Q9QX96 · SALL2_MOUSE
- ProteinSal-like protein 2
- GeneSall2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1004 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Probable transcription factor that plays a role in eye development before, during, and after optic fissure closure.
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 | nucleus | |
Molecular Function | DNA-binding transcription factor activity, RNA polymerase II-specific | |
Molecular Function | metal ion binding | |
Molecular Function | protein-containing complex binding | |
Molecular Function | RNA polymerase II cis-regulatory region sequence-specific DNA binding | |
Biological Process | eye development | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | neural tube development | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameSal-like protein 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 accessionQ9QX96
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
No overt phenotypic abnormalities. Histologic analysis of the eyes reveales a colobomatous phenotype, with delayed apposition of the optic fissure margins and persistence of an anterior retinal coloboma phenotype after birth. Deficient embryos display correct posterior closure toward the optic nerve head, and upon contact of the fissure margins, dissolution of the basal lamina occurs and PAX2, known to be critical for this process, is expressed normally. Anterior closure is disrupted with the fissure margins failing to meet, or in some cases misaligning leading to a retinal lesion.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 66 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000047023 | 1-1004 | Sal-like protein 2 | |||
Sequence: MSRRKQRRPQQLISDCEGPSASENGDASEEDHPQVCAKCCAQFSDPTEFLAHQNSCCTDPPVMVIIGGQENPSNSSASSAPRPEGHSRSQVMDTEHSNPPDSGSSGAPDPTWGPERRGEESSGQFLVAATGTAAGGGGGLILASPKLGATPLPPESTPAPPPPPPPPPPPGVGSGHLNIPLILEELRVLQQRQIHQMQMTEQICRQVLLLGSLGQTVGAPASPSELPGTGAASSTKPLLPLFSPIKPAQTGKTLASSSSSSSSSGAEPPKQAFFHLYHPLGSQHPFSVGGVGRSHKPTPAPSPALPGSTDQLIASPHLAFPGTTGLLAAQCLGAARGLEAAASPGLLKPKNGSGELGYGEVISSLEKPGGRHKCRFCAKVFGSDSALQIHLRSHTGERPYKCNVCGNRFTTRGNLKVHFHRHREKYPHVQMNPHPVPEHLDYVITSSGLPYGMSVPPEKAEEEAGTPGGGVERKPLVASTTALSATESLTLLSTGTSTAVAPGLPTFNKFVLMKAVEPKSKADENTPPGSEGSAIAGVADSGSATRMQLSKLVTSLPSWALLTNHLKSTGSFPFPYVLEPLGASPSETSKLQQLVEKIDRQGAVAVASTASGAPTTSAPAPSSSASGPNQCVICLRVLSCPRALRLHYGQHGGERPFKCKVCGRAFSTRGNLRAHFVGHKTSPAARAQNSCPICQKKFTNAVTLQQHVRMHLGGQIPNGGSALSEGGGAAQENSSEQSTASGPGSFPQPQSQQPSPEEEMSEEEEEDEEEEEDVTDEDSLAGRGSESGGEKAISVRGDSEEVSGAEEEVATSVAAPTTVKEMDSNEKAPQHTLPPPPPPPDNLDHPQPMEQGTSDVSGAMEEEAKLEGTSSPMAALTQEGEGTSTPLVEELNLPEAMKKDPGESSGRKACEVCGQSFPTQTALEEHQKTHPKDGPLFTCVFCRQGFLDRATLKKHMLLAHHQVPPFAPHGPQNIATLSLVPGCSSSIPSPGLSPFPRKDDPTMP | ||||||
Modified residue | 243 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 794 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 799 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 803 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 908 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed throughout embryonic development. In adult predominantly in brain.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, zinc finger, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-33 | Disordered | ||||
Sequence: MSRRKQRRPQQLISDCEGPSASENGDASEEDHP | ||||||
Zinc finger | 34-56 | C2H2-type 1; atypical | ||||
Sequence: QVCAKCCAQFSDPTEFLAHQNSC | ||||||
Region | 51-122 | Disordered | ||||
