HUMAN:COF1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	CFL1 (synonyms: CFL)
Protein Name(s)	Cofilin-1 18 kDa phosphoprotein p18 Cofilin, non-muscle isoform
External Links
UniProt	P23528
EMBL	D00682 U21909 X95404 BT006846 AK097690 CH471076 BC011005 BC012265 BC012318 BC018256
CCDS	CCDS8114.1
PIR	S12632
RefSeq	NP_005498.1
UniGene	Hs.170622
PDB	1Q8G 1Q8X 3J0S 4BEX 5HVK 5L6W
PDBsum	1Q8G 1Q8X 3J0S 4BEX 5HVK 5L6W
ProteinModelPortal	P23528
SMR	P23528
BioGrid	107499
DIP	DIP-33000N
IntAct	P23528
MINT	MINT-4999473
STRING	9606.ENSP00000309629
ChEMBL	CHEMBL1075129
DrugBank	DB04147
iPTMnet	P23528
PhosphoSitePlus	P23528
SwissPalm	P23528
BioMuta	CFL1
DMDM	116848
DOSAC-COBS-2DPAGE	P23528
OGP	P23528
REPRODUCTION-2DPAGE	IPI00012011
SWISS-2DPAGE	P23528
UCD-2DPAGE	P23528
EPD	P23528
PaxDb	P23528
PeptideAtlas	P23528
PRIDE	P23528
TopDownProteomics	P23528
DNASU	1072
Ensembl	ENST00000308162 ENST00000525451
GeneID	1072
KEGG	hsa:1072
CTD	1072
DisGeNET	1072
GeneCards	CFL1
H-InvDB	HIX0009009
HGNC	HGNC:1874
HPA	CAB033687 CAB037077 HPA053761
MIM	601442
neXtProt	NX_P23528
OpenTargets	ENSG00000172757
PharmGKB	PA26423
eggNOG	KOG1735 ENOG41122P5
GeneTree	ENSGT00440000033289
HOGENOM	HOG000039697
HOVERGEN	HBG000381
InParanoid	P23528
KO	K05765
PhylomeDB	P23528
TreeFam	TF328601
Reactome	[www.reactome.org/content/detail/R-HSA-114608 R-HSA-114608] [www.reactome.org/content/detail/R-HSA-2029482 R-HSA-2029482] [www.reactome.org/content/detail/R-HSA-3928662 R-HSA-3928662] [www.reactome.org/content/detail/R-HSA-399954 R-HSA-399954]
SignaLink	P23528
SIGNOR	P23528
ChiTaRS	CFL1
EvolutionaryTrace	P23528
GeneWiki	Cofilin_1
GenomeRNAi	1072
PMAP-CutDB	P23528
PRO	PR:P23528
Proteomes	UP000005640
Bgee	ENSG00000172757
ExpressionAtlas	P23528
Genevisible	P23528
GO	GO:0015629 GO:0005737 GO:0043197 GO:0070062 GO:0031012 GO:0005615 GO:0030175 GO:0005925 GO:0030426 GO:0031258 GO:0016020 GO:0031966 GO:0043025 GO:0016363 GO:0005634 GO:0032587 GO:0031982 GO:0051015 GO:1902936 GO:0030036 GO:0030042 GO:0030030 GO:0071364 GO:0071362 GO:0070301 GO:1990314 GO:0071347 GO:0071354 GO:0071356 GO:0007010 GO:0021766 GO:0032232 GO:0043066 GO:0007162 GO:2000146 GO:0045792 GO:1902951 GO:0010593 GO:0051511 GO:0044794 GO:2000814 GO:2000147 GO:0060999 GO:2000784 GO:0051894 GO:0010592 GO:1904783 GO:1904377 GO:0045862 GO:0031915 GO:0097107 GO:0006606 GO:0022604 GO:0061001 GO:0014823 GO:0014070 GO:0009615 GO:0007266
CDD	cd11286
Gene3D	3.40.20.10
InterPro	IPR002108 IPR029006 IPR017904 IPR027234
PANTHER	PTHR11913 PTHR11913:SF37
Pfam	PF00241
PRINTS	PR00006
SMART	SM00102
PROSITE	PS51263

