Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Coactosin-like protein  

UniProtKB / Swiss-Prot ID :  COTL1_HUMAN

Gene Name (Synonyms) : 
COTL1, CLP  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytoskeleton (By similarity). 

Protein Function :  Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization. 

Protein Sequence MATKIDKEACRAAYNLVRDDGSAVIWVTFKYDGSTIVPGEQGAEYQHFIQQCTDDVRLFAFVRFTTGDAM...
Predicted Secondary Structure CCCCHHHHHHHHHHHHHHCCCCCCCEEEEEECCCEEEEECCCCCHHHHHHHCCCCEEEEEEEEEEECCCC...
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
14PhosphotyrosineCRAAYNLVR
HHHHHHHHH
14.19Phosphositeplus
Link
102N6-acetyllysineKTLVKEVVQ
HHHHHHHHC
48.15HPRD
Link
102N6-acetyllysineKTLVKEVVQ
HHHHHHHHC
48.15Phosphositeplus
Link
102N6-acetyllysine.KTLVKEVVQ
HHHHHHHHC
48.15UniProtKB
Link
110N6-acetyllysineQNFAKEFVI
CCCEEEEEE
47.77HPRD
Link
115PhosphoserineEFVISDRKE
EEEECCHHC
26.51PhosphoELM
Link
115PhosphoserineEFVISDRKE
EEEECCHHC
26.51Phosphositeplus
Link
115Phosphoserine.EFVISDRKE
EEEECCHHC
26.51UniProtKB
Link
126N6-acetyllysineEDFIKSELK
HHHHHHHHH
37.56HPRD
Link
126N6-acetyllysineEDFIKSELK
HHHHHHHHH
37.56Phosphositeplus
Link
126N6-acetyllysine.EDFIKSELK
HHHHHHHHH
37.56UniProtKB
Link
127PhosphoserineDFIKSELKK
HHHHHHHHH
43.26HPRD
Link
137PhosphotyrosineGGANYDAQT
CCCCCCCCC
16.48Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ACTS_HUMANin vitro
in vivo
HPRD:09482HPRD11583571
LOX5_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:09482HPRD11297527
10051563
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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
"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-102 AND LYS-126, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC.";
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.;
Proteomics 5:3589-3599(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures