CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015558
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase UBR3 
Protein Synonyms/Alias
 N-recognin-3; Ubiquitin-protein ligase E3-alpha-3; Ubiquitin-protein ligase E3-alpha-III; Zinc finger protein 650 
Gene Name
 UBR3 
Gene Synonyms/Alias
 KIAA2024; ZNF650 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
236AADGPSEKDLNKVLQubiquitination[1, 2, 3]
277LTNQQNYKDLTSGLGubiquitination[2]
1044SLVAERRKKFQEIINubiquitination[2]
1045LVAERRKKFQEIINRubiquitination[2, 4]
1141AVERILLKAASQSRMubiquitination[2, 4]
1274RDNVEPKKLPISEEEubiquitination[2]
1390PWQRPSNKSIQDLIKubiquitination[2]
1733ERHAEQGKALLIQESubiquitination[1]
1853DRDLRRGKPLYICKEubiquitination[2]
Reference
 [1] 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]
 [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] 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]
 [4] 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] 
Functional Description
 E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Does not bind 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). 
Sequence Annotation
 ZN_FING 118 189 UBR-type.
 ZN_FING 1306 1364 RING-type; degenerate.  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Ligase; Membrane; Metal-binding; Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1888 AA 
Protein Sequence
MAAAAAAAVG GQQPSQPELP APGLALDKAA TAAHLKAALS RPDNRAGAEE LQALLERVLS 60
AERPLAAAAG GEDAAAAGGG GGPGAAEEEA LEWCKCLLAG GGGYDEFCAA VRAYDPAALC 120
GLVWTANFVA YRCRTCGISP CMSLCAECFH QGDHTGHDFN MFRSQAGGAC DCGDSNVMRE 180
SGFCKRHQIK SSSNIPCVPK DLLMMSEFVL PRFIFCLIQY LREGYNEPAA DGPSEKDLNK 240
VLQLLEPQIS FLEDLTKMGG AMRSVLTQVL TNQQNYKDLT SGLGENACVK KSHEKYLIAL 300
KSSGLTYPED KLVYGVQEPS AGTSSLAVQG FIGATGTLGQ VDSSDEDDQD GSQGLGKRKR 360
VKLSSGTKDQ SIMDVLKHKS FLEELLFWTI KYEFPQKMVT FLLNMLPDQE YKVAFTKTFV 420
QHYAFIMKTL KKSHESDTMS NRIVHISVQL FSNEELARQV TEECQLLDIM VTVLLYMMES 480
CLIKSELQDE ENSLHVVVNC GEALLKNNTY WPLVSDFINI LSHQSVAKRF LEDHGLLVTW 540
MNFVSFFQGM NLNKRELNEH VEFESQTYYA AFAAELEACA QPMWGLLSHC KVRETQEYTR 600
NVVRYCLEAL QDWFDAINFV DEPAPNQVTF HLPLHRYYAM FLSKAVKCQE LDLDSVLPDQ 660
EMLMKLMIHP LQIQASLAEI HSNMWVRNGL QIKGQAMTYV QSHFCNSMID PDIYLLQVCA 720
SRLDPDYFIS SVFERFKVVD LLTMASQHQN TVLDAEHERS MLEGALTFLV ILLSLRLHLG 780
MSDDEILRAE MVAQLCMNDR THSSLLDLIP ENPNPKSGII PGSYSFESVL SAVADFKAPV 840
FEPGGSMQQG MYTPKAEVWD QEFDPVMVIL RTVYRRDVQS AMDRYTAFLK QSGKFPGNPW 900
PPYKKRTSLH PSYKGLMRLL HCKTLHIVLF TLLYKILMDH QNLSEHVLCM VLYLIELGLE 960
NSAEEESDEE ASVGGPERCH DSWFPGSNLV SNMRHFINYV RVRVPETAPE VKRDSPASTS 1020
SDNLGSLQNS GTAQVFSLVA ERRKKFQEII NRSSSEANQV VRPKTSSKWS APGSAPQLTT 1080
AILEIKESIL SLLIKLHHKL SGKQNSYYPP WLDDIEILIQ PEIPKYSHGD GITAVERILL 1140
KAASQSRMNK RIIEEICRKV TPPVPPKKVT AAEKKTLDKE ERRQKARERQ QKLLAEFASR 1200
QKSFMETAMD VDSPENDIPM EITTAEPQVS EAVYDCVICG QSGPSSEDRP TGLVVLLQAS 1260
SVLGQCRDNV EPKKLPISEE EQIYPWDTCA AVHDVRLSLL QRYFKDSSCL LAVSIGWEGG 1320
VYVQTCGHTL HIDCHKSYME SLRNDQVLQG FSVDKGEFTC PLCRQFANSV LPCYPGSNVE 1380
NNPWQRPSNK SIQDLIKEVE ELQGRPGAFP SETNLSKEME SVMKDIKNTT QKKYRDYSKT 1440
PGSPDNDFLF MYSVARTNLE LELIHRGGNL CSGGASTAGK RSCLNQLFHV LALHMRLYSI 1500
DSEYNPWRKL TQLEEMNPQL GYEEQQPEVP ILYHDVTSLL LIQILMMPQP LRKDHFTCIV 1560
KVLFTLLYTQ ALAALSVKCS EEDRSAWKHA GALKKSTCDA EKSYEVLLSF VISELFKGKL 1620
YHEEGTQECA MVNPIAWSPE SMEKCLQDFC LPFLRITSLL QHHLFGEDLP SCQEEEEFSV 1680
LASCLGLLPT FYQTEHPFIS ASCLDWPVPA FDIITQWCFE IKSFTERHAE QGKALLIQES 1740
KWKLPHLLQL PENYNTIFQY YHRKTCSVCT KVPKDPAVCL VCGTFVCLKG LCCKQQSYCE 1800
CVLHSQNCGA GTGIFLLINA SVIIIIRGHR FCLWGSVYLD AHGEEDRDLR RGKPLYICKE 1860
RYKVLEQQWI SHTFDHINKR WGPHYNGL 1888 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0009790; P:embryo development; ISS:UniProtKB.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0042048; P:olfactory behavior; IEA:Compara.
 GO:0007608; P:sensory perception of smell; ISS:UniProtKB.
 GO:0001967; P:suckling behavior; ISS:UniProtKB.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB. 
Interpro
 IPR003126; Znf_N-recognin. 
Pfam
 PF02207; zf-UBR 
SMART
  
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2
 PS51157; ZF_UBR 
PRINTS