Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cofilin-2

Gene

CFL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Biological processi

  1. actin filament depolymerization Source: InterPro
  2. muscle cell cellular homeostasis Source: Ensembl
  3. positive regulation of actin filament depolymerization Source: UniProtKB
  4. regulation of dendritic spine morphogenesis Source: Ensembl
  5. sarcomere organization Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cofilin-2
Alternative name(s):
Cofilin, muscle isoform
Gene namesi
Name:CFL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:1875. CFL2.

Subcellular locationi

Nucleus matrix By similarity. Cytoplasmcytoskeleton By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: InterPro
  2. extracellular space Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. I band Source: UniProtKB
  5. nuclear matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

Nemaline myopathy 7 (NEM7)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of nemaline myopathy. Nemaline myopathies are muscular disorders characterized by muscle weakness of varying severity and onset, and abnormal thread-like or rod-shaped 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.

See also OMIM:610687
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351A → T in NEM7; protein is less soluble when expressed in Escherichia coli. 1 Publication
VAR_031989

Keywords - Diseasei

Disease mutation, Nemaline myopathy

Organism-specific databases

MIMi610687. phenotype.
Orphaneti171436. Typical nemaline myopathy.
PharmGKBiPA26424.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 166165Cofilin-2PRO_0000214907Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine5 Publications
Modified residuei3 – 31Phosphoserine2 Publications
Modified residuei6 – 61PhosphothreonineBy similarity

Post-translational modificationi

The phosphorylation of Ser-24 may prevent recognition of the nuclear localization signal.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y281.
PaxDbiQ9Y281.
PRIDEiQ9Y281.

PTM databases

PhosphoSiteiQ9Y281.

Expressioni

Tissue specificityi

Isoform CFL2b is expressed predominantly in skeletal muscle and heart. Isoform CFL2a is expressed in various tissues.

Gene expression databases

BgeeiQ9Y281.
CleanExiHS_CFL2.
ExpressionAtlasiQ9Y281. baseline and differential.
GenevestigatoriQ9Y281.

Organism-specific databases

HPAiCAB037078.
HPA045599.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTBP607093EBI-351218,EBI-353944
ACTG1P632612EBI-351218,EBI-351292
CSRP3P504612EBI-351218,EBI-5658719

Protein-protein interaction databases

BioGridi107500. 12 interactions.
DIPiDIP-33178N.
IntActiQ9Y281. 5 interactions.
MINTiMINT-1161448.
STRINGi9606.ENSP00000298159.

Structurei

3D structure databases

ProteinModelPortaliQ9Y281.
SMRiQ9Y281. Positions 1-166.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 153150ADF-HPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi30 – 345Nuclear localization signalSequence Analysis

Sequence similaritiesi

Belongs to the actin-binding proteins ADF family.Curated
Contains 1 ADF-H domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG303866.
GeneTreeiENSGT00440000033289.
HOGENOMiHOG000039697.
HOVERGENiHBG000381.
InParanoidiQ9Y281.
KOiK05765.
OMAiGLYDATY.
OrthoDBiEOG7353Z9.
PhylomeDBiQ9Y281.
TreeFamiTF328601.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin/Destrin.
[Graphical view]
PANTHERiPTHR11913. PTHR11913. 1 hit.
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
PRINTSiPR00006. COFILIN.
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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

Isoform CFL2b (identifier: Q9Y281-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MASGVTVNDE VIKVFNDMKV RKSSTQEEIK KRKKAVLFCL SDDKRQIIVE
60 70 80 90 100
EAKQILVGDI GDTVEDPYTS FVKLLPLNDC RYALYDATYE TKESKKEDLV
110 120 130 140 150
FIFWAPESAP LKSKMIYASS KDAIKKKFTG IKHEWQVNGL DDIKDRSTLG
160
EKLGGNVVVS LEGKPL
Length:166
Mass (Da):18,737
Last modified:November 1, 1999 - v1
Checksum:i48B6CDCCAE9FE1CC
GO
Isoform CFL2a (identifier: Q9Y281-2)

Sequence is not available
Length:
Mass (Da):
Isoform 3 (identifier: Q9Y281-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.

Note: Gene prediction based on EST data.

Show »
Length:149
Mass (Da):16,917
Checksum:i208CA2A540FB2A78
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351A → T in NEM7; protein is less soluble when expressed in Escherichia coli. 1 Publication
VAR_031989
Natural varianti47 – 471I → M in a breast cancer sample; somatic mutation. 1 Publication
VAR_036458

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1717Missing in isoform 3. CuratedVSP_046831Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF134802 mRNA. Translation: AAD31280.1.
AF134803 mRNA. Translation: AAD31281.1.
AF283513 Genomic DNA. Translation: AAF97934.1.
AF242299 Genomic DNA. Translation: AAF64498.1.
AL355885 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65912.1.
BC011444 mRNA. Translation: AAH11444.1.
BC022364 mRNA. Translation: AAH22364.1.
BC022876 mRNA. Translation: AAH22876.1.
CCDSiCCDS58311.1. [Q9Y281-3]
CCDS9649.1. [Q9Y281-1]
CCDS9650.1. [Q9Y281-1]
RefSeqiNP_001230574.1. NM_001243645.1. [Q9Y281-3]
NP_068733.1. NM_021914.7. [Q9Y281-1]
NP_619579.1. NM_138638.4. [Q9Y281-1]
UniGeneiHs.180141.

Genome annotation databases

EnsembliENST00000298159; ENSP00000298159; ENSG00000165410. [Q9Y281-1]
ENST00000341223; ENSP00000340635; ENSG00000165410. [Q9Y281-1]
ENST00000555765; ENSP00000452451; ENSG00000165410. [Q9Y281-3]
ENST00000556161; ENSP00000452188; ENSG00000165410. [Q9Y281-3]
GeneIDi1073.
KEGGihsa:1073.
UCSCiuc001wsg.3. human. [Q9Y281-1]

Polymorphism databases

DMDMi6831517.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Cofilin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF134802 mRNA. Translation: AAD31280.1.
AF134803 mRNA. Translation: AAD31281.1.
AF283513 Genomic DNA. Translation: AAF97934.1.
AF242299 Genomic DNA. Translation: AAF64498.1.
AL355885 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65912.1.
BC011444 mRNA. Translation: AAH11444.1.
BC022364 mRNA. Translation: AAH22364.1.
BC022876 mRNA. Translation: AAH22876.1.
CCDSiCCDS58311.1. [Q9Y281-3]
CCDS9649.1. [Q9Y281-1]
CCDS9650.1. [Q9Y281-1]
RefSeqiNP_001230574.1. NM_001243645.1. [Q9Y281-3]
NP_068733.1. NM_021914.7. [Q9Y281-1]
NP_619579.1. NM_138638.4. [Q9Y281-1]
UniGeneiHs.180141.

3D structure databases

ProteinModelPortaliQ9Y281.
SMRiQ9Y281. Positions 1-166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107500. 12 interactions.
DIPiDIP-33178N.
IntActiQ9Y281. 5 interactions.
MINTiMINT-1161448.
STRINGi9606.ENSP00000298159.

PTM databases

PhosphoSiteiQ9Y281.

Polymorphism databases

DMDMi6831517.

Proteomic databases

MaxQBiQ9Y281.
PaxDbiQ9Y281.
PRIDEiQ9Y281.

Protocols and materials databases

DNASUi1073.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298159; ENSP00000298159; ENSG00000165410. [Q9Y281-1]
ENST00000341223; ENSP00000340635; ENSG00000165410. [Q9Y281-1]
ENST00000555765; ENSP00000452451; ENSG00000165410. [Q9Y281-3]
ENST00000556161; ENSP00000452188; ENSG00000165410. [Q9Y281-3]
GeneIDi1073.
KEGGihsa:1073.
UCSCiuc001wsg.3. human. [Q9Y281-1]

Organism-specific databases

CTDi1073.
GeneCardsiGC14M035179.
GeneReviewsiCFL2.
HGNCiHGNC:1875. CFL2.
HPAiCAB037078.
HPA045599.
MIMi601443. gene.
610687. phenotype.
neXtProtiNX_Q9Y281.
Orphaneti171436. Typical nemaline myopathy.
PharmGKBiPA26424.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG303866.
GeneTreeiENSGT00440000033289.
HOGENOMiHOG000039697.
HOVERGENiHBG000381.
InParanoidiQ9Y281.
KOiK05765.
OMAiGLYDATY.
OrthoDBiEOG7353Z9.
PhylomeDBiQ9Y281.
TreeFamiTF328601.

Miscellaneous databases

ChiTaRSiCFL2. human.
GeneWikiiCFL2_(gene).
GenomeRNAii1073.
NextBioi4480.
PROiQ9Y281.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y281.
CleanExiHS_CFL2.
ExpressionAtlasiQ9Y281. baseline and differential.
GenevestigatoriQ9Y281.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin/Destrin.
[Graphical view]
PANTHERiPTHR11913. PTHR11913. 1 hit.
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
PRINTSiPR00006. COFILIN.
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of two isoforms of human cofilin cDNA."
    Jin J., Li G., Hu S., Li W., Yuan J., Qiang B.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CFL2A AND CFL2B).
  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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS CFL2A AND CFL2B).
    Tissue: Bone marrow, Placenta and Skeletal muscle.
  6. Bienvenut W.V., Calvo F., Kolch W.
    Submitted (FEB-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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  7. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. "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(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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-47.
  15. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT NEM7 THR-35, CHARACTERIZATION OF VARIANT NEM7 THR-35.

Entry informationi

Entry nameiCOF2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y281
Secondary accession number(s): G3V5P4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: March 4, 2015
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.