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0051015	actin filament binding	PMID:11812157^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	PMID:11812157^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051015	actin filament binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P10668	F		Seeded From UniProt	complete
involved_in	GO:0044794	positive regulation by host of viral process	PMID:25556234^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:25556234^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031982	vesicle	PMID:19190083^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002202)	Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:21423176^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0061001	regulation of dendritic spine morphogenesis	PMID:24464040^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0002608)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001831)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[9]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:23580065^[10]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001827)	Seeded From UniProt	complete
part_of	GO:0030027	lamellipodium	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P18760	C		Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	PMID:24052308^[11]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0022604	regulation of cell morphogenesis	PMID:21834987^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009615	response to virus	PMID:16548883^[13]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007010	cytoskeleton organization	PMID:21834987^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:29162887^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0051015	actin filament binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	F		Seeded From UniProt	complete
involved_in	GO:0043200	response to amino acid	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	P		Seeded From UniProt	complete
part_of	GO:0030864	cortical actin cytoskeleton	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	C		Seeded From UniProt	complete
involved_in	GO:0030836	positive regulation of actin filament depolymerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	P		Seeded From UniProt	complete
involved_in	GO:0030043	actin filament fragmentation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	P		Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	P		Seeded From UniProt	complete
part_of	GO:0030027	lamellipodium	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	C		Seeded From UniProt	complete
involved_in	GO:0030010	establishment of cell polarity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	P		Seeded From UniProt	complete
involved_in	GO:0007015	actin filament organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	P		Seeded From UniProt	complete
part_of	GO:0005911	cell-cell junction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	C		Seeded From UniProt	complete
enables	GO:0005102	signaling receptor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	F		Seeded From UniProt	complete
involved_in	GO:0001842	neural fold formation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	P		Seeded From UniProt	complete
involved_in	GO:0001755	neural crest cell migration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	P		Seeded From UniProt	complete
involved_in	GO:0000281	mitotic cytokinesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18760 ensembl:ENSMUSP00000147514	P		Seeded From UniProt	complete
enables	GO:0003779	actin binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002108	F		Seeded From UniProt	complete
part_of	GO:0015629	actin cytoskeleton	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR017904 InterPro:IPR027234	C		Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR017904 InterPro:IPR027234	P		Seeded From UniProt	complete
involved_in	GO:0030036	actin cytoskeleton organization	PMID:10436159^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007266	Rho protein signal transduction	PMID:10436159^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:8195165^[16] PMID:16130169^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:16130169^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16130169^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0035722	interleukin-12-mediated signaling pathway	Reactome:R-HSA-9020591	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-8950581	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003779	actin binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0009	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003	C		Seeded From UniProt	complete
Colocalizes with	GO:0005634	nucleus	PMID:28334682^[18]	ECO:0000314			C		Organism: Homo sapiens. Protein Name: Cofilin. Notes: Figure 3G is used. MCF-7 cells (which are human) have their nuclei stained blue and are also immunostained so that cofilin will appear red. As can be seen in the micrographs, cofilin does not have overlap with the nuclei until the cells are exposed to sulforaphane. Thus, a link is established between cofilin and the nucleus, but it is a transient relationship.	complete CACAO 12741
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206 UniProtKB-SubCell:SL-0090	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539	C		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0966	C		Seeded From UniProt	complete
part_of	GO:0032587	ruffle membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0301	C		Seeded From UniProt	complete
part_of	GO:0031258	lamellipodium membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0292	C		Seeded From UniProt	complete
part_of	GO:0030027	lamellipodium	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0291	C		Seeded From UniProt	complete
part_of	GO:0016363	nuclear matrix	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0181	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Yeoh, S et al. (2002) Determining the differences in actin binding by human ADF and cofilin. J. Mol. Biol. 315 911-25 PubMed GONUTS page
↑ ^2.0 ^2.1 Kipper, S et al. (2015) New host factors important for respiratory syncytial virus (RSV) replication revealed by a novel microfluidics screen for interactors of matrix (M) protein. Mol. Cell Proteomics 14 532-43 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Kesimer, M et al. (2009) Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J. 23 1858-68 PubMed GONUTS page
↑ Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Parisiadou, L et al. (2014) LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity. Nat. Neurosci. 17 367-76 PubMed GONUTS page
↑ Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
↑ Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ Pieragostino, D et al. (2013) Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy. Mol Biosyst 9 1108-16 PubMed GONUTS page
↑ Kim, T et al. (2013) Human LilrB2 is a β-amyloid receptor and its murine homolog PirB regulates synaptic plasticity in an Alzheimer's model. Science 341 1399-404 PubMed GONUTS page
↑ ^12.0 ^12.1 Bai, SW et al. (2011) Identification and characterization of a set of conserved and new regulators of cytoskeletal organization, cell morphology and migration. BMC Biol. 9 54 PubMed GONUTS page
↑ Leong, WF & Chow, VT (2006) Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection. Cell. Microbiol. 8 565-80 PubMed GONUTS page
↑ Rogg, M et al. (2017) The WD40-domain containing protein CORO2B is specifically enriched in glomerular podocytes and regulates the ventral actin cytoskeleton. Sci Rep 7 15910 PubMed GONUTS page
↑ ^15.0 ^15.1 Maekawa, M et al. (1999) Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science 285 895-8 PubMed GONUTS page
↑ Ono, S et al. (1994) Characterization of a novel cofilin isoform that is predominantly expressed in mammalian skeletal muscle. J. Biol. Chem. 269 15280-6 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page
↑ Lewinska, A et al. (2017) Phytochemical-induced nucleolar stress results in the inhibition of breast cancer cell proliferation. Redox Biol 12 469-482 PubMed GONUTS page

