Full text data of CFL1
CFL1
(CFL)
[Confidence: high (present in two of the MS resources)]
Cofilin-1 (18 kDa phosphoprotein; p18; Cofilin, non-muscle isoform)
Cofilin-1 (18 kDa phosphoprotein; p18; Cofilin, non-muscle isoform)
hRBCD
IPI00012011
IPI00012011 Cofilin 1 (non-musCle) Widely distributed in various tissues: Platelet, B-cells, 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 soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00012011 Cofilin 1 (non-musCle) Widely distributed in various tissues: Platelet, B-cells, 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 soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P23528
ID COF1_HUMAN Reviewed; 166 AA.
AC P23528; B3KUQ1; Q53Y87; Q9UCA2;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 159.
DE RecName: Full=Cofilin-1;
DE AltName: Full=18 kDa phosphoprotein;
DE Short=p18;
DE AltName: Full=Cofilin, non-muscle isoform;
GN Name=CFL1; Synonyms=CFL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=2263493; DOI=10.1093/nar/18.23.7169;
RA Ogawa K., Tashima M., Yumoto Y., Okuda T., Sawada H., Okuma M.,
RA Maruyama Y.;
RT "Coding sequence of human placenta cofilin cDNA.";
RL Nucleic Acids Res. 18:7169-7169(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pre-B cell;
RX PubMed=7552146;
RA van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J.,
RA Anzevino R., Velona I., Den Dunnen J.T., Scheffer H., Brahe C.,
RA van Ommen G.J.B., Buys C.H.C.M.;
RT "A provisional transcript map of the spinal muscular atrophy (SMA)
RT critical region.";
RL Eur. J. Hum. Genet. 3:87-95(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8800436; DOI=10.1111/j.1469-1809.1996.tb00423.x;
RA Gillett G.T., Fox M.F., Rowe P.S.N., Casimir C.M., Povey S.;
RT "Mapping of human non-muscle type cofilin (CFL1) to chromosome 11q13
RT and muscle-type cofilin (CFL2) to chromosome 14.";
RL Ann. Hum. Genet. 60:201-211(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Ovary, Placenta, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-21.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP PROTEIN SEQUENCE OF 2-13 AND 54-73, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Quadroni M., Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 34-45; 54-73; 82-92; 96-112; 133-146 AND 153-166,
RP AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 52-71.
RC TISSUE=Platelet;
RX PubMed=8037689;
RA Davidson M.M., Haslam R.J.;
RT "Dephosphorylation of cofilin in stimulated platelets: roles for a
RT GTP-binding protein and Ca2+.";
RL Biochem. J. 301:41-47(1994).
RN [12]
RP PHOSPHORYLATION AT SER-3 BY NRK.
RX PubMed=12837278; DOI=10.1016/S0014-4827(03)00136-8;
RA Nakano K., Kanai-Azuma M., Kanai Y., Moriyama K., Yazaki K.,
RA Hayashi Y., Kitamura N.;
RT "Cofilin phosphorylation and actin polymerization by NRK/NESK, a
RT member of the germinal center kinase family.";
RL Exp. Cell Res. 287:219-227(2003).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEPHOSPHORYLATION BY PDXP.
RX PubMed=15580268; DOI=10.1038/ncb1201;
RA Gohla A., Birkenfeld J., Bokoch G.M.;
RT "Chronophin, a novel HAD-type serine protein phosphatase, regulates
RT cofilin-dependent actin dynamics.";
RL Nat. Cell Biol. 7:21-29(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [16]
RP INDUCTION, AND MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells
RT reveal differential cellular gene expression in response to
RT enterovirus 71 infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-156, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-68 AND SER-156, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-13; LYS-73 AND
RP LYS-144, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3; THR-25 AND SER-156, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and
RT migration.";
RL BMC Biol. 9:54-54(2011).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [27]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=23633677; DOI=10.1126/scisignal.2003627;
RA Borroni E.M., Cancellieri C., Vacchini A., Benureau Y., Lagane B.,
RA Bachelerie F., Arenzana-Seisdedos F., Mizuno K., Mantovani A.,
RA Bonecchi R., Locati M.;
RT "Beta-arrestin-dependent activation of the cofilin pathway is required
RT for the scavenging activity of the atypical chemokine receptor D6.";
RL Sci. Signal. 6:RA30-RA30(2013).
RN [28]
RP STRUCTURE BY NMR.
RX PubMed=14627701; DOI=10.1074/jbc.M310148200;
RA Pope B.J., Zierler-Gould K.M., Kuhne R., Weeds A.G., Ball L.J.;
RT "Solution structure of human cofilin: actin binding, pH sensitivity,
RT and relationship to actin-depolymerizing factor.";
RL J. Biol. Chem. 279:4840-4848(2004).
CC -!- FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin
CC depolymerizing activity. Regulates actin cytoskeleton dynamics.
CC Important for normal progress through mitosis and normal
CC cytokinesis. Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. Required for the up-regulation of
CC atypical chemokine receptor ACKR2 from endosomal compartment to
CC cell membrane, increasing its efficiency in chemokine uptake and
CC degradation.
CC -!- SUBUNIT: Can bind G- and F-actin in a 1:1 ratio of cofilin to
CC actin. It is a major component of intranuclear and cytoplasmic
CC actin rods.
CC -!- INTERACTION:
CC P54253:ATXN1; NbExp=5; IntAct=EBI-352733, EBI-930964;
CC Q13393:PLD1; NbExp=4; IntAct=EBI-352733, EBI-2827556;
CC O14939:PLD2; NbExp=2; IntAct=EBI-352733, EBI-1053996;
CC Q8WYL5:SSH1; NbExp=2; IntAct=EBI-352733, EBI-1222387;
CC P63104:YWHAZ; NbExp=3; IntAct=EBI-352733, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix. Cytoplasm, cytoskeleton.
CC Cell projection, ruffle membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cell projection, lamellipodium membrane;
CC Peripheral membrane protein; Cytoplasmic side. Note=Colocalizes
CC with the actin cytoskeleton in membrane ruffles and lamellipodia.
CC Detected at the cleavage furrow and contractile ring during
CC cytokinesis. Almost completely in nucleus in cells exposed to heat
CC shock or 10% dimethyl sulfoxide.
CC -!- TISSUE SPECIFICITY: Widely distributed in various tissues.
CC -!- INDUCTION: Up-regulated in response to enterovirus 71 (EV71)
CC infection (at protein level).
CC -!- PTM: Inactivated by phosphorylation on Ser-3. Phosphorylated on
CC Ser-3 in resting cells (By similarity). Dephosphorylated by
CC PDXP/chronophin; this restores its activity in promoting actin
CC filament depolymerization. The phosphorylation of Ser-24 may
CC prevent recognition of the nuclear localization signal (By
CC similarity). Phosphorylated via a ARRB1-RAC1-LIMK1-PAK1 cascade
CC upon active ligand stimulation of atypical chemokine receptor
CC ACKR2.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC -!- SIMILARITY: Contains 1 ADF-H domain.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Cofilin entry;
CC URL="http://en.wikipedia.org/wiki/Cofilin";
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DR EMBL; D00682; BAA00589.1; -; mRNA.
DR EMBL; U21909; AAA64501.1; -; mRNA.
DR EMBL; X95404; CAA64685.1; -; mRNA.
DR EMBL; BT006846; AAP35492.1; -; mRNA.
DR EMBL; AK097690; BAG53513.1; -; mRNA.
DR EMBL; CH471076; EAW74449.1; -; Genomic_DNA.
DR EMBL; BC011005; AAH11005.1; -; mRNA.
DR EMBL; BC012265; AAH12265.1; -; mRNA.
DR EMBL; BC012318; AAH12318.1; -; mRNA.
DR EMBL; BC018256; AAH18256.1; -; mRNA.
DR PIR; S12632; S12632.
DR RefSeq; NP_005498.1; NM_005507.2.
DR UniGene; Hs.170622; -.
DR PDB; 1Q8G; NMR; -; A=1-166.
DR PDB; 1Q8X; NMR; -; A=1-166.
DR PDB; 3J0S; EM; 9.00 A; M/N/O/P/Q/R/S/T/U/V/W/X=1-166.
DR PDB; 4BEX; X-ray; 2.80 A; 1=1-166.
DR PDBsum; 1Q8G; -.
DR PDBsum; 1Q8X; -.
DR PDBsum; 3J0S; -.
DR PDBsum; 4BEX; -.
DR ProteinModelPortal; P23528; -.
DR SMR; P23528; 1-166.
DR DIP; DIP-33000N; -.
DR IntAct; P23528; 44.
DR MINT; MINT-4999473; -.
DR STRING; 9606.ENSP00000309629; -.
DR ChEMBL; CHEMBL1075129; -.
DR PhosphoSite; P23528; -.
DR DMDM; 116848; -.
DR DOSAC-COBS-2DPAGE; P23528; -.
DR OGP; P23528; -.
DR REPRODUCTION-2DPAGE; IPI00012011; -.
DR SWISS-2DPAGE; P23528; -.
DR UCD-2DPAGE; P23528; -.
DR PaxDb; P23528; -.
DR PRIDE; P23528; -.
DR DNASU; 1072; -.
DR Ensembl; ENST00000308162; ENSP00000309629; ENSG00000172757.
DR Ensembl; ENST00000525451; ENSP00000432660; ENSG00000172757.
DR GeneID; 1072; -.
DR KEGG; hsa:1072; -.
DR UCSC; uc001ofs.3; human.
DR CTD; 1072; -.
DR GeneCards; GC11M065622; -.
DR H-InvDB; HIX0009009; -.
DR HGNC; HGNC:1874; CFL1.
DR HPA; CAB037077; -.
DR MIM; 601442; gene.
DR neXtProt; NX_P23528; -.
DR PharmGKB; PA26423; -.
DR eggNOG; NOG286948; -.
DR HOGENOM; HOG000039697; -.
DR HOVERGEN; HBG000381; -.
DR InParanoid; P23528; -.
DR KO; K05765; -.
DR OrthoDB; EOG7353Z9; -.
DR PhylomeDB; P23528; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P23528; -.
DR ChiTaRS; CFL1; human.
DR EvolutionaryTrace; P23528; -.
DR GeneWiki; Cofilin_1; -.
DR GenomeRNAi; 1072; -.
DR NextBio; 4476; -.
DR PMAP-CutDB; P23528; -.
DR PRO; PR:P23528; -.
DR ArrayExpress; P23528; -.
DR Bgee; P23528; -.
DR Genevestigator; P23528; -.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
DR GO; GO:0030042; P:actin filament depolymerization; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0000910; P:cytokinesis; IEA:Ensembl.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
DR GO; GO:0001842; P:neural fold formation; IEA:Ensembl.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0043200; P:response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:ProtInc.
DR InterPro; IPR002108; Actin-bd_cofilin/tropomyosin.
DR InterPro; IPR017904; ADF/Cofilin/Destrin.
DR PANTHER; PTHR11913; PTHR11913; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR PRINTS; PR00006; COFILIN.
DR SMART; SM00102; ADF; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell membrane;
KW Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 166 Cofilin-1.
FT /FTId=PRO_0000214898.
FT DOMAIN 4 153 ADF-H.
FT MOTIF 30 34 Nuclear localization signal (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 3 3 Phosphoserine; by NRK.
FT MOD_RES 8 8 Phosphoserine (By similarity).
FT MOD_RES 13 13 N6-acetyllysine.
FT MOD_RES 25 25 Phosphothreonine.
FT MOD_RES 68 68 Phosphotyrosine.
FT MOD_RES 73 73 N6-acetyllysine.
FT MOD_RES 140 140 Phosphotyrosine.
FT MOD_RES 144 144 N6-acetyllysine.
FT MOD_RES 156 156 Phosphoserine.
FT HELIX 9 18
FT TURN 28 30
FT STRAND 31 40
FT STRAND 42 45
FT STRAND 46 56
FT HELIX 57 59
FT HELIX 60 64
FT HELIX 67 74
FT STRAND 77 79
FT STRAND 81 90
FT STRAND 95 104
FT HELIX 111 119
FT HELIX 121 125
FT STRAND 133 137
FT HELIX 140 143
FT HELIX 146 154
FT HELIX 155 157
FT STRAND 161 164
SQ SEQUENCE 166 AA; 18502 MW; 589EF8FC1EC13719 CRC64;
MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV
GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS
KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL
//
ID COF1_HUMAN Reviewed; 166 AA.
AC P23528; B3KUQ1; Q53Y87; Q9UCA2;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 159.
DE RecName: Full=Cofilin-1;
DE AltName: Full=18 kDa phosphoprotein;
DE Short=p18;
DE AltName: Full=Cofilin, non-muscle isoform;
GN Name=CFL1; Synonyms=CFL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=2263493; DOI=10.1093/nar/18.23.7169;
RA Ogawa K., Tashima M., Yumoto Y., Okuda T., Sawada H., Okuma M.,
RA Maruyama Y.;
RT "Coding sequence of human placenta cofilin cDNA.";
RL Nucleic Acids Res. 18:7169-7169(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pre-B cell;
RX PubMed=7552146;
RA van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J.,
RA Anzevino R., Velona I., Den Dunnen J.T., Scheffer H., Brahe C.,
RA van Ommen G.J.B., Buys C.H.C.M.;
RT "A provisional transcript map of the spinal muscular atrophy (SMA)
RT critical region.";
RL Eur. J. Hum. Genet. 3:87-95(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8800436; DOI=10.1111/j.1469-1809.1996.tb00423.x;
RA Gillett G.T., Fox M.F., Rowe P.S.N., Casimir C.M., Povey S.;
RT "Mapping of human non-muscle type cofilin (CFL1) to chromosome 11q13
RT and muscle-type cofilin (CFL2) to chromosome 14.";
RL Ann. Hum. Genet. 60:201-211(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Ovary, Placenta, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-21.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP PROTEIN SEQUENCE OF 2-13 AND 54-73, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Quadroni M., Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 34-45; 54-73; 82-92; 96-112; 133-146 AND 153-166,
RP AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 52-71.
RC TISSUE=Platelet;
RX PubMed=8037689;
RA Davidson M.M., Haslam R.J.;
RT "Dephosphorylation of cofilin in stimulated platelets: roles for a
RT GTP-binding protein and Ca2+.";
RL Biochem. J. 301:41-47(1994).
RN [12]
RP PHOSPHORYLATION AT SER-3 BY NRK.
RX PubMed=12837278; DOI=10.1016/S0014-4827(03)00136-8;
RA Nakano K., Kanai-Azuma M., Kanai Y., Moriyama K., Yazaki K.,
RA Hayashi Y., Kitamura N.;
RT "Cofilin phosphorylation and actin polymerization by NRK/NESK, a
RT member of the germinal center kinase family.";
RL Exp. Cell Res. 287:219-227(2003).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEPHOSPHORYLATION BY PDXP.
RX PubMed=15580268; DOI=10.1038/ncb1201;
RA Gohla A., Birkenfeld J., Bokoch G.M.;
RT "Chronophin, a novel HAD-type serine protein phosphatase, regulates
RT cofilin-dependent actin dynamics.";
RL Nat. Cell Biol. 7:21-29(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [16]
RP INDUCTION, AND MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells
RT reveal differential cellular gene expression in response to
RT enterovirus 71 infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-156, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-68 AND SER-156, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-13; LYS-73 AND
RP LYS-144, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3; THR-25 AND SER-156, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and
RT migration.";
RL BMC Biol. 9:54-54(2011).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [27]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=23633677; DOI=10.1126/scisignal.2003627;
RA Borroni E.M., Cancellieri C., Vacchini A., Benureau Y., Lagane B.,
RA Bachelerie F., Arenzana-Seisdedos F., Mizuno K., Mantovani A.,
RA Bonecchi R., Locati M.;
RT "Beta-arrestin-dependent activation of the cofilin pathway is required
RT for the scavenging activity of the atypical chemokine receptor D6.";
RL Sci. Signal. 6:RA30-RA30(2013).
RN [28]
RP STRUCTURE BY NMR.
RX PubMed=14627701; DOI=10.1074/jbc.M310148200;
RA Pope B.J., Zierler-Gould K.M., Kuhne R., Weeds A.G., Ball L.J.;
RT "Solution structure of human cofilin: actin binding, pH sensitivity,
RT and relationship to actin-depolymerizing factor.";
RL J. Biol. Chem. 279:4840-4848(2004).
CC -!- FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin
CC depolymerizing activity. Regulates actin cytoskeleton dynamics.
CC Important for normal progress through mitosis and normal
CC cytokinesis. Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. Required for the up-regulation of
CC atypical chemokine receptor ACKR2 from endosomal compartment to
CC cell membrane, increasing its efficiency in chemokine uptake and
CC degradation.
CC -!- SUBUNIT: Can bind G- and F-actin in a 1:1 ratio of cofilin to
CC actin. It is a major component of intranuclear and cytoplasmic
CC actin rods.
CC -!- INTERACTION:
CC P54253:ATXN1; NbExp=5; IntAct=EBI-352733, EBI-930964;
CC Q13393:PLD1; NbExp=4; IntAct=EBI-352733, EBI-2827556;
CC O14939:PLD2; NbExp=2; IntAct=EBI-352733, EBI-1053996;
CC Q8WYL5:SSH1; NbExp=2; IntAct=EBI-352733, EBI-1222387;
CC P63104:YWHAZ; NbExp=3; IntAct=EBI-352733, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix. Cytoplasm, cytoskeleton.
CC Cell projection, ruffle membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cell projection, lamellipodium membrane;
CC Peripheral membrane protein; Cytoplasmic side. Note=Colocalizes
CC with the actin cytoskeleton in membrane ruffles and lamellipodia.
CC Detected at the cleavage furrow and contractile ring during
CC cytokinesis. Almost completely in nucleus in cells exposed to heat
CC shock or 10% dimethyl sulfoxide.
CC -!- TISSUE SPECIFICITY: Widely distributed in various tissues.
CC -!- INDUCTION: Up-regulated in response to enterovirus 71 (EV71)
CC infection (at protein level).
CC -!- PTM: Inactivated by phosphorylation on Ser-3. Phosphorylated on
CC Ser-3 in resting cells (By similarity). Dephosphorylated by
CC PDXP/chronophin; this restores its activity in promoting actin
CC filament depolymerization. The phosphorylation of Ser-24 may
CC prevent recognition of the nuclear localization signal (By
CC similarity). Phosphorylated via a ARRB1-RAC1-LIMK1-PAK1 cascade
CC upon active ligand stimulation of atypical chemokine receptor
CC ACKR2.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC -!- SIMILARITY: Contains 1 ADF-H domain.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Cofilin entry;
CC URL="http://en.wikipedia.org/wiki/Cofilin";
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DR EMBL; D00682; BAA00589.1; -; mRNA.
DR EMBL; U21909; AAA64501.1; -; mRNA.
DR EMBL; X95404; CAA64685.1; -; mRNA.
DR EMBL; BT006846; AAP35492.1; -; mRNA.
DR EMBL; AK097690; BAG53513.1; -; mRNA.
DR EMBL; CH471076; EAW74449.1; -; Genomic_DNA.
DR EMBL; BC011005; AAH11005.1; -; mRNA.
DR EMBL; BC012265; AAH12265.1; -; mRNA.
DR EMBL; BC012318; AAH12318.1; -; mRNA.
DR EMBL; BC018256; AAH18256.1; -; mRNA.
DR PIR; S12632; S12632.
DR RefSeq; NP_005498.1; NM_005507.2.
DR UniGene; Hs.170622; -.
DR PDB; 1Q8G; NMR; -; A=1-166.
DR PDB; 1Q8X; NMR; -; A=1-166.
DR PDB; 3J0S; EM; 9.00 A; M/N/O/P/Q/R/S/T/U/V/W/X=1-166.
DR PDB; 4BEX; X-ray; 2.80 A; 1=1-166.
DR PDBsum; 1Q8G; -.
DR PDBsum; 1Q8X; -.
DR PDBsum; 3J0S; -.
DR PDBsum; 4BEX; -.
DR ProteinModelPortal; P23528; -.
DR SMR; P23528; 1-166.
DR DIP; DIP-33000N; -.
DR IntAct; P23528; 44.
DR MINT; MINT-4999473; -.
DR STRING; 9606.ENSP00000309629; -.
DR ChEMBL; CHEMBL1075129; -.
DR PhosphoSite; P23528; -.
DR DMDM; 116848; -.
DR DOSAC-COBS-2DPAGE; P23528; -.
DR OGP; P23528; -.
DR REPRODUCTION-2DPAGE; IPI00012011; -.
DR SWISS-2DPAGE; P23528; -.
DR UCD-2DPAGE; P23528; -.
DR PaxDb; P23528; -.
DR PRIDE; P23528; -.
DR DNASU; 1072; -.
DR Ensembl; ENST00000308162; ENSP00000309629; ENSG00000172757.
DR Ensembl; ENST00000525451; ENSP00000432660; ENSG00000172757.
DR GeneID; 1072; -.
DR KEGG; hsa:1072; -.
DR UCSC; uc001ofs.3; human.
DR CTD; 1072; -.
DR GeneCards; GC11M065622; -.
DR H-InvDB; HIX0009009; -.
DR HGNC; HGNC:1874; CFL1.
DR HPA; CAB037077; -.
DR MIM; 601442; gene.
DR neXtProt; NX_P23528; -.
DR PharmGKB; PA26423; -.
DR eggNOG; NOG286948; -.
DR HOGENOM; HOG000039697; -.
DR HOVERGEN; HBG000381; -.
DR InParanoid; P23528; -.
DR KO; K05765; -.
DR OrthoDB; EOG7353Z9; -.
DR PhylomeDB; P23528; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P23528; -.
DR ChiTaRS; CFL1; human.
DR EvolutionaryTrace; P23528; -.
DR GeneWiki; Cofilin_1; -.
DR GenomeRNAi; 1072; -.
DR NextBio; 4476; -.
DR PMAP-CutDB; P23528; -.
DR PRO; PR:P23528; -.
DR ArrayExpress; P23528; -.
DR Bgee; P23528; -.
DR Genevestigator; P23528; -.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
DR GO; GO:0030042; P:actin filament depolymerization; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0000910; P:cytokinesis; IEA:Ensembl.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
DR GO; GO:0001842; P:neural fold formation; IEA:Ensembl.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0043200; P:response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:ProtInc.
DR InterPro; IPR002108; Actin-bd_cofilin/tropomyosin.
DR InterPro; IPR017904; ADF/Cofilin/Destrin.
DR PANTHER; PTHR11913; PTHR11913; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR PRINTS; PR00006; COFILIN.
DR SMART; SM00102; ADF; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell membrane;
KW Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 166 Cofilin-1.
FT /FTId=PRO_0000214898.
FT DOMAIN 4 153 ADF-H.
FT MOTIF 30 34 Nuclear localization signal (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 3 3 Phosphoserine; by NRK.
FT MOD_RES 8 8 Phosphoserine (By similarity).
FT MOD_RES 13 13 N6-acetyllysine.
FT MOD_RES 25 25 Phosphothreonine.
FT MOD_RES 68 68 Phosphotyrosine.
FT MOD_RES 73 73 N6-acetyllysine.
FT MOD_RES 140 140 Phosphotyrosine.
FT MOD_RES 144 144 N6-acetyllysine.
FT MOD_RES 156 156 Phosphoserine.
FT HELIX 9 18
FT TURN 28 30
FT STRAND 31 40
FT STRAND 42 45
FT STRAND 46 56
FT HELIX 57 59
FT HELIX 60 64
FT HELIX 67 74
FT STRAND 77 79
FT STRAND 81 90
FT STRAND 95 104
FT HELIX 111 119
FT HELIX 121 125
FT STRAND 133 137
FT HELIX 140 143
FT HELIX 146 154
FT HELIX 155 157
FT STRAND 161 164
SQ SEQUENCE 166 AA; 18502 MW; 589EF8FC1EC13719 CRC64;
MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV
GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS
KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL
//
MIM
601442
*RECORD*
*FIELD* NO
601442
*FIELD* TI
*601442 COFILIN 1; CFL1
;;COFILIN, NONMUSCLE
*FIELD* TX
DESCRIPTION
Cofilin is a widely distributed intracellular actin-modulating protein
read morethat binds and depolymerizes filamentous F-actin and inhibits the
polymerization of monomeric G-actin in a pH-dependent manner. It is
involved in the translocation of actin-cofilin complex from cytoplasm to
nucleus (summary by Gillett et al., 1996).
