UniProt Accession

 ERI1_MOUSE; Q7TMF2; Q3TA98; Q3TNT0; Q80UN4; Q8BWR6; Q9CQ63 

Genbank Protein ID

 AK014041; AK014410; AK050230; AK165026; AK172005; BC046412 

Genbank Nucleotide ID

 BAB29127.2; BAB29333.2; BAC34136.1; BAE38007.1; BAE42771.1; AAH46412.1 

Protein Name

 3'-5' exoribonuclease 1 

Protein Synonyms/Alias

 3'-5' exonuclease ERI1; Eri-1 homolog; Histone mRNA 3'-exonuclease 1 

Gene Name

 Eri1 

Gene Synonyms/Alias

 3'exo; Thex1 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
245	QCRLSRLKHPAFAKK	ubiquitination	[1]
252	KHPAFAKKWINIRKS	acetylation	[2]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 

Functional Description

 RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Binds with high affinity to the 3' side of the stem-loop structure and to the downstream cleavage product (DCP) of histone pre-mRNAs. Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs (By similarity). Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA. 

Sequence Annotation

 DOMAIN 72 106 SAP.
 DOMAIN 126 302 Exonuclease.
 ACT_SITE 132 132 Proton acceptor (Potential).
 ACT_SITE 289 289 Proton acceptor (Potential).
 METAL 130 130 Magnesium 1 (By similarity).
 METAL 130 130 Magnesium 2 (By similarity).
 METAL 132 132 Magnesium 1 (By similarity).
 METAL 230 230 Magnesium 2 (By similarity).
 METAL 294 294 Magnesium 1 (By similarity).
 BINDING 132 132 AMP (By similarity).
 BINDING 133 133 AMP; via amide nitrogen and carbonyl
 BINDING 289 289 AMP (By similarity).
 MOD_RES 58 58 Phosphoserine (By similarity).  

Keyword

 Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleus; Phosphoprotein; Reference proteome; RNA-binding; RNA-mediated gene silencing; rRNA processing. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 345 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0071204; C:histone pre-mRNA 3'end processing complex; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0008408; F:3'-5' exonuclease activity; ISS:UniProtKB.
 GO:0071207; F:histone pre-mRNA stem-loop binding; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0043022; F:ribosome binding; IDA:UniProtKB.
 GO:0019843; F:rRNA binding; IDA:UniProtKB.
 GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
 GO:0031125; P:rRNA 3'-end processing; IDA:UniProtKB. 

Interpro

 IPR006055; Exonuclease.
 IPR013520; Exonuclease_RNaseT/DNA_pol3.
 IPR012337; RNaseH-like_dom.
 IPR003034; SAP_dom. 

Pfam

 PF00929; RNase_T
 PF02037; SAP 

SMART

 SM00479; EXOIII
 SM00513; SAP 

PROSITE

 PS50800; SAP 

PRINTS