[PMID:11812157-1] 1.0 ^1.1 Yeoh, S et al. (2002) Determining the differences in actin binding by human ADF and cofilin. J. Mol. Biol. 315 911-25 PubMed GONUTS page

[PMID:25556234-2] 2.0 ^2.1 Kipper, S et al. (2015) New host factors important for respiratory syncytial virus (RSV) replication revealed by a novel microfluidics screen for interactors of matrix (M) protein. Mol. Cell Proteomics 14 532-43 PubMed GONUTS page

[PMID:23533145-3] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19190083-4] Kesimer, M et al. (2009) Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J. 23 1858-68 PubMed GONUTS page

[PMID:21423176-5] Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page

[PMID:19946888-6] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:24464040-7] Parisiadou, L et al. (2014) LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity. Nat. Neurosci. 17 367-76 PubMed GONUTS page

[PMID:19199708-8] Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page

[PMID:20458337-9] Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:23580065-10] Pieragostino, D et al. (2013) Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy. Mol Biosyst 9 1108-16 PubMed GONUTS page

[PMID:24052308-11] Kim, T et al. (2013) Human LilrB2 is a β-amyloid receptor and its murine homolog PirB regulates synaptic plasticity in an Alzheimer's model. Science 341 1399-404 PubMed GONUTS page

[PMID:21834987-12] 12.0 ^12.1 Bai, SW et al. (2011) Identification and characterization of a set of conserved and new regulators of cytoskeletal organization, cell morphology and migration. BMC Biol. 9 54 PubMed GONUTS page

[PMID:16548883-13] Leong, WF & Chow, VT (2006) Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection. Cell. Microbiol. 8 565-80 PubMed GONUTS page

[PMID:29162887-14] Rogg, M et al. (2017) The WD40-domain containing protein CORO2B is specifically enriched in glomerular podocytes and regulates the ventral actin cytoskeleton. Sci Rep 7 15910 PubMed GONUTS page

[PMID:10436159-15] 15.0 ^15.1 Maekawa, M et al. (1999) Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science 285 895-8 PubMed GONUTS page

[PMID:8195165-16] Ono, S et al. (1994) Characterization of a novel cofilin isoform that is predominantly expressed in mammalian skeletal muscle. J. Biol. Chem. 269 15280-6 PubMed GONUTS page

[PMID:16130169-17] 17.0 ^17.1 ^17.2 Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

[PMID:28334682-18] Lewinska, A et al. (2017) Phytochemical-induced nucleolar stress results in the inhibition of breast cancer cell proliferation. Redox Biol 12 469-482 PubMed GONUTS page

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HUMAN:COF1

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