CLONING
Two cofilin isoforms have been identified in mouse: muscle, or M-type
(601443) and nonmuscle, or NM-type (Ono et al., 1994). The mouse M-type
cofilin is expressed in heart, skeletal muscle, and testis, whereas the
NM-type is found in a wide variety of tissues, including heart and
testis. NM-type cofilin expression is minimal in mature mammalian
skeletal muscle. Ogawa et al. (1990) isolated a cDNA encoding a
placentally expressed cofilin. Gillett et al. (1996) cloned CFL1, a
nonmuscle-type cofilin, from a human promyelocytic cDNA library. The
cDNA encodes a 166-amino acid polypeptide with a molecular mass of
approximately 18.5 kD.
GENE FUNCTION
Cofilin exhibits actin-depolymerizing activity that is inhibited as a
result of its phosphorylation by LIM kinase (see 601329). Maekawa et al.
(1999) demonstrated that cofilin was phosphorylated during
lysophosphatidic acid-induced, Rho-mediated neurite retraction. This
phosphorylation was sensitive to Y-27632, a specific inhibitor of the
Rho-associated kinase ROCK (601702). ROCK, which is a downstream
effector of Rho, did not phosphorylate cofilin directly but
phosphorylated LIM kinase, which in turn was activated to phosphorylate
cofilin. Maekawa et al. (1999) concluded that phosphorylation of LIM
kinase by ROCK and, consequently, increased phosphorylation of cofilin
by LIM kinase, contribute to Rho-induced reorganization of the actin
cytoskeleton.
Kuhn et al. (2000) reviewed evidence from studies of several avian and
mammalian primary neural cultures and neuronal cell lines that showed a
role for ADF and cofilin in neurite outgrowth.
To study the in vivo biochemical action of cofilin and the subsequent
cellular response, Ghosh et al. (2004) used a general caging method for
proteins that are regulated by phosphorylation. By acute and local
activation of a chemically engineered, light-sensitive phosphocofilin
mimic, they demonstrated that cofilin polymerizes actin, generates
protrusions, and determines the direction of cell migration. Ghosh et
al. (2004) proposed a role for cofilin that is distinct from its role as
an actin-depolymerizing factor.
MAPPING
Gillett et al. (1996) mapped CFL1 to 11q12-q13.3 by analysis of somatic
cell hybrids and to 11q13 by fluorescence in situ hybridization (FISH).
Fernandes et al. (1998) used FISH and mouse/hamster somatic cell hybrid
analysis to map the Cfl1 gene to mouse chromosome 19.
Courseaux et al. (1996) used a combination of methods to refine maps of
the approximately 5-Mb region of 11q13 that includes the MEN1 locus
(131100). They proposed the following gene order:
cen--PTA--FTH1--UGB--AHNAK--ROM1--MDU1--CHRM1--COX8--EMK1--FKBP2--PLCB3--[PYGM,
ZFM1]--FAU--CAPN1-- [MLK3, RELA]--FOSL1--SEA--CFL1--tel.
ANIMAL MODEL
Because deletion of n-cofilin results in embryonic lethality in mice,
Bellenchi et al. (2007) used a conditional knockout approach to examine
the role of n-cofilin in brain development. Homozygous mutant pups were
obtained at the expected mendelian frequency, but more than 90% died
within the first 3 postnatal days. The few that survived up to 30 days
showed growth retardation, ataxia, and signs of epileptic seizures.
Gross analysis of mutant brains revealed an overall normal organization,
but the cerebral cortex had a translucent appearance and enlarged
ventricles. Golgi staining of coronal sections showed that cortical
layers II to IV and parts of layer V were missing in mutant brains.
Studies performed on cultured cortical neuronal progenitors revealed
that loss of n-cofilin impaired their radial migration. Neuronal
progenitors in the ventricular zone showed increased cell cycle exit and
exaggerated neuronal differentiation, leading to depletion of the
neuronal progenitor pool.
*FIELD* RF
1. Bellenchi, G. C.; Gurniak, C. B.; Perlas, E.; Middei, S.; Ammassari-Teule,
M.; Witke, W.: N-cofilin is associated with neuronal migration disorders
and cell cycle control in the cerebral cortex. Genes Dev. 21: 2347-2357,
2007.
2. Courseaux, A.; Grosgeorge, J.; Gaudray, P.; Pannett, A. A. J.;
Forbes, S. A.; Williamson, C.; Bassett, D.; Thakker, R. V.; Teh, B.
T.; Farnebo, F.; Shepherd, J.; Skogseid, B.; Larsson, C.; Giraud,
S.; Zhang, C. X.; Salandre, J.; Calender, A.: Definition of the minimal
MEN1 candidate area based on a 5-Mb integrated map of proximal 11q13. Genomics 37:
354-365, 1996.
3. Fernandes, M.; Poirier, C.; Lespinasse, F.; Carle, G. F.: The
mouse homologs of human GIF, DDB1, and CFL1 genes are located on chromosome
19. Mammalian Genome 9: 339-342, 1998.
4. Ghosh, M.; Song, X.; Mouneimne, G.; Sidani, M.; Lawrence, D. S.;
Condeelis, J. S.: Cofilin promotes actin polymerization and defines
the direction of cell motility. Science 304: 743-746, 2004.
