| Tag | Content |
|---|
| CPLM ID | CPLM-014450 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | E3 ubiquitin-protein ligase UBR5 |
Protein Synonyms/Alias | 100 kDa protein; E3 ubiquitin-protein ligase, HECT domain-containing 1; Hyperplastic discs protein homolog |
Gene Name | Ubr5 |
Gene Synonyms/Alias | Dd5; Edd; Edd1; Hyd |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 1098 | LRELLSAKDARGMTP | ubiquitination | [1] |
|
Reference | [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis. Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J. J Proteome Res. 2012 Sep 7;11(9):4722-32. [ PMID: 22871113] |
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) 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). |
Sequence Annotation | DOMAIN 2367 2444 PABC.
DOMAIN 2451 2788 HECT.
ZN_FING 1166 1234 UBR-type.
ACT_SITE 2757 2757 Glycyl thioester intermediate (By
MOD_RES 100 100 Phosphoserine (By similarity).
MOD_RES 317 317 Phosphoserine (By similarity).
MOD_RES 342 342 Phosphoserine (By similarity).
MOD_RES 567 567 Phosphoserine (By similarity).
MOD_RES 601 601 Phosphoserine (By similarity).
MOD_RES 626 626 Phosphothreonine (By similarity).
MOD_RES 797 797 Phosphoserine (By similarity).
MOD_RES 917 917 Phosphoserine (By similarity).
MOD_RES 1007 1007 Phosphoserine (By similarity).
MOD_RES 1104 1104 Phosphothreonine (By similarity).
MOD_RES 1124 1124 Phosphothreonine (By similarity).
MOD_RES 1216 1216 Phosphoserine (By similarity).
MOD_RES 1297 1297 Phosphoserine (By similarity).
MOD_RES 1344 1344 Phosphoserine (By similarity).
MOD_RES 1364 1364 Phosphoserine (By similarity).
MOD_RES 1470 1470 Phosphoserine (By similarity).
MOD_RES 1538 1538 Phosphoserine (By similarity).
MOD_RES 1725 1725 Phosphothreonine (By similarity).
MOD_RES 1730 1730 Phosphoserine (By similarity).
MOD_RES 1735 1735 Phosphotyrosine (By similarity).
MOD_RES 1769 1769 Phosphoserine (By similarity).
MOD_RES 1959 1959 Phosphothreonine (By similarity).
MOD_RES 2016 2016 Phosphoserine (By similarity).
MOD_RES 2018 2018 Phosphoserine (By similarity).
MOD_RES 2020 2020 Phosphothreonine (By similarity).
MOD_RES 2061 2061 Phosphoserine (By similarity).
MOD_RES 2066 2066 Phosphoserine (By similarity).
MOD_RES 2203 2203 Phosphothreonine (By similarity).
MOD_RES 2279 2279 Phosphoserine (By similarity).
MOD_RES 2473 2473 Phosphoserine (By similarity).
MOD_RES 2475 2475 Phosphoserine (By similarity). |
Keyword | 3D-structure; Complete proteome; DNA damage; DNA repair; Ligase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 2788 AA |
Protein Sequence | MNKQAVKRLH MLREVSEKLN KYNLNSHPPL NVLEQATIKQ CVVGPNHAAF LLEDGRICRI 60
GFSVQPDRLE LGKPDNNDGS KLNSSSGTGR TSRPGRTSDS PWFLSGSETL GRLAGNTLGS 120
RWSSGVGGSG GGSSGRSSAG ARDSRRQTRV IRTGRDRGSG LLGSQPQPVI PASVIPEELI 180
SQAQVVLQGK SRSVIIRELQ RTNLDVNLAV NNLLSRDDED GDDGDDTASE SYLPGEDLMS 240
LLDADIHSAH PSVIIDADAM FSEDISYFGY PSFRRSSLSR LGSSRVLLLP LERDSELLRE 300
RESVLRLRER RWLDGASFDN ERGSTSKEGE PNPDKKNTPV QSPVSLGEDL QWWPDKDGTK 360
FTCIGALYSE LVAVSSKGEL YQWKWTESEP YRNAQNPSLH HPRATFLGLT NEKIVLLSAN 420
SIRATVATEN NKVATWVDET LSSVASKLEH TAQTYSELQG ERIVSLHCCA LYTCAQLENN 480
LYWWGVVPFS QRKKMLEKAR AKNKKPKSSA GVQSLNVRGG RQVCLRNNPL YHAGAVAFSI 540
SAGIPKVGVL MESVWNMNDS CRFQLRSPES LKSMEKASKT IETKPESKQE PVKTEMGPPP 600
SPASTCSDAS SIASSASMPY KRRRSTPAPK EEEKVNEEQW SLREVVFVED VKNVPVGKVL 660
KVDGAYVAVK FPGTSSNTNC QNSSGPDADP SSLLQDCRLL RIDELQVVKT GGTPKVPDCF 720
QRTPKKLCIP EKTEILAVNV DSKGVHAVLK TGNWVRYCIF DLATGKAEQE NNFPTSSVAF 780
LGQNERSVAI FTAGQESPII LRDGNGTIYP MAKDCMGGIR DPDWLDLPPI SSLGMGVHSL 840
INLPANSTIK KKAAIIIMAV EKQTLMQHIL RCDYEACRQY LVNLEQAVVL EQNLQMLQTF 900
ISHRCDGNRN ILHACVSVCF PTSNKETKEE EEAERSERNT FAERLSAVEA IANAISVVSS 960
NGPGNRAGSS SSRSLRLREM MRRSLRAAGL GRHEAGASSS DHQDPVSPPI APPSWVPDPP 1020
SMDPDGDIDF ILAPAVGSLT TAATGGGQGP STSTIPGPST EPSVVESKDR KANAHFILKL 1080
LCDSAVLQPY LRELLSAKDA RGMTPFMSAV SGRAYPAAIT ILETAQKIAK AEVSGSEKEE 1140
DVFMGMVCPS GTNPDDSPLY VLCCNDTCSF TWTGAEHINQ DIFECRTCGL LESLCCCTEC 1200
ARVCHKGHDC KLKRTSPTAY CDCWEKCKCK TLIAGQKSAR LDLLYRLLTA TNLVTLPNSR 1260
GEHLLLFLVQ TVARQTVEHC QYRPPRIRED RNRKTASPDD SDMPDHDLEP PRFAQLALER 1320
VLQDWNALRS MIMFGSQENK DPLSASSRIG HLLPEEQVYL NQQSGTIRLD CFTHCLIVKC 1380
TADILLLDTL LGTLVKELQN KYTPGRREEA IAVTMRFLRS VARVFVILSV EMASSKKKNN 1440
FIPQPIGKCK RVFQALLPYA VEELCNVAES LIVPVRMGIA RPTAPFTLAS TSIDAMQGSE 1500
ELFSVEPLPP RPSSDQSSSS SQSQSSYIIR NPQQRRISQS QPVRGREEEQ DDIVSADVEE 1560
VEVVEGVAGE EDHHDEQEEH GEENAEAEGH HDEHDEDGSD MELDLLAAAE TESDSESNHS 1620
NQDNASGRRS VVTAATAGSE AGASSVPAFF SEDDSQSNDS SDSDSSSSQS DDIEQETFML 1680
DEPLERTTNS SHANGAAQAP RSMQWAVRNT QHQRAASTAP SSTSTPAASS AGLIYIDPSN 1740
LRRSGTISTS AAAAAAALEA SNASSYLTSA SSLARAYSIV IRQISDLMGL IPKYNHLVYS 1800
QIPAAVKLTY QDAVNLQNYV EEKLIPTWNW MVSIMDSTEA QLRYGSALAS AGDPGHPNHP 1860
LHASQNSARR ERMTAREEAS LRTLEGRRRR ATLLSARQGM MSARGDFLNY ALSLMRSHND 1920
EHSDVLPVLD VCSLKHVAYV FQALIYWIKA MNQQTTLDTP QLERKRTREL LELGIDNEDS 1980
EHENDDDTSQ SATLNDKDDE SLPAETGQNH PFFRRSDSMT FLGCIPPNPF EVPLAEAIPL 2040
ADQPHLLQPN ARKEDLFGRP SQGLYSSSAG SGKCLVEVTM DRNCLEVLPT KMSYAANLKN 2100
VMNMQNRQKK AGEDQSMLAE EADSSKPGPS AHDVAAQLKS SLLAEIGLTE SEGPPLTSFR 2160
PQCSFMGMVI SHDMLLGRWR LSLELFGRVF MEDVGAEPGS ILTELGGFEV KESKFRREME 2220
KLRNQQSRDL SLEVDRDRDL LIQQTMRQLN NHFGRRCATT PMAVHRVKVT FKDEPGEGSG 2280
VARSFYTAIA QAFLSNEKLP NLDCIQNANK GTHTSLMQRL RNRGERDRER EREREMRRSS 2340
GLRAGSRRDR DRDFRRQLSI DTRPFRPASE GNPSDDPDPL PAHRQALGER LYPRVQAMQP 2400
AFASKITGML LELSPAQLLL LLASEDSLRA RVEEAMELIV AHGRENGADS ILDLGLLDSS 2460
EKVQENRKRH GSSRSVVDMD LDDTDDGDDN APLFYQPGKR GFYTPRPGKN TEARLNCFRN 2520
IGRILGLCLL QNELCPITLN RHVIKVLLGR KVNWHDFAFF DPVMYESLRQ LILASQSSDA 2580
DAVFSAMDLA FAVDLCKEEG GGQVELIPNG VNIPVTPQNV YEYVRKYAEH RMLVVAEQPL 2640
HAMRKGLLDV LPKNSLEDLT AEDFRLLVNG CGEVNVQMLI SFTSFNDESG ENAEKLLQFK 2700
RWFWSIVERM SMTERQDLVY FWTSSPSLPA SEEGFQPMPS ITIRPPDDQH LPTANTCISR 2760
LYVPLYSSKQ ILKQKLLLAI KTKNFGFV 2788 |
Gene Ontology | GO:0005737; C:cytoplasm; IBA:RefGenome. GO:0005634; C:nucleus; IBA:RefGenome. GO:0003723; F:RNA binding; IEA:InterPro. GO:0004842; F:ubiquitin-protein ligase activity; IBA:RefGenome. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006281; P:DNA repair; IEA:UniProtKB-KW. GO:2000780; P:negative regulation of double-strand break repair; ISS:UniProtKB. GO:1901315; P:negative regulation of histone H2A K63-linked ubiquitination; ISS:UniProtKB. GO:0050847; P:progesterone receptor signaling pathway; IBA:RefGenome. GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:RefGenome. GO:0006974; P:response to DNA damage stimulus; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |