AVIL_MOUSE - dbPTM
AVIL_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AVIL_MOUSE
UniProt AC O88398
Protein Name Advillin
Gene Name Avil
Organism Mus musculus (Mouse).
Sequence Length 819
Subcellular Localization Cytoplasm, cytoskeleton. Cell projection. Cell projection, axon.
Protein Description Ca(2+)-regulated actin-binding protein. May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1-mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis..
Protein Sequence MSLSSAFRAVSNDPRIITWRIEKMELALVPLSAHGNFYEGDCYIVLSTRRVGSLLSQNIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHREVQYHESDTFRGYFKQGIIYKKGGVASGMKHVETNTYDVKRLLHVKGKRNIQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAASPGLMTVLQDTLGRRSMIKPAVSDEIMDQQQKSSIMLYHVSDTAGQLSVTEVATRPLVQDLLNHDDCYILDQSGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGYPSSTNVETVNDGAESAMFKQLFQKWSVKDQTTGLGKIFSTGKIAKIFQDKFDVSLLHTKPEVAAQERMVDDGKGQVEVWRIENLELVPVEYQWHGFFYGGDCYLVLYTYDVNGKPHYILYIWQGRHASRDELAASAYRAVEVDQQFDGAPVQVRVSMGKEPRHFMAIFKGKLVIYEGGTSRKGNEEPDPPVRLFQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDGNADTVAEGQEPPEFWDLLGGKTAYANDKRLQQETLDVQVRLFECSNKTGRFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRDPDTPILIIKQGFEPPTFTGWFLAWDPHIWSEGKSYEQLKNELGDATAIVRITADMKNATLYLNPSDGEPKYYPVEVLLKGQNQELPEDVDPAKKENYLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF
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
85PhosphorylationYTTQLDDYLGGSPVQ
EEECHHHHCCCCCCC
13.6022817900
221PhosphorylationAASPGLMTVLQDTLG
HCCCCHHHHHHHHHC
24.0928285833
226PhosphorylationLMTVLQDTLGRRSMI
HHHHHHHHHCCCCCC
20.3928285833
360PhosphorylationTGLGKIFSTGKIAKI
CCCCHHHCCCHHHHH
39.4624719451
458PhosphorylationDELAASAYRAVEVDQ
HHHHHHHHHHEECHH
9.1622817900
622PhosphorylationQVRLFECSNKTGRFL
EEEEEECCCCCCCEE
33.8822871156
721PhosphorylationHIWSEGKSYEQLKNE
HHHCCCCCHHHHHHH
44.7729895711
739PhosphorylationATAIVRITADMKNAT
CEEEEEEEECCCCCE
13.1729895711
746PhosphorylationTADMKNATLYLNPSD
EECCCCCEEEECCCC
25.9029895711
748PhosphorylationDMKNATLYLNPSDGE
CCCCCEEEECCCCCC
10.4829895711
758PhosphorylationPSDGEPKYYPVEVLL
CCCCCCCEEEEEEEE
24.5822817900
759PhosphorylationSDGEPKYYPVEVLLK
CCCCCCEEEEEEEEC
13.6124759943

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 AVIL_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AVIL_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 AVIL_MOUSE !!

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

Oops, there are no PPI records of AVIL_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AVIL_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-85; TYR-748 AND TYR-758,AND MASS SPECTROMETRY.

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