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THEX1 (human)

Overview THEX1 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. Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Interacts in a cooperative manner with SLBP to the mature 3'-end of histone mRNAs. Binds to 40S and 60S ribosomal subunits and to 80S assembled ribosomes. Found in a ternary complex with SLBP and the stem-loop structure of the 3'-end of histone mRNAs. Although it can bind simultaneously with SLBP to the 3'-end of histone mRNA, the presence of SLBP prevents the exonuclease activity. Note: This description may include information from UniProtKB. Protein type: Hydrolase; EC 3.1.-.- Cellular Component: cytoplasm; nucleolus; nucleus Molecular Function: rRNA binding; metal ion binding; ribosome binding; 3'-5' exonuclease activity Biological Process: RNA-mediated gene silencing; rRNA 3'-end processing Reference #:  Q8IV48 (UniProtKB) Alt. Names/Synonyms: 3' exoribonuclease; 3'-5' exonuclease ERI1; 3'-5' exoribonuclease 1; 3'EXO; 3'HEXO; enhanced RNAi three prime mRNA exonuclease homolog 1; Eri-1 homolog; ERI1; exoribonuclease 1; HEXO; histone mRNA 3' end-specific exonuclease; Histone mRNA 3'-end-specific exoribonuclease; Histone mRNA 3'-exonuclease 1; MGC35395; Protein 3'hExo; THEX1; three prime histone mRNA exonuclease 1; three prime mRNA exonuclease 1 Gene Symbols: ERI1 Molecular weight: 40,064 Da Basal Isoelectric point: 6.29  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below THEX1 1W0H - A=123-322 (human) 1ZBH - A/B/C/D=51-349 (human) 1ZBU - A/B/C/D=1-349 (human) 4HXH - C=125-223 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1W0H 1ZBH 1ZBU 4HXH  |  ENZYME  |  Phospho3D  |  DISEASE  |  Source  |  InnateDB  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		K52-u	GQETKGSkFITSSAs
0	5		S59-p	kFITSSAsDFsDPVy
0	3		S62-p	TSSAsDFsDPVykEI
0	174		Y66-p	sDFsDPVykEIAITN
0	1		K67-a	DFsDPVykEIAITNG
0	1		K99-a	KLETRGVkDVLKKRL
0	1		K103	RGVkDVLKKRLKNYY
0	1		K104	GVkDVLKKRLKNYYK
0	2		S120	QKLMLKESNFADSYY
0	2		N121	KLMLKESNFADSYYD
0	1		K249	QCQLSRLKYPPFAKK
0	1		K269-u	KSYGNFYkVPRSQTK

	mouse
K48	GKETDGSKFISSNGS
S55	KFISSNGSDFSDPVy
S58	SSNGSDFSDPVyKEI
Y62-p	SDFSDPVyKEIAMTN
K63	DFSDPVyKEIAMTNG
K95	KLETRGVKDVLkkRL
K99-u	RGVKDVLkkRLKNYY
K100-u	GVKDVLkkRLKNYYK
S116-p	QKLMLKEssAGDSYY
S117-p	KLMLKEssAGDSYYD
K245-u	QCRLSRLkHPAFAKK
K265	KSYGNFYKVPRSQTK

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