5. 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.
6. Kuhn, T. B.; Meberg, P. J.; Brown, M. D.; Bernstein, B. W.; Minamide,
L. S.; Jensen, J. R.; Okada, K.; Soda, E. A.; Bamburg, J. R.: Regulating
actin dynamics in neuronal growth cones by ADF/cofilin and Rho family
GTPases. J. Neurobiol. 44: 126-144, 2000.
7. Maekawa, M.; Ishizaki, T.; Boku, S.; Watanabe, N.; Fujita, A.;
Iwamatsu, A.; Obinata, T.; Ohashi, K.; Mizuno, K.; Narumiya, S.:
Signaling from Rho to the actin cytoskeleton through protein kinases
ROCK and LIM-kinase. Science 285: 895-898, 1999.
8. 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 only, 1990.
9. Ono, S.; Minami, N.; Abe, H.; Obinata, T.: Characterization of
a novel cofilin isoform that is predominantly expressed in mammalian
skeletal muscle. J. Biol. Chem. 269: 15280-15286, 1994.
*FIELD* CN
Patricia A. Hartz - updated: 10/17/2007
Patricia A. Hartz - updated: 10/16/2007
Ada Hamosh - updated: 5/7/2004
Patricia A. Hartz - updated: 10/22/2003
Ada Hamosh - updated: 8/5/1999
Victor A. McKusick - updated: 9/3/1998
Victor A. McKusick - updated: 4/10/1997
Alan F. Scott - updated: 12/2/1996
*FIELD* CD
Lori M. Kelman: 9/23/1996
*FIELD* ED
carol: 04/22/2011
terry: 4/20/2011
carol: 2/9/2011
wwang: 4/30/2008
terry: 4/25/2008
mgross: 10/17/2007
terry: 10/16/2007
alopez: 5/7/2004
terry: 5/7/2004
mgross: 10/22/2003
alopez: 8/5/1999
carol: 9/3/1998
terry: 8/5/1997
terry: 7/29/1997
alopez: 6/27/1997
mark: 4/10/1997
joanna: 4/9/1997
joanna: 12/2/1996
mark: 9/23/1996
*RECORD*
*FIELD* NO
601442
*FIELD* TI
*601442 COFILIN 1; CFL1
;;COFILIN, NONMUSCLE
*FIELD* TX
DESCRIPTION
Cofilin is a widely distributed intracellular actin-modulating protein
read morethat binds and depolymerizes filamentous F-actin and inhibits the
polymerization of monomeric G-actin in a pH-dependent manner. It is
involved in the translocation of actin-cofilin complex from cytoplasm to
nucleus (summary by Gillett et al., 1996).
CLONING
Two cofilin isoforms have been identified in mouse: muscle, or M-type
(601443) and nonmuscle, or NM-type (Ono et al., 1994). The mouse M-type
cofilin is expressed in heart, skeletal muscle, and testis, whereas the
NM-type is found in a wide variety of tissues, including heart and
testis. NM-type cofilin expression is minimal in mature mammalian
skeletal muscle. Ogawa et al. (1990) isolated a cDNA encoding a
placentally expressed cofilin. Gillett et al. (1996) cloned CFL1, a
nonmuscle-type cofilin, from a human promyelocytic cDNA library. The
cDNA encodes a 166-amino acid polypeptide with a molecular mass of
approximately 18.5 kD.
GENE FUNCTION
Cofilin exhibits actin-depolymerizing activity that is inhibited as a
result of its phosphorylation by LIM kinase (see 601329). Maekawa et al.
(1999) demonstrated that cofilin was phosphorylated during
lysophosphatidic acid-induced, Rho-mediated neurite retraction. This
phosphorylation was sensitive to Y-27632, a specific inhibitor of the
Rho-associated kinase ROCK (601702). ROCK, which is a downstream
effector of Rho, did not phosphorylate cofilin directly but
phosphorylated LIM kinase, which in turn was activated to phosphorylate
cofilin. Maekawa et al. (1999) concluded that phosphorylation of LIM
kinase by ROCK and, consequently, increased phosphorylation of cofilin
by LIM kinase, contribute to Rho-induced reorganization of the actin
cytoskeleton.
Kuhn et al. (2000) reviewed evidence from studies of several avian and
mammalian primary neural cultures and neuronal cell lines that showed a
role for ADF and cofilin in neurite outgrowth.
To study the in vivo biochemical action of cofilin and the subsequent
cellular response, Ghosh et al. (2004) used a general caging method for
proteins that are regulated by phosphorylation. By acute and local
activation of a chemically engineered, light-sensitive phosphocofilin
mimic, they demonstrated that cofilin polymerizes actin, generates
protrusions, and determines the direction of cell migration. Ghosh et
al. (2004) proposed a role for cofilin that is distinct from its role as
an actin-depolymerizing factor.
MAPPING
Gillett et al. (1996) mapped CFL1 to 11q12-q13.3 by analysis of somatic
cell hybrids and to 11q13 by fluorescence in situ hybridization (FISH).
Fernandes et al. (1998) used FISH and mouse/hamster somatic cell hybrid
analysis to map the Cfl1 gene to mouse chromosome 19.
Courseaux et al. (1996) used a combination of methods to refine maps of
the approximately 5-Mb region of 11q13 that includes the MEN1 locus
(131100). They proposed the following gene order:
cen--PTA--FTH1--UGB--AHNAK--ROM1--MDU1--CHRM1--COX8--EMK1--FKBP2--PLCB3--[PYGM,
ZFM1]--FAU--CAPN1-- [MLK3, RELA]--FOSL1--SEA--CFL1--tel.
ANIMAL MODEL
Because deletion of n-cofilin results in embryonic lethality in mice,
Bellenchi et al. (2007) used a conditional knockout approach to examine
the role of n-cofilin in brain development. Homozygous mutant pups were
obtained at the expected mendelian frequency, but more than 90% died
within the first 3 postnatal days. The few that survived up to 30 days
showed growth retardation, ataxia, and signs of epileptic seizures.
Gross analysis of mutant brains revealed an overall normal organization,
but the cerebral cortex had a translucent appearance and enlarged
ventricles. Golgi staining of coronal sections showed that cortical
layers II to IV and parts of layer V were missing in mutant brains.
Studies performed on cultured cortical neuronal progenitors revealed
that loss of n-cofilin impaired their radial migration. Neuronal
progenitors in the ventricular zone showed increased cell cycle exit and
exaggerated neuronal differentiation, leading to depletion of the
neuronal progenitor pool.
*FIELD* RF
1. Bellenchi, G. C.; Gurniak, C. B.; Perlas, E.; Middei, S.; Ammassari-Teule,
M.; Witke, W.: N-cofilin is associated with neuronal migration disorders
and cell cycle control in the cerebral cortex. Genes Dev. 21: 2347-2357,
2007.
2. Courseaux, A.; Grosgeorge, J.; Gaudray, P.; Pannett, A. A. J.;
Forbes, S. A.; Williamson, C.; Bassett, D.; Thakker, R. V.; Teh, B.
T.; Farnebo, F.; Shepherd, J.; Skogseid, B.; Larsson, C.; Giraud,
S.; Zhang, C. X.; Salandre, J.; Calender, A.: Definition of the minimal
MEN1 candidate area based on a 5-Mb integrated map of proximal 11q13. Genomics 37:
354-365, 1996.
3. Fernandes, M.; Poirier, C.; Lespinasse, F.; Carle, G. F.: The
mouse homologs of human GIF, DDB1, and CFL1 genes are located on chromosome
19. Mammalian Genome 9: 339-342, 1998.
4. Ghosh, M.; Song, X.; Mouneimne, G.; Sidani, M.; Lawrence, D. S.;
Condeelis, J. S.: Cofilin promotes actin polymerization and defines
the direction of cell motility. Science 304: 743-746, 2004.
5. 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.
6. Kuhn, T. B.; Meberg, P. J.; Brown, M. D.; Bernstein, B. W.; Minamide,
L. S.; Jensen, J. R.; Okada, K.; Soda, E. A.; Bamburg, J. R.: Regulating
actin dynamics in neuronal growth cones by ADF/cofilin and Rho family
GTPases. J. Neurobiol. 44: 126-144, 2000.
7. Maekawa, M.; Ishizaki, T.; Boku, S.; Watanabe, N.; Fujita, A.;
Iwamatsu, A.; Obinata, T.; Ohashi, K.; Mizuno, K.; Narumiya, S.:
Signaling from Rho to the actin cytoskeleton through protein kinases
ROCK and LIM-kinase. Science 285: 895-898, 1999.
8. 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 only, 1990.
9. Ono, S.; Minami, N.; Abe, H.; Obinata, T.: Characterization of
a novel cofilin isoform that is predominantly expressed in mammalian
skeletal muscle. J. Biol. Chem. 269: 15280-15286, 1994.
*FIELD* CN
Patricia A. Hartz - updated: 10/17/2007
Patricia A. Hartz - updated: 10/16/2007
Ada Hamosh - updated: 5/7/2004
Patricia A. Hartz - updated: 10/22/2003
Ada Hamosh - updated: 8/5/1999
Victor A. McKusick - updated: 9/3/1998
Victor A. McKusick - updated: 4/10/1997
Alan F. Scott - updated: 12/2/1996
*FIELD* CD
Lori M. Kelman: 9/23/1996
*FIELD* ED
carol: 04/22/2011
terry: 4/20/2011
carol: 2/9/2011
wwang: 4/30/2008
terry: 4/25/2008
mgross: 10/17/2007
terry: 10/16/2007
alopez: 5/7/2004
terry: 5/7/2004
mgross: 10/22/2003
alopez: 8/5/1999
carol: 9/3/1998
terry: 8/5/1997
terry: 7/29/1997
alopez: 6/27/1997
mark: 4/10/1997
joanna: 4/9/1997
joanna: 12/2/1996
mark: 9/23/1996