P23528 (COF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cofilin-1

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

Gene names

Name:	CFL1
Synonyms:	CFL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

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

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. Ref.14 Ref.22
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. Cytoplasm › cytoskeleton. Cell projection › ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection › lamellipodium 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. Ref.12 Ref.14
Sequence similarities	Belongs to the actin-binding proteins ADF family. Contains 1 ADF-H domain.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane Nucleus
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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 cytokinesis Inferred from electronic annotation. Source: Compara establishment of cell polarity Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Traceable author statement PubMed 16130169. Source: UniProtKB neural crest cell migration Inferred from electronic annotation. Source: Compara neural fold formation Inferred from electronic annotation. Source: Compara 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: Compara protein phosphorylation Inferred from electronic annotation. Source: Compara regulation of cell morphogenesis Inferred from mutant phenotype Ref.22. Source: UniProtKB response to amino acid stimulus Inferred from electronic annotation. Source: Compara response to virus Inferred from expression pattern Ref.16. Source: UniProtKB
Cellular_component	cortical actin cytoskeleton Inferred from electronic annotation. Source: Compara cytoplasm Traceable author statement PubMed 16130169. Source: UniProtKB 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATXN1	P54253	5	EBI-352733,EBI-930964
YWHAZ	P63104	2	EBI-352733,EBI-347088

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8 Ref.9

Chain

2 – 166

165

Cofilin-1

PRO_0000214898

Regions

Domain

4 – 153

150

ADF-H

Motif

30 – 34

5

Nuclear localization signal Potential

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.9 Ref.18 Ref.20 Ref.21 Ref.24

Modified residue

3

1

Phosphoserine; by NRK Ref.12 Ref.15 Ref.17 Ref.18 Ref.21 Ref.24

Modified residue

8

1

Phosphoserine By similarity

Modified residue

13

1

N6-acetyllysine Ref.20

Modified residue

25

1

Phosphothreonine Ref.21

Modified residue

68

1

Phosphotyrosine Ref.19

Modified residue

73

1

N6-acetyllysine Ref.20

Modified residue

140

1

Phosphotyrosine Ref.13

Modified residue

144

1

N6-acetyllysine Ref.20

Modified residue

156

1

Phosphoserine Ref.17 Ref.19 Ref.21

Secondary structure

1

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166

Helix Strand Turn

Details...

Helix

10 – 20

11

Helix

26 – 29

4

Beta strand

33 – 40

8

Beta strand

42 – 45

4

Beta strand

47 – 57

11

Helix

58 – 60

3

Turn

61 – 63

3

Helix

67 – 73

7

Beta strand

77 – 79

3

Beta strand

81 – 83

3

Beta strand

89 – 93

5

Beta strand

99 – 104

6

Helix

111 – 113

3

Helix

115 – 128

14

Beta strand

132 – 139

8

Helix

140 – 143

4

Helix

146 – 149

4

Turn

150 – 154

5

Helix

155 – 157

3

Beta strand

161 – 164

4

Sequences

	Sequence		Length	Mass (Da)
	P23528 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 589EF8FC1EC13719	FASTA	166	18,502
	10 20 30 40 50 60 MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV 70 80 90 100 110 120 GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS 130 140 150 160 KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Coding sequence of human placenta cofilin cDNA." Ogawa K., Tashima M., Yumoto Y., Okuda T., Sawada H., Okuma M., Maruyama Y. Nucleic Acids Res. 18:7169-7169(1990) [PubMed] [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. , 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. , 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, 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, 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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, MASS SPECTROMETRY.
[19]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[20]	"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, MASS SPECTROMETRY.
[21]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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.
[23]	"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].
[24]	"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, MASS SPECTROMETRY.
[25]	"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.

IPI

IPI00012011.

PIR

S12632.

RefSeq

NP_005498.1. NM_005507.2.

UniGene

Hs.170622.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q8G	NMR	-	A	1-166	[»]
1Q8X	NMR	-	A	1-166	[»]
3J0S	electron microscopy	9.00	M/N/O/P/Q/R/S/T/U/V/W/X	1-166	[»]

ProteinModelPortal

P23528.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33000N.

IntAct

P23528. 33 interactions.

MINT

MINT-4999473.

STRING

9606.ENSP00000309629.

PTM databases

PhosphoSite

P23528.

Polymorphism databases

DMDM

116848.

2D gel databases

DOSAC-COBS-2DPAGE

P23528.

OGP

P23528.

REPRODUCTION-2DPAGE

IPI00012011.

SWISS-2DPAGE

P23528.

UCD-2DPAGE

P23528.

Proteomic databases

PaxDb

P23528.

PRIDE

P23528.

Protocols and materials databases

DNASU

1072.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000308162; ENSP00000309629; ENSG00000172757.
ENST00000525451; ENSP00000432660; ENSG00000172757.

GeneID

1072.

KEGG

hsa:1072.

UCSC

uc001ofs.3. human.

Organism-specific databases

CTD

1072.

GeneCards

GC11M065622.

H-InvDB

HIX0009009.

HGNC

HGNC:1874. CFL1.

HPA

CAB037077.

MIM

601442. gene.

neXtProt

NX_P23528.

PharmGKB

PA26423.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG286948.

HOGENOM

HOG000039697.

HOVERGEN

HBG000381.

InParanoid

P23528.

KO

K05765.

OrthoDB

EOG4WSWBP.

PhylomeDB

P23528.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P23528.

Bgee

P23528.

Genevestigator

P23528.

GermOnline

ENSG00000172757. Homo sapiens.

Family and domain databases

InterPro

IPR002108. Actin-bd_cofilin/tropomyosin.
IPR017904. ADF/Cofilin/Destrin.
IPR027234. Cofilin_1/2.
[Graphical view]

PANTHER

PTHR11913. PTHR11913. 1 hit.
PTHR11913:SF2. PTHR11913:SF2. 1 hit.

Pfam

PF00241. Cofilin_ADF. 1 hit.
[Graphical view]

PRINTS

PR00006. COFILIN.

SMART

SM00102. ADF. 1 hit.
[Graphical view]

PROSITE

PS51263. ADF_H. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075129.

ChiTaRS

CFL1. human.

EvolutionaryTrace

P23528.

GenomeRNAi

1072.

NextBio

4476.

PMAP-CutDB

P23528.

SOURCE

Search...

Entry information

Entry name

COF1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 152 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.