CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031430
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 5'-3' exoribonuclease 2 
Protein Synonyms/Alias
 cDNA FLJ55645, highly similar to 5'-3' exoribonuclease 2 (EC 3.1.11.-) 
Gene Name
 XRN2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
69SRRFRASKEGMEAAVubiquitination[1]
78GMEAAVEKQRVREEIubiquitination[1, 2, 3]
118EFMDNLAKCLRYYIAubiquitination[1, 4]
135LNNDPGWKNLTVILSubiquitination[1, 2, 5]
153APGEGEHKIMDYIRRubiquitination[1]
230EGLPREKKGKHDELAubiquitination[1]
232LPREKKGKHDELADSubiquitination[1]
314DRLVNIYKNVVHKTGubiquitination[1]
319IYKNVVHKTGGYLTEubiquitination[1, 5]
439PSPLGGIKRKAEDSDubiquitination[1, 2, 5]
463RLWEAGWKQRYYKNKubiquitination[1, 3, 6]
468GWKQRYYKNKFDVDAubiquitination[1]
470KQRYYKNKFDVDAADubiquitination[1, 2, 3]
479DVDAADEKFRRKVVQubiquitination[1, 2, 3, 5, 6, 7]
483ADEKFRRKVVQSYVEubiquitination[1]
562FLPPSWRKLMSDPDSubiquitination[1]
586FAIDLNGKKYAWQGVacetylation[8]
586FAIDLNGKKYAWQGVubiquitination[2]
587AIDLNGKKYAWQGVAubiquitination[1]
702TVVSINFKDPQFAEDubiquitination[2]
713FAEDYIFKAVMLPGAubiquitination[2]
722VMLPGARKPAAVLKPubiquitination[1]
742SSNGRQWKPQLGFNRacetylation[3, 8]
742SSNGRQWKPQLGFNRubiquitination[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] 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]
 [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] 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]
 [5] 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]
 [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] 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] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 896 AA 
Protein Sequence
MNGIIHPCTH PEDKPAPKNE DEMMVAIFEY IDRLFSIVRP RRLLYMAIDG VAPRAKMNQQ 60
RSRRFRASKE GMEAAVEKQR VREEILAKGG FLPPEEIKER FDSNCITPGT EFMDNLAKCL 120
RYYIADRLNN DPGWKNLTVI LSDASAPGEG EHKIMDYIRR QRAQPNHDPN THHCLCGADA 180
DLIMLGLATH EPNFTIIREE FKPNKPKPCG LCNQFGHEVK DCEGLPREKK GKHDELADSL 240
PCAEGEFIFL RLNVLREYLE RELTMASLPF TFDVERSIDD WVFMCFFVGN DFLPHLPSLE 300
IRENAIDRLV NIYKNVVHKT GGYLTESGYV NLQRVQMIML AVGEVEDSIF KKRKDDEDSF 360
RRRQKEKRKR MKRDQPAFTP SGILTPHALG SRNSPGSQVA SNPRQAAYEM RMQNNSSPSI 420
SPNTSFTSDG SPSPLGGIKR KAEDSDSEPE PEDNVRLWEA GWKQRYYKNK FDVDAADEKF 480
RRKVVQSYVE GLCWVLRYYY QGCASWKWYY PFHYAPFASD FEGIADMPSD FEKGTKPFKP 540
LEQLMGVFPA ASGNFLPPSW RKLMSDPDSS IIDFYPEDFA IDLNGKKYAW QGVALLPFVD 600
ERRLRAALEE VYPDLTPEET RRNSLGGDVL FVGKHHPLHD FILELYQTGS TEPVEVPPEL 660
CHGIQGKFSL DEEAILPDQI VCSPVPMLRD LTQNTVVSIN FKDPQFAEDY IFKAVMLPGA 720
RKPAAVLKPS DWEKSSNGRQ WKPQLGFNRD RRPVHLDQAA FRTLGHVMPR GSGTGIYSNA 780
APPPVTYQGN LYRPLLRGQA QIPKLMSNMR PQDSWRGPPP LFQQQRFDRG VGAEPLLPWN 840
RMLQTQNAAF QPNQYQMLAG PGGYPPRRDD RGGRQGYPRE GRKYPLPPPS GRYNWN 896 
Gene Ontology
 GO:0016235; C:aggresome; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0004534; F:5'-3' exoribonuclease activity; IEA:InterPro.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0016049; P:cell growth; IEA:Compara.
 GO:0016070; P:RNA metabolic process; IEA:Compara.
 GO:0007283; P:spermatogenesis; IEA:Compara. 
Interpro
 IPR027073; 5_3_exoribonuclease.
 IPR017151; 5_3_exoribonuclease_2.
 IPR004859; Put_53exo.
 IPR001878; Znf_CCHC. 
Pfam
 PF03159; XRN_N 
SMART
 SM00343; ZnF_C2HC 
PROSITE
  
PRINTS