ARPC3_MOUSE - dbPTM
ARPC3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARPC3_MOUSE
UniProt AC Q9JM76
Protein Name Actin-related protein 2/3 complex subunit 3
Gene Name Arpc3
Organism Mus musculus (Mouse).
Sequence Length 178
Subcellular Localization Cytoplasm, cytoskeleton. Cell projection.
Protein Description Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks..
Protein Sequence MPAYHSSLMDPDTKLIGNMALLPLRSQFKGPAPRETKDTDIVDEAIYYFKANVFFKNYEIKNEADRTLIYITLYISECLKKLQKCNSKSQGEKEMYTLGITNFPIPGEPGFPLNAIYAKPASKQEDEMMRAYLQQLRQETGLRLCEKVFDPQSDKPSKWWTCFVKRQFMNKSLSGPGQ
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
6Phosphorylation--MPAYHSSLMDPDT
--CCCCCCCCCCCCC		16.7021183079
7Phosphorylation-MPAYHSSLMDPDTK
-CCCCCCCCCCCCCC		17.8821183079
14UbiquitinationSLMDPDTKLIGNMAL
CCCCCCCCEECCEEH		45.5522790023
29SuccinylationLPLRSQFKGPAPRET
HHHHHCCCCCCCCCC		57.2423954790
29AcetylationLPLRSQFKGPAPRET
HHHHHCCCCCCCCCC		57.2422826441
29MalonylationLPLRSQFKGPAPRET
HHHHHCCCCCCCCCC		57.2426320211
29UbiquitinationLPLRSQFKGPAPRET
HHHHHCCCCCCCCCC		57.2427667366
36PhosphorylationKGPAPRETKDTDIVD
CCCCCCCCCCCCHHH		35.1825367039
37UbiquitinationGPAPRETKDTDIVDE
CCCCCCCCCCCHHHH		54.6122790023
39PhosphorylationAPRETKDTDIVDEAI
CCCCCCCCCHHHHHH		29.2225367039
47PhosphorylationDIVDEAIYYFKANVF
CHHHHHHHHHHHCEE		15.1925177544
48PhosphorylationIVDEAIYYFKANVFF
HHHHHHHHHHHCEEE		7.7825367039
56AcetylationFKANVFFKNYEIKNE
HHHCEEEECCEECCH		47.3422826441
56SuccinylationFKANVFFKNYEIKNE
HHHCEEEECCEECCH		47.3423954790
61UbiquitinationFFKNYEIKNEADRTL
EEECCEECCHHHHHH		36.4727667366
61AcetylationFFKNYEIKNEADRTL
EEECCEECCHHHHHH		36.4722826441
61SuccinylationFFKNYEIKNEADRTL
EEECCEECCHHHHHH		36.4723954790
123UbiquitinationIYAKPASKQEDEMMR
EEECCCCHHHHHHHH		60.8727667366
147AcetylationTGLRLCEKVFDPQSD
HCCHHHHHHCCCCCC		47.4022826441
155AcetylationVFDPQSDKPSKWWTC
HCCCCCCCCCCCEEE		57.3423954790
158AcetylationPQSDKPSKWWTCFVK
CCCCCCCCCEEEEHH		56.1022826441
165AcetylationKWWTCFVKRQFMNKS
CCEEEEHHHHHHCHH		21.8922826441
171AcetylationVKRQFMNKSLSGPGQ
HHHHHHCHHCCCCCC		40.7722826441
174PhosphorylationQFMNKSLSGPGQ---
HHHCHHCCCCCC---		50.4630635358
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 ARPC3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARPC3_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 ARPC3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ARPC3_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARPC3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-47, AND MASSSPECTROMETRY.

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