Q9H0D6 · XRN2_HUMAN

  • 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 (By similarity).
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 (PubMed:21700224).

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 Componentmembrane
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Cellular Componentnucleus
Molecular Function3'-5'-RNA exonuclease activity
Molecular Function5'-3' exonuclease activity
Molecular Function5'-3' RNA exonuclease activity
Molecular Functionidentical protein binding
Molecular Functionmetal ion binding
Molecular Functionnuclease activity
Molecular FunctionRNA binding
Molecular Functiontranscription termination site sequence-specific DNA binding
Biological Processhippocampus development
Biological ProcessmRNA processing
Biological Processneuron differentiation
Biological Processnuclear-transcribed mRNA catabolic process
Biological Processretina development in camera-type eye
Biological ProcessRNA catabolic process
Biological ProcessRNA metabolic process
Biological ProcessRNA processing
Biological ProcessrRNA processing
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
    • DHM1-like protein (DHP protein)

Gene names

    • Name
      XRN2

Organism names

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

Accessions

  • Primary accession
    Q9H0D6
  • Secondary accessions
    • Q3L8N4
    • Q6KGZ9
    • Q9BQL1
    • Q9NTW0
    • Q9NXS6
    • Q9UL53

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_027516743in dbSNP:rs6137324
Natural variantVAR_053002925in dbSNP:rs6047420

Variants

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

The viewer provides 870 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, modified residue, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00000713961-950UniProt5'-3' exoribonuclease 2
Modified residue286UniProtN6-acetyllysine
Modified residue (large scale data)433PRIDEPhosphothreonine
Modified residue (large scale data)435PRIDEPhosphoserine
Modified residue439UniProtPhosphothreonine
Modified residue (large scale data)439PRIDEPhosphothreonine
Modified residue (large scale data)445PRIDEPhosphoserine
Modified residue448UniProtPhosphoserine
Modified residue (large scale data)448PRIDEPhosphoserine
Modified residue (large scale data)451PRIDEPhosphoserine
Modified residue (large scale data)455PRIDEPhosphoserine
Modified residue (large scale data)470PRIDEPhosphoserine
Modified residue471UniProtPhosphoserine
Modified residue (large scale data)471PRIDEPhosphoserine
Modified residue473UniProtPhosphoserine
Modified residue (large scale data)473PRIDEPhosphoserine
Modified residue475UniProtPhosphoserine
Modified residue (large scale data)475PRIDEPhosphoserine
Modified residue (large scale data)478PRIDEPhosphothreonine
Modified residue482UniProtPhosphoserine
Modified residue (large scale data)482PRIDEPhosphoserine
Modified residue (large scale data)485PRIDEPhosphoserine
Modified residue487UniProtPhosphoserine
Modified residue (large scale data)487PRIDEPhosphoserine
Modified residue499UniProtPhosphoserine
Modified residue (large scale data)499PRIDEPhosphoserine
Modified residue501UniProtPhosphoserine
Modified residue (large scale data)501PRIDEPhosphoserine
Modified residue678UniProtPhosphoserine
Modified residue (large scale data)678PRIDEPhosphoserine
Modified residue824UniProtAsymmetric dimethylarginine; alternate
Modified residue824UniProtOmega-N-methylarginine; alternate
Modified residue847UniProtAsymmetric dimethylarginine; alternate
Modified residue847UniProtOmega-N-methylarginine; alternate
Modified residue851UniProtAsymmetric dimethylarginine; alternate
Modified residue851UniProtOmega-N-methylarginine; alternate
Modified residue880UniProtAsymmetric dimethylarginine
Modified residue883UniProtAsymmetric dimethylarginine; alternate
Modified residue883UniProtOmega-N-methylarginine; alternate
Modified residue895UniProtOmega-N-methylarginine
Modified residue946UniProtAsymmetric dimethylarginine; alternate
Modified residue946UniProtOmega-N-methylarginine; alternate

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in the spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocytes, heart, brain, placenta, lung, liver, skeletal muscle, kidney, and pancreas. Isoform 2 is expressed predominantly in peripheral blood leukocytes.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with POLR2A and SMN1/SMN2 (PubMed:26700805).
Interacts with CDKN2AIP and NKRF (PubMed:24462208).
Interacts with CDKN2AIPNL; the interaction is direct (PubMed:26779609).
Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner (PubMed:23125361).
Interacts with DHX34; the interaction is RNA-independent (PubMed:25220460).

Binary interactions

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for zinc finger, region, compositional bias.

