Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Cofilin-1  

UniProtKB / Swiss-Prot ID :  COF1_HUMAN

Gene Name (Synonyms) : 
CFL1, CFL  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus matrix. Cytoplasm, cytoskeleton. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, lamellipodium membrane; Peripheral membrane protein; Cytoplasmic side. Note=Colocalizes with the actin cytoskeleton 

Protein Function :  Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization. 

Protein Sequence MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYAT...
Predicted Secondary Structure CCCCCEECHHHHHHHHHHHCCCCCCHHHHCCCCEEEEEEECCCCEEEEEEECCCCCCCCCCCCCCCCHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MASGVA
---CCCCCE
18.26UniProtKB
Link
3DePhosphoserine--MASGVAV
--CCCCCEE
32.28HPRD
Link
3Phosphoserine--MASGVAV
--CCCCCEE
32.28Phosphositeplus
Link
3Phosphoserine--MASGVAV
--CCCCCEE
32.28SysPTM
Link
3Phosphoserine (LIMK1)--MASGVAV
--CCCCCEE
32.28HPRD
Link
3Phosphoserine (LIMK1;LIMK1;LIMK2;TESK1;TESK2)--MASGVAV
--CCCCCEE
32.28PhosphoELM
Link
3Phosphoserine (LIMK2)--MASGVAV
--CCCCCEE
32.28HPRD
Link
3Phosphoserine (NRK)--MASGVAV
--CCCCCEE
32.28HPRD
Link
3Phosphoserine (TESK1)--MASGVAV
--CCCCCEE
32.28HPRD
Link
3Phosphoserine (TESK2)--MASGVAV
--CCCCCEE
32.28HPRD
Link
3Phosphoserine; by NRK.--MASGVAV
--CCCCCEE
32.28UniProtKB
Link
8PhosphoserineGVAVSDGVI
CCEECHHHH
20.93HPRD
Link
8PhosphoserineGVAVSDGVI
CCEECHHHH
20.93Phosphositeplus
Link
13Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DGVIKVFND
HHHHHHHHH
38.07Phosphositeplus
Link
13N6-acetyllysineDGVIKVFND
HHHHHHHHH
38.07HPRD
Link
13N6-acetyllysineDGVIKVFND
HHHHHHHHH
38.07Phosphositeplus
Link
13N6-acetyllysine.DGVIKVFND
HHHHHHHHH
38.07UniProtKB
Link
19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FNDMKVRKS
HHHHHCCCC
41.57Phosphositeplus
Link
19N6-acetyllysineFNDMKVRKS
HHHHHCCCC
41.57HPRD
Link
19N6-acetyllysineFNDMKVRKS
HHHHHCCCC
41.57Phosphositeplus
Link
19N6-acetyllysine.FNDMKVRKS
HHHHHCCCC
41.57UniProtKB
Link
23PhosphoserineKVRKSSTPE
HCCCCCCHH
28.96HPRD
Link
23PhosphoserineKVRKSSTPE
HCCCCCCHH
28.96Phosphositeplus
Link
24PhosphoserineVRKSSTPEE
CCCCCCHHH
51.52HPRD
Link
24PhosphoserineVRKSSTPEE
CCCCCCHHH
51.52Phosphositeplus
Link
25PhosphothreonineRKSSTPEEV
CCCCCHHHH
41.64HPRD
Link
25PhosphothreonineRKSSTPEEV
CCCCCHHHH
41.64PhosphoELM
Link
25PhosphothreonineRKSSTPEEV
CCCCCHHHH
41.64Phosphositeplus
Link
25Phosphothreonine.RKSSTPEEV
CCCCCHHHH
41.64UniProtKB
Link
41PhosphoserineLFCLSEDKK
EEEECCCCE
44.95HPRD
Link
41PhosphoserineLFCLSEDKK
EEEECCCCE
44.95Phosphositeplus
Link
41PhosphoserineLFCLSEDKK
EEEECCCCE
44.95SysPTM
Link
41Phosphoserine.LFCLSEDKK
EEEECCCCE
44.95UniProtKB
Link
45Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SEDKKNIIL
CCCCEEEEE
66.74Phosphositeplus
Link
53Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LEEGKEILV
EEECCCCCC
44.88Phosphositeplus
Link
68PhosphotyrosineVDDPYATFV
CCCCHHHHH
25.85HPRD
Link
68PhosphotyrosineVDDPYATFV
CCCCHHHHH
25.85PhosphoELM
Link
68PhosphotyrosineVDDPYATFV
CCCCHHHHH
25.85Phosphositeplus
Link
68Phosphotyrosine.VDDPYATFV
CCCCHHHHH
25.85UniProtKB
Link
73Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ATFVKMLPD
HHHHHHCCC
30.45Phosphositeplus
Link
73N6-acetyllysineATFVKMLPD
HHHHHHCCC
30.45HPRD
Link
73N6-acetyllysineATFVKMLPD
HHHHHHCCC
30.45Phosphositeplus
Link
73N6-acetyllysine.ATFVKMLPD
HHHHHHCCC
30.45UniProtKB
Link
82PhosphotyrosineKDCRYALYD
CCCEEEEEE
13.80Phosphositeplus
Link
85PhosphotyrosineRYALYDATY
EEEEEEEEE
8.72HPRD
Link
85PhosphotyrosineRYALYDATY
EEEEEEEEE
8.72Phosphositeplus
Link
88PhosphothreonineLYDATYETK
EEEEEEEEC
20.99Phosphositeplus
Link
89PhosphotyrosineYDATYETKE
EEEEEEECC
24.26HPRD
Link
89PhosphotyrosineYDATYETKE
EEEEEEECC
24.26Phosphositeplus
Link
89Phosphotyrosine.YDATYETKE
EEEEEEECC
24.26UniProtKB
Link
92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TYETKESKK
EEEECCCCC
48.31Phosphositeplus
Link
92N6-acetyllysineTYETKESKK
EEEECCCCC
48.31HPRD
Link
112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SAPLKSKMI
CCCHHHEEE
47.15Phosphositeplus
Link
114Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PLKSKMIYA
CHHHEEEEH
27.94Phosphositeplus
Link
114N6-acetyllysinePLKSKMIYA
CHHHEEEEH
27.94HPRD
Link
117PhosphotyrosineSKMIYASSK
HEEEEHHHH
9.27Phosphositeplus
Link
121N6-acetyllysineYASSKDAIK
EHHHHHHHH
49.00HPRD
Link
132N6-acetyllysineLTGIKHELQ
HCCEEEEEE
32.16Phosphositeplus
Link
132N6-acetyllysine.LTGIKHELQ
HCCEEEEEE
32.16UniProtKB
Link
139S-nitrosocysteineLQANCYEEV
EEECCHHHC
5.19HPRD
Link
140PhosphotyrosineQANCYEEVK
EECCHHHCC
18.22HPRD
Link
140PhosphotyrosineQANCYEEVK
EECCHHHCC
18.22PhosphoELM
Link
140PhosphotyrosineQANCYEEVK
EECCHHHCC
18.22Phosphositeplus
Link
140Phosphotyrosine.QANCYEEVK
EECCHHHCC
18.22UniProtKB
Link
144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YEEVKDRCT
HHHCCHHHH
42.61Phosphositeplus
Link
144N6-acetyllysineYEEVKDRCT
HHHCCHHHH
42.61HPRD
Link
144N6-acetyllysineYEEVKDRCT
HHHCCHHHH
42.61Phosphositeplus
Link
144N6-acetyllysine.YEEVKDRCT
HHHCCHHHH
42.61UniProtKB
Link
147S-nitrosocysteineVKDRCTLAE
CCHHHHHHH
5.40dbSNO
Link
156PhosphoserineKLGGSAVIS
HCCCEEEEE
19.98HPRD
Link
156PhosphoserineKLGGSAVIS
HCCCEEEEE
19.98PhosphoELM
Link
156PhosphoserineKLGGSAVIS
HCCCEEEEE
19.98Phosphositeplus
Link
156PhosphoserineKLGGSAVIS
HCCCEEEEE
19.98SysPTM
Link
156Phosphoserine.KLGGSAVIS
HCCCEEEEE
19.98UniProtKB
Link
164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SLEGKPL
EEECCCC
33.50Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ATX1_HUMANphysical interactionMINT-2857618MINT16713569
ATX1_HUMANphysical interactionMINT-2857637MINT16713569
ATX1_HUMANphysical interactionMINT-2857656MINT16713569
ATX1_HUMANphysical interactionMINT-2855860MINT16713569
ACTB_HUMANphysical interactionMINT-66034MINT16189514
1433G_HUMANphysical interactionMINT-51033MINT15598710
1433Z_HUMANphysical interactionMINT-15476MINT12361576
HS105_HUMANphysical interactionMINT-46015MINT14733918
HS105_HUMANphysical interactionMINT-46017MINT14733918
HS105_HUMANphysical interactionMINT-46016MINT14733918
MYCBP_HUMANphysical interactionMINT-65265MINT16169070
ACTB_HUMANphysical interactionEBI-752497
intact16189514
Q5U0D2_HUMANphysical interactionEBI-1077740
intact17353931
ACTC_HUMANin vivoHPRD:03261HPRD12207032
ACTS_HUMANin vitro
yeast 2-hybrid
HPRD:03261HPRD11707283
10366597
ACTA_HUMANin vitroHPRD:03261HPRD11707283
TPIS_HUMANin vivoHPRD:03261HPRD12359716
AT1A1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:03261HPRD11139403
1433Z_HUMANin vitro
in vivo
HPRD:03261HPRD12361576
12323073
1433G_HUMANin vitroHPRD:03261HPRD15598710
ATX1_HUMANyeast 2-hybridHPRD:03261HPRD16713569
MYCBP_HUMANyeast 2-hybridHPRD:03261HPRD16169070
CLCN5_HUMANin vitro
yeast 2-hybrid
HPRD:03261HPRD12904289
SSH2_HUMANENSP00000309629STRING
ACTC_HUMANENSP00000309629STRING
SSH3_HUMANENSP00000309629STRING
SSH1_HUMANENSP00000309629STRING
ACTG_HUMANENSP00000309629STRING
LIMK1_HUMANENSP00000309629STRING
ACTB_HUMANENSP00000309629STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-19; LYS-73 ANDLYS-144, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Cofilin phosphorylation and actin polymerization by NRK/NESK, amember of the germinal center kinase family.";
Nakano K., Kanai-Azuma M., Kanai Y., Moriyama K., Yazaki K.,Hayashi Y., Kitamura N.;
Exp. Cell Res. 287:219-227(2003).
Cited for: PHOSPHORYLATION AT SER-3 BY NRK.
"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-140, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND THR-25, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, 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 SER-3; SER-41 AND SER-156,AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89 AND TYR-140, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, 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 SER-3; TYR-68 AND SER-156,AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures