CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017140
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 5'-3' exoribonuclease 1 
Protein Synonyms/Alias
 Strand-exchange protein 1 homolog 
Gene Name
 XRN1 
Gene Synonyms/Alias
 SEP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
79FRIIKPRKVFFMAVDubiquitination[1, 2]
118KIKKAIEKGETLPTEubiquitination[3]
338LNLPRFEKYLVKLSDubiquitination[3]
364DLKWFESKVGNKYLNubiquitination[3]
368FESKVGNKYLNEAAGubiquitination[3, 4]
736AVSDGETKFYLEEPPubiquitination[3]
765KVVHLGDKEQSNWAKubiquitination[3]
805AQLLTGRKYQINQNGubiquitination[3]
847DSRFSNIKTLDDLFPubiquitination[1, 2, 3, 4, 5]
910NQHKYSIKYNPGYVLubiquitination[3]
950RNPHGDHKANVGLNLubiquitination[3]
971EEVPGYTKKVGSEWMubiquitination[3]
972EVPGYTKKVGSEWMYubiquitination[3]
1035QEIITWLKGHPVSTLubiquitination[3]
1130RGTIIGIKGANREADubiquitination[3]
1281GFNDNSVKYQQRKHDubiquitination[3]
1308KAECWSQKMSNKQPNubiquitination[3]
Reference
 [1] 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]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] 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]
 [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] 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
 Major 5'-3' exoribonuclease involved in mRNA decay. Required for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA (By similarity). Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS). 
Sequence Annotation
  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; DNA-binding; Exonuclease; Hydrolase; Nuclease; Polymorphism; Reference proteome; RNA-binding; Tumor suppressor. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1706 AA 
Protein Sequence
MGVPKFYRWI SERYPCLSEV VKEHQIPEFD NLYLDMNGII HQCSHPNDDD VHFRISDDKI 60
FTDIFHYLEV LFRIIKPRKV FFMAVDGVAP RAKMNQQRGR RFRSAKEAED KIKKAIEKGE 120
TLPTEARFDS NCITPGTEFM ARLHEHLKYF VNMKISTDKS WQGVTIYFSG HETPGEGEHK 180
IMEFIRSEKA KPDHDPNTRH CLYGLDADLI MLGLTSHEAH FSLLREEVRF GGKKTQRVCA 240
PEETTFHLLH LSLMREYIDY EFSVLKEKIT FKYDIERIID DWILMGFLVG NDFIPHLPHL 300
HINHDALPLL YGTYVTILPE LGGYINESGH LNLPRFEKYL VKLSDFDREH FSEVFVDLKW 360
FESKVGNKYL NEAAGVAAEE ARNYKEKKKL KGQENSLCWT ALDKNEGEMI TSKDNLEDET 420
EDDDLFETEF RQYKRTYYMT KMGVDVVSDD FLADQAACYV QAIQWILHYY YHGVQSWSWY 480
YPYHYAPFLS DIHNISTLKI HFELGKPFKP FEQLLAVLPA ASKNLLPACY QHLMTNEDSP 540
IIEYYPPDFK TDLNGKQQEW EAVVLIPFID EKRLLEAMET CNHSLKKEER KRNQHSECLM 600
CWYDRDTEFI YPSPWPEKFP AIERCCTRYK IISLDAWRVD INKNKITRID QKALYFCGFP 660
TLKHIRHKFF LKKSGVQVFQ QSSRGENMML EILVDAESDE LTVENVASSV LGKSVFVNWP 720
HLEEARVVAV SDGETKFYLE EPPGTQKLYS GRTAPPSKVV HLGDKEQSNW AKEVQGISEH 780
YLRRKGIIIN ETSAVVYAQL LTGRKYQINQ NGEVRLEKQW SKQVVPFVYQ TIVKDIRAFD 840
SRFSNIKTLD DLFPLRSMVF MLGTPYYGCT GEVQDSGDVI TEGRIRVIFS IPCEPNLDAL 900
IQNQHKYSIK YNPGYVLASR LGVSGYLVSR FTGSIFIGRG SRRNPHGDHK ANVGLNLKFN 960
KKNEEVPGYT KKVGSEWMYS SAAEQLLAEY LERAPELFSY IAKNSQEDVF YEDDIWPGEN 1020
ENGAEKVQEI ITWLKGHPVS TLSRSSCDLQ ILDAAIVEKI EEEVEKCKQR KNNKKVRVTV 1080
KPHLLYRPLE QQHGVIPDRD AEFCLFDRVV NVRENFSVPV GLRGTIIGIK GANREADVLF 1140
EVLFDEEFPG GLTIRCSPGR GYRLPTSALV NLSHGSRSET GNQKLTAIVK PQPAVHQHSS 1200
SSSVSSGHLG ALNHSPQSLF VPTQVPTKDD DEFCNIWQSL QGSGKMQYFQ PTIQEKGAVL 1260
PQEISQVNQH HKSGFNDNSV KYQQRKHDPH RKFKEECKSP KAECWSQKMS NKQPNSGIEN 1320
FLASLNISKE NEVQSSHHGE PPSEEHLSPQ SFAMGTRMLK EILKIDGSNT VDHKNEIKQI 1380
ANEIPVSSNR RDEYGLPSQP KQNKKLASYM NKPHSANEYH NVQSMDNMCW PAPSQIPPVS 1440
TPVTELSRIC SLVGMPQPDF SFLRMPQTMT VCQVKLSNGL LVHGPQCHSE NEAKEKAALF 1500
ALQQLGSLGM NFPLPSQVFA NYPSAVPPGT IPPAFPPPTG WDHYGSNYAL GAANIMPSSS 1560
HLFGSMPWGP SVPVPGKPFH HTLYSGTMPM AGGIPGGVHN QFIPLQVTKK RVANKKNFEN 1620
KEAQSSQATP VQTSQPDSSN IVKVSPRESS SASLKSSPIA QPASSFQVET ASQGHSISHH 1680
KSTPISSSRR KSRKLAVNFG VSKPSE 1706 
Gene Ontology
 GO:0000932; C:cytoplasmic mRNA processing body; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0008409; F:5'-3' exonuclease activity; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; TAS:Reactome.
 GO:0010467; P:gene expression; TAS:Reactome.
 GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB.
 GO:0071028; P:nuclear mRNA surveillance; IMP:UniProtKB.
 GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
 GO:0016075; P:rRNA catabolic process; IMP:UniProtKB. 
Interpro
 IPR027073; 5_3_exoribonuclease.
 IPR016494; 5_3_exoribonuclease_1.
 IPR004859; Put_53exo. 
Pfam
 PF03159; XRN_N 
SMART
  
PROSITE
  
PRINTS