COF1_RAT - dbPTM
COF1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COF1_RAT
UniProt AC P45592
Protein Name Cofilin-1
Gene Name Cfl1
Organism Rattus norvegicus (Rat).
Sequence Length 166
Subcellular Localization Nucleus matrix . Cytoplasm, cytoskeleton . Cell projection, ruffle membrane
Peripheral membrane protein
Cytoplasmic side . Cell projection, lamellipodium membrane
Peripheral membrane protein
Cytoplasmic side . Cell projection, lamellipodium .
Protein Description 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. Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Required for neural tube morphogenesis and neural crest cell migration (By similarity)..
Protein Sequence MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYTTFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL
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------MASGVAVSD
------CCCCEEECC
18.269877327
3Phosphorylation-----MASGVAVSDG
-----CCCCEEECCC
32.2823984901
8PhosphorylationMASGVAVSDGVIKVF
CCCCEEECCCEEEEE
20.9322673903
13AcetylationAVSDGVIKVFNDMKV
EECCCEEEEECCCCC
38.0722902405
19AcetylationIKVFNDMKVRKSSTP
EEEECCCCCCCCCCH
41.57134749
22SuccinylationFNDMKVRKSSTPEEV
ECCCCCCCCCCHHHH
52.3126843850
23PhosphorylationNDMKVRKSSTPEEVK
CCCCCCCCCCHHHHH
28.9628432305
24PhosphorylationDMKVRKSSTPEEVKK
CCCCCCCCCHHHHHH
51.5228432305
25PhosphorylationMKVRKSSTPEEVKKR
CCCCCCCCHHHHHHH
41.6429779826
30AcetylationSSTPEEVKKRKKAVL
CCCHHHHHHHHCEEE
50.5722902405
41PhosphorylationKAVLFCLSEDKKNII
CEEEEECCCCCCEEE
44.9527097102
44AcetylationLFCLSEDKKNIILEE
EEECCCCCCEEEECC
43.6022902405
45UbiquitinationFCLSEDKKNIILEEG
EECCCCCCEEEECCC
66.74-
53UbiquitinationNIILEEGKEILVGDV
EEEECCCCEEEECCC
44.88-
68PhosphorylationGQTVDDPYTTFVKML
CCCCCCCCCCHHEEC
25.96-
70PhosphorylationTVDDPYTTFVKMLPD
CCCCCCCCHHEECCC
22.16-
73UbiquitinationDPYTTFVKMLPDKDC
CCCCCHHEECCCCCC
30.45-
73AcetylationDPYTTFVKMLPDKDC
CCCCCHHEECCCCCC
30.45-
78SuccinylationFVKMLPDKDCRYALY
HHEECCCCCCCHHEE
57.7126843850
89PhosphorylationYALYDATYETKESKK
HHEEECCCCCCCCCC
24.26-
92UbiquitinationYDATYETKESKKEDL
EECCCCCCCCCCCCE
48.31-
92AcetylationYDATYETKESKKEDL
EECCCCCCCCCCCCE
48.3122902405
112UbiquitinationAPESAPLKSKMIYAS
CCCCCCCCCCEEEEC
47.15-
114AcetylationESAPLKSKMIYASSK
CCCCCCCCEEEECCH
27.9422648279
114UbiquitinationESAPLKSKMIYASSK
CCCCCCCCEEEECCH
27.94-
121AcetylationKMIYASSKDAIKKKL
CEEEECCHHHHHHHH
49.008273227
140PhosphorylationHELQANCYEEVKDRC
HHHHHCHHHHHHHHC
18.2221940666
144AcetylationANCYEEVKDRCTLAE
HCHHHHHHHHCHHHH
42.6125786129
156PhosphorylationLAEKLGGSAVISLEG
HHHHHCCCEEEEECC
19.9821738781
160PhosphorylationLGGSAVISLEGKPL-
HCCCEEEEECCEEC-
17.4827097102

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
3SPhosphorylationKinaseILKQ13418
PSP
3SPhosphorylationKinaseLIMK1P53667
PSP
3SPhosphorylationKinaseLIMK1P53669
PSP
3SPhosphorylationKinaseLIMK2P53671
PSP
3SPhosphorylationKinaseTESK2Q924U5
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
3SPhosphorylation

9877327
3SPhosphorylation

9877327
24SPhosphorylation

-

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 COF1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AT1A1_RATAtp1a1physical
11139403

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COF1_RAT

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Complete amino acid sequences and phosphorylation sites, determinedby Edman degradation and mass spectrometry, of rat parotid destrin-and cofilin-like proteins.";
Kanamori T., Suzuki M., Titani K.;
Arch. Oral Biol. 43:955-967(1998).
Cited for: PROTEIN SEQUENCE OF 2-166, ACETYLATION AT ALA-2, PHOSPHORYLATION ATSER-3, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Complete amino acid sequences and phosphorylation sites, determinedby Edman degradation and mass spectrometry, of rat parotid destrin-and cofilin-like proteins.";
Kanamori T., Suzuki M., Titani K.;
Arch. Oral Biol. 43:955-967(1998).
Cited for: PROTEIN SEQUENCE OF 2-166, ACETYLATION AT ALA-2, PHOSPHORYLATION ATSER-3, AND MASS SPECTROMETRY.

TOP