UniProt ID | HOME1_RAT | |
---|---|---|
UniProt AC | Q9Z214 | |
Protein Name | Homer protein homolog 1 {ECO:0000305} | |
Gene Name | Homer1 {ECO:0000312|RGD:628725} | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 366 | |
Subcellular Localization | Cytoplasm. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cell junction, synapse . Cell projection, dendritic spine . Isoform 1 inhibits surface expression of GRM5 causing it to be retained in the endoplasmic reticulum.. | |
Protein Description | Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Differentially regulates the functions of the calcium activated channel ryanodine receptors RYR1 and RYR2. Isoform 1 decreases the activity of RYR2, and increases the activity of RYR1, whereas isoform 3 counteracts the effects by competing for binding sites. Isoform 1 regulates the trafficking and surface expression of GRM5. Isoform 3 acts as a natural dominant negative, in dynamic competition with constitutively expressed isoform 1, and isoform 2 to regulate synaptic metabotropic glutamate function. Isoform 3, may be involved in the structural changes that occur at synapses during long-lasting neuronal plasticity and development. Forms a high-order complex with SHANK1, which in turn is necessary for the structural and functional integrity of dendritic spines. [PubMed: 19345194] | |
Protein Sequence | MGEQPIFSTRAHVFQIDPNTKKNWVPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMTFTKTSQKFGQWADSRANTVYGLGFSSEHHLSKFAEKFQEFKEAARLAKEKSQEKMELTSTPSQESAGGDLQSPLTPESINGTDDERTPDVTQNSEPRAEPAQNALPFSHSAGDRTQGLSHASSAISKHWEAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELECVSSQANAVHSHKTELSQTVQELEETLKVKEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSELEQRLEKSQSEQDAFRSNLKTLLEILDGKIFELTELRDNLAKLLECS | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MGEQPIFST ------CCCCCCEEC | 42.10 | - | |
62 | Phosphorylation | AIINSTITPNMTFTK EEECCCCCCCCEEEE | 14.54 | 25403869 | |
98 | Acetylation | SSEHHLSKFAEKFQE CCHHHHHHHHHHHHH | 55.76 | 22902405 | |
102 | Acetylation | HLSKFAEKFQEFKEA HHHHHHHHHHHHHHH | 49.25 | 22902405 | |
208 | Ubiquitination | TLKGNNAKLTAALLE HHHCCCHHHHHHHHH | 48.79 | - | |
221 | Ubiquitination | LESTANVKQWKQQLA HHHHHCHHHHHHHHH | 50.69 | - | |
302 | Acetylation | QRDSLTQKLQEVEIR HHHHHHHHHHHHHHH | 47.07 | 22902405 | |
311 | Ubiquitination | QEVEIRNKDLEGQLS HHHHHHCCCHHHHHH | 54.57 | - | |
318 | Phosphorylation | KDLEGQLSELEQRLE CCHHHHHHHHHHHHH | 32.04 | - |
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 HOME1_RAT !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HOME1_RAT !! |
* 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 HOME1_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SHAN1_RAT | Shank1 | physical | 10433269 | |
SHAN3_RAT | Shank3 | physical | 10433269 | |
GRM5_MOUSE | Grm5 | physical | 9808458 | |
GRM1_RAT | Grm1 | physical | 9808458 | |
HOME3_HUMAN | HOMER3 | physical | 9808458 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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