Gene Symbol | SPOCK2 |
Entrez ID | 9806 |
Uniprot ID | Q92563 |
Description | sparc/osteonectin, cwcv and kazal-like domains proteoglycan (testican) 2 |
Chromosomal Location | chr10: 72,059,035-72,089,032 |
Ontology | GO ID | GO Term | Definition | Evidence |
---|---|---|---|---|
BP |
GO:0007165 |
signal transduction |
The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. |
IEA |
BP |
GO:0007416 |
synapse assembly |
The aggregation, arrangement and bonding together of a set of components to form a synapse. |
NAS |
BP |
GO:0010811 |
positive regulation of cell-substrate adhesion |
Any process that increases the frequency, rate or extent of cell-substrate adhesion. Cell-substrate adhesion is the attachment of a cell to the underlying substrate via adhesion molecules. |
IEA |
BP |
GO:0010951 |
negative regulation of endopeptidase activity |
Any process that decreases the frequency, rate or extent of endopeptidase activity, the endohydrolysis of peptide bonds within proteins. |
TAS |
BP |
GO:0019800 |
peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan |
The formation of a cross-link between peptide chains mediated by a chondroitin 4-sulfate glycosaminoglycan that originates from a typical O-glycosidic link to serine of one chain; the other chain is esterified, via the alpha-carbon of its C-terminal Asp, to C-6 of an internal N-acetylgalactosamine of the glycosaminoglycan chain. |
IEA |
BP |
GO:0030198 |
extracellular matrix organization |
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix. |
NAS |
BP |
GO:0045595 |
regulation of cell differentiation |
Any process that modulates the frequency, rate or extent of cell differentiation, the process in which relatively unspecialized cells acquire specialized structural and functional features. |
NAS |
BP |
GO:2000147 |
positive regulation of cell motility |
Any process that activates or increases the frequency, rate or extent of cell motility. |
TAS |
CC |
GO:0005578 |
proteinaceous extracellular matrix |
A layer consisting mainly of proteins (especially collagen) and glycosaminoglycans (mostly as proteoglycans) that forms a sheet underlying or overlying cells such as endothelial and epithelial cells. The proteins are secreted by cells in the vicinity. An example of this component is found in Mus musculus. |
NAS |
MF |
GO:0005509 |
calcium ion binding |
Interacting selectively and non-covalently with calcium ions (Ca2+). |
IDA |
MF |
GO:0005539 |
glycosaminoglycan binding |
Interacting selectively and non-covalently with any glycan (polysaccharide) containing a substantial proportion of aminomonosaccharide residues. |
IEA |
MF |
GO:0008191 |
metalloendopeptidase inhibitor activity |
Stops, prevents or reduces the activity of metalloendopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain and contain a chelated metal ion at their active sites which is essential to their catalytic activity. |
TAS |
MF |
GO:0050840 |
extracellular matrix binding |
Interacting selectively and non-covalently with a component of the extracellular matrix. |
IEA |
Domain ID | Description |
---|---|
IPR000716 |
Thyroglobulin type-1 |
IPR002350 |
Kazal domain |
IPR011992 |
EF-hand domain pair |
IPR019577 |
SPARC/Testican, calcium-binding domain |
Tissue | Cell Type |
---|---|
caudate |
neuronal cells |
cerebellum |
cells in granular layer |
cerebellum |
cells in molecular layer |
cerebellum |
Purkinje cells |
Pubmed ID | Author | Year | Title |
---|---|---|---|
22617121 |
Ouandaogo et al. |
2012 |
Differences in transcriptomic profiles of human cumulus cells isolated from oocytes at GV, MI and MII stages after in vivo andin vitro oocyte maturation |
Gene Symbol | Entrez ID | Uniprot ID | Score |
---|---|---|---|
TES |
26136 |
Q9UGI8 |
0.52 |
PLXNB3 |
5365 |
Q9ULL4 |
0.63 |
SPOCK3 |
50859 |
Q9BQ16 |
0.73 |