UniProt ID | CBLN1_MOUSE | |
---|---|---|
UniProt AC | Q9R171 | |
Protein Name | Cerebellin-1 | |
Gene Name | Cbln1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 193 | |
Subcellular Localization | Secreted. Cell junction, synapse, postsynaptic cell membrane. Interaction with CBLN3 may cause partial retention in the endoplasmic reticulum. | |
Protein Description | Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the matching and maintenance of pre- and post-synaptic elements at parallel fiber-Purkinje cell synapses, the establishment of the proper pattern of climbing fiber-Purkinje cell innervation, and induction of long-term depression at parallel fiber-Purkinje cell synapses. [PubMed: 16234806 Plays a role as a synaptic organizer that acts bidirectionally on both pre- and post-synaptic components] | |
Protein Sequence | MLGVVELLLLGTAWLAGPARGQNETEPIVLEGKCLVVCDSNPTSDPTGTALGISVRSGSAKVAFSAIRSTNHEPSEMSNRTMIIYFDQVLVNIGNNFDSERSTFIAPRKGIYSFNFHVVKVYNRQTIQVSLMLNGWPVISAFAGDQDVTREAASNGVLIQMEKGDRAYLKLERGNLMGGWKYSTFSGFLVFPL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
23 | N-linked_Glycosylation | AGPARGQNETEPIVL HCCCCCCCCCCCEEE | 62.07 | 29782851 | |
79 | N-linked_Glycosylation | HEPSEMSNRTMIIYF CCCCCCCCCEEEEEE | 41.97 | 29782851 | |
182 | Phosphorylation | NLMGGWKYSTFSGFL CCCCCEEEECCCEEE | 13.36 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of CBLN1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CBLN1_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CBLN1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of CBLN1_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Cbln1 is essential for synaptic integrity and plasticity in thecerebellum."; Hirai H., Pang Z., Bao D., Miyazaki T., Li L., Miura E., Parris J.,Rong Y., Watanabe M., Yuzaki M., Morgan J.I.; Nat. Neurosci. 8:1534-1541(2005). Cited for: FUNCTION, MUTAGENESIS OF ASN-23 AND ASN-79, AND GLYCOSYLATION ATASN-23 AND ASN-79. |