CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017035
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase UBR2 
Protein Synonyms/Alias
 N-recognin-2; Ubiquitin-protein ligase E3-alpha-2; Ubiquitin-protein ligase E3-alpha-II 
Gene Name
 UBR2 
Gene Synonyms/Alias
 C6orf133; KIAA0349 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
27SAEEIAGKWLQATDLubiquitination[1]
48HLAHYVPKIYCRGPNubiquitination[1]
104HLCGRVFKVGEPTYSubiquitination[1]
255KAVNCTQKEAIGFATubiquitination[1, 2, 3]
284FQYCEQAKSVIVRNTubiquitination[1]
443NLMSIIIKTFMDHLRubiquitination[4]
779VNATDEIKREIIHQLubiquitination[1, 3, 4]
789IIHQLSIKPMAHSELubiquitination[1]
821IEAVAHFKKPGLTGRubiquitination[5]
822EAVAHFKKPGLTGRGubiquitination[5]
994DMIRWILKTFNAVKKubiquitination[5, 6]
1044IARLRREKIMAQMSEubiquitination[1, 3]
1187YFDSVQAKEQRRQQRubiquitination[1, 2, 3, 4, 6, 7, 8]
1255RTISQQIKALQFLRKubiquitination[1, 3, 5]
1352RILSDEDKPLFGPLPubiquitination[7]
1496QYTGSALKEIPSGWHubiquitination[2]
1599RYPRESNKLINLPEDubiquitination[1]
1687QVLFLAGKTKGCFYSubiquitination[1]
1718GNPLHLCKERFKKIQubiquitination[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] 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]
 [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] 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] 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]
 [7] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [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
 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. Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth. 
Sequence Annotation
 ZN_FING 97 168 UBR-type.
 ZN_FING 1108 1214 RING-type; atypical.  
Keyword
 3D-structure; Alternative splicing; Coiled coil; Complete proteome; Ligase; Metal-binding; Nucleus; Polymorphism; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1755 AA 
Protein Sequence
MASELEPEVQ AIDRSLLECS AEEIAGKWLQ ATDLTREVYQ HLAHYVPKIY CRGPNPFPQK 60
EDMLAQHVLL GPMEWYLCGE DPAFGFPKLE QANKPSHLCG RVFKVGEPTY SCRDCAVDPT 120
CVLCMECFLG SIHRDHRYRM TTSGGGGFCD CGDTEAWKEG PYCQKHELNT SEIEEEEDPL 180
VHLSEDVIAR TYNIFAITFR YAVEILTWEK ESELPADLEM VEKSDTYYCM LFNDEVHTYE 240
QVIYTLQKAV NCTQKEAIGF ATTVDRDGRR SVRYGDFQYC EQAKSVIVRN TSRQTKPLKV 300
QVMHSSIVAH QNFGLKLLSW LGSIIGYSDG LRRILCQVGL QEGPDGENSS LVDRLMLSDS 360
KLWKGARSVY HQLFMSSLLM DLKYKKLFAV RFAKNYQQLQ RDFMEDDHER AVSVTALSVQ 420
FFTAPTLARM LITEENLMSI IIKTFMDHLR HRDAQGRFQF ERYTALQAFK FRRVQSLILD 480
LKYVLISKPT EWSDELRQKF LEGFDAFLEL LKCMQGMDPI TRQVGQHIEM EPEWEAAFTL 540
QMKLTHVISM MQDWCASDEK VLIEAYKKCL AVLMQCHGGY TDGEQPITLS ICGHSVETIR 600
YCVSQEKVSI HLPVSRLLAG LHVLLSKSEV AYKFPELLPL SELSPPMLIE HPLRCLVLCA 660
QVHAGMWRRN GFSLVNQIYY YHNVKCRREM FDKDVVMLQT GVSMMDPNHF LMIMLSRFEL 720
YQIFSTPDYG KRFSSEITHK DVVQQNNTLI EEMLYLIIML VGERFSPGVG QVNATDEIKR 780
EIIHQLSIKP MAHSELVKSL PEDENKETGM ESVIEAVAHF KKPGLTGRGM YELKPECAKE 840
FNLYFYHFSR AEQSKAEEAQ RKLKRQNRED TALPPPVLPP FCPLFASLVN ILQSDVMLCI 900
MGTILQWAVE HNGYAWSESM LQRVLHLIGM ALQEEKQHLE NVTEEHVVTF TFTQKISKPG 960
EAPKNSPSIL AMLETLQNAP YLEVHKDMIR WILKTFNAVK KMRESSPTSP VAETEGTIME 1020
ESSRDKDKAE RKRKAEIARL RREKIMAQMS EMQRHFIDEN KELFQQTLEL DASTSAVLDH 1080
SPVASDMTLT ALGPAQTQVP EQRQFVTCIL CQEEQEVKVE SRAMVLAAFV QRSTVLSKNR 1140
SKFIQDPEKY DPLFMHPDLS CGTHTSSCGH IMHAHCWQRY FDSVQAKEQR RQQRLRLHTS 1200
YDVENGEFLC PLCECLSNTV IPLLLPPRNI FNNRLNFSDQ PNLTQWIRTI SQQIKALQFL 1260
RKEESTPNNA STKNSENVDE LQLPEGFRPD FRPKIPYSES IKEMLTTFGT ATYKVGLKVH 1320
PNEEDPRVPI MCWGSCAYTI QSIERILSDE DKPLFGPLPC RLDDCLRSLT RFAAAHWTVA 1380
SVSVVQGHFC KLFASLVPND SHEELPCILD IDMFHLLVGL VLAFPALQCQ DFSGISLGTG 1440
DLHIFHLVTM AHIIQILLTS CTEENGMDQE NPPCEEESAV LALYKTLHQY TGSALKEIPS 1500
GWHLWRSVRA GIMPFLKCSA LFFHYLNGVP SPPDIQVPGT SHFEHLCSYL SLPNNLICLF 1560
QENSEIMNSL IESWCRNSEV KRYLEGERDA IRYPRESNKL INLPEDYSSL INQASNFSCP 1620
KSGGDKSRAP TLCLVCGSLL CSQSYCCQTE LEGEDVGACT AHTYSCGSGV GIFLRVRECQ 1680
VLFLAGKTKG CFYSPPYLDD YGETDQGLRR GNPLHLCKER FKKIQKLWHQ HSVTEEIGHA 1740
QEANQTLVGI DWQHL 1755 
Gene Ontology
 GO:0000785; C:chromatin; IEA:Compara.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0000151; C:ubiquitin ligase complex; IEA:Compara.
 GO:0070728; F:leucine binding; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0071233; P:cellular response to leucine; IDA:UniProtKB.
 GO:0006342; P:chromatin silencing; ISS:UniProtKB.
 GO:0033522; P:histone H2A ubiquitination; ISS:UniProtKB.
 GO:0007141; P:male meiosis I; IEA:Compara.
 GO:0032007; P:negative regulation of TOR signaling cascade; IMP:UniProtKB.
 GO:0007283; P:spermatogenesis; IEA:Compara.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Compara. 
Interpro
 IPR003769; ClpS_core.
 IPR014719; Ribosomal_L7/12_C/ClpS-like.
 IPR003126; Znf_N-recognin.
 IPR013993; Znf_N-recognin_met.
 IPR001841; Znf_RING. 
Pfam
 PF02617; ClpS
 PF02207; zf-UBR 
SMART
 SM00184; RING
 SM00396; ZnF_UBR1 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2
 PS51157; ZF_UBR 
PRINTS