Q9H0D6 · XRN2_HUMAN
- Protein5'-3' exoribonuclease 2
- GeneXRN2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids950 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | aggresome | |
Cellular Component | membrane | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | 3'-5'-RNA exonuclease activity | |
Molecular Function | 5'-3' exonuclease activity | |
Molecular Function | 5'-3' RNA exonuclease activity | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | nuclease activity | |
Molecular Function | RNA binding | |
Molecular Function | transcription termination site sequence-specific DNA binding | |
Biological Process | hippocampus development | |
Biological Process | mRNA processing | |
Biological Process | neuron differentiation | |
Biological Process | nuclear-transcribed mRNA catabolic process | |
Biological Process | retina development in camera-type eye | |
Biological Process | RNA catabolic process | |
Biological Process | RNA metabolic process | |
Biological Process | RNA processing | |
Biological Process | rRNA processing | |
Biological Process | spermatogenesis | |
Biological Process | termination of RNA polymerase II transcription |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name5'-3' exoribonuclease 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H0D6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_027516 | 743 | in dbSNP:rs6137324 | |||
Sequence: R → M | ||||||
Natural variant | VAR_053002 | 925 | in dbSNP:rs6047420 | |||
Sequence: R → C |
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.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000071396 | 1-950 | UniProt | 5'-3' exoribonuclease 2 | |||
Sequence: MGVPAFFRWLSRKYPSIIVNCVEEKPKECNGVKIPVDASKPNPNDVEFDNLYLDMNGIIHPCTHPEDKPAPKNEDEMMVAIFEYIDRLFSIVRPRRLLYMAIDGVAPRAKMNQQRSRRFRASKEGMEAAVEKQRVREEILAKGGFLPPEEIKERFDSNCITPGTEFMDNLAKCLRYYIADRLNNDPGWKNLTVILSDASAPGEGEHKIMDYIRRQRAQPNHDPNTHHCLCGADADLIMLGLATHEPNFTIIREEFKPNKPKPCGLCNQFGHEVKDCEGLPREKKGKHDELADSLPCAEGEFIFLRLNVLREYLERELTMASLPFTFDVERSIDDWVFMCFFVGNDFLPHLPSLEIRENAIDRLVNIYKNVVHKTGGYLTESGYVNLQRVQMIMLAVGEVEDSIFKKRKDDEDSFRRRQKEKRKRMKRDQPAFTPSGILTPHALGSRNSPGSQVASNPRQAAYEMRMQNNSSPSISPNTSFTSDGSPSPLGGIKRKAEDSDSEPEPEDNVRLWEAGWKQRYYKNKFDVDAADEKFRRKVVQSYVEGLCWVLRYYYQGCASWKWYYPFHYAPFASDFEGIADMPSDFEKGTKPFKPLEQLMGVFPAASGNFLPPSWRKLMSDPDSSIIDFYPEDFAIDLNGKKYAWQGVALLPFVDERRLRAALEEVYPDLTPEETRRNSLGGDVLFVGKHHPLHDFILELYQTGSTEPVEVPPELCHGIQGKFSLDEEAILPDQIVCSPVPMLRDLTQNTVVSINFKDPQFAEDYIFKAVMLPGARKPAAVLKPSDWEKSSNGRQWKPQLGFNRDRRPVHLDQAAFRTLGHVMPRGSGTGIYSNAAPPPVTYQGNLYRPLLRGQAQIPKLMSNMRPQDSWRGPPPLFQQQRFDRGVGAEPLLPWNRMLQTQNAAFQPNQYQMLAGPGGYPPRRDDRGGRQGYPREGRKYPLPPPSGRYNWN | |||||||
Modified residue | 286 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 433 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 435 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 439 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 439 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 445 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 448 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 448 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 451 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 455 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 470 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 471 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 471 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 473 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 473 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 475 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 475 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 478 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 482 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 482 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 485 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 487 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 487 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 499 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 499 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 501 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 501 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 678 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 678 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 824 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 824 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 847 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 847 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 851 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 851 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 880 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 883 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 883 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 895 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 946 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 946 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R |
Keywords
- PTM
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).
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9H0D6 | CDKN2AIP Q9NXV6 | 7 | EBI-372110, EBI-2559836 | |
BINARY | Q9H0D6 | CDKN2AIPNL Q96HQ2 | 4 | EBI-372110, EBI-10038935 | |
BINARY | Q9H0D6 | CRY2 Q49AN0 | 3 | EBI-372110, EBI-2212355 | |
BINARY | Q9H0D6 | DISC1 Q9NRI5 | 3 | EBI-372110, EBI-529989 | |
BINARY | Q9H0D6 | LCN2 P80188 | 3 | EBI-372110, EBI-11911016 | |
BINARY | Q9H0D6 | PLEKHF2 Q9H8W4 | 3 | EBI-372110, EBI-742388 | |
BINARY | Q9H0D6 | TARDBP Q13148 | 7 | EBI-372110, EBI-372899 | |
BINARY | Q9H0D6 | TTC23 Q5W5X9-3 | 3 | EBI-372110, EBI-9090990 | |
BINARY | Q9H0D6 | XRN2 Q9H0D6 | 3 | EBI-372110, EBI-372110 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 262-278 | CCHC-type | ||||
Sequence: PCGLCNQFGHEVKDCEG | ||||||
Region | 408-508 | Disordered | ||||
Sequence: KDDEDSFRRRQKEKRKRMKRDQPAFTPSGILTPHALGSRNSPGSQVASNPRQAAYEMRMQNNSSPSISPNTSFTSDGSPSPLGGIKRKAEDSDSEPEPEDN | ||||||
Compositional bias | 440-486 | Polar residues | ||||
Sequence: PHALGSRNSPGSQVASNPRQAAYEMRMQNNSSPSISPNTSFTSDGSP | ||||||
Compositional bias | 493-508 | Basic and acidic residues | ||||
Sequence: KRKAEDSDSEPEPEDN | ||||||
Region | 911-950 | Disordered | ||||
Sequence: MLAGPGGYPPRRDDRGGRQGYPREGRKYPLPPPSGRYNWN |
Sequence similarities
Belongs to the 5'-3' exonuclease family. XRN2/RAT1 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- Name1
- SynonymsXRN2a
- Length950
- Mass (Da)108,582
- Last updated2001-03-01 v1
- Checksum763B5E0E628F97A8
Q9H0D6-2
- Name2
- SynonymsXRN2b
- Differences from canonical
- 1-76: Missing
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_020596 | 1-76 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 14 | in Ref. 1; AAQ13577 | ||||
Sequence: Y → C | ||||||
Sequence conflict | 109 | in Ref. 1; AAD55138/AAQ13577 | ||||
Sequence: A → V | ||||||
Sequence conflict | 122-124 | in Ref. 1; AAD55138 | ||||
Sequence: SKE → IKR | ||||||
Sequence conflict | 240-245 | in Ref. 1; AAQ13577 | ||||
Sequence: GLATHE → AFPHMN | ||||||
Sequence conflict | 259 | in Ref. 1; AAD55138/AAQ13577 | ||||
Sequence: K → R | ||||||
Sequence conflict | 280 | in Ref. 1; AAD55138/AAQ13577 | ||||
Sequence: P → S | ||||||
Sequence conflict | 313 | in Ref. 1; AAQ13577 | ||||
Sequence: L → V | ||||||
Compositional bias | 440-486 | Polar residues | ||||
Sequence: PHALGSRNSPGSQVASNPRQAAYEMRMQNNSSPSISPNTSFTSDGSP | ||||||
Sequence conflict | 463 | in Ref. 1; AAD55138 | ||||
Sequence: E → D | ||||||
Compositional bias | 493-508 | Basic and acidic residues | ||||
Sequence: KRKAEDSDSEPEPEDN | ||||||
Sequence conflict | 582 | in Ref. 1; AAQ13577 | ||||
Sequence: P → S | ||||||
Sequence conflict | 584 | in Ref. 1; AAD55138 | ||||
Sequence: D → E | ||||||
Sequence conflict | 737 | in Ref. 1; AAD55138 | ||||
Sequence: S → A | ||||||
Sequence conflict | 760 | in Ref. 2; AAR24369 | ||||
Sequence: F → L | ||||||
Sequence conflict | 787 | in Ref. 1; AAD55138 | ||||
Sequence: E → G | ||||||
Sequence conflict | 874 | in Ref. 2; AAR24369 | ||||
Sequence: P → L |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |