Reviewed,
UniProtKB/Swiss-Prot Q5FVM4 (NONO_RAT)
Last modified
January 19, 2010.
Version 48.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Non-POU domain-containing octamer-binding protein Short name=NonO protein | ||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 476 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | DNA- and RNA binding protein, involved in several nuclear processes. Binds the conventional octamer sequence in double stranded DNA. Also binds single-stranded DNA and RNA at a site independent of the duplex site. Involved in pre-mRNA splicing, probably as an heterodimer with SFPQ. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1. The SFPQ-NONO heteromer may be involved in DNA nonhomologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends. In vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. Nono is involved in transcriptional regulation. The SFPQ-NONO-NR5A1/SF-1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription By similarity. |
| Subunit structure | Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits. NONO is a component of spliceosome and U5.4/6 snRNP complexes. Interacts with PSPC1 and SNRPA/U1A. Part of complex consisting of SFPQ, NONO and MATR3. Part of a complex consisting of SFPQ, NONO and NR5A1/SF-1. Part of a complex consisting of SFPQ, NONO and TOP1. Interacts with SPI1 By similarity. Interacts with RNF43 By similarity. |
| Subcellular location | Nucleus By similarity. |
| Sequence similarities | Contains 2 RRM (RNA recognition motif) domains. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 476 | 476 | Non-POU domain-containing octamer-binding protein | PRO_0000081686 | |||||
Regions | |||||||||
| Domain | 80 – 147 | 68 | RRM 1 | ||||||
| Domain | 154 – 235 | 82 | RRM 2 | ||||||
| Region | 60 – 379 | 320 | DBHS By similarity | ||||||
| Coiled coil | 274 – 378 | 105 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 5 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 11 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 101 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 152 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 203 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 433 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 455 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 472 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Spleen. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC089880 mRNA. Translation: AAH89880.1. |
| IPI | IPI00205912. |
| RefSeq | NP_001012356.1. |
| UniGene | Rn.8381 |
3D structure databases | |
| SMR | Q5FVM4. Positions 72-156, 77-211. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q5FVM4. |
PTM databases | |
| PhosphoSite | Q5FVM4. |
Proteomic databases | |
| PRIDE | Q5FVM4. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000004911; ENSRNOP00000004911; ENSRNOG00000003689; Rattus norvegicus. [Genome view] |
| GeneID | 317259. |
| KEGG | rno:317259. |
| UCSC | NM_001012356. rat. |
Organism-specific databases | |
| CTD | 317259. |
| RGD | 1549738. Nono. |
Phylogenomic databases | |
| eggNOG | roNOG12392. |
| HOVERGEN | Q5FVM4. |
| InParanoid | Q5FVM4. |
| OMA | KQNHAPR. |
| OrthoDB | EOG941SXM. |
Gene expression databases | |
| ArrayExpress | Q5FVM4. |
| Genevestigator | Q5FVM4. |
| GermOnline | ENSRNOG00000003689. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR012677. a_b_plait_nuc_bd. IPR012975. NOPS. IPR000504. RRM_RNP1. [Graphical view] |
| Gene3D | G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits. |
| Pfam | PF08075. NOPS. 1 hit. PF00076. RRM_1. 2 hits. [Graphical view] |
| SMART | SM00360. RRM. 2 hits. [Graphical view] |
| PROSITE | PS50102. RRM. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 671515. |
Entry information
| Entry name | NONO_RAT | ||||||||
| Accession | Primary (citable) accession number: Q5FVM4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


