuei1344 – 13441PhosphoserineBy similarity
Modified residuei1364 – 13641PhosphoserineBy similarity
Modified residuei1470 – 14701PhosphoserineBy similarity
Modified residuei1538 – 15381PhosphoserineBy similarity
Modified residuei1725 – 17251PhosphothreonineBy similarity
Modified residuei1730 – 17301PhosphoserineBy similarity
Modified residuei1735 – 17351PhosphotyrosineBy similarity
Modified residuei1769 – 17691PhosphoserineBy similarity
Modified residuei1959 – 19591PhosphothreonineBy similarity
Modified residuei1980 – 19801PhosphoserineBy similarity
Modified residuei2016 – 20161PhosphoserineBy similarity
Modified residuei2018 – 20181PhosphoserineBy similarity
Modified residuei2020 – 20201PhosphothreonineBy similarity
Modified residuei2066 – 20661PhosphoserineBy similarity
Modified residuei2203 – 22031PhosphothreonineBy similarity
Modified residuei2231 – 22311PhosphoserineCombined sources
Modified residuei2279 – 22791PhosphoserineBy similarity
Modified residuei2473 – 24731PhosphoserineBy similarity
Modified residuei2475 – 24751PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ62671.
PRIDEiQ62671.

PTM databases

iPTMnetiQ62671.
PhosphoSiteiQ62671.

Expressioni

Tissue specificityi

Highest levels found in testis. Also present in liver, kidney, lung and brain.1 Publication

Developmental stagei

In early postnatal life, expression in the testis increases to reach a maximum around day 28.1 Publication

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. Interacts with PIH1D1.By similarity

GO - Molecular functioni

  • protein domain specific binding Source: RGD

Protein-protein interaction databases

IntActiQ62671. 1 interaction.
STRINGi10116.ENSRNOP00000009115.

Structurei

Secondary structure

1
2788
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2383 – 239614Combined sources
Helixi2400 – 24023Combined sources
Helixi2403 – 24108Combined sources
Helixi2415 – 24239Combined sources
Helixi2425 – 243915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NTWX-ray2.60A/C2383-2442[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2367 – 244478PABCPROSITE-ProRule annotationAdd
BLAST
Domaini2451 – 2788338HECTPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1613 – 167058Ser-richAdd
BLAST
Compositional biasi2319 – 236648Arg-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 fingeri1166 – 123469UBR-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0943. Eukaryota.
COG5021. LUCA.
HOGENOMiHOG000046848.
InParanoidiQ62671.

Family and domain databases

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.

Q62671-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKQAVKRLH MLREVSEKLN KYNLNSHPPL NVLEQATIKQ CVVGPNHAAF
60 70 80 90 100
LLEDGRICRI GFSVQPDRLE LGKPDNNDGS KLNSSSGTGR TSRPGRTSDS
110 120 130 140 150
PWFLSGSETL GRLAGNTLGS RWSSGVGGSG GGSSGRSSAG ARDSRRQTRV
160 170 180 190 200
IRTGRDRGSG LLGSQPQPVI PASVIPEELI SQAQVVLQGK SRSVIIRELQ
210 220 230 240 250
RTNLDVNLAV NNLLSRDDED GDDGDDTASE SYLPGEDLMS LLDADIHSAH
260 270 280 290 300
PSVIIDADAM FSEDISYFGY PSFRRSSLSR LGSSRVLLLP LERDSELLRE
310 320 330 340 350
RESVLRLRER RWLDGASFDN ERGSTSKEGE PNPDKKNTPV QSPVSLGEDL
360 370 380 390 400
QWWPDKDGTK FTCIGALYSE LVAVSSKGEL YQWKWTESEP YRNAQNPSLH
410 420 430 440 450
HPRATFLGLT NEKIVLLSAN SIRATVATEN NKVATWVDET LSSVASKLEH
460 470 480 490 500
TAQTYSELQG ERIVSLHCCA LYTCAQLENN LYWWGVVPFS QRKKMLEKAR
510 520 530 540 550
AKNKKPKSSA GVQSLNVRGG RQVCLRNNPL YHAGAVAFSI SAGIPKVGVL
560 570 580 590 600
MESVWNMNDS CRFQLRSPES LKSMEKASKT IETKPESKQE PVKTEMGPPP
610 620 630 640 650
SPASTCSDAS SIASSASMPY KRRRSTPAPK EEEKVNEEQW SLREVVFVED
660 670 680 690 700
VKNVPVGKVL KVDGAYVAVK FPGTSSNTNC QNSSGPDADP SSLLQDCRLL
710 720 730 740 750
RIDELQVVKT GGTPKVPDCF QRTPKKLCIP EKTEILAVNV DSKGVHAVLK
760 770 780 790 800
TGNWVRYCIF DLATGKAEQE NNFPTSSVAF LGQNERSVAI FTAGQESPII
810 820 830 840 850
LRDGNGTIYP MAKDCMGGIR DPDWLDLPPI SSLGMGVHSL INLPANSTIK
860 870 880 890 900
KKAAIIIMAV EKQTLMQHIL RCDYEACRQY LVNLEQAVVL EQNLQMLQTF
910 920 930 940 950
ISHRCDGNRN ILHACVSVCF PTSNKETKEE EEAERSERNT FAERLSAVEA
960 970 980 990 1000
IANAISVVSS NGPGNRAGSS SSRSLRLREM MRRSLRAAGL GRHEAGASSS
1010 1020 1030 1040 1050
DHQDPVSPPI APPSWVPDPP SMDPDGDIDF ILAPAVGSLT TAATGGGQGP
1060 1070 1080 1090 1100
STSTIPGPST EPSVVESKDR KANAHFILKL LCDSAVLQPY LRELLSAKDA
1110 1120 1130 1140 1150
RGMTPFMSAV SGRAYPAAIT ILETAQKIAK AEVSGSEKEE DVFMGMVCPS
1160 1170 1180 1190 1200
GTNPDDSPLY VLCCNDTCSF TWTGAEHINQ DIFECRTCGL LESLCCCTEC
1210 1220 1230 1240 1250
ARVCHKGHDC KLKRTSPTAY CDCWEKCKCK TLIAGQKSAR LDLLYRLLTA
1260 1270 1280 1290 1300
TNLVTLPNSR GEHLLLFLVQ TVARQTVEHC QYRPPRIRED RNRKTASPDD
1310 1320 1330 1340 1350
SDMPDHDLEP PRFAQLALER VLQDWNALRS MIMFGSQENK DPLSASSRIG
1360 1370 1380 1390 1400
HLLPEEQVYL NQQSGTIRLD CFTHCLIVKC TADILLLDTL LGTLVKELQN
1410 1420 1430 1440 1450
KYTPGRREEA IAVTMRFLRS VARVFVILSV EMASSKKKNN FIPQPIGKCK
1460 1470 1480 1490 1500
RVFQALLPYA VEELCNVAES LIVPVRMGIA RPTAPFTLAS TSIDAMQGSE
1510 1520 1530 1540 1550
ELFSVEPLPP RPSSDQSSSS SQSQSSYIIR NPQQRRISQS QPVRGREEEQ
1560 1570 1580 1590 1600
DDIVSADVEE VEVVEGVAGE EDHHDEQEEH GEENAEAEGH HDEHDEDGSD
1610 1620 1630 1640 1650
MELDLLAAAE TESDSESNHS NQDNASGRRS VVTAATAGSE AGASSVPAFF
1660 1670 1680 1690 1700
SEDDSQSNDS SDSDSSSSQS DDIEQETFML DEPLERTTNS SHANGAAQAP
1710 1720 1730 1740 1750
RSMQWAVRNT QHQRAASTAP SSTSTPAASS AGLIYIDPSN LRRSGTISTS
1760 1770 1780 1790 1800
AAAAAAALEA SNASSYLTSA SSLARAYSIV IRQISDLMGL IPKYNHLVYS
1810 1820 1830 1840 1850
QIPAAVKLTY QDAVNLQNYV EEKLIPTWNW MVSIMDSTEA QLRYGSALAS
1860 1870 1880 1890 1900
AGDPGHPNHP LHASQNSARR ERMTAREEAS LRTLEGRRRR ATLLSARQGM
1910 1920 1930 1940 1950
MSARGDFLNY ALSLMRSHND EHSDVLPVLD VCSLKHVAYV FQALIYWIKA
1960 1970 1980 1990 2000
MNQQTTLDTP QLERKRTREL LELGIDNEDS EHENDDDTSQ SATLNDKDDE
2010 2020 2030 2040 2050
SLPAETGQNH PFFRRSDSMT FLGCIPPNPF EVPLAEAIPL ADQPHLLQPN
2060 2070 2080 2090 2100
ARKEDLFGRP SQGLYSSSAG SGKCLVEVTM DRNCLEVLPT KMSYAANLKN
2110 2120 2130 2140 2150
VMNMQNRQKK AGEDQSMLAE EADSSKPGPS AHDVAAQLKS SLLAEIGLTE
2160 2170 2180 2190 2200
SEGPPLTSFR PQCSFMGMVI SHDMLLGRWR LSLELFGRVF MEDVGAEPGS
2210 2220 2230 2240 2250
ILTELGGFEV KESKFRREME KLRNQQSRDL SLEVDRDRDL LIQQTMRQLN
2260 2270 2280 2290 2300
NHFGRRCATT PMAVHRVKVT FKDEPGEGSG VARSFYTAIA QAFLSNEKLP
2310 2320 2330 2340 2350
NLDCIQNANK GTHTSLMQRL RNRGERDRER EREREMRRSS GLRAGSRRDR
2360 2370 2380 2390 2400
DRDFRRQLSI DTRPFRPASE GNPSDDPDPL PAHRQALGER LYPRVQAMQP
2410 2420 2430 2440 2450
AFASKITGML LELSPAQLLL LLASEDSLRA RVEEAMELIV AHGRENGADS
2460 2470 2480 2490 2500
ILDLGLLDSS EKVQENRKRH GSSRSVVDMD LDDTDDGDDN APLFYQPGKR
2510 2520 2530 2540 2550
GFYTPRPGKN TEARLNCFRN IGRILGLCLL QNELCPITLN RHVIKVLLGR
2560 2570 2580 2590 2600
KVNWHDFAFF DPVMYESLRQ LILASQSSDA DAVFSAMDLA FAVDLCKEEG
2610 2620 2630 2640 2650
GGQVELIPNG VNIPVTPQNV YEYVRKYAEH RMLVVAEQPL HAMRKGLLDV
2660 2670 2680 2690 2700
LPKNSLEDLT AEDFRLLVNG CGEVNVQMLI SFTSFNDESG ENAEKLLQFK
2710 2720 2730 2740 2750
RWFWSIVERM SMTERQDLVY FWTSSPSLPA SEEGFQPMPS ITIRPPDDQH
2760 2770 2780
LPTANTCISR LYVPLYSSKQ ILKQKLLLAI KTKNFGFV
Length:2,788
Mass (Da):308,027
Last modified:February 22, 2012 - v3
Checksum:iC2EA68B962627231
GO

Sequence cautioni

The sequence CAA45756.1 differs from that shown. Reason: Frameshift at position 30. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1890 – 18901Missing in CAA45756 (PubMed:1533713).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64411 mRNA. Translation: CAA45756.1. Frameshift.
PIRiS22659.
UniGeneiRn.54812.

Genome annotation databases

UCSCiRGD:621236. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64411 mRNA. Translation: CAA45756.1. Frameshift.
PIRiS22659.
UniGeneiRn.54812.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NTWX-ray2.60A/C2383-2442[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ62671. 1 interaction.
STRINGi10116.ENSRNOP00000009115.

PTM databases

iPTMnetiQ62671.
PhosphoSiteiQ62671.

Proteomic databases

PaxDbiQ62671.
PRIDEiQ62671.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:621236. rat.

Organism-specific databases

RGDi621236. Ubr5.

Phylogenomic databases

eggNOGiKOG0943. Eukaryota.
COG5021. LUCA.
HOGENOMiHOG000046848.
InParanoidiQ62671.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ62671.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Molecular characterization of a novel rat protein structurally related to poly(A) binding proteins and the 70K protein of the U1 small nuclear ribonucleoprotein particle (snRNP)."
    Mueller D., Rehbein M., Baumeister H., Richter D.
    Nucleic Acids Res. 20:1471-1475(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1868-2788.
    Strain: Wistar.
    Tissue: Testis.
  3. Erratum
    Mueller D., Rehbein M., Baumeister H., Richter D.
    Nucleic Acids Res. 20:2624-2624(1992)
  4. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE FRAMESHIFT.
  5. "Characterization of rat100, a 300-kilodalton ubiquitin-protein ligase induced in germ cells of the rat testis and similar to the Drosophila hyperplastic discs gene."
    Oughtred R., Bedard N., Adegoke O.A.J., Morales C.R., Trasler J., Rajapurohitam V., Wing S.S.
    Endocrinology 143:3740-3747(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2231 AND SER-2475, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUBR5_RAT
AccessioniPrimary (citable) accession number: Q62671
Secondary accession number(s): F1LRS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 22, 2012
Last modified: June 8, 2016
This is version 122 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.