ARP3_MOUSE - dbPTM
ARP3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARP3_MOUSE
UniProt AC Q99JY9
Protein Name Actin-related protein 3
Gene Name Actr3
Organism Mus musculus (Mouse).
Sequence Length 418
Subcellular Localization Cytoplasm, cytoskeleton . Cell projection . In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes).
Protein Description Functions as ATP-binding 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. Seems to contact the pointed end of the daughter actin filament. Plays a role in ciliogenesis (By similarity)..
Protein Sequence MAGRLPACVVDCGTGYTKLGYAGNTEPQFIIPSCIAIKESAKVGDQAQRRVMKGVDDLDFFIGDEAIEKPTYATKWPIRHGIVEDWDLMERFMEQVIFKYLRAEPEDHYFLLTEPPLNTPENREYTAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLRDREVGIPPEQSLETAKAVKERYSYVCPDLVKEFNKYDTDGSKWIKQYTGVNAISKKEFSIDVGYERFLGPEIFFHPEFANPDFTQPISEVVDEVIQNCPIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDLKRTVDARLKLSEELSGGRLKPKPIDVQVITHHMQRYAVWFGGSMLASTPEFYQVCHTKKDYEEIGPSICRHNPVFGVMS
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------MAGRLPACV
------CCCCCCEEE		16.29-
12GlutathionylationLPACVVDCGTGYTKL
CCEEEEECCCCCEEC		3.3824333276
14PhosphorylationACVVDCGTGYTKLGY
EEEEECCCCCEECCC		33.0926026062
16PhosphorylationVVDCGTGYTKLGYAG
EEECCCCCEECCCCC		10.6717242355
17PhosphorylationVDCGTGYTKLGYAGN
EECCCCCEECCCCCC		22.5717242355
34S-nitrosylationPQFIIPSCIAIKESA
CCEECCCCEEEHHHH		1.7221278135
34GlutathionylationPQFIIPSCIAIKESA
CCEECCCCEEEHHHH		1.7224333276
34S-nitrosocysteinePQFIIPSCIAIKESA
CCEECCCCEEEHHHH		1.72-
53UbiquitinationQAQRRVMKGVDDLDF
HHHHHHHCCCCCCCE		53.58-
69UbiquitinationIGDEAIEKPTYATKW
CCHHHCCCCCCCCCC		36.22-
71PhosphorylationDEAIEKPTYATKWPI
HHHCCCCCCCCCCCC		36.5320531401
72PhosphorylationEAIEKPTYATKWPIR
HHCCCCCCCCCCCCC		22.3220531401
74PhosphorylationIEKPTYATKWPIRHG
CCCCCCCCCCCCCCC		24.1920531401
75UbiquitinationEKPTYATKWPIRHGI
CCCCCCCCCCCCCCC		42.68-
75AcetylationEKPTYATKWPIRHGI
CCCCCCCCCCCCCCC		42.6824625005
99UbiquitinationFMEQVIFKYLRAEPE
HHHHHHHHHHHCCCC		32.05-
100PhosphorylationMEQVIFKYLRAEPED
HHHHHHHHHHCCCCC		7.23-
109PhosphorylationRAEPEDHYFLLTEPP
HCCCCCCEEECCCCC		14.2918563927
189S-palmitoylationEGYVIGSCIKHIPIA
CCEEEHHHHHCCCCC		3.9728680068
189GlutathionylationEGYVIGSCIKHIPIA
CCEEEHHHHHCCCCC		3.9724333276
191UbiquitinationYVIGSCIKHIPIAGR
EEEHHHHHCCCCCCC		39.55-
202PhosphorylationIAGRDITYFIQQLLR
CCCCHHHHHHHHHHH		10.0627180971
225AcetylationEQSLETAKAVKERYS
HHHHHHHHHHHHHHH		62.2223954790
231PhosphorylationAKAVKERYSYVCPDL
HHHHHHHHHCCCHHH		12.8725367039
232PhosphorylationKAVKERYSYVCPDLV
HHHHHHHHCCCHHHH		19.8125367039
233PhosphorylationAVKERYSYVCPDLVK
HHHHHHHCCCHHHHH		9.3529514104
235S-nitrosylationKERYSYVCPDLVKEF
HHHHHCCCHHHHHHH		1.3224895380
235S-palmitoylationKERYSYVCPDLVKEF
HHHHHCCCHHHHHHH		1.3228526873
240AcetylationYVCPDLVKEFNKYDT
CCCHHHHHHHHHCCC		64.9823806337
240UbiquitinationYVCPDLVKEFNKYDT
CCCHHHHHHHHHCCC		64.98-
240MalonylationYVCPDLVKEFNKYDT
CCCHHHHHHHHHCCC		64.9826320211
244AcetylationDLVKEFNKYDTDGSK
HHHHHHHHCCCCCCH		50.2323806337
244MalonylationDLVKEFNKYDTDGSK
HHHHHHHHCCCCCCH		50.2326320211
251MalonylationKYDTDGSKWIKQYTG
HCCCCCCHHHHHHHC		59.4726320211
251AcetylationKYDTDGSKWIKQYTG
HCCCCCCHHHHHHHC		59.4723201123
251UbiquitinationKYDTDGSKWIKQYTG
HCCCCCCHHHHHHHC		59.47-
254AcetylationTDGSKWIKQYTGVNA
CCCCHHHHHHHCCCC		35.8222826441
254MalonylationTDGSKWIKQYTGVNA
CCCCHHHHHHHCCCC		35.8226320211
254UbiquitinationTDGSKWIKQYTGVNA
CCCCHHHHHHHCCCC		35.82-
264UbiquitinationTGVNAISKKEFSIDV
HCCCCCCCCEEEEEC		50.65-
265UbiquitinationGVNAISKKEFSIDVG
CCCCCCCCEEEEECC		58.14-
265MalonylationGVNAISKKEFSIDVG
CCCCCCCCEEEEECC		58.1426320211
268PhosphorylationAISKKEFSIDVGYER
CCCCCEEEEECCCHH		20.97-
317AcetylationDVRRPLYKNIVLSGG
CCCCCCCCCEEECCC		48.1322826441
317UbiquitinationDVRRPLYKNIVLSGG
CCCCCCCCCEEECCC		48.13-
348MalonylationRTVDARLKLSEELSG
HHHHHHHHCCHHHCC		44.4026320211
348UbiquitinationRTVDARLKLSEELSG
HHHHHHHHCCHHHCC		44.40-
348AcetylationRTVDARLKLSEELSG
HHHHHHHHCCHHHCC		44.4023806337
361UbiquitinationSGGRLKPKPIDVQVI
CCCCCCCCCCCHHHH		53.68-
398UbiquitinationYQVCHTKKDYEEIGP
HHHHCCCCCHHHHCH		67.70-
408S-nitrosocysteineEEIGPSICRHNPVFG
HHHCHHHHCCCCCCC		4.20-
408GlutathionylationEEIGPSICRHNPVFG
HHHCHHHHCCCCCCC		4.2024333276
408S-nitrosylationEEIGPSICRHNPVFG
HHHCHHHHCCCCCCC		4.2024926564
408S-palmitoylationEEIGPSICRHNPVFG
HHHCHHHHCCCCCCC		4.2028526873
418PhosphorylationNPVFGVMS-------
CCCCCCCC-------		34.3625521595
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 ARP3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARP3_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 ARP3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ARP3_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARP3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, AND MASSSPECTROMETRY.
"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-418, AND MASSSPECTROMETRY.

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