Q80U58 · PUM2_MOUSE
- ProteinPumilio homolog 2
- GenePum2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1066 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation. Also mediates deadenylation-independent repression by promoting accessibility of miRNAs. Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation. Plays a role in cytoplasmic sensing of viral infection. Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm. May regulate DCUN1D3 mRNA levels. May support proliferation and self-renewal of stem cells. Binds specifically to miRNA MIR199A precursor, with PUM1, regulates miRNA MIR199A expression at a postranscriptional level (By similarity).
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended namePumilio homolog 2
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ80U58
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS1 and SNAPIN in the perinuclear region of germ cells (By similarity).
Colocalizes with NANOS3 in the stress granules (PubMed:19861488).
Colocalizes with NANOS3 in the stress granules (PubMed:19861488).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000075920 | 1-1066 | Pumilio homolog 2 | |||
Sequence: MNHDFQALALESRGMGELLPTKKFWEPDDSTKDGQKGIFLGDDEWRETAWGTSHHSMSQPIMVQRRSGQSFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGTFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQDDEDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPSTNPPEGLGPLPNPTANKPLVEEFSNPETQNLDAMDQVGLDSLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTSALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAASNTANQQAASQAQPGQQQVLRPGAGQRPITPSQGQQGQQAESLAAAANPTLAFGQSLAAGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSTAAQAAAAAAAAGGTANSLTGSTNGLFRPIGTQPPQQQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSASLGFGSGSSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQIVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQVISEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGML | ||||||
Modified residue | 67 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 70 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 82 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 102 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 136 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 177 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 181 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 183 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 395 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 587 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 592 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 674 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 684 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 700 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed. Expressed in embryonic stem cells, heart, kidney, lung, skin, intestine, spleen and thymus. Expressed at intermediate level in brain and liver. Weakly or not expressed in muscles and stomach. Expressed at various stages of myeloid and lymphoid cell development. In the testis expressed in the spermatogoni, spermatocytes, spermatids and Sertoli cells.
Gene expression databases
Interaction
Subunit
Homodimer; homodimerizes in vitro. Interacts with DAZ1, DAZL and NANOS1 via its pumilio repeats. Interacts with NANOS3 (By similarity).
Interacts with SNAPIN. Recruits the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation. Interacts with DDX20. In case of viral infection, interacts with DHX58 (By similarity).
Interacts with SNAPIN. Recruits the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation. Interacts with DDX20. In case of viral infection, interacts with DHX58 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-260 | Interaction with SNAPIN | ||||
Sequence: MNHDFQALALESRGMGELLPTKKFWEPDDSTKDGQKGIFLGDDEWRETAWGTSHHSMSQPIMVQRRSGQSFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGTFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQDDEDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPSTNPPEGLGPLPNPTANKPLVEEFSNPETQNLDAMDQVGLDSLQFDYPGNQVPMDSSGATVGLFDYNSQ | ||||||
Compositional bias | 106-156 | Basic and acidic residues | ||||
Sequence: KLDSRFRKGTFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQDDEDSKIN | ||||||
Region | 106-203 | Disordered | ||||
Sequence: KLDSRFRKGTFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQDDEDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPSTNPPEGLGPLP | ||||||
Compositional bias | 368-385 | Polar residues | ||||
Sequence: TANQQAASQAQPGQQQVL | ||||||
Region | 368-408 | Disordered | ||||
Sequence: TANQQAASQAQPGQQQVLRPGAGQRPITPSQGQQGQQAESL | ||||||
Compositional bias | 393-408 | Polar residues | ||||
Sequence: PITPSQGQQGQQAESL | ||||||
Region | 490-551 | Disordered | ||||
Sequence: TGSTNGLFRPIGTQPPQQQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSASL | ||||||
Region | 620-650 | Disordered | ||||
Sequence: SPIGMPLPSQTPGHSLTPPPSLSSHGSSSSL | ||||||
Domain | 706-1048 | PUM-HD | ||||
Sequence: GRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQIVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQVISEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYY | ||||||
Repeat | 726-761 | Pumilio 1 | ||||
Sequence: DLIGHIVEFSQDQHGSRFIQQKLERATPAERQIVFN | ||||||
Region | 741-745 | Adenine-nucleotide binding in RNA target | ||||
Sequence: SRFIQ | ||||||
Repeat | 762-797 | Pumilio 2 | ||||
Sequence: EILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALAT | ||||||
Region | 777-781 | Uracil-nucleotide binding in RNA target | ||||
Sequence: NYVIQ | ||||||
Repeat | 798-835 | Pumilio 3 | ||||
Sequence: RIRGHVLPLALQMYGCRVIQKALESISSDQQVISEMVK | ||||||
Region | 813-817 | Adenine-nucleotide binding in RNA target | ||||
Sequence: CRVIQ | ||||||
Repeat | 836-871 | Pumilio 4 | ||||
Sequence: ELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIID | ||||||
Region | 851-855 | Non-specific-nucleotide binding in RNA target | ||||
Sequence: NHVVQ | ||||||
Repeat | 872-907 | Pumilio 5 | ||||
Sequence: AFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLPILE | ||||||
Region | 887-891 | Adenine-nucleotide binding in RNA target | ||||
Sequence: CRVIQ | ||||||
Repeat | 908-943 | Pumilio 6 | ||||
Sequence: ELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVS | ||||||
Region | 923-927 | Uracil-nucleotide binding in RNA target | ||||
Sequence: NYVIQ | ||||||
Repeat | 944-979 | Pumilio 7 | ||||
Sequence: EIRGKVLALSQHKFASNVVEKCVTHASRAERALLID | ||||||
Region | 959-963 | Guanine-nucleotide binding in RNA target | ||||
Sequence: SNVVE | ||||||
Repeat | 980-1022 | Pumilio 8 | ||||
Sequence: EVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMH | ||||||
Region | 1002-1006 | Uracil-nucleotide binding in RNA target | ||||
Sequence: NYVVQ |
Domain
The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. RNA-binding occurs on the concave side of the surface (PubMed:19540345).
PUM2 is composed of 8 pumilio repeats of 36 residues; each repeat binds a single nucleotide in its RNA target. Residues at positions 12 and 16 of the pumilio repeat bind each RNA base via hydrogen bonding or van der Waals contacts with the Watson-Crick edge, while the amino acid at position 13 makes a stacking interaction. The recognition of RNA by pumilio repeats is base specific: cysteine and glutamine at position 12 and 16, respectively, bind adenine; asparagine and glutamine bind uracil; and serine and glutamate bind guanine (By similarity).
PUM2 is composed of 8 pumilio repeats of 36 residues; each repeat binds a single nucleotide in its RNA target. Residues at positions 12 and 16 of the pumilio repeat bind each RNA base via hydrogen bonding or van der Waals contacts with the Watson-Crick edge, while the amino acid at position 13 makes a stacking interaction. The recognition of RNA by pumilio repeats is base specific: cysteine and glutamine at position 12 and 16, respectively, bind adenine; asparagine and glutamine bind uracil; and serine and glutamate bind guanine (By similarity).
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q80U58-1
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
- Length1,066
- Mass (Da)114,314
- Last updated2004-02-02 v2
- Checksum027AC00FA91B055E
Q80U58-2
- Name2
Q80U58-3
- Name3
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_009321 | 1-56 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 106-156 | Basic and acidic residues | ||||
Sequence: KLDSRFRKGTFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQDDEDSKIN | ||||||
Compositional bias | 368-385 | Polar residues | ||||
Sequence: TANQQAASQAQPGQQQVL | ||||||
Compositional bias | 393-408 | Polar residues | ||||
Sequence: PITPSQGQQGQQAESL | ||||||
Sequence conflict | 461 | in Ref. 3; BAC65507 | ||||
Sequence: M → I | ||||||
Sequence conflict | 547 | in Ref. 2; AAG31805 | ||||
Sequence: G → A | ||||||
Sequence conflict | 553 | in Ref. 2; AAG31805 | ||||
Sequence: F → C | ||||||
Sequence conflict | 559-560 | in Ref. 2; AAG31805 | ||||
Sequence: LG → VR | ||||||
Sequence conflict | 570 | in Ref. 2; AAG31805 | ||||
Sequence: F → C | ||||||
Alternative sequence | VSP_009322 | 574-652 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 592 | in Ref. 2; AAG31805 | ||||
Sequence: S → A | ||||||
Sequence conflict | 628 | in Ref. 2; AAG31805 | ||||
Sequence: S → G | ||||||
Alternative sequence | VSP_009323 | 829-830 | in isoform 2 and isoform 3 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY027917 EMBL· GenBank· DDBJ | AAK21966.1 EMBL· GenBank· DDBJ | mRNA | ||
AF315590 EMBL· GenBank· DDBJ | AAG31805.1 EMBL· GenBank· DDBJ | mRNA | ||
AK122225 EMBL· GenBank· DDBJ | BAC65507.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC013765 EMBL· GenBank· DDBJ | AAH13765.1 EMBL· GenBank· DDBJ | mRNA | ||
BC041773 EMBL· GenBank· DDBJ | AAH41773.1 EMBL· GenBank· DDBJ | mRNA |