CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021218
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
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
113LNNDPGWKNLTVILSubiquitination[1]
297IYKNVVHKTGGYLTEubiquitination[1]
417PSPLGGIKRKAEDSDubiquitination[1]
457DVDAADEKFRRKVVQubiquitination[1]
Reference
 [1] 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] 
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
MMVAIFEYID RLFSIVRPRR LLYMAIDGVA PRAKMNQQRS RRFRASKEGM EAAVEKQRVR 60
EEILAKGGFL PPEEIKERFD SNCITPGTEF MDNLAKCLRY YIADRLNNDP GWKNLTVILS 120
DASAPGEGEH KIMDYIRRQR AQPNHDPNTH HCLCGADADL IMLGLATHEP NFTIIREEFK 180
PNKPKPCGLC NQFGHEVKDC EGLPREKKGK HDELADSLPC AEGEFIFLRL NVLREYLERE 240
LTMASLPFTF DVERSIDDWV FMCFFVGNDF LPHLPSLEIR ENAIDRLVNI YKNVVHKTGG 300
YLTESGYVNL QRVQMIMLAV GEVEDSIFKK RKDDEDSFRR RQKEKRKRMK RDQPAFTPSG 360
ILTPHALGSR NSPGSQVASN PRQAAYEMRM QNNSSPSISP NTSFTSDGSP SPLGGIKRKA 420
EDSDSEPEPE DNVRLWEAGW KQRYYKNKFD VDAADEKFRR KVVQSYVEGL CWVLRYYYQG 480
CASWKWYYPF HYAPFASDFE GIADMPSDFE KGTKPFKPLE QLMGVFPAAS GNFLPPSWRK 540
LMSDPDSSII DFYPEDFAID LNGKKYAWQG VALLPFVDER RLRAALEEVY PDLTPEETRR 600
NSLGGDVLFV GKHHPLHDFI LELYQTGSTE PVEVPPELCH GIQGKFSLDE EAILPDQIVC 660
SPVPMLRDLT QNTVVSINFK DPQFAEDYIF KAVMLPGARK PAAVLKPSDW EKSSNGRQWK 720
PQLGFNRDRR PVHLDQAAFR TLGHVMPRGS GTGIYSNAAP PPVTYQGNLY RPLLRGQAQI 780
PKLMSNMRPQ DSWRGPPPLF QQQRFDRGVG AEPLLPWNRM LQTQNAAFQP NQYQMLAGPG 840
GYPPRRDDRG GRQGYPREGR KYPLPPPSGR YNWN 874 
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