TWF2_MOUSE - dbPTM
TWF2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TWF2_MOUSE
UniProt AC Q9Z0P5
Protein Name Twinfilin-2
Gene Name Twf2
Organism Mus musculus (Mouse).
Sequence Length 349
Subcellular Localization Cytoplasm, cytoskeleton . Cytoplasm, perinuclear region . Cell projection, stereocilium . Perinuclear and G-actin-rich cortical actin structure sublocalization. Isoform 2 found also along myofibrils in cardiomyocytes (PubMed:18837697). Localized in c
Protein Description Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. May play a role in regulating the mature length of the middle and short rows of stereocilia..
Protein Sequence MAHQTGIHATEELKEFFAKARAGSIRLIKVIIEDEQLVLGASQEPVGRWDQDYDRAVLPLLDAQEPCYLLFRLDSQNAQGFEWLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDELFGTVKDDLSLAGYQKHLSSCAAPAPLTSAERELQQIRINEVKTEISVESKHQTLQGLAFPLQPEAQRALQQLKQKTVNYIQLKLDLERETIELVHTEPTNVAQLPSRIPRDAARYHFFLYKHTHEGDALESVVFIYSMPGYKCSIKERMLYSSCKSRLLDSVEQDFQLEIAKKIEIGDGAELTAEFLYDEVHPKQHAFKQAFAKPKGPGGKRGHKRLIRGPGENGEDS
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------MAHQTGIHA
------CCCCCCCCC
11.96-
14AcetylationIHATEELKEFFAKAR
CCCCHHHHHHHHHHH
56.6122826441
24PhosphorylationFAKARAGSIRLIKVI
HHHHHCCCEEEEEEE
11.9881017669
67GlutathionylationLLDAQEPCYLLFRLD
HCCCCCCEEEEEEEC
3.5324333276
98AcetylationDNSPVRLKMLYAATR
CCCHHHHHHHHHHHH
19.1222826441
141GlutathionylationYQKHLSSCAAPAPLT
HHHHHHCCCCCCCCC
3.1724333276
167PhosphorylationNEVKTEISVESKHQT
CCCCCEEEECCCCCC
17.38101544679
170PhosphorylationKTEISVESKHQTLQG
CCEEEECCCCCCHHH
33.0329176673
211PhosphorylationKLDLERETIELVHTE
EEHHHHCEEEEEECC
26.4426239621
217PhosphorylationETIELVHTEPTNVAQ
CEEEEEECCCCCHHH
35.8626239621
220PhosphorylationELVHTEPTNVAQLPS
EEEECCCCCHHHCCC
35.7726239621
277PhosphorylationMLYSSCKSRLLDSVE
HHHHHHHHHHHHHHC
32.2724068923
282PhosphorylationCKSRLLDSVEQDFQL
HHHHHHHHHCHHHHH
27.7624068923
309PhosphorylationELTAEFLYDEVHPKQ
EEEEHHHHCCCCHHH
18.5122817900
349PhosphorylationPGENGEDS-------
CCCCCCCC-------
37.5126824392

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 TWF2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TWF2_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 TWF2_MOUSE !!

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

Oops, there are no PPI records of TWF2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TWF2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, AND MASSSPECTROMETRY.

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