TWF1_HUMAN - dbPTM
TWF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TWF1_HUMAN
UniProt AC Q12792
Protein Name Twinfilin-1
Gene Name TWF1
Organism Homo sapiens (Human).
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 (By similarity)..
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 (By similarity)..
Protein Sequence MSHQTGIQASEDVKEIFARARNGKYRLLKISIENEQLVIGSYSQPSDSWDKDYDSFVLPLLEDKQPCYILFRLDSQNAQGYEWIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVFGTVKEDVSLHGYKKYLLSQSSPAPLTAAEEELRQIKINEVQTDVGVDTKHQTLQGVAFPISREAFQALEKLNNRQLNYVQLEIDIKNEIIILANTTNTELKDLPKRIPKDSARYHFFLYKHSHEGDYLESIVFIYSMPGYTCSIRERMLYSSCKSRLLEIVERQLQMDVIRKIEIDNGDELTADFLYEEVHPKQHAHKQSFAKPKGPAGKRGIRRLIRGPAETEATTD
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
2Phosphorylation------MSHQTGIQA
------CCCCCCCCC		25.0522199227
2Acetylation------MSHQTGIQA
------CCCCCCCCC		25.05-
5Phosphorylation---MSHQTGIQASED
---CCCCCCCCCCHH		30.7223663014
10PhosphorylationHQTGIQASEDVKEIF
CCCCCCCCHHHHHHH		20.2523663014
81PhosphorylationDSQNAQGYEWIFIAW
CCCCCCCCEEEEEEE		8.94142199
118UbiquitinationEFGGGHIKDEVFGTV
HHCCCCCCCCEEEEC		42.0129967540
124PhosphorylationIKDEVFGTVKEDVSL
CCCCEEEECCCEEEC		19.5528258704
130PhosphorylationGTVKEDVSLHGYKKY
EECCCEEECCCHHHH		27.2828258704
134PhosphorylationEDVSLHGYKKYLLSQ
CEEECCCHHHHHHHC		8.1128258704
1352-HydroxyisobutyrylationDVSLHGYKKYLLSQS
EEECCCHHHHHHHCC		39.26-
136UbiquitinationVSLHGYKKYLLSQSS
EECCCHHHHHHHCCC		32.4229967540
137PhosphorylationSLHGYKKYLLSQSSP
ECCCHHHHHHHCCCC		14.5529255136
140PhosphorylationGYKKYLLSQSSPAPL
CHHHHHHHCCCCCCC		25.9730266825
142PhosphorylationKKYLLSQSSPAPLTA
HHHHHHCCCCCCCCH		34.6130266825
143PhosphorylationKYLLSQSSPAPLTAA
HHHHHCCCCCCCCHH		19.9029255136
148PhosphorylationQSSPAPLTAAEEELR
CCCCCCCCHHHHHHH		23.8230266825
158UbiquitinationEEELRQIKINEVQTD
HHHHHHCCCCCCCCC		31.0129967540
161PhosphorylationLRQIKINEVQTDVGV
HHHCCCCCCCCCCCC		39.2018669648
1712-HydroxyisobutyrylationTDVGVDTKHQTLQGV
CCCCCCCCCCEECEE		29.29-
171UbiquitinationTDVGVDTKHQTLQGV
CCCCCCCCCCEECEE		29.2932015554
174PhosphorylationGVDTKHQTLQGVAFP
CCCCCCCEECEEEEE		22.2928857561
177PhosphorylationTKHQTLQGVAFPISR
CCCCEECEEEEECCH		18.81-
181PhosphorylationTLQGVAFPISREAFQ
EECEEEEECCHHHHH		17.5727251275
192UbiquitinationEAFQALEKLNNRQLN
HHHHHHHHHCCCCCC		58.3224816145
199UbiquitinationKLNNRQLNYVQLEID
HHCCCCCCEEEEEEE		26.9624816145
276UbiquitinationRMLYSSCKSRLLEIV
HHHHHHHHHHHHHHH		40.3324816145
2762-HydroxyisobutyrylationRMLYSSCKSRLLEIV
HHHHHHHHHHHHHHH		40.33-
277PhosphorylationMLYSSCKSRLLEIVE
HHHHHHHHHHHHHHH		32.2724043423
283UbiquitinationKSRLLEIVERQLQMD
HHHHHHHHHHHHCCH		3.4724816145
309PhosphorylationELTADFLYEEVHPKQ
EEEEHHHEEECCHHH		15.2727273156
316PhosphorylationYEEVHPKQHAHKQSF
EEECCHHHCCCCHHC		43.3715592455
322PhosphorylationKQHAHKQSFAKPKGP
HHCCCCHHCCCCCCC		31.7926657352
325AcetylationAHKQSFAKPKGPAGK
CCCHHCCCCCCCCCH		45.307669961
327AcetylationKQSFAKPKGPAGKRG
CHHCCCCCCCCCHHH		76.467669973
327PhosphorylationKQSFAKPKGPAGKRG
CHHCCCCCCCCCHHH		76.4615592455
343PhosphorylationRRLIRGPAETEATTD
HHHHCCCCCCCCCCC		38.88-
345PhosphorylationLIRGPAETEATTD--
HHCCCCCCCCCCC--		32.7823312004
348PhosphorylationGPAETEATTD-----
CCCCCCCCCC-----		25.8430243723
349PhosphorylationPAETEATTD------
CCCCCCCCC------		46.9228355574
356PhosphorylationTD-------------
CC-------------		24719451
367Phosphorylation------------------------
------------------------		18669648
383Phosphorylation----------------------------------------
----------------------------------------		-
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TWF1_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
UN45A_HUMANUNC45Aphysical
22939629
XPO2_HUMANCSE1Lphysical
22939629
UBE2A_HUMANUBE2Aphysical
22939629
UBXN1_HUMANUBXN1physical
22939629
TXND5_HUMANTXNDC5physical
22939629
XPP1_HUMANXPNPEP1physical
22939629
UBP28_HUMANUSP28physical
22939629
UBA3_HUMANUBA3physical
22939629
ZBED1_HUMANZBED1physical
22939629
IPO9_HUMANIPO9physical
22863883
MCTS1_HUMANMCTS1physical
22863883
UBP5_HUMANUSP5physical
22863883
SYWC_HUMANWARSphysical
22863883
AIMP1_HUMANAIMP1physical
26344197
MCA3_HUMANEEF1E1physical
26344197
HNRPF_HUMANHNRNPFphysical
26344197
ICAM1_HUMANICAM1physical
28514442
TIGAR_HUMANC12orf5physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TWF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-349, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, AND MASSSPECTROMETRY.

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