TWF1_MOUSE - dbPTM
TWF1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TWF1_MOUSE
UniProt AC Q91YR1
Protein Name Twinfilin-1
Gene Name Twf1
Organism Mus musculus (Mouse).
Sequence Length 350
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton . Diffuse cytoplasmic localization with perinuclear and G-actin-rich cortical actin structures sublocalization. Also found at membrane ruffles and cell-cell contacts.
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..
Protein Sequence MSHQTGIQASEDVKEIFARARNGKYRLLKISIENEQLVVGSCSPPSDSWEQDYDSFVLPLLEDKQPCYVLFRLDSQNAQGYEWIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVFGTVKEDVSLHGYKKYLLSQSSPAPLTAAEEELRQIKINEVQTDVSVDTKHQTLQGVAFPISRDAFQALEKLSKKQLNYVQLEIDIKNETIILANTENTELRDLPKRIPKDSARYHFFLYKHSHEGDYLESVVFIYSMPGYTCSIRERMLYSSCKSPLLEIVERQLQMDVIRKIEIDNGDELTADFLYDEVHPKQHAHKQSFAKPKGPAGKRGIRRLIRGPAEAEATTD
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------MSHQTGIQA
------CCCCCCCCC
25.05-
2Phosphorylation------MSHQTGIQA
------CCCCCCCCC
25.0526824392
136MalonylationVSLHGYKKYLLSQSS
EECCCHHHHHHHCCC
32.4226320211
136AcetylationVSLHGYKKYLLSQSS
EECCCHHHHHHHCCC
32.4222826441
137PhosphorylationSLHGYKKYLLSQSSP
ECCCHHHHHHHCCCC
14.5524925903
140PhosphorylationGYKKYLLSQSSPAPL
CHHHHHHHCCCCCCC
25.9724925903
142PhosphorylationKKYLLSQSSPAPLTA
HHHHHHCCCCCCCCH
34.6124925903
143PhosphorylationKYLLSQSSPAPLTAA
HHHHHCCCCCCCCHH
19.9025521595
148PhosphorylationQSSPAPLTAAEEELR
CCCCCCCCHHHHHHH
23.8224925903
164PhosphorylationIKINEVQTDVSVDTK
CCCCCCCCCCCCCCC
43.4726239621
167PhosphorylationNEVQTDVSVDTKHQT
CCCCCCCCCCCCCCE
19.6526239621
192UbiquitinationDAFQALEKLSKKQLN
HHHHHHHHHCHHHCC
59.9322790023
273PhosphorylationIRERMLYSSCKSPLL
HHHHHHHHCCCCHHH
25.8723984901
274PhosphorylationRERMLYSSCKSPLLE
HHHHHHHCCCCHHHH
16.4123984901
275GlutathionylationERMLYSSCKSPLLEI
HHHHHHCCCCHHHHH
4.0924333276
277PhosphorylationMLYSSCKSPLLEIVE
HHHHCCCCHHHHHHH
25.7127180971
309PhosphorylationELTADFLYDEVHPKQ
EEEEEEECCCCCHHH
15.2822817900
322PhosphorylationKQHAHKQSFAKPKGP
HHHCCCHHCCCCCCC
31.7926824392
348PhosphorylationGPAEAEATTD-----
CCCHHCCCCC-----
24.0127087446
349PhosphorylationPAEAEATTD------
CCHHCCCCC------
46.9225521595

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 TWF1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TWF1_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 TWF1_MOUSE !!

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

Oops, there are no PPI records of TWF1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TWF1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-349, AND MASSSPECTROMETRY.
"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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