HOME1_MOUSE - dbPTM
HOME1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MGEQPIFST
------CCCCCCEEC
42.10-
22UbiquitinationQIDPNTKKNWVPTSK
EECCCCCCCCCCCCC
54.74-
59PhosphorylationGSKAIINSTITPNMT
CCEEEECCCCCCCCE
15.6929899451
60PhosphorylationSKAIINSTITPNMTF
CEEEECCCCCCCCEE
25.1225521595
117PhosphorylationARLAKEKSQEKMELT
HHHHHHHHHHHHCCC
44.67-
128PhosphorylationMELTSTPSQESAGGD
HCCCCCCCCCCCCCC
46.8229899451
131PhosphorylationTSTPSQESAGGDLQS
CCCCCCCCCCCCCCC
25.2829899451
138PhosphorylationSAGGDLQSPLTPESI
CCCCCCCCCCCHHHC
29.2229899451
141PhosphorylationGDLQSPLTPESINGT
CCCCCCCCHHHCCCC
28.5229899451
144PhosphorylationQSPLTPESINGTDDE
CCCCCHHHCCCCCCC
23.6629899451
153PhosphorylationNGTDDERTPDVTQNS
CCCCCCCCCCCCCCC
23.0729899451
185PhosphorylationGDRTQALSHASSAIS
CCHHHHHHHHHHHHH
21.7419737024
185O-linked_GlycosylationGDRTQALSHASSAIS
CCHHHHHHHHHHHHH
21.7420547801
188PhosphorylationTQALSHASSAISKHW
HHHHHHHHHHHHHHH
18.1921454597
189PhosphorylationQALSHASSAISKHWE
HHHHHHHHHHHHHHH
30.3319737024
203MethylationEAELATLKGNNAKLT
HHHHHHHHCCCHHHH
56.06-
208UbiquitinationTLKGNNAKLTAALLE
HHHCCCHHHHHHHHH
48.79-
221UbiquitinationLESTANVKQWKQQLA
HHHHHCHHHHHHHHH
50.69-
224UbiquitinationTANVKQWKQQLAAYQ
HHCHHHHHHHHHHHH
26.18-
249O-linked_GlycosylationTELECVSSQANAVHS
HHHHHHHHHHHHHHH
16.9655412271
298PhosphorylationELQEQRDSLTQKLQE
HHHHHHHHHHHHHHH
35.1929899451
311UbiquitinationQEVEIRNKDLEGQLS
HHHHHHCCCCCHHHH
54.57-
318PhosphorylationKDLEGQLSDLEQRLE
CCCCHHHHHHHHHHH
32.0625521595
326UbiquitinationDLEQRLEKSQNEQEA
HHHHHHHHCHHHHHH
63.03-
327PhosphorylationLEQRLEKSQNEQEAF
HHHHHHHCHHHHHHH
28.94-
339UbiquitinationEAFRSNLKTLLEILD
HHHHHHHHHHHHHHC
41.18-
361UbiquitinationELRDNLAKLLECS--
HHHHHHHHHHHCC--
57.69-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
117SPhosphorylationKinaseCAMK2AP11798
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HOME1_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRM1_MOUSEGrm1physical
15579147
ITPR1_MOUSEItpr1physical
15579147
HOME1_MOUSEHomer1physical
15579147
GRID2_MOUSEGrid2physical
15579147
1433Z_MOUSEYwhazphysical
16959763
GRM5_MOUSEGrm5physical
9808458
HOME1_RATHomer1physical
9808458
HOME2_MOUSEHomer2physical
9808458
CTIP_HUMANRBBP8physical
26496610
MPZL1_HUMANMPZL1physical
26496610
KIF3B_HUMANKIF3Bphysical
26496610
HOME3_HUMANHOMER3physical
26496610
COBL1_HUMANCOBLL1physical
26496610
LMA2L_HUMANLMAN2Lphysical
26496610
PSRC1_HUMANPSRC1physical
26496610
FRYL_HUMANFRYLphysical
26496610
AGAP2_MOUSEAgap2physical
28671696
BIN1_MOUSEBin1physical
28671696
KCC2A_MOUSECamk2aphysical
28671696
CNTN4_MOUSECntn4physical
28671696
CYH3_MOUSECyth3physical
28671696
DLGP1_MOUSEDlgap1physical
28671696
DYN1_MOUSEDnm1physical
28671696
GIPC1_MOUSEGipc1physical
28671696
GRM1_MOUSEGrm1physical
28671696
GRM5_MOUSEGrm5physical
28671696
LZTS3_MOUSELzts3physical
28671696
M3K5_MOUSEMap3k5physical
28671696
MYH10_MOUSEMyh10physical
28671696
NCAM1_MOUSENcam1physical
28671696
NCDN_MOUSENcdnphysical
28671696
PPIA_MOUSEPpiaphysical
28671696
PP2BA_MOUSEPpp3caphysical
28671696
KPCA_MOUSEPrkcaphysical
28671696
SHAN1_MOUSEShank1physical
28671696
SHAN2_MOUSEShank2physical
28671696
SHAN3_MOUSEShank3physical
28671696
SHPS1_MOUSESirpaphysical
28671696
SPTB2_MOUSESptbn1physical
28671696
TENR_MOUSETnrphysical
28671696
WASF1_MOUSEWasf1physical
28671696
1433B_MOUSEYwhabphysical
28671696
1433E_MOUSEYwhaephysical
28671696
1433F_MOUSEYwhahphysical
28671696
1433Z_MOUSEYwhazphysical
28671696

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HOME1_MOUSE

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Related Literatures of Post-Translational Modification

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