HOME3_HUMAN - dbPTM
HOME3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HOME3_HUMAN
UniProt AC Q9NSC5
Protein Name Homer protein homolog 3 {ECO:0000305}
Gene Name HOMER3 {ECO:0000312|HGNC:HGNC:17514}
Organism Homo sapiens (Human).
Sequence Length 361
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. 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. [PubMed: 18218901]
Protein Sequence MSTAREQPIFSTRAHVFQIDPATKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRANTVYGLGFASEQHLTQFAEKFQEVKEAARLAREKSQDGGELTSPALGLASHQVPPSPLVSANGPGEEKLFRSQSADAPGPTERERLKKMLSEGSVGEVQWEAEFFALQDSNNKLAGALREANAAAAQWRQQLEAQRAEAERLRQRVAELEAQAASEVTPTGEKEGLGQGQSLEQLEALVQTKDQEIQTLKSQTGGPREALEAAEREETQQKVQDLETRNAELEHQLRAMERSLEEARAERERARAEVGRAAQLLDVSLFELSELREGLARLAEAAP
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
2Phosphorylation------MSTAREQPI
------CCCCCCCCC		30.6729083192
3Phosphorylation-----MSTAREQPIF
-----CCCCCCCCCC		28.5629083192
11PhosphorylationAREQPIFSTRAHVFQ
CCCCCCCCCCEEEEE		20.0829083192
12PhosphorylationREQPIFSTRAHVFQI
CCCCCCCCCEEEEEC		22.5629083192
23PhosphorylationVFQIDPATKRNWIPA
EEECCCCCCCCCCCC		35.61-
24UbiquitinationFQIDPATKRNWIPAG
EECCCCCCCCCCCCC		45.93-
36PhosphorylationPAGKHALTVSYFYDA
CCCCCEEEEEEEECC		14.27-
38PhosphorylationGKHALTVSYFYDATR
CCCEEEEEEEECCCC		12.32-
52PhosphorylationRNVYRIISIGGAKAI
CCEEEEEEECCCEEH		16.89-
57UbiquitinationIISIGGAKAIINSTV
EEEECCCEEHEECCC		43.31-
57AcetylationIISIGGAKAIINSTV
EEEECCCEEHEECCC		43.3125953088
76UbiquitinationTFTKTSQKFGQWADS
EEEECCHHHHCHHHH		51.75-
100 (in isoform 5)Phosphorylation-21.37-
110UbiquitinationAEKFQEVKEAARLAR
HHHHHHHHHHHHHHH		40.66-
120PhosphorylationARLAREKSQDGGELT
HHHHHHHCCCCCCCC		28.8429507054
123PhosphorylationAREKSQDGGELTSPA
HHHHCCCCCCCCCHH		24.6832645325
127PhosphorylationSQDGGELTSPALGLA
CCCCCCCCCHHHHCC		28.5028450419
128PhosphorylationQDGGELTSPALGLAS
CCCCCCCCHHHHCCC		22.3228450419
135PhosphorylationSPALGLASHQVPPSP
CHHHHCCCCCCCCCC		21.3525394399
141PhosphorylationASHQVPPSPLVSANG
CCCCCCCCCCCCCCC		25.4622199227
145PhosphorylationVPPSPLVSANGPGEE
CCCCCCCCCCCCCHH		24.5722199227
157PhosphorylationGEEKLFRSQSADAPG
CHHHHCCCCCCCCCC		22.5829255136
159PhosphorylationEKLFRSQSADAPGPT
HHHCCCCCCCCCCCC		29.3929255136
166PhosphorylationSADAPGPTERERLKK
CCCCCCCCHHHHHHH		54.3023403867
176PhosphorylationERLKKMLSEGSVGEV
HHHHHHHHCCCCCEE		36.0926846344
179PhosphorylationKKMLSEGSVGEVQWE
HHHHHCCCCCEEEEE		23.9326846344
207PhosphorylationAGALREANAAAAQWR
HHHHHHHHHHHHHHH		25.9232142685
220PhosphorylationWRQQLEAQRAEAERL
HHHHHHHHHHHHHHH		35.4232142685
231UbiquitinationAERLRQRVAELEAQA
HHHHHHHHHHHHHHH		3.5229967540
239UbiquitinationAELEAQAASEVTPTG
HHHHHHHHHCCCCCC		8.3132142685
240PhosphorylationELEAQAASEVTPTGE
HHHHHHHHCCCCCCC		35.3030266825
243PhosphorylationAQAASEVTPTGEKEG
HHHHHCCCCCCCCCC		15.8730266825
245PhosphorylationAASEVTPTGEKEGLG
HHHCCCCCCCCCCCC		48.9130266825
256PhosphorylationEGLGQGQSLEQLEAL
CCCCCCCCHHHHHHH		40.4729255136
267UbiquitinationLEALVQTKDQEIQTL
HHHHHHCCHHHHHHH		40.0829967540
275UbiquitinationDQEIQTLKSQTGGPR
HHHHHHHHHCCCCHH		43.8632142685
276PhosphorylationQEIQTLKSQTGGPRE
HHHHHHHHCCCCHHH		35.77-
278PhosphorylationIQTLKSQTGGPREAL
HHHHHHCCCCHHHHH		51.72-
302PhosphorylationQKVQDLETRNAELEH
HHHHHHHHHHHHHHH		36.2023879269
317PhosphorylationQLRAMERSLEEARAE
HHHHHHHHHHHHHHH		27.1624719451
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HOME3_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DYL2_HUMANDYNLL2physical
16189514
FRYL_HUMANFRYLphysical
16189514
TRPC1_HUMANTRPC1physical
14505576
TRPC4_HUMANTRPC4physical
14505576
TRPC5_HUMANTRPC5physical
14505576
RYR1_HUMANRYR1physical
12223488
PRS8_HUMANPSMC5physical
22486777
IKKB_HUMANIKBKBphysical
20693425
A4_HUMANAPPphysical
21832049
ABI3_HUMANABI3physical
19060904
GRM5_MOUSEGrm5physical
9808458
HOME1_RATHomer1physical
9808458
HOME2_MOUSEHomer2physical
9808458
PSA2_HUMANPSMA2physical
21988832
HOME3_HUMANHOMER3physical
25416956
HOME1_HUMANHOMER1physical
25416956
P121A_HUMANPOM121physical
25416956
ABI2_HUMANABI2physical
25416956
NEBL_HUMANNEBLphysical
25416956
EAF1_HUMANEAF1physical
25416956
PPR18_HUMANPPP1R18physical
25416956
HOME1_HUMANHOMER1physical
28514442
HOME2_HUMANHOMER2physical
28514442
FRYL_HUMANFRYLphysical
28514442
MPP5_HUMANMPP5physical
28514442
INADL_HUMANINADLphysical
28514442
HNRLL_HUMANHNRNPLLphysical
28514442
PEX14_HUMANPEX14physical
28514442
DREB_HUMANDBN1physical
28514442
ABI1_HUMANABI1physical
28514442
WASF2_HUMANWASF2physical
28514442
ABI2_HUMANABI2physical
28514442
NCKP1_HUMANNCKAP1physical
28514442
IF4E2_HUMANEIF4E2physical
28514442
CYFP2_HUMANCYFIP2physical
28514442
P53_HUMANTP53physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HOME3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, AND MASSSPECTROMETRY.

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