Q3UH99 · SHSA6_MOUSE
- ProteinProtein shisa-6
- GeneShisa6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids525 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May play a role in self-renewal and differentiation of spermatogonial stem cells by inhibiting canonical Wnt signaling pathway (PubMed:28196692).
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 | AMPA glutamate receptor complex | |
Cellular Component | asymmetric, glutamatergic, excitatory synapse | |
Cellular Component | dendritic spine membrane | |
Cellular Component | glutamatergic synapse | |
Cellular Component | postsynaptic density | |
Cellular Component | postsynaptic density membrane | |
Cellular Component | postsynaptic membrane | |
Molecular Function | ionotropic glutamate receptor binding | |
Molecular Function | PDZ domain binding | |
Biological Process | excitatory chemical synaptic transmission | |
Biological Process | negative regulation of canonical Wnt signaling pathway | |
Biological Process | postsynaptic neurotransmitter receptor diffusion trapping | |
Biological Process | regulation of AMPA glutamate receptor clustering | |
Biological Process | regulation of short-term neuronal synaptic plasticity | |
Biological Process | spermatogenesis | |
Biological Process | Wnt signaling pathway |
Keywords
- Biological process
Increases excitatory synaptic currents in a brain reward circuitry relevant to depression (D1-neurons in the nucleus accumbens).
Names & Taxonomy
Protein names
- Recommended nameProtein shisa-6
- Alternative names
Gene names
- Community suggested namesSHISA6
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ3UH99
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 31-180 | Extracellular | ||||
Sequence: ARGRSGNRTLNAGAVGGRRAGGALARGGRELNSTARASGVPEAGSRRGQSAAAAAAAAAAASATVTYETCWGYYDVSGQYDKEFECNNSESGYLYCCGTCYYRFCCKKRHEKLDQRQCTNYQSPVWVQTPSTKVVSPGPENKYDPEKDKT | ||||||
Transmembrane | 181-201 | Helical | ||||
Sequence: NFTVYITCGVIAFVIVAGVFA | ||||||
Topological domain | 202-525 | Cytoplasmic | ||||
Sequence: KVSYDKAHRPPREMNIHRALADILRQQGPIPIAHCERETISAIDTSPKENTPVRSTSKNHYTPVRTAKQTPGDRQYNHPILSSATQTPTHEKPRMNNILTSATEPYDLSFSRSYQNLAHLPPSYESAVKTNPSKYSSLKRLTDKEADEYYMRRRHLPDLAARGTLPLNVIQMSQQKPLPRERPRRPIRAMSQDRVLSPRRGLPDEFGMPYDRILSDEQLLSTERLHSQDPLLSPERTAFPEQSLSRAISHTDVFVSTPVLDRYRMTKMHSHPSASNNSYATLGQSQTAAKRHAFASRRHNTVEQLHYIPGHHTCYTASKTEVTV |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 522-525 | Loss of interaction with PDZ-domain of DLG4. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 18 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-30 | |||||
Sequence: MALRRLLLPPLLLSLLLSLASLHLPPGADA | ||||||
Chain | PRO_0000326155 | 31-525 | Protein shisa-6 | |||
Sequence: ARGRSGNRTLNAGAVGGRRAGGALARGGRELNSTARASGVPEAGSRRGQSAAAAAAAAAAASATVTYETCWGYYDVSGQYDKEFECNNSESGYLYCCGTCYYRFCCKKRHEKLDQRQCTNYQSPVWVQTPSTKVVSPGPENKYDPEKDKTNFTVYITCGVIAFVIVAGVFAKVSYDKAHRPPREMNIHRALADILRQQGPIPIAHCERETISAIDTSPKENTPVRSTSKNHYTPVRTAKQTPGDRQYNHPILSSATQTPTHEKPRMNNILTSATEPYDLSFSRSYQNLAHLPPSYESAVKTNPSKYSSLKRLTDKEADEYYMRRRHLPDLAARGTLPLNVIQMSQQKPLPRERPRRPIRAMSQDRVLSPRRGLPDEFGMPYDRILSDEQLLSTERLHSQDPLLSPERTAFPEQSLSRAISHTDVFVSTPVLDRYRMTKMHSHPSASNNSYATLGQSQTAAKRHAFASRRHNTVEQLHYIPGHHTCYTASKTEVTV | ||||||
Glycosylation | 37 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 62 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 416 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 422 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 434 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 458 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 502 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in other brain structures including olfactory bulb, cortex, amygdala and midbrain (at protein level) (PubMed:26623514, PubMed:26931375).
Also expressed in a subset of spermatogonial stem cells (PubMed:28196692).
Also expressed in eye, heart, kidney, lung, muscle and spleen. Isoform 2: Specifically expressed in hippocampus (PubMed:26931375).
Developmental stage
Gene expression databases
Interaction
Subunit
Interacts (via PDZ-binding motif) with DLG4/PSD-95 (via PDZ domain); the interaction is direct (PubMed:26931375).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 241-294 | Disordered | ||||
Sequence: ISAIDTSPKENTPVRSTSKNHYTPVRTAKQTPGDRQYNHPILSSATQTPTHEKP | ||||||
Compositional bias | 245-294 | Polar residues | ||||
Sequence: DTSPKENTPVRSTSKNHYTPVRTAKQTPGDRQYNHPILSSATQTPTHEKP | ||||||
Region | 469-495 | Disordered | ||||
Sequence: MHSHPSASNNSYATLGQSQTAAKRHAF | ||||||
Compositional bias | 470-492 | Polar residues | ||||
Sequence: HSHPSASNNSYATLGQSQTAAKR | ||||||
Motif | 522-525 | PDZ-binding | ||||
Sequence: EVTV |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q3UH99-1
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
- Length525
- Mass (Da)58,426
- Last updated2005-10-11 v1
- Checksum1F9706B52F0F3C47
Q3UH99-2
- Name2
- Differences from canonical
- 272-272: P → PGHYGKDAYRSGGPDLHNFISSGFVTLGRGHTK
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F6VQZ6 | F6VQZ6_MOUSE | Shisa6 | 501 |
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 245-294 | Polar residues | ||||
Sequence: DTSPKENTPVRSTSKNHYTPVRTAKQTPGDRQYNHPILSSATQTPTHEKP | ||||||
Alternative sequence | VSP_059384 | 272 | in isoform 2 | |||
Sequence: P → PGHYGKDAYRSGGPDLHNFISSGFVTLGRGHTK | ||||||
Compositional bias | 470-492 | Polar residues | ||||
Sequence: HSHPSASNNSYATLGQSQTAAKR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KU707904 EMBL· GenBank· DDBJ | AND76927.1 EMBL· GenBank· DDBJ | mRNA | ||
AK147504 EMBL· GenBank· DDBJ | BAE27958.1 EMBL· GenBank· DDBJ | mRNA |