XRN2 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0007283Biological processspermatogenesis
GO_0021766Biological processhippocampus development
GO_0006397Biological processmRNA processing
GO_0006396Biological processRNA processing
GO_0060041Biological processretina development in camera-type eye
GO_0006369Biological processtermination of RNA polymerase II transcription
GO_0006401Biological processRNA catabolic process
GO_0030182Biological processneuron differentiation
GO_0016070Biological processRNA metabolic process
GO_0000956Biological processnuclear-transcribed mRNA catabolic process
GO_0006364Biological processrRNA processing
GO_0005730Cellular componentnucleolus
GO_0016020Cellular componentmembrane
GO_0005654Cellular componentnucleoplasm
GO_0016235Cellular componentaggresome
GO_0005634Cellular componentnucleus
GO_0008409Molecular function5'-3' exonuclease activity
GO_0042802Molecular functionidentical protein binding
GO_0004518Molecular functionnuclease activity
GO_0046872Molecular functionmetal ion binding
GO_0003723Molecular functionRNA binding
GO_0000175Molecular function3'-5'-RNA exonuclease activity
GO_0004534Molecular function5'-3' RNA exonuclease activity
GO_0005515Molecular functionprotein binding
GO_0001147Molecular functiontranscription termination site sequence-specific DNA binding

IV. Literature review

[source]
Gene nameXRN2
Protein name5'-3' exoribonuclease 2 (EC 3.1.13.-) (DHM1-like protein) (DHP protein)
XRN2 protein
Synonyms
DescriptionFUNCTION: 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 . .

AccessionsQ9H0D6
ENST00000377191.5 [Q9H0D6-1]
A2RRQ1