Sequence: AHQNSCCTDPPVMVIIGGQENPSNSSASSAPRPEGHSRSQVMDTEHSNPPDSGSSGAPDPTWGPERRGEESS | ||||||
Compositional bias | 68-85 | Polar residues | ||||
Sequence: GQENPSNSSASSAPRPEG | ||||||
Region | 137-177 | Disordered | ||||
Sequence: GGGLILASPKLGATPLPPESTPAPPPPPPPPPPPGVGSGHL | ||||||
Compositional bias | 151-174 | Pro residues | ||||
Sequence: PLPPESTPAPPPPPPPPPPPGVGS | ||||||
Region | 220-270 | Disordered | ||||
Sequence: PASPSELPGTGAASSTKPLLPLFSPIKPAQTGKTLASSSSSSSSSGAEPPK | ||||||
Compositional bias | 249-268 | Polar residues | ||||
Sequence: QTGKTLASSSSSSSSSGAEP | ||||||
Region | 285-307 | Disordered | ||||
Sequence: PFSVGGVGRSHKPTPAPSPALPG | ||||||
Zinc finger | 372-394 | C2H2-type 2 | ||||
Sequence: HKCRFCAKVFGSDSALQIHLRSH | ||||||
Zinc finger | 400-422 | C2H2-type 3 | ||||
Sequence: YKCNVCGNRFTTRGNLKVHFHRH | ||||||
Zinc finger | 629-651 | C2H2-type 4 | ||||
Sequence: NQCVICLRVLSCPRALRLHYGQH | ||||||
Zinc finger | 657-679 | C2H2-type 5 | ||||
Sequence: FKCKVCGRAFSTRGNLRAHFVGH | ||||||
Zinc finger | 689-711 | C2H2-type 6 | ||||
Sequence: NSCPICQKKFTNAVTLQQHVRMH | ||||||
Region | 712-910 | Disordered | ||||
Sequence: LGGQIPNGGSALSEGGGAAQENSSEQSTASGPGSFPQPQSQQPSPEEEMSEEEEEDEEEEEDVTDEDSLAGRGSESGGEKAISVRGDSEEVSGAEEEVATSVAAPTTVKEMDSNEKAPQHTLPPPPPPPDNLDHPQPMEQGTSDVSGAMEEEAKLEGTSSPMAALTQEGEGTSTPLVEELNLPEAMKKDPGESSGRKAC | ||||||
Compositional bias | 727-756 | Polar residues | ||||
Sequence: GGAAQENSSEQSTASGPGSFPQPQSQQPSP | ||||||
Compositional bias | 757-777 | Acidic residues | ||||
Sequence: EEEMSEEEEEDEEEEEDVTDE | ||||||
Compositional bias | 830-845 | Pro residues | ||||
Sequence: QHTLPPPPPPPDNLDH | ||||||
Compositional bias | 871-885 | Polar residues | ||||
Sequence: SPMAALTQEGEGTST | ||||||
Zinc finger | 908-930 | C2H2-type 7 | ||||
Sequence: KACEVCGQSFPTQTALEEHQKTH | ||||||
Zinc finger | 937-961 | C2H2-type 8 | ||||
Sequence: FTCVFCRQGFLDRATLKKHMLLAHH |
Sequence similarities
Belongs to the sal C2H2-type zinc-finger protein family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,004
- Mass (Da)104,944
- Last updated2011-07-27 v2
- ChecksumAEEBBDEE04DDE5FF
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2I3BQV4 | A0A2I3BQV4_MOUSE | Sall2 | 1002 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 8 | in Ref. 1; CAB65274 | ||||
Sequence: R → K | ||||||
Sequence conflict | 31 | in Ref. 1; CAB65274 | ||||
Sequence: D → H | ||||||
Compositional bias | 68-85 | Polar residues | ||||
Sequence: GQENPSNSSASSAPRPEG | ||||||
Sequence conflict | 107 | in Ref. 1; CAB65274 | ||||
Sequence: A → P | ||||||
Compositional bias | 151-174 | Pro residues | ||||
Sequence: PLPPESTPAPPPPPPPPPPPGVGS | ||||||
Sequence conflict | 225 | in Ref. 1; CAB65274 | ||||
Sequence: E → K | ||||||
Compositional bias | 249-268 | Polar residues | ||||
Sequence: QTGKTLASSSSSSSSSGAEP | ||||||
Compositional bias | 727-756 | Polar residues | ||||
Sequence: GGAAQENSSEQSTASGPGSFPQPQSQQPSP | ||||||
Compositional bias | 757-777 | Acidic residues | ||||
Sequence: EEEMSEEEEEDEEEEEDVTDE | ||||||
Compositional bias | 830-845 | Pro residues | ||||
Sequence: QHTLPPPPPPPDNLDH | ||||||
Sequence conflict | 869 | in Ref. 1; CAB65274 | ||||
Sequence: T → I | ||||||
Compositional bias | 871-885 | Polar residues | ||||
Sequence: SPMAALTQEGEGTST |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ007396 EMBL· GenBank· DDBJ | CAB65274.1 EMBL· GenBank· DDBJ | mRNA | ||
BC085361 EMBL· GenBank· DDBJ | AAH85361.1 EMBL· GenBank· DDBJ | mRNA |