CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001523
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase UBR5 
Protein Synonyms/Alias
 E3 ubiquitin-protein ligase, HECT domain-containing 1; Hyperplastic discs protein homolog; hHYD; Progestin-induced protein 
Gene Name
 UBR5 
Gene Synonyms/Alias
 EDD; EDD1; HYD; KIAA0896 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
91PDNNDGSKLNSNSGAubiquitination[1, 2]
200AQVVLQGKSRSVIIRubiquitination[1, 2, 3]
337NERGSTSKEGEPNLDubiquitination[1, 4]
346GEPNLDKKNTPVQSPubiquitination[4]
442TVATENNKVATWVDEubiquitination[4]
583LRSPESLKNMEKASKubiquitination[1]
663VVFVEDVKNVPVGKVubiquitination[1]
672VPVGKVLKVDGAYVAubiquitination[1, 4, 5, 6, 7]
720IDELQVVKTGGTPKVubiquitination[1, 4, 5, 7]
726VKTGGTPKVPDCFQRubiquitination[1]
743KKLCIPEKTEILAVNubiquitination[1]
761KGVHAVLKTGNWVRYubiquitination[5, 7]
1109LRELLSAKDARGMTPubiquitination[1, 2, 4, 6, 8]
1305IREDRNRKTASPEDSubiquitination[1, 4]
1340LQDWNALKSMIMFGSubiquitination[4]
1351MFGSQENKDPLSASSubiquitination[1, 4]
2063LLQPNARKEDLFGRPubiquitination[1]
2136PEETESSKPGPSAHDubiquitination[1, 4]
2221ELGGFEVKESKFRREubiquitination[4]
2282HRVKVTFKDEPGEGSubiquitination[1, 4]
2320ECIQNANKGTHTSLMubiquitination[1]
2472GLVDSSEKVQQENRKubiquitination[1, 4, 9]
2510PLFYQPGKRGFYTPRubiquitination[2, 4]
2656QPLHAMRKGLLDVLPubiquitination[1]
2664GLLDVLPKNSLEDLTubiquitination[4]
2780YVPLYSSKQILKQKLubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 2377 2454 PABC.
 DOMAIN 2462 2799 HECT.
 ZN_FING 1177 1245 UBR-type.
 ACT_SITE 2768 2768 Glycyl thioester intermediate (By
 MOD_RES 2 2 N-acetylthreonine.
 MOD_RES 110 110 Phosphoserine.
 MOD_RES 327 327 Phosphoserine.
 MOD_RES 352 352 Phosphoserine.
 MOD_RES 578 578 Phosphoserine.
 MOD_RES 612 612 Phosphoserine.
 MOD_RES 637 637 Phosphothreonine.
 MOD_RES 808 808 Phosphoserine.
 MOD_RES 928 928 Phosphoserine.
 MOD_RES 1018 1018 Phosphoserine.
 MOD_RES 1115 1115 Phosphothreonine.
 MOD_RES 1135 1135 Phosphothreonine.
 MOD_RES 1227 1227 Phosphoserine.
 MOD_RES 1308 1308 Phosphoserine.
 MOD_RES 1355 1355 Phosphoserine.
 MOD_RES 1375 1375 Phosphoserine.
 MOD_RES 1481 1481 Phosphoserine.
 MOD_RES 1549 1549 Phosphoserine.
 MOD_RES 1736 1736 Phosphothreonine.
 MOD_RES 1741 1741 Phosphoserine.
 MOD_RES 1746 1746 Phosphotyrosine.
 MOD_RES 1780 1780 Phosphoserine.
 MOD_RES 1969 1969 Phosphothreonine.
 MOD_RES 2026 2026 Phosphoserine.
 MOD_RES 2028 2028 Phosphoserine.
 MOD_RES 2030 2030 Phosphothreonine.
 MOD_RES 2071 2071 Phosphoserine (By similarity).
 MOD_RES 2076 2076 Phosphoserine.
 MOD_RES 2213 2213 Phosphothreonine.
 MOD_RES 2289 2289 Phosphoserine.
 MOD_RES 2484 2484 Phosphoserine.
 MOD_RES 2486 2486 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; DNA damage; DNA repair; Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2799 AA 
Protein Sequence
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 2799 
Gene Ontology
 GO:0005737; C:cytoplasm; IBA:RefGenome.
 GO:0005634; C:nucleus; IDA:BHF-UCL.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:BHF-UCL.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0008283; P:cell proliferation; TAS:ProtInc.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:2000780; P:negative regulation of double-strand break repair; IMP:UniProtKB.
 GO:1901315; P:negative regulation of histone H2A K63-linked ubiquitination; IMP:UniProtKB.
 GO:0090263; P:positive regulation of canonical Wnt receptor signaling pathway; IMP:BHF-UCL.
 GO:0035413; P:positive regulation of catenin import into nucleus; IMP:BHF-UCL.
 GO:0033160; P:positive regulation of protein import into nucleus, translocation; IMP:BHF-UCL.
 GO:0050847; P:progesterone receptor signaling pathway; IDA:HGNC.
 GO:0000209; P:protein polyubiquitination; IDA:BHF-UCL.
 GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:RefGenome.
 GO:0006974; P:response to DNA damage stimulus; IMP:UniProtKB. 
Interpro
 IPR024725; E3_UbLigase_EDD_UBA.
 IPR000569; HECT.
 IPR002004; PABP_HYD.
 IPR009091; RCC1/BLIP-II.
 IPR003126; Znf_N-recognin.
 IPR013993; Znf_N-recognin_met. 
Pfam
 PF11547; E3_UbLigase_EDD
 PF00632; HECT
 PF00658; PABP
 PF02207; zf-UBR 
SMART
 SM00119; HECTc
 SM00517; PolyA
 SM00396; ZnF_UBR1 
PROSITE
 PS50237; HECT
 PS51309; PABC
 PS51157; ZF_UBR 
PRINTS