TypeIDPosition(s)Description
Zinc finger262-278CCHC-type
Region408-508Disordered
Compositional bias440-486Polar residues
Compositional bias493-508Basic and acidic residues
Region911-950Disordered

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.

Q9H0D6-1

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.

  • Name
    1
  • Synonyms
    XRN2a
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    950
  • Mass (Da)
    108,582
  • Last updated
    2001-03-01 v1
  • Checksum
    763B5E0E628F97A8
MGVPAFFRWLSRKYPSIIVNCVEEKPKECNGVKIPVDASKPNPNDVEFDNLYLDMNGIIHPCTHPEDKPAPKNEDEMMVAIFEYIDRLFSIVRPRRLLYMAIDGVAPRAKMNQQRSRRFRASKEGMEAAVEKQRVREEILAKGGFLPPEEIKERFDSNCITPGTEFMDNLAKCLRYYIADRLNNDPGWKNLTVILSDASAPGEGEHKIMDYIRRQRAQPNHDPNTHHCLCGADADLIMLGLATHEPNFTIIREEFKPNKPKPCGLCNQFGHEVKDCEGLPREKKGKHDELADSLPCAEGEFIFLRLNVLREYLERELTMASLPFTFDVERSIDDWVFMCFFVGNDFLPHLPSLEIRENAIDRLVNIYKNVVHKTGGYLTESGYVNLQRVQMIMLAVGEVEDSIFKKRKDDEDSFRRRQKEKRKRMKRDQPAFTPSGILTPHALGSRNSPGSQVASNPRQAAYEMRMQNNSSPSISPNTSFTSDGSPSPLGGIKRKAEDSDSEPEPEDNVRLWEAGWKQRYYKNKFDVDAADEKFRRKVVQSYVEGLCWVLRYYYQGCASWKWYYPFHYAPFASDFEGIADMPSDFEKGTKPFKPLEQLMGVFPAASGNFLPPSWRKLMSDPDSSIIDFYPEDFAIDLNGKKYAWQGVALLPFVDERRLRAALEEVYPDLTPEETRRNSLGGDVLFVGKHHPLHDFILELYQTGSTEPVEVPPELCHGIQGKFSLDEEAILPDQIVCSPVPMLRDLTQNTVVSINFKDPQFAEDYIFKAVMLPGARKPAAVLKPSDWEKSSNGRQWKPQLGFNRDRRPVHLDQAAFRTLGHVMPRGSGTGIYSNAAPPPVTYQGNLYRPLLRGQAQIPKLMSNMRPQDSWRGPPPLFQQQRFDRGVGAEPLLPWNRMLQTQNAAFQPNQYQMLAGPGGYPPRRDDRGGRQGYPREGRKYPLPPPSGRYNWN

Q9H0D6-2

  • Name
    2
  • Synonyms
    XRN2b
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Sequence caution

The sequence AAR24369.1 differs from that shown. Reason: Frameshift
The sequence BAA90934.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

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

TypeIDPosition(s)Description
Alternative sequenceVSP_0205961-76in isoform 2
Sequence conflict14in Ref. 1; AAQ13577
Sequence conflict109in Ref. 1; AAD55138/AAQ13577
Sequence conflict122-124in Ref. 1; AAD55138
Sequence conflict240-245in Ref. 1; AAQ13577
Sequence conflict259in Ref. 1; AAD55138/AAQ13577
Sequence conflict280in Ref. 1; AAD55138/AAQ13577
Sequence conflict313in Ref. 1; AAQ13577
Compositional bias440-486Polar residues
Sequence conflict463in Ref. 1; AAD55138
Compositional bias493-508Basic and acidic residues
Sequence conflict582in Ref. 1; AAQ13577
Sequence conflict584in Ref. 1; AAD55138
Sequence conflict737in Ref. 1; AAD55138
Sequence conflict760in Ref. 2; AAR24369
Sequence conflict787in Ref. 1; AAD55138
Sequence conflict874in Ref. 2; AAR24369

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF064257
EMBL· GenBank· DDBJ
AAD55138.1
EMBL· GenBank· DDBJ
mRNA
AF152169
EMBL· GenBank· DDBJ
AAQ13577.1
EMBL· GenBank· DDBJ
mRNA
AY382900
EMBL· GenBank· DDBJ
AAR24369.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AL136841
EMBL· GenBank· DDBJ
CAB66775.1
EMBL· GenBank· DDBJ
mRNA
AL117332
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL158013
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AK000084
EMBL· GenBank· DDBJ
BAA90934.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC006417
EMBL· GenBank· DDBJ
AAH06417.2
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp