Q9Y281 (COF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cofilin-2

Alternative name(s):
Cofilin, muscle isoform

Gene names

Name:

CFL2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods By similarity.
Subcellular location	Nucleus matrix By similarity. Cytoplasm › cytoskeleton By similarity.
Tissue specificity	Isoform CFL2b is expressed predominantly in skeletal muscle and heart. Isoform CFL2a is expressed in various tissues.
Post-translational modification	The phosphorylation of Ser-24 may prevent recognition of the nuclear localization signal.
Involvement in disease	Defects in CFL2 are the cause of nemaline myopathy type 7 (NEM7) [MIM:610687]. A form of nemaline myopathy. Nemaline myopathies are muscular disorders characterized by muscle weakness of varying severity and onset, and abnormal thread-or rod-like structures in muscle fibers on histologic examination. Nemaline myopathy type 7 presents at birth with hypotonia and generalized weakness. Major motor milestones are delayed, but independent ambulation is achieved. Ref.11
Sequence similarities	Belongs to the actin-binding proteins ADF family. Contains 1 ADF-H domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Nemaline myopathy
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACTB	P60709	2	EBI-351218,EBI-353944
ACTG1	P63261	2	EBI-351218,EBI-351292

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Select]

Note: Isoforms are identical at the level of the protein sequence.

Isoform CFL2b (identifier: Q9Y281-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform CFL2a (identifier: Q9Y281-2)

The sequence of this isoform is not available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4
	Chain	2 – 166	165	Cofilin-2		PRO_0000214907
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.4 Ref.7
	Modified residue	3	1	Phosphoserine Ref.6 Ref.7
	Modified residue	6	1	Phosphothreonine By similarity
	Modified residue	24	1	Phosphoserine By similarity
	Modified residue	89	1	Phosphotyrosine Ref.5
	Modified residue	92	1	N6-acetyllysine Ref.8
Natural variations
	Natural variant	35	1	A → T in NEM7; protein is less soluble when expressed in Escherichia coli. Ref.11		VAR_031989
	Natural variant	47	1	I → M in a breast cancer sample; somatic mutation. Ref.10		VAR_036458

Sequences

	Sequence		Length	Mass (Da)
	Isoform CFL2b [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 48B6CDCCAE9FE1CC	FASTA	166	18,737
	10 20 30 40 50 60 MASGVTVNDE VIKVFNDMKV RKSSTQEEIK KRKKAVLFCL SDDKRQIIVE EAKQILVGDI 70 80 90 100 110 120 GDTVEDPYTS FVKLLPLNDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS 130 140 150 160 KDAIKKKFTG IKHEWQVNGL DDIKDRSTLG EKLGGNVVVS LEGKPL
	Isoform CFL2a (Sequence not available).		–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of two isoforms of human cofilin cDNA." Jin J., Li G., Hu S., Li W., Yuan J., Qiang B. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Characterization of human muscle type cofilin (CFL2) in normal and regenerating muscle." Thirion C., Stucka R., Mendel B., Gruhler A., Jaksch M., Nowak K.J., Binz N., Laing N.G., Lochmuller H. Eur. J. Biochem. 268:3473-3482(2001) [PubMed: 11422377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow, Placenta and Skeletal muscle.
[4]	Bienvenut W.V., Calvo F., Kolch W. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-21; 35-92; 96-112; 115-125 AND 153-166, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[6]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92, MASS SPECTROMETRY.
[9]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-47.
[11]	"Nemaline myopathy with minicores caused by mutation of the CFL2 gene encoding the skeletal muscle actin-binding protein, cofilin-2." Agrawal P.B., Greenleaf R.S., Tomczak K.K., Lehtokari V.-L., Wallgren-Pettersson C., Wallefeld W., Laing N.G., Darras B.T., Maciver S.K., Dormitzer P.R., Beggs A.H. Am. J. Hum. Genet. 80:162-167(2007) [PubMed: 17160903] [Abstract] Cited for: VARIANT NEM7 THR-35, CHARACTERIZATION OF VARIANT NEM7 THR-35.
+	Additional computationally mapped references.

Web resources

Wikipedia

Cofilin entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF134802 mRNA. Translation: AAD31280.1. AF134803 mRNA. Translation: AAD31281.1. AF283513 Genomic DNA. Translation: AAF97934.1. AF242299 Genomic DNA. Translation: AAF64498.1. BC011444 mRNA. Translation: AAH11444.1. BC022364 mRNA. Translation: AAH22364.1. BC022876 mRNA. Translation: AAH22876.1.
IPI	IPI00413344.
RefSeq	NP_068733.1. NM_021914.7. NP_619579.1. NM_138638.4.
UniGene	Hs.180141.
3D structure databases
ProteinModelPortal	Q9Y281.
SMR	Q9Y281. Positions 1-166.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y281. 3 interactions.
MINT	MINT-1161448.
STRING	Q9Y281.
PTM databases
PhosphoSite	Q9Y281.
Polymorphism databases
DMDM	6831517.
Proteomic databases
PRIDE	Q9Y281.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000298159; ENSP00000298159; ENSG00000165410. ENST00000341223; ENSP00000340635; ENSG00000165410.
GeneID	1073.
KEGG	hsa:1073.
UCSC	uc001wsg.2. human.
Organism-specific databases
CTD	1073.
GeneCards	GC14M035179.
H-InvDB	HIX0009009. HIX0011593.
HGNC	HGNC:1875. CFL2.
HPA	CAB037078.
MIM	601443. gene. 610687. phenotype.
neXtProt	NX_Q9Y281.
Orphanet	607. Nemaline myopathy.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00440000033289.
HOGENOM	HBG628477.
HOVERGEN	HBG000381.
InParanoid	Q9Y281.
OMA	GLYDATY.
OrthoDB	EOG4WSWBP.
PhylomeDB	Q9Y281.
Enzyme and pathway databases
Pathway_Interaction_DB	caspase_pathway. Caspase cascade in apoptosis.
Gene expression databases
ArrayExpress	Q9Y281.
Bgee	Q9Y281.
CleanEx	HS_CFL2.
Genevestigator	Q9Y281.
GermOnline	ENSG00000165410. Homo sapiens.
Family and domain databases
InterPro	IPR002108. Actin-bd_cofilin/tropomyosin. IPR017904. ADF/Cofilin/Destrin. [Graphical view]
KO	K05765.
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
NextBio	4480.
SOURCE	Search...

Entry information

Entry name

COF2_HUMAN

Accession

Primary (citable) accession number: Q9Y281

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 114 of the entry and version 1 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.