HOME3_MOUSE - dbPTM
HOME3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HOME3_MOUSE
UniProt AC Q99JP6
Protein Name Homer protein homolog 3 {ECO:0000305}
Gene Name Homer3 {ECO:0000312|MGI:MGI:1347359}
Organism Mus musculus (Mouse).
Sequence Length 356
Subcellular Localization Cytoplasm. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cell junction, synapse. Postsynaptic density of neuronal cells..
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. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses (By similarity). Negatively regulates T cell activation through negative regulation of IL2 expression by inhibiting calcineurin-NFAT pathway activation through interaction with NFATC2 leading to reduction of interaction between NFATC2 and PPP3CA (By similarity)..
Protein Sequence MSTAREQPIFSTRAHVFQIDPTTKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRANTVYGLGFASEQQLTQFAEKFQEVKEAARLAREKSQDGGEFTSTGLALASHQVPPSPLVSTNGPGEEKLFRSQSADTPGPTERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGEKEATSQSVEQLEARVQTKDQTLKNQSTGTREAPDTAEREETQQQVQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAAP
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
52PhosphorylationRNVYRIISIGGAKAI
CCEEEEEEECCCEEE
16.8930352176
65PhosphorylationAIINSTVTPNMTFTK
EEEECCCCCCCEEEE
14.72-
69PhosphorylationSTVTPNMTFTKTSQK
CCCCCCCEEEECCHH
34.4929899451
120PhosphorylationARLAREKSQDGGEFT
HHHHHHHCCCCCCCC
28.8425521595
127PhosphorylationSQDGGEFTSTGLALA
CCCCCCCCCHHHHHH
22.5225521595
128PhosphorylationQDGGEFTSTGLALAS
CCCCCCCCHHHHHHC
26.2926643407
129PhosphorylationDGGEFTSTGLALASH
CCCCCCCHHHHHHCC
32.9126643407
135PhosphorylationSTGLALASHQVPPSP
CHHHHHHCCCCCCCC
18.4629899451
141PhosphorylationASHQVPPSPLVSTNG
HCCCCCCCCCCCCCC
25.4624925903
157PhosphorylationGEEKLFRSQSADTPG
CHHHHCCCCCCCCCC
22.5825521595
159PhosphorylationEKLFRSQSADTPGPT
HHHCCCCCCCCCCCC
29.3825521595
162PhosphorylationFRSQSADTPGPTERE
CCCCCCCCCCCCHHH
29.8425521595
166PhosphorylationSADTPGPTERERLKK
CCCCCCCCHHHHHHH
54.3020415495
176PhosphorylationERLKKMLSEGSVGEV
HHHHHHHHCCCCCEE
36.0929899451
179PhosphorylationKKMLSEGSVGEVQWE
HHHHHCCCCCEEEEE
23.9329899451
195PhosphorylationEFFALQDSNQRLAGA
EEEEEECCCHHHHHH
23.15-
252PhosphorylationAGEKEATSQSVEQLE
CCCCCCCHHCHHHHH
27.7529899451
254PhosphorylationEKEATSQSVEQLEAR
CCCCCHHCHHHHHHH
27.6529899451

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

Oops, there are no upstream regulatory protein records of HOME3_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HOME3_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 HOME3_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRM1_MOUSEGrm1physical
22486777

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HOME3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, AND MASSSPECTROMETRY.

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