CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020529
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Coactosin-like protein 
Protein Synonyms/Alias
  
Gene Name
 Cotl1 
Gene Synonyms/Alias
 Clp 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
7*MATKIDKEACRAAYacetylation[1]
75DAMSKRSKFALITWIacetylation[1]
102GTDKTLVKEVVQNFAacetylation[1]
102GTDKTLVKEVVQNFAubiquitination[2]
110EVVQNFAKEFVISDRacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization. Acts as a chaperone for ALOX5 (5LO), influencing both its stability and activity in leukotrienes synthesis (By similarity). 
Sequence Annotation
 DOMAIN 2 130 ADF-H.
 REGION 66 75 Flexible and important for F-actin
 MOD_RES 102 102 N6-acetyllysine (By similarity).
 MOD_RES 141 141 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Actin-binding; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 142 AA 
Protein Sequence
MATKIDKEAC RAAYNLVRDD GSAVIWVTFR YDGATIVPGD QGADYQHFIQ QCTDDVRLFA 60
FVRFTTGDAM SKRSKFALIT WIGEDVSGLQ RAKTGTDKTL VKEVVQNFAK EFVISDRKEL 120
EEDFIRSELK KAGGANYDAQ SE 142 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
 GO:0003779; F:actin binding; IDA:MGI.
 GO:0050832; P:defense response to fungus; IDA:UniProtKB. 
Interpro
 IPR002108; Actin-bd_cofilin/tropomyosin. 
Pfam
 PF00241; Cofilin_ADF 
SMART
 SM00102; ADF 
PROSITE
 PS51263; ADF_H 
PRINTS