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UniProtKB/Swiss-Prot entry P23528


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name COF1_HUMAN
Primary accession number P23528
Secondary accession numbers Q53Y87 Q9UCA2
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 103)
Name and origin of the protein
Protein name Cofilin-1
Synonyms Cofilin, non-muscle isoform
18 kDa phosphoprotein
p18
Gene name
Name: CFL1
Synonyms: CFL
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
DOI=10.1093/nar/18.23.7169; PubMed=2263493 [NCBI, ExPASy, EBI, Israel, Japan]
Ogawa K., Tashima M., Yumoto Y., Okuda T., Sawada H., Okuma M., Maruyama Y.;
"Coding sequence of human placenta cofilin cDNA.";
Nucleic Acids Res. 18:7169-7169(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pre-B cell;
PubMed=7552146 [NCBI, ExPASy, EBI, Israel, Japan]
van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., Anzevino R., Velona I., Den Dunnen J.T., Scheffer H., Brahe C., van Ommen G.J.B., Buys C.H.C.M.;
"A provisional transcript map of the spinal muscular atrophy (SMA) critical region.";
Eur. J. Hum. Genet. 3:87-95(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8800436 [NCBI, ExPASy, EBI, Israel, Japan]
Gillett G.T., Fox M.F., Rowe P.S.N., Casimir C.M., Povey S.;
"Mapping of human non-muscle type cofilin (CFL1) to chromosome 11q13 and muscle-type cofilin (CFL2) to chromosome 14.";
Ann. Hum. Genet. 60:201-211(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, Ovary, Placenta, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-21.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[7]
PROTEIN SEQUENCE OF 2-13 AND 54-73, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Quadroni M., Bienvenut W.V.;
Submitted (MAR-2005) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 52-71.
TISSUE=Platelet;
PubMed=8037689 [NCBI, ExPASy, EBI, Israel, Japan]
Davidson M.M., Haslam R.J.;
"Dephosphorylation of cofilin in stimulated platelets: roles for a GTP-binding protein and Ca2+.";
Biochem. J. 301:41-47(1994).
[9]
PROTEIN SEQUENCE OF 54-73 AND 96-112, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[10]
PHOSPHORYLATION AT SER-3 BY NRK.
DOI=10.1016/S0014-4827(03)00136-8; PubMed=12837278 [NCBI, ExPASy, EBI, Israel, Japan]
Nakano K., Kanai-Azuma M., Kanai Y., Moriyama K., Yazaki K., Hayashi Y., Kitamura N.;
"Cofilin phosphorylation and actin polymerization by NRK/NESK, a member of the germinal center kinase family.";
Exp. Cell Res. 287:219-227(2003).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND THR-25, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[16]
STRUCTURE BY NMR.
DOI=10.1074/jbc.M310148200; PubMed=14627701 [NCBI, ExPASy, EBI, Israel, Japan]
Pope B.J., Zierler-Gould K.M., Kuhne R., Weeds A.G., Ball L.J.;
"Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor.";
J. Biol. Chem. 279:4840-4848(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D00682; BAA00589.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U21909; AAA64501.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X95404; CAA64685.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006846; AAP35492.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011005; AAH11005.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012265; AAH12265.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012318; AAH12318.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018256; AAH18256.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S12632; S12632.
RefSeq NP_005498.1; -.
UniGene Hs.170622
3D structure databases
PDB
1Q8G; NMR; -; A=1-166.[ExPASy / RCSB / EBI]
1Q8X; NMR; -; A=1-166.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1Q8G; -.
1Q8X; -.
ModBase P23528.
Protein-protein interaction databases
IntAct P23528; -.
PTM databases
PhosphoSite P23528; -.
2D gel databases
SWISS-2DPAGE P23528; -.
Aarhus/Ghent-2DPAGE 4; IEF.
DOSAC-COBS-2DPAGE P23528; -.
OGP P23528; -.
REPRODUCTION-2DPAGE IPI00012011; -.
Organism-specific databases
H-InvDB HIX0009808; -.
HGNC HGNC:1874; CFL1.
GenAtlas CFL1.
MIM 601442; gene. [NCBI / EBI]
PharmGKB PA26423; -.
GeneCards P23528.
Gene expression databases
ArrayExpress P23528; -.
CleanEx HS_CFL1; -.
GermOnline ENSG00000172757; Homo sapiens.
Ontologies
GO
GO:0016363; Cellular component: nuclear matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003779; Molecular function: actin binding (inferred from electronic annotation from InterPro).
GO:0006916; Biological process: anti-apoptosis (traceable author statement from UniProtKB).
GO:0007266; Biological process: Rho protein signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR002108; Cofilin_actin_bd.
Graphical view of domain structure.
Pfam PF00241; Cofilin_ADF; 1.
Pfam graphical view of domain structure.
PRINTS PR00006; COFILIN.
SMART SM00102; ADF; 1.
SMART graphical view of domain structure.
PROSITE PS51263; ADF_H; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P23528.
ProtoNet P23528.
Genome annotation databases
Ensembl ENSG00000172757; Homo sapiens. [Contig view]
GeneID 1072; -.
KEGG hsa:1072; -.
Phylogenomic databases
HOGENOM P23528; -.
HOVERGEN P23528; -.
Other
LinkHub P23528; -.
NextBio 4476; -.
SOURCE CFL1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Direct protein sequencing; Nucleus; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   166  165     Cofilin-1. PRO_0000214898
DOMAIN   4   153  150     ADF-H. 
MOTIF   30    34  5     Nuclear localization signal (Potential). 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   3     3        Phosphoserine; by NRK. 
MOD_RES   25    25        Phosphothreonine. 
MOD_RES   68    68        Phosphotyrosine (By similarity). 
MOD_RES   132   132        N6-acetyllysine. 
MOD_RES   140   140        Phosphotyrosine. 
MOD_RES   156   156        Phosphoserine. 
HELIX   10    20  11      
HELIX   26    29  4      
STRAND   33    40  8      
STRAND   42    45  4      
STRAND   47    57  11      
HELIX   58    60  3      
TURN   61    63  3      
HELIX   67    73  7      
STRAND   89    93  5      
STRAND   99   104  6      
HELIX   111   113  3      
HELIX   115   128  14      
STRAND   132   139  8      
HELIX   140   143  4      
HELIX   146   149  4      
TURN   150   154  5      
HELIX   155   157  3      
STRAND   161   164  4      
Sequence information
Length: 166 AA [This is the length of the unprocessed precursor] Molecular weight: 18502 Da [This is the MW of the unprocessed precursor] CRC64: 589EF8FC1EC13719 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV 

        70         80         90        100        110        120 
GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS 

       130        140        150        160 
KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL 

P23528 in FASTA format

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View entry in raw text format (no links)
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