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P23528 (COF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cofilin-1
Alternative name(s):
18 kDa phosphoprotein
Short name=p18
Cofilin, non-muscle isoform
Gene names
Name:CFL1
Synonyms:CFL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length166 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Ref.14 Ref.23 Ref.28

Subunit structure

Can bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is a major component of intranuclear and cytoplasmic actin rods.

Subcellular location

Nucleus matrix. Cytoplasmcytoskeleton. Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionlamellipodium membrane; Peripheral membrane protein; Cytoplasmic side. Note: Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide. Ref.14

Tissue specificity

Widely distributed in various tissues.

Induction

Up-regulated in response to enterovirus 71 (EV71) infection (at protein level). Ref.16

Post-translational modification

Inactivated by phosphorylation on Ser-3. Phosphorylated on Ser-3 in resting cells By similarity. Dephosphorylated by PDXP/chronophin; this restores its activity in promoting actin filament depolymerization. The phosphorylation of Ser-24 may prevent recognition of the nuclear localization signal By similarity. Phosphorylated via a ARRB1-RAC1-LIMK1-PAK1 cascade upon active ligand stimulation of atypical chemokine receptor ACKR2. Ref.12 Ref.14 Ref.28

Sequence similarities

Belongs to the actin-binding proteins ADF family.

Contains 1 ADF-H domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

Rho protein signal transduction

Traceable author statement PubMed 10436159. Source: ProtInc

actin cytoskeleton organization

Traceable author statement PubMed 10436159. Source: ProtInc

actin filament depolymerization

Inferred from electronic annotation. Source: InterPro

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cytoskeleton organization

Inferred from mutant phenotype Ref.23. Source: UniProtKB

establishment of cell polarity

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Traceable author statement PubMed 16130169. Source: UniProtKB

negative regulation of cell size

Inferred from electronic annotation. Source: Ensembl

neural crest cell migration

Inferred from electronic annotation. Source: Ensembl

neural fold formation

Inferred from electronic annotation. Source: Ensembl

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of actin filament depolymerization

Inferred from electronic annotation. Source: Ensembl

protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of cell morphogenesis

Inferred from mutant phenotype Ref.23. Source: UniProtKB

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to virus

Inferred from expression pattern Ref.16. Source: UniProtKB

   Cellular_componentcortical actin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Traceable author statement PubMed 16130169. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708PubMed 20458337PubMed 23376485. Source: UniProt

lamellipodium membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Traceable author statement PubMed 16130169. Source: UniProtKB

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 12361576PubMed 15161933PubMed 16713569PubMed 17853892PubMed 21525957. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.9
Chain2 – 166165Cofilin-1
PRO_0000214898

Regions

Domain4 – 153150ADF-H
Motif30 – 345Nuclear localization signal Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.18 Ref.19 Ref.21 Ref.22 Ref.25 Ref.26 Ref.27
Modified residue31Phosphoserine; by NRK Ref.12 Ref.15 Ref.17 Ref.19 Ref.22 Ref.25
Modified residue81Phosphoserine By similarity
Modified residue131N6-acetyllysine Ref.21
Modified residue251Phosphothreonine Ref.22
Modified residue681Phosphotyrosine Ref.20
Modified residue731N6-acetyllysine Ref.21
Modified residue1401Phosphotyrosine Ref.13
Modified residue1441N6-acetyllysine Ref.21
Modified residue1561Phosphoserine Ref.17 Ref.20 Ref.22

Secondary structure

................................ 166
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23528 [UniParc].

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

FASTA16618,502
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung, Ovary, Placenta and Uterus.
[8]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
Tissue: Platelet.
[9]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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[10]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 34-45; 54-73; 82-92; 96-112; 133-146 AND 153-166, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[11]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 52-71.
Tissue: Platelet.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-3 BY NRK.
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics."
Gohla A., Birkenfeld J., Bokoch G.M.
Nat. Cell Biol. 7:21-29(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DEPHOSPHORYLATION BY PDXP.
[15]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
Leong W.F., Chow V.T.
Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-156, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-68 AND SER-156, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-13; LYS-73 AND LYS-144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; THR-25 AND SER-156, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Beta-arrestin-dependent activation of the cofilin pathway is required for the scavenging activity of the atypical chemokine receptor D6."
Borroni E.M., Cancellieri C., Vacchini A., Benureau Y., Lagane B., Bachelerie F., Arenzana-Seisdedos F., Mizuno K., Mantovani A., Bonecchi R., Locati M.
Sci. Signal. 6:RA30-RA30(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[29]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Web resources

Wikipedia

Cofilin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00682 mRNA. Translation: BAA00589.1.
U21909 mRNA. Translation: AAA64501.1.
X95404 mRNA. Translation: CAA64685.1.
BT006846 mRNA. Translation: AAP35492.1.
AK097690 mRNA. Translation: BAG53513.1.
CH471076 Genomic DNA. Translation: EAW74449.1.
BC011005 mRNA. Translation: AAH11005.1.
BC012265 mRNA. Translation: AAH12265.1.
BC012318 mRNA. Translation: AAH12318.1.
BC018256 mRNA. Translation: AAH18256.1.
CCDSCCDS8114.1.
PIRS12632.
RefSeqNP_005498.1. NM_005507.2.
UniGeneHs.170622.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q8GNMR-A1-166[»]
1Q8XNMR-A1-166[»]
3J0Selectron microscopy9.00M/N/O/P/Q/R/S/T/U/V/W/X1-166[»]
4BEXX-ray2.8011-166[»]
ProteinModelPortalP23528.
SMRP23528. Positions 1-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107499. 54 interactions.
DIPDIP-33000N.
IntActP23528. 44 interactions.
MINTMINT-4999473.
STRING9606.ENSP00000309629.

Chemistry

ChEMBLCHEMBL1075129.

PTM databases

PhosphoSiteP23528.

Polymorphism databases

DMDM116848.

2D gel databases

DOSAC-COBS-2DPAGEP23528.
OGPP23528.
REPRODUCTION-2DPAGEIPI00012011.
SWISS-2DPAGEP23528.
UCD-2DPAGEP23528.

Proteomic databases

MaxQBP23528.
PaxDbP23528.
PRIDEP23528.

Protocols and materials databases

DNASU1072.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308162; ENSP00000309629; ENSG00000172757.
ENST00000525451; ENSP00000432660; ENSG00000172757.
GeneID1072.
KEGGhsa:1072.
UCSCuc001ofs.3. human.

Organism-specific databases

CTD1072.
GeneCardsGC11M065622.
H-InvDBHIX0009009.
HGNCHGNC:1874. CFL1.
HPACAB037077.
MIM601442. gene.
neXtProtNX_P23528.
PharmGKBPA26423.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG286948.
HOGENOMHOG000039697.
HOVERGENHBG000381.
InParanoidP23528.
KOK05765.
OrthoDBEOG7353Z9.
PhylomeDBP23528.
TreeFamTF328601.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP23528.

Gene expression databases

ArrayExpressP23528.
BgeeP23528.
GenevestigatorP23528.

Family and domain databases

Gene3D3.40.20.10. 1 hit.
InterProIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin/Destrin.
IPR027234. Cofilin_1.
[Graphical view]
PANTHERPTHR11913. PTHR11913. 1 hit.
PTHR11913:SF17. PTHR11913:SF17. 1 hit.
PfamPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
PRINTSPR00006. COFILIN.
SMARTSM00102. ADF. 1 hit.
[Graphical view]
PROSITEPS51263. ADF_H. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCFL1. human.
EvolutionaryTraceP23528.
GeneWikiCofilin_1.
GenomeRNAi1072.
NextBio4476.
PMAP-CutDBP23528.
PROP23528.
SOURCESearch...

Entry information

Entry nameCOF1_HUMAN
AccessionPrimary (citable) accession number: P23528
Secondary accession number(s): B3KUQ1, Q53Y87, Q9UCA2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 11

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