UniProt Accession

 ERI1_HUMAN; Q8IV48; A8K4U7; Q9NSX3 

Genbank Protein ID

 AY310909; AK291062; AL137679; BC035279 

Genbank Nucleotide ID

 AAQ21219.1; BAF83751.1; CAB70871.2; AAH35279.1 

Protein Name

 3'-5' exoribonuclease 1 

Protein Synonyms/Alias

 3'-5' exonuclease ERI1; Eri-1 homolog; Histone mRNA 3'-end-specific exoribonuclease; Histone mRNA 3'-exonuclease 1; Protein 3'hExo; HEXO 

Gene Name

 ERI1 

Gene Synonyms/Alias

 3'EXO; THEX1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
52	GQETKGSKFITSSAS	ubiquitination	[1, 2]
67	DFSDPVYKEIAITNG	ubiquitination	[2, 3]
81	GCINRMSKEELRAKL	ubiquitination	[2]
87	SKEELRAKLSEFKLE	ubiquitination	[2]
92	RAKLSEFKLETRGVK	ubiquitination	[2]
103	RGVKDVLKKRLKNYY	ubiquitination	[2]
217	VIDWMKLKELGTKYK	ubiquitination	[2]
249	QCQLSRLKYPPFAKK	ubiquitination	[2]
262	KKWINIRKSYGNFYK	ubiquitination	[2]
269	KSYGNFYKVPRSQTK	ubiquitination	[2, 3, 4, 5]
276	KVPRSQTKLTIMLEK	ubiquitination	[2]
300	HCGLDDSKNIARIAV	ubiquitination	[2]

Reference

 [1] 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]
 [2] 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]
 [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] 

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). Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA. Binds with high affinity to the stem-loop structure of replication- dependent histone pre-mRNAs. 

Sequence Annotation

 DOMAIN 76 110 SAP.
 DOMAIN 130 306 Exonuclease.
 ACT_SITE 136 136 Proton acceptor (Potential).
 ACT_SITE 293 293 Proton acceptor (Potential).
 METAL 134 134 Magnesium 1.
 METAL 134 134 Magnesium 2.
 METAL 136 136 Magnesium 1.
 METAL 234 234 Magnesium 2.
 METAL 298 298 Magnesium 1.
 BINDING 136 136 AMP.
 BINDING 137 137 AMP; via amide nitrogen and carbonyl
 BINDING 293 293 AMP.
 MOD_RES 62 62 Phosphoserine.  

Keyword

 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; RNA-binding; RNA-mediated gene silencing; rRNA processing. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 349 AA 

Protein Sequence

Gene Ontology

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