O55112 · AFF2_MOUSE
- ProteinAF4/FMR2 family member 2
- GeneAff2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1272 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
RNA-binding protein. Might be involved in alternative splicing regulation through an interaction with G-quartet RNA structure.
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 | nuclear speck | |
Cellular Component | nucleus | |
Molecular Function | G-quadruplex RNA binding | |
Biological Process | learning or memory | |
Biological Process | mRNA processing | |
Biological Process | negative regulation of gene expression | |
Biological Process | nuclear speck organization | |
Biological Process | regulation of gene expression | |
Biological Process | regulation of RNA splicing | |
Biological Process | RNA splicing |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameAF4/FMR2 family member 2
- Alternative names
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 accessionO55112
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: When splicing or transcription are inhibited, accumulates in large, rounded speckles and in the nucleolus.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000215913 | 1-1272 | AF4/FMR2 family member 2 | |||
Sequence: MDLFDFFRDWDLEQQCHYEQDRSALKKREWERRNQEVQQEEDLFSSGFDLFGEPYKVAEYTNKGDALANRVQNTLGSYDEMKDLLSNHSSQNHLVGIPKNSAPQTPISKSEASFYPEQKNRMIPSHQETTHSSTPMPPPSVVILNSTLIHSNRKSKSEWPRDSHNTSPAQASQTSSQPNKMQTSTQDPPQTRLEDFFVYPAEQPQIGTVEKSNPSSKEENNPNSGGEDTFKEIFQSNSPEESEFTVQAPGSPLVASSLLAPSSGLSVPTFPPGLYCKTSMGQQKPTAYVRPMDGQDQATDISPTLKPSIEFENSFGNLSFGSLLDGKPSAVSSKTKLPKFTILQTSEVSLTSDPSCVEEILRESQHLTPGFTLQKWSDPSSRASTKMLEDDLKLSSDEDDLEPVKTLTTQCTANELYQAVEKAKPKNNPVNPLLATPQSTPATQTNVGSGSSSESESSSESDSDTESSTTDSESNEAPRVATPEPEPPSTNKWQLDKWLNKVTSQNKSFICGQNETPTETISLPPPIIQPVEVQVKVKPNPSQAVAVPKERPLLSLIREKARPRPTQKTPETKALKHKLSTSVDTVSQRTIGKKQPKKVEKNTSFEEFTWPKPNITNSTPKEKGSVELPDPPRSRNKATAHKPVPRKEPRPHVPLATEKKKYRGPGKIVPKSREFIETDSSTSDSNTDQEETLQIKVLPPCITSKSKETSNASLTLSTLTNGNSNNLSTSNEETAFSPPPAMQTELLSPLRDHENPKNLWVKIDLDLLSRVPGQNSVPVTPAKTDYKETASKPKRQTAATAVEKPAPKGKRKHKPAETAEKIPEKKQRLEDNTTICLLPPCISPAPPHKPPSTRENSSRRANRKKEEKLFPPALSPLAEDPPRRRNVSGNNGHFGQDKNISMAGQITSSKPKRSEGKFCATFKGISINEGDAPKKAASATVTVANMALATATATATVPAIVTATVTATATTTATATTTTTTTTISSITPTITSGLMDSSHLEMTSWAALPLLSSSSANVRRPKLTFDDSVHNADFYMQEAKKLKHKADALFEKFGKAVNYADAALSFTECGNAMERDPLEAKSPYTMYSETVELLRYAMRLKNFASPLASDGDKKLAVLCYRCLSLLYLRMFKLKKDHAMKYSRSLMEYFKQNASKVTQIPSPWVGNGKNTPSPVSLNNVSPINSVGNCNNGPVTIPQRIHHMAASHVNITSNVLRGYEHWDMADKLTRDNKEFFGDLDTLMGPLTQHSSMTNLVRYVRQGLCWLRIDAHLL | ||||||
Modified residue | 395 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 482 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in the hippocampus, the piriform cortex, Purkinje cells and the cingulate gyrus.
Developmental stage
Expressed before day 7 in the embryo and reached its highest levels at 10.5-11.5 days. In the embryo at day 11, expression is more specific in the roof of the hind brain and the lateral ventricle of the brain.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 151-190 | Disordered | ||||
Sequence: SNRKSKSEWPRDSHNTSPAQASQTSSQPNKMQTSTQDPPQ | ||||||
Compositional bias | 162-190 | Polar residues | ||||
Sequence: DSHNTSPAQASQTSSQPNKMQTSTQDPPQ | ||||||
Region | 204-231 | Disordered | ||||
Sequence: PQIGTVEKSNPSSKEENNPNSGGEDTFK | ||||||
Compositional bias | 206-231 | Polar residues | ||||
Sequence: IGTVEKSNPSSKEENNPNSGGEDTFK | ||||||
Region | 372-401 | Disordered | ||||
Sequence: TLQKWSDPSSRASTKMLEDDLKLSSDEDDL | ||||||
Compositional bias | 384-401 | Basic and acidic residues | ||||
Sequence: STKMLEDDLKLSSDEDDL | ||||||
Region | 422-497 | Disordered | ||||
Sequence: KAKPKNNPVNPLLATPQSTPATQTNVGSGSSSESESSSESDSDTESSTTDSESNEAPRVATPEPEPPSTNKWQLDK | ||||||
Compositional bias | 431-477 | Polar residues | ||||
Sequence: NPLLATPQSTPATQTNVGSGSSSESESSSESDSDTESSTTDSESNEA | ||||||
Compositional bias | 557-578 | Basic and acidic residues | ||||
Sequence: IREKARPRPTQKTPETKALKHK | ||||||
Region | 557-694 | Disordered | ||||
Sequence: IREKARPRPTQKTPETKALKHKLSTSVDTVSQRTIGKKQPKKVEKNTSFEEFTWPKPNITNSTPKEKGSVELPDPPRSRNKATAHKPVPRKEPRPHVPLATEKKKYRGPGKIVPKSREFIETDSSTSDSNTDQEETLQ | ||||||
Compositional bias | 591-605 | Basic and acidic residues | ||||
Sequence: IGKKQPKKVEKNTSF | ||||||
Compositional bias | 607-623 | Polar residues | ||||
Sequence: EFTWPKPNITNSTPKEK | ||||||
Compositional bias | 626-678 | Basic and acidic residues | ||||
Sequence: VELPDPPRSRNKATAHKPVPRKEPRPHVPLATEKKKYRGPGKIVPKSREFIET | ||||||
Compositional bias | 679-693 | Polar residues | ||||
Sequence: DSSTSDSNTDQEETL | ||||||
Compositional bias | 715-738 | Polar residues | ||||
Sequence: TLSTLTNGNSNNLSTSNEETAFSP | ||||||
Region | 715-743 | Disordered | ||||
Sequence: TLSTLTNGNSNNLSTSNEETAFSPPPAMQ | ||||||
Region | 772-899 | Disordered | ||||
Sequence: PGQNSVPVTPAKTDYKETASKPKRQTAATAVEKPAPKGKRKHKPAETAEKIPEKKQRLEDNTTICLLPPCISPAPPHKPPSTRENSSRRANRKKEEKLFPPALSPLAEDPPRRRNVSGNNGHFGQDKN | ||||||
Compositional bias | 810-831 | Basic and acidic residues | ||||
Sequence: KRKHKPAETAEKIPEKKQRLED | ||||||
Compositional bias | 853-870 | Basic and acidic residues | ||||
Sequence: TRENSSRRANRKKEEKLF |
Sequence similarities
Belongs to the AF4 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,272
- Mass (Da)140,181
- Last updated2010-02-09 v2
- Checksum1CE41F1AEFE9C2B4
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 162-190 | Polar residues | ||||
Sequence: DSHNTSPAQASQTSSQPNKMQTSTQDPPQ | ||||||
Compositional bias | 206-231 | Polar residues | ||||
Sequence: IGTVEKSNPSSKEENNPNSGGEDTFK | ||||||
Compositional bias | 384-401 | Basic and acidic residues | ||||
Sequence: STKMLEDDLKLSSDEDDL | ||||||
Compositional bias | 431-477 | Polar residues | ||||
Sequence: NPLLATPQSTPATQTNVGSGSSSESESSSESDSDTESSTTDSESNEA | ||||||
Sequence conflict | 432 | in Ref. 1; CAA04821 | ||||
Sequence: P → S | ||||||
Sequence conflict | 544 | in Ref. 1; CAA04821 | ||||
Sequence: A → S | ||||||
Compositional bias | 557-578 | Basic and acidic residues | ||||
Sequence: IREKARPRPTQKTPETKALKHK | ||||||
Compositional bias | 591-605 | Basic and acidic residues | ||||
Sequence: IGKKQPKKVEKNTSF | ||||||
Compositional bias | 607-623 | Polar residues | ||||
Sequence: EFTWPKPNITNSTPKEK | ||||||
Compositional bias | 626-678 | Basic and acidic residues | ||||
Sequence: VELPDPPRSRNKATAHKPVPRKEPRPHVPLATEKKKYRGPGKIVPKSREFIET | ||||||
Compositional bias | 679-693 | Polar residues | ||||
Sequence: DSSTSDSNTDQEETL | ||||||
Compositional bias | 715-738 | Polar residues | ||||
Sequence: TLSTLTNGNSNNLSTSNEETAFSP | ||||||
Compositional bias | 810-831 | Basic and acidic residues | ||||
Sequence: KRKHKPAETAEKIPEKKQRLED | ||||||
Compositional bias | 853-870 | Basic and acidic residues | ||||
Sequence: TRENSSRRANRKKEEKLF | ||||||
Sequence conflict | 941 | in Ref. 1; CAA04821 | ||||
Sequence: V → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ001549 EMBL· GenBank· DDBJ | CAA04821.1 EMBL· GenBank· DDBJ | mRNA | ||
AL663113 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL672120 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL808131 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BX294655 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |