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Sequence of UBR5_HUMAN

EC Number:2.3.2.26

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
HECT-type E3 ubiquitin transferase
O95071
Homo sapiens
2799
309352
Reaction
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
Other sequences found for EC No. 2.3.2.26

General information:

Sequence
show sequence in fasta format
   0 MTSIHFVVHP LPGTEDQLND RLREVSEKLN KYNLNSHPPL NVLEQATIKQ CVVGPNHAAF
  60 LLEDGRVCRI GFSVQPDRLE LGKPDNNDGS KLNSNSGAGR TSRPGRTSDS PWFLSGSETL
 120 GRLAGNTLGS RWSSGVGGSG GGSSGRSSAG ARDSRRQTRV IRTGRDRGSG LLGSQPQPVI
 180 PASVIPEELI SQAQVVLQGK SRSVIIRELQ RTNLDVNLAV NNLLSRDDED GDDGDDTASE
 240 SYLPGEDLMS LLDADIHSAH PSVIIDADAM FSEDISYFGY PSFRRSSLSR LGSSRVLLLP
 300 LERDSELLRE RESVLRLRER RWLDGASFDN ERGSTSKEGE PNLDKKNTPV QSPVSLGEDL
 360 QWWPDKDGTK FICIGALYSE LLAVSSKGEL YQWKWSESEP YRNAQNPSLH HPRATFLGLT
 420 NEKIVLLSAN SIRATVATEN NKVATWVDET LSSVASKLEH TAQTYSELQG ERIVSLHCCA
 480 LYTCAQLENS LYWWGVVPFS QRKKMLEKAR AKNKKPKSSA GISSMPNITV GTQVCLRNNP
 540 LYHAGAVAFS ISAGIPKVGV LMESVWNMND SCRFQLRSPE SLKNMEKASK TTEAKPESKQ
 600 EPVKTEMGPP PSPASTCSDA SSIASSASMP YKRRRSTPAP KEEEKVNEEQ WSLREVVFVE
 660 DVKNVPVGKV LKVDGAYVAV KFPGTSSNTN CQNSSGPDAD PSSLLQDCRL LRIDELQVVK
 720 TGGTPKVPDC FQRTPKKLCI PEKTEILAVN VDSKGVHAVL KTGNWVRYCI FDLATGKAEQ
 780 ENNFPTSSIA FLGQNERNVA IFTAGQESPI ILRDGNGTIY PMAKDCMGGI RDPDWLDLPP
 840 ISSLGMGVHS LINLPANSTI KKKAAVIIMA VEKQTLMQHI LRCDYEACRQ YLMNLEQAVV
 900 LEQNLQMLQT FISHRCDGNR NILHACVSVC FPTSNKETKE EEEAERSERN TFAERLSAVE
 960 AIANAISVVS SNGPGNRAGS SSSRSLRLRE MMRRSLRAAG LGRHEAGASS SDHQDPVSPP
1020 IAPPSWVPDP PAMDPDGDID FILAPAVGSL TTAATGTGQG PSTSTIPGPS TEPSVVESKD
1080 RKANAHFILK LLCDSVVLQP YLRELLSAKD ARGMTPFMSA VSGRAYPAAI TILETAQKIA
1140 KAEISSSEKE EDVFMGMVCP SGTNPDDSPL YVLCCNDTCS FTWTGAEHIN QDIFECRTCG
1200 LLESLCCCTE CARVCHKGHD CKLKRTSPTA YCDCWEKCKC KTLIAGQKSA RLDLLYRLLT
1260 ATNLVTLPNS RGEHLLLFLV QTVARQTVEH CQYRPPRIRE DRNRKTASPE DSDMPDHDLE
1320 PPRFAQLALE RVLQDWNALK SMIMFGSQEN KDPLSASSRI GHLLPEEQVY LNQQSGTIRL
1380 DCFTHCLIVK CTADILLLDT LLGTLVKELQ NKYTPGRREE AIAVTMRFLR SVARVFVILS
1440 VEMASSKKKN NFIPQPIGKC KRVFQALLPY AVEELCNVAE SLIVPVRMGI ARPTAPFTLA
1500 STSIDAMQGS EELFSVEPLP PRPSSDQSSS SSQSQSSYII RNPQQRRISQ SQPVRGRDEE
1560 QDDIVSADVE EVEVVEGVAG EEDHHDEQEE HGEENAEAEG QHDEHDEDGS DMELDLLAAA
1620 ETESDSESNH SNQDNASGRR SVVTAATAGS EAGASSVPAF FSEDDSQSND SSDSDSSSSQ
1680 SDDIEQETFM LDEPLERTTN SSHANGAAQA PRSMQWAVRN TQHQRAASTA PSSTSTPAAS
1740 SAGLIYIDPS NLRRSGTIST SAAAAAAALE ASNASSYLTS ASSLARAYSI VIRQISDLMG
1800 LIPKYNHLVY SQIPAAVKLT YQDAVNLQNY VEEKLIPTWN WMVSIMDSTE AQLRYGSALA
1860 SAGDPGHPNH PLHASQNSAR RERMTAREEA SLRTLEGRRR ATLLSARQGM MSARGDFLNY
1920 ALSLMRSHND EHSDVLPVLD VCSLKHVAYV FQALIYWIKA MNQQTTLDTP QLERKRTREL
1980 LELGIDNEDS EHENDDDTNQ SATLNDKDDD SLPAETGQNH PFFRRSDSMT FLGCIPPNPF
2040 EVPLAEAIPL ADQPHLLQPN ARKEDLFGRP SQGLYSSSAS SGKCLMEVTV DRNCLEVLPT
2100 KMSYAANLKN VMNMQNRQKK EGEEQPVLPE ETESSKPGPS AHDLAAQLKS SLLAEIGLTE
2160 SEGPPLTSFR PQCSFMGMVI SHDMLLGRWR LSLELFGRVF MEDVGAEPGS ILTELGGFEV
2220 KESKFRREME KLRNQQSRDL SLEVDRDRDL LIQQTMRQLN NHFGRRCATT PMAVHRVKVT
2280 FKDEPGEGSG VARSFYTAIA QAFLSNEKLP NLECIQNANK GTHTSLMQRL RNRGERDRER
2340 EREREMRRSS GLRAGSRRDR DRDFRRQLSI DTRPFRPASE GNPSDDPEPL PAHRQALGER
2400 LYPRVQAMQP AFASKITGML LELSPAQLLL LLASEDSLRA RVDEAMELII AHGRENGADS
2460 ILDLGLVDSS EKVQQENRKR HGSSRSVVDM DLDDTDDGDD NAPLFYQPGK RGFYTPRPGK
2520 NTEARLNCFR NIGRILGLCL LQNELCPITL NRHVIKVLLG RKVNWHDFAF FDPVMYESLR
2580 QLILASQSSD ADAVFSAMDL AFAIDLCKEE GGGQVELIPN GVNIPVTPQN VYEYVRKYAE
2640 HRMLVVAEQP LHAMRKGLLD VLPKNSLEDL TAEDFRLLVN GCGEVNVQML ISFTSFNDES
2700 GENAEKLLQF KRWFWSIVEK MSMTERQDLV YFWTSSPSLP ASEEGFQPMP SITIRPPDDQ
2760 HLPTANTCIS RLYVPLYSSK QILKQKLLLA IKTKNFGFV
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
751679
Callaghan M.J.,Russell A.J.,Woollatt E.,Sutherland G.R.,Sutherland R.L.,Watts C.K.W.
Identification of a human HECT family protein with homology to the Drosophila tumor suppressor gene hyperplastic discs.
Oncogene
17
3479-3491
1998
751680
Honda Y.,Tojo M.,Matsuzaki K.,Anan T.,Matsumoto M.,Ando M.,Saya H.,Nakao M.
Cooperation of HECT-domain ubiquitin ligase hHYD and DNA topoisomerase II-binding protein for DNA damage response.
J. Biol. Chem.
277
3599-3605
2002
751681
Nagase T.,Ishikawa K.,Suyama M.,Kikuno R.,Hirosawa M.,Miyajima N.,Tanaka A.,Kotani H.,Nomura N.,Ohara O.
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.
DNA Res.
5
355-364
1998
751682
Nakajima D.,Okazaki N.,Yamakawa H.,Kikuno R.,Ohara O.,Nagase T.
Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.
DNA Res.
9
99-106
2002
751684
Nusbaum C.,Mikkelsen T.S.,Zody M.C.,Asakawa S.,Taudien S.,Garber M.,Kodira C.D.,Schueler M.G.,Shimizu A.,Whittaker C.A.,Chang J.L.,Cuomo C.A.,Dewar K.,FitzGerald M.G.,Yang X.,Allen N.R.,Anderson S.,Asakawa T.,Blechschmidt K.,Bloom T.,Borowsky M.L.,Butler J.,Cook A.,Corum B.,DeArellano K.,DeCaprio D.,Dooley K.T.,Dorris L. III,Engels R.,Gloeckner G.,Hafez N.,Hagopian D.S.,Hall J.L.,Ishikawa S.K.,Jaffe D.B.,Kamat A.,Kudoh J.,Lehmann R.,Lokitsang T.,Macdonald P.,Major J.E.,Matthews C.D.,Mauceli E.,Menzel U.,Mihalev A.H.,Minoshima S.,Murayama Y.,Naylor J.W.,Nicol R.,Nguyen C.,O'Leary S.B.,O'Neill K.,Parker S.C.J.,Polley A.,Raymond C.K.,Reichwald K.,Rodriguez J.,Sasaki T.,Schilhabel M.,Siddiqui R.,Smith C.L.,Sneddon T.P.,Talamas J.A.,Tenzin P.,Topham K.,Venkataraman V.,Wen G.,Yamazaki S.,Young S.K.,Zeng Q.,Zimmer A.R.,Rosenthal A.,Birren B.W.,Platzer M.,Shimizu N.,Lander E.S.
DNA sequence and analysis of human chromosome 8.
Nature
439
331-335
2006
751685
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
751686
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.
Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.
Nat. Biotechnol.
23
94-101
2005
751687
Olsen J.V.,Blagoev B.,Gnad F.,Macek B.,Kumar C.,Mortensen P.,Mann M.
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
Cell
127
635-648
2006
751688
Daub H.,Olsen J.V.,Bairlein M.,Gnad F.,Oppermann F.S.,Korner R.,Greff Z.,Keri G.,Stemmann O.,Mann M.
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
Mol. Cell
31
438-448
2008
751689
Dephoure N.,Zhou C.,Villen J.,Beausoleil S.A.,Bakalarski C.E.,Elledge S.J.,Gygi S.P.
A quantitative atlas of mitotic phosphorylation.
Proc. Natl. Acad. Sci. U.S.A.
105
10762-10767
2008
751690
Gauci S.,Helbig A.O.,Slijper M.,Krijgsveld J.,Heck A.J.,Mohammed S.
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
Anal. Chem.
81
4493-4501
2009
751691
Oppermann F.S.,Gnad F.,Olsen J.V.,Hornberger R.,Greff Z.,Keri G.,Mann M.,Daub H.
Large-scale proteomics analysis of the human kinome.
Mol. Cell. Proteomics
8
1751-1764
2009
751692
Maddika S.,Chen J.
Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 ligase.
Nat. Cell Biol.
11
409-419
2009
751693
Mayya V.,Lundgren D.H.,Hwang S.-I.,Rezaul K.,Wu L.,Eng J.K.,Rodionov V.,Han D.K.
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
Sci. Signal.
2
0-0
2009
751694
Olsen J.V.,Vermeulen M.,Santamaria A.,Kumar C.,Miller M.L.,Jensen L.J.,Gnad F.,Cox J.,Jensen T.S.,Nigg E.A.,Brunak S.,Mann M.
Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
Sci. Signal.
3
0-0
2010
751695
Burkard T.R.,Planyavsky M.,Kaupe I.,Breitwieser F.P.,Buerckstuemmer T.,Bennett K.L.,Superti-Furga G.,Colinge J.
Initial characterization of the human central proteome.
BMC Syst. Biol.
5
17-17
2011
751696
Cojocaru M.,Bouchard A.,Cloutier P.,Cooper J.J.,Varzavand K.,Price D.H.,Coulombe B.
Transcription factor IIS cooperates with the E3 ligase UBR5 to ubiquitinate the CDK9 subunit of the positive transcription elongation factor B.
J. Biol. Chem.
286
5012-5022
2011
751697
Bethard J.R.,Zheng H.,Roberts L.,Eblen S.T.
Identification of phosphorylation sites on the E3 ubiquitin ligase UBR5/EDD.
J. Proteomics
75
603-609
2011
751698
Jiang W.,Wang S.,Xiao M.,Lin Y.,Zhou L.,Lei Q.,Xiong Y.,Guan K.L.,Zhao S.
Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase.
Mol. Cell
43
33-44
2011
751699
Rigbolt K.T.,Prokhorova T.A.,Akimov V.,Henningsen J.,Johansen P.T.,Kratchmarova I.,Kassem M.,Mann M.,Olsen J.V.,Blagoev B.
System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
Sci. Signal.
4
0-0
2011
751700
Gudjonsson T.,Altmeyer M.,Savic V.,Toledo L.,Dinant C.,Grofte M.,Bartkova J.,Poulsen M.,Oka Y.,Bekker-Jensen S.,Mailand N.,Neumann B.,Heriche J.K.,Shearer R.,Saunders D.,Bartek J.,Lukas J.,Lukas C.
TRIP12 and UBR5 Suppress Spreading of Chromatin Ubiquitylation at Damaged Chromosomes.
Cell
150
697-709
2012
751701
Zhou H.,Di Palma S.,Preisinger C.,Peng M.,Polat A.N.,Heck A.J.,Mohammed S.
Toward a comprehensive characterization of a human cancer cell phosphoproteome.
J. Proteome Res.
12
260-271
2013
751702
Horejsi Z.,Stach L.,Flower T.G.,Joshi D.,Flynn H.,Skehel J.M.,O'Reilly N.J.,Ogrodowicz R.W.,Smerdon S.J.,Boulton S.J.
Phosphorylation-dependent PIH1D1 interactions define substrate specificity of the R2TP cochaperone complex.
Cell Rep.
7
19-26
2014
751703
Bian Y.,Song C.,Cheng K.,Dong M.,Wang F.,Huang J.,Sun D.,Wang L.,Ye M.,Zou H.
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
J. Proteomics
96
253-262
2014
751704
Panfil A.R.,Al-Saleem J.,Howard C.M.,Shkriabai N.,Kvaratskhelia M.,Green P.L.
Stability of the HTLV-1 Antisense-Derived Protein, HBZ, Is Regulated by the E3 Ubiquitin-Protein Ligase, UBR5.
Front. Microbiol.
9
80-80
2018
751705
Deo R.C.,Sonenberg N.,Burley S.K.
X-ray structure of the human hyperplastic discs protein: an ortholog of the C-terminal domain of poly(A)-binding protein.
Proc. Natl. Acad. Sci. U.S.A.
98
4414-4419
2001