Cofilin-1 - Homo sapiens (Human)

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Names and origin

Protein names

Recommended name:
    Cofilin-1
Alternative name(s):
    Cofilin, non-muscle isoform
    18 kDa phosphoprotein
    p18

Gene names

Name:	CFL1
Synonyms:	CFL

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	166 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods.
Subcellular location	Nucleus matrix. Cytoplasm › cytoskeleton. Note= Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide.
Tissue specificity	Widely distributed in various tissues.
Post-translational modification	Phosphorylated on Ser-3 in resting cells By similarity.
Sequence similarities	Belongs to the actin-binding proteins ADF family. Contains 1 ADF-H domain.

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Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Nucleus
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	Rho protein signal transduction Traceable author statement. Source: ProtInc anti-apoptosis Traceable author statement. Source: UniProtKB
Cellular component	nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
ATXN1	P54253	1	EBI-352733,EBI-930964
TAGLN	Q5U0D2	1	EBI-352733,EBI-1052446
YWHAZ	P63104	1	EBI-352733,EBI-347088

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 166

165

Cofilin-1

PRO_0000214898

Regions

Domain

4 – 153

150

ADF-H

Motif

30 – 34

Nuclear localization signal Potential

Amino acid modifications

Modified residue

N-acetylalanine

Modified residue

Phosphoserine; by NRK

Modified residue

Phosphothreonine

Modified residue

Phosphotyrosine By similarity

Modified residue

132

N6-acetyllysine

Modified residue

140

Phosphotyrosine

Modified residue

156

Phosphoserine

Secondary structure

166

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P23528-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 589EF8FC1EC13719
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FASTA

166

18,502

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Coding sequence of human placenta cofilin cDNA." Ogawa K., Tashima M., Yumoto Y., Okuda T., Sawada H., Okuma M., Maruyama Y. Nucleic Acids Res. 18:7169-7169(1990) [PubMed: 2263493] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"A provisional transcript map of the spinal muscular atrophy (SMA) critical region." 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. Eur. J. Hum. Genet. 3:87-95(1995) [PubMed: 7552146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pre-B cell.
[3]	"Mapping of human non-muscle type cofilin (CFL1) to chromosome 11q13 and muscle-type cofilin (CFL2) to chromosome 14." Gillett G.T., Fox M.F., Rowe P.S.N., Casimir C.M., Povey S. Ann. Hum. Genet. 60:201-211(1996) [PubMed: 8800436] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung, Ovary, Placenta and Uterus.
[6]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21. Tissue: Platelet.
[7]	Quadroni M., Bienvenut W.V. Submitted (MAR-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13 AND 54-73, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[8]	"Dephosphorylation of cofilin in stimulated platelets: roles for a GTP-binding protein and Ca2+." Davidson M.M., Haslam R.J. Biochem. J. 301:41-47(1994) [PubMed: 8037689] [Abstract] Cited for: PROTEIN SEQUENCE OF 52-71. Tissue: Platelet.
[9]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 54-73 AND 96-112, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[10]	"Cofilin phosphorylation and actin polymerization by NRK/NESK, a member 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) [PubMed: 12837278] [Abstract] Cited for: PHOSPHORYLATION AT SER-3 BY NRK.
[11]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." 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) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, MASS SPECTROMETRY.
[12]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND THR-25, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"Substrate and functional diversity of lysine acetylation revealed by a 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) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, MASS SPECTROMETRY. Tissue: Epithelium.
[15]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases 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. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, MASS SPECTROMETRY.
[16]	"Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor." Pope B.J., Zierler-Gould K.M., Kuhne R., Weeds A.G., Ball L.J. J. Biol. Chem. 279:4840-4848(2004) [PubMed: 14627701] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

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Web resources

Wikipedia

Cofilin entry

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Cross-references

Sequence databases

D00682 mRNA. Translation: BAA00589.1.
U21909 mRNA. Translation: AAA64501.1.
X95404 mRNA. Translation: CAA64685.1.
BT006846 mRNA. Translation: AAP35492.1.
BC011005 mRNA. Translation: AAH11005.1.
BC012265 mRNA. Translation: AAH12265.1.
BC012318 mRNA. Translation: AAH12318.1.
BC018256 mRNA. Translation: AAH18256.1.

PIR

S12632.

RefSeq

NP_005498.1.

UniGene

Hs.170622

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q8G	NMR	-	A	1-166	[»]
1Q8X	NMR	-	A	1-166	[»]

ModBase

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Protein-protein interaction databases

IntAct

P23528.

PTM databases

PhosphoSite

P23528.

2-D gel databases

SWISS-2DPAGE

P23528.

Aarhus/Ghent-2DPAGE

4. IEF.

DOSAC-COBS-2DPAGE

P23528.

OGP

P23528.

REPRODUCTION-2DPAGE

IPI00012011.

Genome annotation databases

Ensembl

ENSG00000172757. Homo sapiens. [Contig view]

GeneID

1072.

KEGG

hsa:1072.

Organism-specific databases

H-InvDB

HIX0009808.

HGNC

HGNC:1874. CFL1.

MIM

601442. gene.

PharmGKB

PA26423.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P23528.

HOVERGEN

P23528.

Gene expression databases

ArrayExpress

P23528.

CleanEx

HS_CFL1.

GermOnline

ENSG00000172757. Homo sapiens.

Family and domain databases

InterPro

IPR002108. Cofilin_actin_bd.
[Graphical view]

Pfam

PF00241. Cofilin_ADF. 1 hit.
[Graphical view]

PRINTS

PR00006. COFILIN.

SMART

SM00102. ADF. 1 hit.
[Graphical view]

PROSITE

PS51263. ADF_H. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P23528.

NextBio

4476.

SOURCE

Search...

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Entry information

Entry name

COF1_HUMAN

Accession

Primary (citable) accession number: P23528
Secondary accession number(s): Q53Y87, Q9UCA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents