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Q9DBR1 · XRN2_MOUSE

  • Protein
    5'-3' exoribonuclease 2
  • Gene
    Xrn2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Possesses 5'->3' exoribonuclease activity. May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5' fragment which is subsequently processed to form the mature mRNA and a 3' fragment which remains attached to the elongating polymerase. The processive degradation of this 3' fragment by this protein may promote termination of transcription. Binds to RNA polymerase II (RNAp II) transcription termination R-loops formed by G-rich pause sites (By similarity).

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
Cellular Componentaggresome
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Molecular Function5'-3' exonuclease activity
Molecular Function5'-3' RNA exonuclease activity
Molecular Functionidentical protein binding
Molecular Functionmetal ion binding
Molecular Functiontranscription termination site sequence-specific DNA binding
Biological ProcessDNA recombination
Biological ProcessDNA repair
Biological Processhippocampus development
Biological Processmicrotubule-based process
Biological ProcessmRNA processing
Biological Processneuron differentiation
Biological Processretina development in camera-type eye
Biological ProcessRNA metabolic process
Biological Processspermatogenesis
Biological Processtermination of RNA polymerase II transcription

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    5'-3' exoribonuclease 2
  • EC number
  • Alternative names
    • Protein Dhm1

Gene names

    • Name
      Xrn2
    • Synonyms
      Dhm1

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • Czech II
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9DBR1
  • Secondary accessions
    • Q3TI26
    • Q3TKF2
    • Q3UZT9
    • Q61489
    • Q99KS7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00000713971-9515'-3' exoribonuclease 2
Modified residue286N6-acetyllysine
Modified residue439Phosphothreonine
Modified residue448Phosphoserine
Modified residue471Phosphoserine
Modified residue473Phosphoserine
Modified residue475Phosphoserine
Modified residue482Phosphoserine
Modified residue487Phosphoserine
Modified residue499Phosphoserine
Modified residue501Phosphoserine
Modified residue678Phosphoserine
Modified residue824Asymmetric dimethylarginine; alternate
Modified residue824Omega-N-methylarginine; alternate
Modified residue847Asymmetric dimethylarginine; alternate
Modified residue847Omega-N-methylarginine; alternate
Modified residue851Asymmetric dimethylarginine; alternate
Modified residue851Omega-N-methylarginine; alternate
Modified residue880Asymmetric dimethylarginine
Modified residue883Asymmetric dimethylarginine; alternate
Modified residue883Omega-N-methylarginine; alternate
Modified residue895Omega-N-methylarginine
Modified residue947Asymmetric dimethylarginine; alternate
Modified residue947Omega-N-methylarginine; alternate

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in the spleen, testis, heart, brain, lung, liver, skeletal muscle, and kidney.

Gene expression databases

Interaction

Subunit

Interacts with POLR2A and SMN1/SMN2. Interacts with CDKN2AIP and NKRF. Interacts with CDKN2AIPNL; the interaction is direct. Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner (By similarity).
Interacts with DHX34; the interaction is RNA-independent (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for zinc finger, region, compositional bias.

Type
IDPosition(s)Description
Zinc finger262-278CCHC-type
Region408-508Disordered
Compositional bias440-455Polar residues
Compositional bias462-485Polar residues
Compositional bias493-508Basic and acidic residues
Region907-951Disordered
Compositional bias919-933Basic and acidic residues

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9DBR1-1

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
    951
  • Mass (Da)
    108,687
  • Last updated
    2001-06-01 v1
  • MD5 Checksum
    4F9ACCE339D6CF0321BEC6EE23C6AFC9
MGVPAFFRWLSRKYPSIIVNCVEEKPKECNGVKIPVDASKPNPNDVEFDNLYLDMNGIIHPCTHPEDKPAPKNEDEMMVAIFEYIDRLFNIVRPRRLLYMAIDGVAPRAKMNQQRSRRFRASKEGMEAAVEKQRVREEILAKGGFLPPEEIKERFDSNCITPGTEFMDNLAKCLRYYIADRLNNDPGWKNLTVILSDASAPGEGEHKIMDYIRRQRAQPNHDPNTHHCLCGADADLIMLGLATHEPNFTIIREEFKPNKPKPCALCNQFGHEVKDCEGLPREKKGKHDELADSLPCAEGEFIFLRLNVLREYLERELTMASLPFPFDVERSIDDWVFMCFFVGNDFLPHLPSLEIREGAIDRLVNIYKNVVHKTGGYLTESGYVNLQRVQMIMLAVGEVEDSIFKKRKDDEDSFRRRQKEKRKRMKRDQPAFTPSGILTPHALGSRNSPGCQVASNPRQAAYEMRMQRNSSPSISPNTSFASDGSPSPLGGIKRKAEDSDSEPEPEDNVRLWEAGWKQRYYKNKFDVDAADEKFRRKVVQSYVEGLCWVLRYYYQGCASWKWYYPFHYAPFASDFEGIADMSSEFEKGTKPFKPLEQLMGVFPAASGNFLPPTWRKLMSDPDSSIIDFYPEDFAIDLNGKKYAWQGVALLPFVDERRLRAALEEVYPDLTPEENRRNSLGGDVLFVGKLHPLRDFILELYQTGSTEPVDVPPELCHGIQGTFSLDEEAILPDQTVCSPVPMLRDLTQNTAVSINFKDPQFAEDYVFKAAMLPGARKPATVLKPGDWEKSSNGRQWKPQLGFNRDRRPVHLDQAAFRTLGHVTPRGSGTSVYTNTALPPANYQGNNYRPLLRGQAQIPKLMSNMRPQDSWRGPPPLFQQHRFERSVGAEPLLPWNRMIQNQNAAFQPNQYQMLGGPGGYPPRRDDHRGGRQGYPREGRKYPLPPPSGRYSWN

Q9DBR1-2

  • Name
    2
  • Note
    May result from the retention of an intron in the cDNA.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 931-951: GYPREGRKYPLPPPSGRYSWN → VISTMWAVEGKQHTAHC

Sequence caution

The sequence AAH04028.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for sequence conflict, compositional bias, alternative sequence.

Type
IDPosition(s)Description
Sequence conflict122-124in Ref. 1; BAA07524
Sequence conflict221in Ref. 1; BAA07524
Sequence conflict306in Ref. 2; BAE40020
Sequence conflict332in Ref. 1; BAA07524
Sequence conflict336in Ref. 1; BAA07524
Sequence conflict440in Ref. 2; BAE40020
Compositional bias440-455Polar residues
Sequence conflict449in Ref. 2; BAE40020
Compositional bias462-485Polar residues
Sequence conflict493in Ref. 1; BAA07524
Compositional bias493-508Basic and acidic residues
Sequence conflict563in Ref. 1; BAA07524
Sequence conflict712in Ref. 2; BAC27318
Sequence conflict734in Ref. 2; BAC27318
Sequence conflict837in Ref. 1; BAA07524
Sequence conflict866in Ref. 1; BAA07524
Sequence conflict889in Ref. 2; BAC27318
Compositional bias919-933Basic and acidic residues
Sequence conflict923in Ref. 2; BAE40020
Sequence conflict930in Ref. 2; BAC27318
Alternative sequenceVSP_007235931-951in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D38517
EMBL· GenBank· DDBJ
BAA07524.1
EMBL· GenBank· DDBJ
mRNA
AK004800
EMBL· GenBank· DDBJ
BAB23573.1
EMBL· GenBank· DDBJ
mRNA
AK031247
EMBL· GenBank· DDBJ
BAC27318.1
EMBL· GenBank· DDBJ
mRNA
AK053643
EMBL· GenBank· DDBJ
BAC35458.1
EMBL· GenBank· DDBJ
mRNA
AK133654
EMBL· GenBank· DDBJ
BAE21766.1
EMBL· GenBank· DDBJ
mRNA
AK167019
EMBL· GenBank· DDBJ
BAE39193.1
EMBL· GenBank· DDBJ
mRNA
AK168037
EMBL· GenBank· DDBJ
BAE40020.1
EMBL· GenBank· DDBJ
mRNA
BC004028
EMBL· GenBank· DDBJ
AAH04028.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC054743
EMBL· GenBank· DDBJ
AAH54743.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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