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Entry version 172 (12 Aug 2020)
Sequence version 3 (23 Jan 2007)
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Protein

3'-5' exoribonuclease 1

Gene

ERI1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.2 Publications

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+Note: Binds 2 magnesium ions per subunit.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi134Magnesium 11
Metal bindingi134Magnesium 21
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei136Proton acceptorSequence analysis1
Metal bindingi136Magnesium 11
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei136AMP1 Publication1
Binding sitei137AMP; via amide nitrogen and carbonyl oxygen1 Publication1
Metal bindingi234Magnesium 21
Active sitei293Proton acceptorSequence analysis1
Binding sitei293AMP1 Publication1
Metal bindingi298Magnesium 11

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionExonuclease, Hydrolase, Nuclease, RNA-binding
Biological processRNA-mediated gene silencing, rRNA processing
LigandMagnesium, Metal-binding

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
Q8IV48

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-6791226, Major pathway of rRNA processing in the nucleolus and cytosol

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended 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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ERI1
Synonyms:3'EXO, THEX1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000104626.14

Human Gene Nomenclature Database

More...
HGNCi
HGNC:23994, ERI1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
608739, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q8IV48

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi92K → 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. 1 Publication1
Mutagenesisi96R → A: Does not inhibit RNA-binding to the stem-loop structure. 1 Publication1
Mutagenesisi99K → A: Reduces slightly RNA-binding to the stem-loop structure. 1 Publication1
Mutagenesisi104K → 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. 1 Publication1
Mutagenesisi105R → A: Inhibits RNA-binding to the stem-loop structure. 1 Publication1
Mutagenesisi109Y → A: Reduces slightly RNA-binding to the stem-loop structure; when associated with A-110. 1 Publication1
Mutagenesisi110Y → A: Reduces slightly RNA-binding to the stem-loop structure; when associated with A-109. 1 Publication1
Mutagenesisi111K → A: Reduces RNA-binding to the stem-loop structure but not 3'-end histone mRNA exonuclease activity; when associated with A-112. 1 Publication1
Mutagenesisi112K → A: Reduces RNA-binding to the stem-loop structure but not 3'-end histone mRNA exonuclease activity; when associated with A-111. 1 Publication1
Mutagenesisi234D → A: Inhibits 3'-end histone mRNA exonuclease activity. 1 Publication1
Mutagenesisi235M → A: Inhibits RNA-binding to the stem-loop structure and 3'-end histone mRNA exonuclease activity. 1 Publication1
Mutagenesisi298D → A: Inhibits 3'-end histone mRNA exonuclease activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
90459

Open Targets

More...
OpenTargetsi
ENSG00000104626

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA164719226

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q8IV48, Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
ERI1

Domain mapping of disease mutations (DMDM)

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DMDMi
45476938

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001870072 – 3493'-5' exoribonuclease 1Add BLAST348

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei59PhosphoserineCombined sources1
Modified residuei62PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q8IV48

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q8IV48

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q8IV48

MaxQB - The MaxQuant DataBase

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MaxQBi
Q8IV48

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q8IV48

PeptideAtlas

More...
PeptideAtlasi
Q8IV48

PRoteomics IDEntifications database

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PRIDEi
Q8IV48

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
70659

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q8IV48

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q8IV48

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000104626, Expressed in secondary oocyte and 180 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q8IV48, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q8IV48, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000104626, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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.

By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
124718, 22 interactors

Database of interacting proteins

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DIPi
DIP-61409N

Protein interaction database and analysis system

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IntActi
Q8IV48, 16 interactors

Molecular INTeraction database

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MINTi
Q8IV48

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000429615

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q8IV48, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1349
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q8IV48

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q8IV48

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini76 – 110SAPPROSITE-ProRule annotationAdd BLAST35
Domaini130 – 306ExonucleaseAdd BLAST177

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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.

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0542, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00530000063205

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_037266_4_1_1

KEGG Orthology (KO)

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KOi
K18416

Identification of Orthologs from Complete Genome Data

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OMAi
PQFAKKW

Database of Orthologous Groups

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OrthoDBi
809000at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q8IV48

TreeFam database of animal gene trees

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TreeFami
TF313449

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.720.30, 1 hit
3.30.420.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR013520, Exonuclease_RNaseT/DNA_pol3
IPR012337, RNaseH-like_sf
IPR036397, RNaseH_sf
IPR003034, SAP_dom
IPR036361, SAP_dom_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF00929, RNase_T, 1 hit
PF02037, SAP, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00479, EXOIII, 1 hit
SM00513, SAP, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53098, SSF53098, 1 hit
SSF68906, SSF68906, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50800, SAP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q8IV48-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEDPQSKEPA GEAVALALLE SPRPEGGEEP PRPSPEETQQ CKFDGQETKG
60 70 80 90 100
SKFITSSASD FSDPVYKEIA ITNGCINRMS KEELRAKLSE FKLETRGVKD
110 120 130 140 150
VLKKRLKNYY KKQKLMLKES NFADSYYDYI CIIDFEATCE EGNPPEFVHE
160 170 180 190 200
IIEFPVVLLN THTLEIEDTF QQYVRPEINT QLSDFCISLT GITQDQVDRA
210 220 230 240 250
DTFPQVLKKV IDWMKLKELG TKYKYSLLTD GSWDMSKFLN IQCQLSRLKY
260 270 280 290 300
PPFAKKWINI RKSYGNFYKV PRSQTKLTIM LEKLGMDYDG RPHCGLDDSK
310 320 330 340
NIARIAVRML QDGCELRINE KMHAGQLMSV SSSLPIEGTP PPQMPHFRK
Length:349
Mass (Da):40,064
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD5837AA05F09410C
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E5RIV7E5RIV7_HUMAN
3'-5' exoribonuclease 1
ERI1
99Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RJM3E5RJM3_HUMAN
3'-5' exoribonuclease 1
ERI1
44Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAB70871 differs from that shown. Reason: Frameshift.Curated
The sequence CAB70871 differs from that shown. Reason: Erroneous termination. Truncated C-terminus.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01810716L → P1 PublicationCorresponds to variant dbSNP:rs2288672Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AY310909 mRNA Translation: AAQ21219.1
AK291062 mRNA Translation: BAF83751.1
AL137679 mRNA Translation: CAB70871.2 Sequence problems.
BC035279 mRNA Translation: AAH35279.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS5972.1

Protein sequence database of the Protein Information Resource

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PIRi
T46432

NCBI Reference Sequences

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RefSeqi
NP_699163.2, NM_153332.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000250263; ENSP00000250263; ENSG00000104626
ENST00000519292; ENSP00000430190; ENSG00000104626

Database of genes from NCBI RefSeq genomes

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GeneIDi
90459

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:90459

UCSC genome browser

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UCSCi
uc003wsk.2, human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY310909 mRNA Translation: AAQ21219.1
AK291062 mRNA Translation: BAF83751.1
AL137679 mRNA Translation: CAB70871.2 Sequence problems.
BC035279 mRNA Translation: AAH35279.1
CCDSiCCDS5972.1
PIRiT46432
RefSeqiNP_699163.2, NM_153332.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W0HX-ray1.59A123-322[»]
1ZBHX-ray3.00A/B/C/D51-349[»]
1ZBUX-ray3.00A/B/C/D1-349[»]
4L8RX-ray2.60B/E55-349[»]
4QOZX-ray2.30B/E55-349[»]
SMRiQ8IV48
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi124718, 22 interactors
DIPiDIP-61409N
IntActiQ8IV48, 16 interactors
MINTiQ8IV48
STRINGi9606.ENSP00000429615

PTM databases

iPTMnetiQ8IV48
PhosphoSitePlusiQ8IV48

Polymorphism and mutation databases

BioMutaiERI1
DMDMi45476938

Proteomic databases

EPDiQ8IV48
jPOSTiQ8IV48
MassIVEiQ8IV48
MaxQBiQ8IV48
PaxDbiQ8IV48
PeptideAtlasiQ8IV48
PRIDEiQ8IV48
ProteomicsDBi70659

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
8346, 281 antibodies

The DNASU plasmid repository

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DNASUi
90459

Genome annotation databases

EnsembliENST00000250263; ENSP00000250263; ENSG00000104626
ENST00000519292; ENSP00000430190; ENSG00000104626
GeneIDi90459
KEGGihsa:90459
UCSCiuc003wsk.2, human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
90459
DisGeNETi90459
EuPathDBiHostDB:ENSG00000104626.14

GeneCards: human genes, protein and diseases

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GeneCardsi
ERI1
HGNCiHGNC:23994, ERI1
HPAiENSG00000104626, Low tissue specificity
MIMi608739, gene
neXtProtiNX_Q8IV48
OpenTargetsiENSG00000104626
PharmGKBiPA164719226

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG0542, Eukaryota
GeneTreeiENSGT00530000063205
HOGENOMiCLU_037266_4_1_1
KOiK18416
OMAiPQFAKKW
OrthoDBi809000at2759
PhylomeDBiQ8IV48
TreeFamiTF313449

Enzyme and pathway databases

PathwayCommonsiQ8IV48
ReactomeiR-HSA-6791226, Major pathway of rRNA processing in the nucleolus and cytosol

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
90459, 25 hits in 878 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
ERI1, human
EvolutionaryTraceiQ8IV48

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
90459
PharosiQ8IV48, Tbio

Protein Ontology

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PROi
PR:Q8IV48
RNActiQ8IV48, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000104626, Expressed in secondary oocyte and 180 other tissues
ExpressionAtlasiQ8IV48, baseline and differential
GenevisibleiQ8IV48, HS

Family and domain databases

Gene3Di1.10.720.30, 1 hit
3.30.420.10, 1 hit
InterProiView protein in InterPro
IPR013520, Exonuclease_RNaseT/DNA_pol3
IPR012337, RNaseH-like_sf
IPR036397, RNaseH_sf
IPR003034, SAP_dom
IPR036361, SAP_dom_sf
PfamiView protein in Pfam
PF00929, RNase_T, 1 hit
PF02037, SAP, 1 hit
SMARTiView protein in SMART
SM00479, EXOIII, 1 hit
SM00513, SAP, 1 hit
SUPFAMiSSF53098, SSF53098, 1 hit
SSF68906, SSF68906, 1 hit
PROSITEiView protein in PROSITE
PS50800, SAP, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiERI1_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8IV48
Secondary accession number(s): A8K4U7, Q9NSX3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: January 23, 2007
Last modified: August 12, 2020
This is version 172 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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