UniProt Accession

 XRN2_HUMAN; Q9H0D6; Q3L8N4; Q6KGZ9; Q9BQL1; Q9NTW0; Q9NXS6; Q9UL53 

Genbank Protein ID

 AF064257; AF152169; AY382900; AL136841; AL117332; AL158013; AL158013; AL117332; AK000084; BC006417 

Genbank Nucleotide ID

 AAD55138.1; AAQ13577.1; AAR24369.1; CAB66775.1; CAI19756.1; CAI19756.1; CAH71495.1; CAH71495.1; BAA90934.1; AAH06417.2 

Protein Name

 5'-3' exoribonuclease 2 

Protein Synonyms/Alias

 DHM1-like protein; DHP protein 

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
123	SRRFRASKEGMEAAV	ubiquitination	[1]
132	GMEAAVEKQRVREEI	ubiquitination	[1, 2]
172	EFMDNLAKCLRYYIA	ubiquitination	[1]
189	LNNDPGWKNLTVILS	ubiquitination	[1, 2]
207	APGEGEHKIMDYIRR	ubiquitination	[1]
284	EGLPREKKGKHDELA	ubiquitination	[1]
286	LPREKKGKHDELADS	ubiquitination	[1]
368	DRLVNIYKNVVHKTG	ubiquitination	[1]
373	IYKNVVHKTGGYLTE	ubiquitination	[1]
493	PSPLGGIKRKAEDSD	ubiquitination	[1, 2]
517	RLWEAGWKQRYYKNK	ubiquitination	[1, 2, 3]
522	GWKQRYYKNKFDVDA	ubiquitination	[1]
524	KQRYYKNKFDVDAAD	ubiquitination	[1, 2]
533	DVDAADEKFRRKVVQ	ubiquitination	[1, 2, 3, 4, 5]
537	ADEKFRRKVVQSYVE	ubiquitination	[1]
616	FLPPSWRKLMSDPDS	ubiquitination	[1]
640	FAIDLNGKKYAWQGV	ubiquitination	[2]
641	AIDLNGKKYAWQGVA	ubiquitination	[1]
756	TVVSINFKDPQFAED	ubiquitination	[2, 6]
767	FAEDYIFKAVMLPGA	ubiquitination	[2]
776	VMLPGARKPAAVLKP	ubiquitination	[1]
796	SSNGRQWKPQLGFNR	acetylation	[7]
796	SSNGRQWKPQLGFNR	ubiquitination	[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] 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]
 [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]
 [5] 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]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 

Functional Description

 Possesses 5'->3' exoribonuclease activity (By similarity). May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5' fragment which is subsequently processed to form the mature mRNA and a 3' fragment which remains attached to the elongating polymerase. The processive degradation of this 3' fragment by this protein may promote termination of transcription. 

Sequence Annotation

 ZN_FING 262 278 CCHC-type.
 MOD_RES 439 439 Phosphothreonine.
 MOD_RES 448 448 Phosphoserine.
 MOD_RES 471 471 Phosphoserine.
 MOD_RES 473 473 Phosphoserine.
 MOD_RES 475 475 Phosphoserine.
 MOD_RES 499 499 Phosphoserine.
 MOD_RES 501 501 Phosphoserine.  

Keyword

 Alternative splicing; Complete proteome; Exonuclease; Hydrolase; Metal-binding; mRNA processing; Nuclease; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Transcription termination; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 950 AA 

Protein Sequence

Gene Ontology

 GO:0016235; C:aggresome; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0004534; F:5'-3' exoribonuclease activity; TAS:UniProtKB.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0016049; P:cell growth; ISS:UniProtKB.
 GO:0000738; P:DNA catabolic process, exonucleolytic; IDA:UniProtKB.
 GO:0006353; P:DNA-dependent transcription, termination; IEA:UniProtKB-KW.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006401; P:RNA catabolic process; TAS:ProtInc.
 GO:0006396; P:RNA processing; TAS:ProtInc.
 GO:0007283; P:spermatogenesis; IEP:UniProtKB. 

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

 PS50158; ZF_CCHC 

PRINTS