Homer1
entrez
29546
canonical
uniprot
Q9Z214
canonical
ensembl
ENSRNOG00000047014
resolver
ensp
ENSRNOP00000086769
resolver
genesymbol
Homer1
resolver
genesymbol_syn
Homer
resolver
genesymbol_syn
Vesl
resolver
uniprot
O08567
resolver
uniprot
O88800
resolver
uniprot
Q9QUJ8
resolver
uniprot
Q9QWN5
resolver
uniprot_entry
HOME1_RAT
resolver
uniprot_sec
O08567
resolver
uniprot_sec
O88800
resolver
uniprot_sec
Q9QUJ8
resolver
uniprot_sec
Q9QWN5
resolver
amino_acid_sequence
MGEQPIFSTRAHVFQIDPNTKKNWVPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMTFTKTSQKFGQWADSRANTVYGLGFSSEHHLSKFAEKFQEFKEAARLAKEKSQEKMELTSTPSQESAGGDLQSPLTPESINGTDDERTPDVTQNSEPRAEPAQNALPFSHSAGDRTQGLSHASSAISKHWEAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELECVSSQANAVHSHKTELSQTVQELEETLKVKEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSELEQRLEKSQSEQDAFRSNLKTLLEILDGKIFELTELRDNLAKLLECS
uniprot
proteins
function
FUNCTION: 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). Negatively regulates T cell activation by inhibiting the calcineurin-NFAT pathway. Acts by competing with calcineurin/PPP3CA for NFAT protein binding, hence preventing NFAT activation by PPP3CA (By similarity). {ECO:0000250|UniProtKB:Q86YM7, ECO:0000269|PubMed:14528310, ECO:0000269|PubMed:19345194}.
uniprot
proteins
mass_dalton
41305
uniprot
proteins
mutagenesis
MUTAGEN 24; /note="W->A: Disrupts binding to both GRM1 and SHANK3. Does not form the high-order complex with SHANK1."; /evidence="ECO:0000269|PubMed:10798399, ECO:0000269|PubMed:19345194"; MUTAGEN 24; /note="W->Y: Disrupts binding to GRM1."; /evidence="ECO:0000269|PubMed:10798399"; MUTAGEN 70; /note="T->A: Normal binding."; /evidence="ECO:0000269|PubMed:10798399"; MUTAGEN 70; /note="T->E: Disrupts binding to SHANK3."; /evidence="ECO:0000269|PubMed:10798399"; MUTAGEN 74; /note="F->A: Eliminates binding to both GRM1 and SHANK3."; /evidence="ECO:0000269|PubMed:10798399"; MUTAGEN 76; /note="Q->A: Normal binding."; /evidence="ECO:0000269|PubMed:10798399"; MUTAGEN 76; /note="Q->R: Normal binding."; /evidence="ECO:0000269|PubMed:10798399"; MUTAGEN 85; /note="V->A: Diminishes binding to GRM1."; /evidence="ECO:0000269|PubMed:10798399"; MUTAGEN 89; /note="G->A: Eliminates binding to both GRM1 and SHANK3."; /evidence="ECO:0000269|PubMed:10798399"; MUTAGEN 89; /note="G->N: Eliminates binding to both GRM1 and SHANK3."; /evidence="ECO:0000269|PubMed:10798399"; MUTAGEN 344; /note="I->R: Dimeric form; when associated with E-349. Does not form the high-order complex with SHANK1; when associated with E-349. Does not change its interaction with STX12; when associated with E-349. Reduces localization to the spine; when associated with E-349. Affects dendritic spine structure; when associated with E-349. Decreases synaptic transmission; when associated with E-349. Does not affect glutamate receptors ratio; when associated with E-349."; /evidence="ECO:0000269|PubMed:19345194"; MUTAGEN 349; /note="I->E: Dimeric form; when associated with R-344. Does not form the high-order complex with SHANK1; when associated with R-344. Does not change its interaction with STX12; when associated with R-344. Reduces localization to the spine; when associated with R-344. Affects dendritic spine structure; when associated with R-344. Decreases synaptic transmission; when associated with R-344. Does not affect glutamate receptors ratio; when associated with R-344."; /evidence="ECO:0000269|PubMed:19345194
uniprot
proteins
protein_family
Homer family
uniprot
proteins
pubmed
10433269
uniprot
proteins
pubmed
10798399
uniprot
proteins
pubmed
10851183
uniprot
proteins
pubmed
11118290
uniprot
proteins
pubmed
12054806
uniprot
proteins
pubmed
12810060
uniprot
proteins
pubmed
12887973
uniprot
proteins
pubmed
14528310
uniprot
proteins
pubmed
15034583
uniprot
proteins
pubmed
17584991
uniprot
proteins
pubmed
19345194
uniprot
proteins
pubmed
30021165
uniprot
proteins
pubmed
9069287
uniprot
proteins
pubmed
9257717
uniprot
proteins
pubmed
9727012
uniprot
proteins
pubmed
9808458
uniprot
proteins
pubmed
9808459
uniprot
proteins
pubmed
9824313
uniprot
proteins
sequence_length
366
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse {ECO:0000269|PubMed:10433269}. Cell projection, dendritic spine {ECO:0000269|PubMed:19345194, ECO:0000269|PubMed:30021165}. Note=Isoform 1 inhibits surface expression of GRM5 causing it to be retained in the endoplasmic reticulum. {ECO:0000250}.
uniprot
proteins