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Q8IV48 (ERI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3'-5' exoribonuclease 1

EC=3.1.-.-
Alternative name(s):
3'-5' exonuclease ERI1
Eri-1 homolog
Histone mRNA 3'-end-specific exoribonuclease
Histone mRNA 3'-exonuclease 1
Protein 3'hExo
Short name=HEXO
Gene names
Name:ERI1
Synonyms:3'EXO, THEX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6

Cofactor

Binds 2 magnesium ions per subunit.

Enzyme regulation

Although it can bind simultaneously with SLBP to the 3'-end of histone mRNA, the presence of SLBP prevents the exonuclease activity. Ref.1

Subunit structure

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 By similarity. 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. Ref.6

Subcellular location

Cytoplasm. Nucleus. Nucleusnucleolus Ref.6.

Domain

The SAP domain is necessary for binding to the stem-loop structure of histone mRNAs and to form the ternary complex with SLBP, but not for 3'-end histone mRNA exonuclease activity.

Sequence similarities

Contains 1 exonuclease domain.

Contains 1 SAP domain.

Sequence caution

The sequence CAB70871.2 differs from that shown. Reason: Erroneous termination at position 159. Translated as Leu.

The sequence CAB70871.2 differs from that shown. Reason: Frameshift at position 117.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Probable
Chain2 – 3493483'-5' exoribonuclease 1
PRO_0000187007

Regions

Domain76 – 11035SAP
Domain130 – 306177Exonuclease

Sites

Active site1361Proton acceptor Potential
Active site2931Proton acceptor Potential
Metal binding1341Magnesium 1
Metal binding1341Magnesium 2
Metal binding1361Magnesium 1
Metal binding2341Magnesium 2
Metal binding2981Magnesium 1
Binding site1361AMP
Binding site1371AMP; via amide nitrogen and carbonyl oxygen
Binding site2931AMP

Amino acid modifications

Modified residue621Phosphoserine Ref.7

Natural variations

Natural variant161L → P. Ref.2
Corresponds to variant rs2288672 [ dbSNP | Ensembl ].
VAR_018107

Experimental info

Mutagenesis921K → A: Does not inhibit RNA-binding to the stem-loop structure. Does not inhibit RNA-binding to the stem-loop structure, when associated with A-104. Ref.6
Mutagenesis961R → A: Does not inhibit RNA-binding to the stem-loop structure. Ref.6
Mutagenesis991K → A: Reduces slightly RNA-binding to the stem-loop structure. Ref.6
Mutagenesis1041K → A: Does not inhibit RNA-binding to the stem-loop structure. Does not inhibit RNA-binding to the stem-loop structure, when associated with A-92. Ref.6
Mutagenesis1051R → A: Inhibits RNA-binding to the stem-loop structure. Ref.6
Mutagenesis1091Y → A: Reduces slightly RNA-binding to the stem-loop structure; when associated with A-110. Ref.6
Mutagenesis1101Y → A: Reduces slightly RNA-binding to the stem-loop structure; when associated with A-109. Ref.6
Mutagenesis1111K → A: Reduces RNA-binding to the stem-loop structure but not 3'-end histone mRNA exonuclease activity; when associated with A-112. Ref.6
Mutagenesis1121K → A: Reduces RNA-binding to the stem-loop structure but not 3'-end histone mRNA exonuclease activity; when associated with A-111. Ref.6
Mutagenesis2341D → A: Inhibits 3'-end histone mRNA exonuclease activity. Ref.6
Mutagenesis2351M → A: Inhibits RNA-binding to the stem-loop structure and 3'-end histone mRNA exonuclease activity. Ref.6
Mutagenesis2981D → A: Inhibits 3'-end histone mRNA exonuclease activity. Ref.6

Secondary structure

........................................... 349
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8IV48 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D5837AA05F09410C

FASTA34940,064
        10         20         30         40         50         60 
MEDPQSKEPA GEAVALALLE SPRPEGGEEP PRPSPEETQQ CKFDGQETKG SKFITSSASD 

        70         80         90        100        110        120 
FSDPVYKEIA ITNGCINRMS KEELRAKLSE FKLETRGVKD VLKKRLKNYY KKQKLMLKES 

       130        140        150        160        170        180 
NFADSYYDYI CIIDFEATCE EGNPPEFVHE IIEFPVVLLN THTLEIEDTF QQYVRPEINT 

       190        200        210        220        230        240 
QLSDFCISLT GITQDQVDRA DTFPQVLKKV IDWMKLKELG TKYKYSLLTD GSWDMSKFLN 

       250        260        270        280        290        300 
IQCQLSRLKY PPFAKKWINI RKSYGNFYKV PRSQTKLTIM LEKLGMDYDG RPHCGLDDSK 

       310        320        330        340 
NIARIAVRML QDGCELRINE KMHAGQLMSV SSSLPIEGTP PPQMPHFRK 

« Hide

References

« Hide 'large scale' references
[1]"A 3' exonuclease that specifically interacts with the 3' end of histone mRNA."
Dominski Z., Yang X.-C., Kaygun H., Dadlez M., Marzluff W.F.
Mol. Cell 12:295-305(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-23; 43-48; 53-67; 161-172; 200-208; 225-237; 263-269 AND 284-291, FUNCTION, ENZYME REGULATION, ENZYME ACTIVITY, RNA-BINDING.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PRO-16.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"A conserved siRNA-degrading RNase negatively regulates RNA interference in C. elegans."
Kennedy S., Wang D., Ruvkun G.
Nature 427:645-649(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY IN VITRO.
[6]"Characterization of 3'hExo, a 3' exonuclease specifically interacting with the 3' end of histone mRNA."
Yang X.-C., Purdy M., Marzluff W.F., Dominski Z.
J. Biol. Chem. 281:30447-30454(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A TERNARY COMPLEX, ENZYME ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-92; ARG-96; LYS-99; LYS-104; ARG-105; THY-109; THY-110; LYS-111; LYS-112; ASP-234; MET-235 AND ASP-298, RNA-BINDING.
[7]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Crystallographic structure of the nuclease domain of 3'hExo, a DEDDh family member, bound to rAMP."
Cheng Y., Patel D.J.
J. Mol. Biol. 343:305-312(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 123-322 IN COMPLEX WITH MAGNESIUM IONS AND AMP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY310909 mRNA. Translation: AAQ21219.1.
AK291062 mRNA. Translation: BAF83751.1.
AL137679 mRNA. Translation: CAB70871.2. Sequence problems.
BC035279 mRNA. Translation: AAH35279.1.
PIRT46432.
RefSeqNP_699163.2. NM_153332.3.
UniGeneHs.20000.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W0HX-ray1.59A123-322[»]
1ZBHX-ray3.00A/B/C/D51-348[»]
1ZBUX-ray3.00A/B/C/D2-348[»]
4L8RX-ray2.60B/E55-349[»]
ProteinModelPortalQ8IV48.
SMRQ8IV48. Positions 60-349.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124718. 5 interactions.
STRING9606.ENSP00000250263.

Chemistry

DrugBankDB00131. Adenosine monophosphate.

PTM databases

PhosphoSiteQ8IV48.

Polymorphism databases

DMDM45476938.

Proteomic databases

PaxDbQ8IV48.
PeptideAtlasQ8IV48.
PRIDEQ8IV48.

Protocols and materials databases

DNASU90459.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250263; ENSP00000250263; ENSG00000104626.
ENST00000519292; ENSP00000430190; ENSG00000104626.
ENST00000523898; ENSP00000429615; ENSG00000104626.
GeneID90459.
KEGGhsa:90459.
UCSCuc003wsk.2. human.

Organism-specific databases

CTD90459.
GeneCardsGC08P008900.
HGNCHGNC:23994. ERI1.
HPACAB033838.
MIM608739. gene.
neXtProtNX_Q8IV48.
PharmGKBPA164719226.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5018.
HOGENOMHOG000006635.
HOVERGENHBG048925.
InParanoidQ8IV48.
KOK01175.
OMAFLNIQCR.
OrthoDBEOG7BGHM2.
PhylomeDBQ8IV48.
TreeFamTF313449.

Gene expression databases

ArrayExpressQ8IV48.
BgeeQ8IV48.
CleanExHS_ERI1.
GenevestigatorQ8IV48.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
InterProIPR006055. Exonuclease.
IPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
IPR003034. SAP_dom.
[Graphical view]
PfamPF00929. RNase_T. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTSM00479. EXOIII. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
SUPFAMSSF53098. SSF53098. 1 hit.
PROSITEPS50800. SAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8IV48.
GenomeRNAi90459.
NextBio76770.
PROQ8IV48.
SOURCESearch...

Entry information

Entry nameERI1_HUMAN
AccessionPrimary (citable) accession number: Q8IV48
Secondary accession number(s): A8K4U7, Q9NSX3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM