O43414 · ERI3_HUMAN

  • Protein
    ERI1 exoribonuclease 3
  • Gene
    ERI3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 2 magnesium ions per subunit.

Features

Showing features for binding site, active site.

133750100150200250300
TypeIDPosition(s)Description
Binding site150Mg2+ 1 (UniProtKB | ChEBI)
Binding site150Mg2+ 2 (UniProtKB | ChEBI)
Active site152Proton acceptor
Binding site152AMP (UniProtKB | ChEBI)
Binding site152Mg2+ 1 (UniProtKB | ChEBI)
Binding site249Mg2+ 2 (UniProtKB | ChEBI)
Active site307Proton acceptor
Binding site307AMP (UniProtKB | ChEBI)
Binding site312Mg2+ 1 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Function3'-5'-RNA exonuclease activity
Molecular Functionmetal ion binding
Molecular FunctionRNA binding
Biological Processexonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ERI1 exoribonuclease 3
  • EC number
  • Alternative names
    • Prion interactor 1
    • Prion protein-interacting protein

Gene names

    • Name
      ERI3
    • Synonyms
      PINT1, PRNPIP, PRNPIP1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    O43414
  • Secondary accessions
    • B1AK98
    • Q5T2T7
    • Q5T2T9
    • Q5TG35
    • Q9BQA0
    • Q9UEB4

Proteomes

Organism-specific databases

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 295 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003176261-337ERI1 exoribonuclease 3

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with PRNP.

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain146-320Exonuclease

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

O43414-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    337
  • Mass (Da)
    37,238
  • Last updated
    2008-03-18 v2
  • Checksum
    28E8A691659B4D67
MATASPAADGGRGRPWEGGLVSWPPAPPLTLPWTWMGPSWGQHPGHWGFPALTEPSASPAAGLGIFEVRRVLDASGCSMLAPLQTGAARFSSYLLSRARKVLGSHLFSPCGVPEFCSISTRKLAAHGFGASMAAMVSFPPQRYHYFLVLDFEATCDKPQIHPQEIIEFPILKLNGRTMEIESTFHMYVQPVVHPQLTPFCTELTGIIQAMVDGQPSLQQVLERVDEWMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQYLGLPVADYFKQWINLKKAYSFAMGCWPKNGLLDMNKGLSLQHIGRPHSGIDDCKNIANIMKTLAYRGFIFKQTSKPF

O43414-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-163: MATASPAADGGRGRPWEGGLVSWPPAPPLTLPWTWMGPSWGQHPGHWGFPALTEPSASPAAGLGIFEVRRVLDASGCSMLAPLQTGAARFSSYLLSRARKVLGSHLFSPCGVPEFCSISTRKLAAHGFGASMAAMVSFPPQRYHYFLVLDFEATCDKPQIHPQ → MFVMLQVPWLQSCANLVQIGAPLPLLGCLGQYFEVLGSMEVLAGQYGM

O43414-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 6 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F6QUN3F6QUN3_HUMANERI3176
H0Y4B0H0Y4B0_HUMANERI3202
A0A3B3ISV9A0A3B3ISV9_HUMANERI3315
A0A3B3IU35A0A3B3IU35_HUMANERI373
A0A3B3ITJ5A0A3B3ITJ5_HUMANERI328
F6UGJ8F6UGJ8_HUMANERI3250

Sequence caution

The sequence AAC19158.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0311031-163in isoform 2
Alternative sequenceVSP_0311041-209in isoform 3

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF007157
EMBL· GenBank· DDBJ
AAC19158.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK290567
EMBL· GenBank· DDBJ
BAF83256.1
EMBL· GenBank· DDBJ
mRNA
AL035417
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL390776
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC004254
EMBL· GenBank· DDBJ
AAC04618.1
EMBL· GenBank· DDBJ
Genomic DNA
BC001072
EMBL· GenBank· DDBJ
AAH01072.1
EMBL· GenBank· DDBJ
mRNA
BC004456
EMBL· GenBank· DDBJ
AAH04456.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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