CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036844
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 E3 ubiquitin-protein ligase UBR5 
Protein Synonyms/Alias
  
Gene Name
 UBR5 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
83PDRLELGKPDNNDGSubiquitination[1]
91PDNNDGSKLNSNSGAubiquitination[1, 2, 3]
200AQVVLQGKSRSVIIRubiquitination[2, 3]
331NERGSTSKEGEPNLDubiquitination[1, 2, 4]
340GEPNLDKKNTPVQSPubiquitination[4]
436TVATENNKVATWVDEubiquitination[4, 5]
577LRSPESLKNMEKASKubiquitination[2]
657VVFVEDVKNVPVGKVacetylation[6]
657VVFVEDVKNVPVGKVubiquitination[2]
666VPVGKVLKVDGAYVAubiquitination[2, 4, 7, 8]
714IDELQVVKTGGTPKVubiquitination[1, 2, 4, 5, 7]
720VKTGGTPKVPDCFQRubiquitination[2]
737KKLCIPEKTEILAVNubiquitination[2]
755KGVHAVLKTGNWVRYubiquitination[7]
1103LRELLSAKDARGMTPubiquitination[1, 2, 3, 4, 8]
1299IREDRNRKTASPEDSubiquitination[1, 2, 4]
1334LQDWNALKSMIMFGSubiquitination[4, 5]
1345MFGSQENKDPLSASSubiquitination[2, 4, 5]
2057LLQPNARKEDLFGRPubiquitination[2]
2095CLEVLPTKMSYAANLubiquitination[1]
2130PEETESSKPGPSAHDubiquitination[2, 4]
2503PLFYQPGKRGFYTPRubiquitination[3, 4]
2649QPLHAMRKGLLDVLPubiquitination[2]
2773YVPLYSSKQILKQKLubiquitination[2]
Reference
 [1] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [2] 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]
 [3] 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]
 [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] 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]
 [6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [7] 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]
 [8] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Ligase; Reference proteome; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2792 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 LGSSRERDSE 300
LLRERESVLR LRERRWLDGA SFDNERGSTS KEGEPNLDKK NTPVQSPVSL GEDLQWWPDK 360
DGTKFICIGA LYSELLAVSS KGELYQWKWS ESEPYRNAQN PSLHHPRATF LGLTNEKIVL 420
LSANSIRATV ATENNKVATW VDETLSSVAS KLEHTAQTYS ELQGERIVSL HCCALYTCAQ 480
LENSLYWWGV VPFSQRKKML EKARAKNKKP KSSAGISSMP NITVGTQVCL RNNPLYHAGA 540
VAFSISAGIP KVGVLMESVW NMNDSCRFQL RSPESLKNME KASKTTEAKP ESKQEPVKTE 600
MGPPPSPAST CSDASSIASS ASMPYKRRRS TPAPKEEEKV NEEQWSLREV VFVEDVKNVP 660
VGKVLKVDGA YVAVKFPGTS SNTNCQNSSG PDADPSSLLQ DCRLLRIDEL QVVKTGGTPK 720
VPDCFQRTPK KLCIPEKTEI LAVNVDSKGV HAVLKTGNWV RYCIFDLATG KAEQENNFPT 780
SSIAFLGQNE RNVAIFTAGQ ESPIILRDGN GTIYPMAKDC MGGIRDPDWL DLPPISSLGM 840
GVHSLINLPA NSTIKKKAAV IIMAVEKQTL MQHILRCDYE ACRQYLMNLE QAVVLEQNLQ 900
MLQTFISHRC DGNRNILHAC VSVCFPTSNK ETKEEEEAER SERNTFAERL SAVEAIANAI 960
SVVSSNGPGN RAGSSSSRSL RLREMMRRSL RAAGLGRHEA GASSSDHQDP VSPPIAPPSW 1020
VPDPPAMDPD GDIDFILAPA VGSLTTAATG TGQGPSTSTI PGPSTEPSVV ESKDRKANAH 1080
FILKLLCDSV VLQPYLRELL SAKDARGMTP FMSAVSGRAY PAAITILETA QKIAKAEISS 1140
SEKEEDVFMG MVCPSGTNPD DSPLYVLCCN DTCSFTWTGA EHINQDIFEC RTCGLLESLC 1200
CCTECARVCH KGHDCKLKRT SPTAYCDCWE KCKCKTLIAG QKSARLDLLY RLLTATNLVT 1260
LPNSRGEHLL LFLVQTVARQ TVEHCQYRPP RIREDRNRKT ASPEDSDMPD HDLEPPRFAQ 1320
LALERVLQDW NALKSMIMFG SQENKDPLSA SSRIGHLLPE EQVYLNQQSG TIRLDCFTHC 1380
LIVKCTADIL LLDTLLGTLV KELQNKYTPG RREEAIAVTM RFLRSVARVF VILSVEMASS 1440
KKKNNFIPQP IGKCKRVFQA LLPYAVEELC NVAESLIVPV RMGIARPTAP FTLASTSIDA 1500
MQGSEELFSV EPLPPRPSSD QSSSSSQSQS SYIIRNPQQR RISQSQPVRG RDEEQDDIVS 1560
ADVEEVEVVE GVAGEEDHHD EQEEHGEENA EAEGQHDEHD EDGSDMELDL LAAAETESDS 1620
ESNHSNQDNA SGRRSVVTAA TAGSEAGASS VPAFFSEDDS QSNDSSDSDS SSSQSDDIEQ 1680
ETFMLDEPLE RTTNSSHANG AAQAPRSMQW AVRNTQHQRA ASTAPSSTST PAASSAGLIY 1740
IDPSNLRRSG TISTSAAAAA AALEASNASS YLTSASSLAR AYSIVIRQIS DLMGLIPKYN 1800
HLVYSQIPAA VKLTYQDAVN LQNYVEEKLI PTWNWMVSIM DSTEAQLRYG SALASAGDPG 1860
HPNHPLHASQ NSARRERMTA REEASLRTLE GRRRATLLSA RQGMMSARGD FLNYALSLMR 1920
SHNDEHSDVL PVLDVCSLKH VAYVFQALIY WIKAMNQQTT LDTPQLERKR TRELLELGID 1980
NEDSEHENDD DTNQSATLND KDDDSLPAET GQNHPFFRRS DSMTFLGCIP PNPFEVPLAE 2040
AIPLADQPHL LQPNARKEDL FGRPSQGLYS SSASSGKCLM EVTVDRNCLE VLPTKMSYAA 2100
NLKNVMNMQN RQKKEGEEQP VLPEETESSK PGPSAHDLAA QLKSSLLAEI GLTESEGPPL 2160
TSFRPQCSFM GMVISHDMLL GRWRLSLELF GRVFMEDVGA EPGSILTELG GFEVKESKFR 2220
REMEKLRNQQ SRDLSLEVDR DRDLLIQQTM RQLNNHFGRR CATTPMAVHR VKVTFKDEPG 2280
EGSGVARSFY TAIAQAFLSN EKLPNLECIQ NANKGTHTSL MQRLRNRGER DREREREREM 2340
RRSSGLRAGS RRDRDRDFRR QLSIDTRPFR PASEGNPSDD PEPLPAHRQA LGERLYPRVQ 2400
AMQPAFASKI TGMLLELSPA QLLLLLASED SLRARVDEAM ELIIAHGREN GADSILDLGL 2460
VDSSEKVQEN RKRHGSSRSV VDMDLDDTDD GDDNAPLFYQ PGKRGFYTPR PGKNTEARLN 2520
CFRNIGRILG LCLLQNELCP ITLNRHVIKV LLGRKVNWHD FAFFDPVMYE SLRQLILASQ 2580
SSDADAVFSA MDLAFAIDLC KEEGGGQVEL IPNGVNIPVT PQNVYEYVRK YAEHRMLVVA 2640
EQPLHAMRKG LLDVLPKNSL EDLTAEDFRL LVNGCGEVNV QMLISFTSFN DESGENAEKL 2700
LQFKRWFWSI VEKMSMTERQ DLVYFWTSSP SLPASEEGFQ PMPSITIRPP DDQHLPTANT 2760
CISRLYVPLY SSKQILKQKL LLAIKTKNFG FV 2792 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0016567; P:protein ubiquitination; IEA:GOC. 
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