UniProt ID | HOME1_MOUSE | |
---|---|---|
UniProt AC | Q9Z2Y3 | |
Protein Name | Homer protein homolog 1 {ECO:0000305} | |
Gene Name | Homer1 {ECO:0000312|MGI:MGI:1347345} | |
Organism | Mus musculus (Mouse). | |
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. T | |
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. Isoform 1 regulates the trafficking and surface expression of GRM5. 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 5 counteracts the effects by competing for binding sites. Isoform 3 regulates the trafficking and surface expression of GRM5. Isoform 5 acts as a natural dominant negative, in dynamic competition with constitutively expressed isoform 1, isoform 2 and isoform 3 to regulate synaptic metabotropic glutamate function. Isoform 5, may be involved in the structural changes that occur at synapses during long-lasting neuronal plasticity and development (By similarity). Forms a high-order complex with SHANK1, which in turn is necessary for the structural and functional integrity of dendritic spines (By similarity).. | |
Protein Sequence | MGEQPIFSTRAHVFQIDPNTKKNWVPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMTFTKTSQKFGQWADSRANTVYGLGFSSEHHLSKFAEKFQEFKEAARLAKEKSQEKMELTSTPSQESAGGDLQSPLTPESINGTDDERTPDVTQNSEPRAEPTQNALPFPHSAGDRTQALSHASSAISKHWEAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELECVSSQANAVHSHKTELNQTVQELEETLKVKEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRSNLKTLLEILDGKIFELTELRDNLAKLLECS | |
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 | - | |
22 | Ubiquitination | QIDPNTKKNWVPTSK EECCCCCCCCCCCCC | 54.74 | - | |
59 | Phosphorylation | GSKAIINSTITPNMT CCEEEECCCCCCCCE | 15.69 | 29899451 | |
60 | Phosphorylation | SKAIINSTITPNMTF CEEEECCCCCCCCEE | 25.12 | 25521595 | |
117 | Phosphorylation | ARLAKEKSQEKMELT HHHHHHHHHHHHCCC | 44.67 | - | |
128 | Phosphorylation | MELTSTPSQESAGGD HCCCCCCCCCCCCCC | 46.82 | 29899451 | |
131 | Phosphorylation | TSTPSQESAGGDLQS CCCCCCCCCCCCCCC | 25.28 | 29899451 | |
138 | Phosphorylation | SAGGDLQSPLTPESI CCCCCCCCCCCHHHC | 29.22 | 29899451 | |
141 | Phosphorylation | GDLQSPLTPESINGT CCCCCCCCHHHCCCC | 28.52 | 29899451 | |
144 | Phosphorylation | QSPLTPESINGTDDE CCCCCHHHCCCCCCC | 23.66 | 29899451 | |
153 | Phosphorylation | NGTDDERTPDVTQNS CCCCCCCCCCCCCCC | 23.07 | 29899451 | |
185 | Phosphorylation | GDRTQALSHASSAIS CCHHHHHHHHHHHHH | 21.74 | 19737024 | |
185 | O-linked_Glycosylation | GDRTQALSHASSAIS CCHHHHHHHHHHHHH | 21.74 | 20547801 | |
188 | Phosphorylation | TQALSHASSAISKHW HHHHHHHHHHHHHHH | 18.19 | 21454597 | |
189 | Phosphorylation | QALSHASSAISKHWE HHHHHHHHHHHHHHH | 30.33 | 19737024 | |
203 | Methylation | EAELATLKGNNAKLT HHHHHHHHCCCHHHH | 56.06 | - | |
208 | Ubiquitination | TLKGNNAKLTAALLE HHHCCCHHHHHHHHH | 48.79 | - | |
221 | Ubiquitination | LESTANVKQWKQQLA HHHHHCHHHHHHHHH | 50.69 | - | |
224 | Ubiquitination | TANVKQWKQQLAAYQ HHCHHHHHHHHHHHH | 26.18 | - | |
249 | O-linked_Glycosylation | TELECVSSQANAVHS HHHHHHHHHHHHHHH | 16.96 | 55412271 | |
298 | Phosphorylation | ELQEQRDSLTQKLQE HHHHHHHHHHHHHHH | 35.19 | 29899451 | |
311 | Ubiquitination | QEVEIRNKDLEGQLS HHHHHHCCCCCHHHH | 54.57 | - | |
318 | Phosphorylation | KDLEGQLSDLEQRLE CCCCHHHHHHHHHHH | 32.06 | 25521595 | |
326 | Ubiquitination | DLEQRLEKSQNEQEA HHHHHHHHCHHHHHH | 63.03 | - | |
327 | Phosphorylation | LEQRLEKSQNEQEAF HHHHHHHCHHHHHHH | 28.94 | - | |
339 | Ubiquitination | EAFRSNLKTLLEILD HHHHHHHHHHHHHHC | 41.18 | - | |
361 | Ubiquitination | ELRDNLAKLLECS-- HHHHHHHHHHHCC-- | 57.69 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
117 | S | Phosphorylation | Kinase | CAMK2A | P11798 | PSP |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of HOME1_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of HOME1_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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