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Protein

Cofilin-1

Gene

CFL1

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

Functioni

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.3 Publications

GO - Biological processi

  • actin cytoskeleton organization Source: ProtInc
  • actin filament depolymerization Source: InterPro
  • axon guidance Source: Reactome
  • blood coagulation Source: Reactome
  • cytoskeleton organization Source: UniProtKB
  • ephrin receptor signaling pathway Source: Reactome
  • establishment of cell polarity Source: Ensembl
  • Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  • innate immune response Source: Reactome
  • mitotic cytokinesis Source: Ensembl
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell size Source: Ensembl
  • neural crest cell migration Source: Ensembl
  • neural fold formation Source: Ensembl
  • platelet activation Source: Reactome
  • platelet degranulation Source: Reactome
  • positive regulation of actin filament depolymerization Source: Ensembl
  • protein import into nucleus Source: Ensembl
  • protein phosphorylation Source: Ensembl
  • regulation of cell morphogenesis Source: UniProtKB
  • regulation of dendritic spine morphogenesis Source: ParkinsonsUK-UCL
  • response to amino acid Source: Ensembl
  • response to virus Source: UniProtKB
  • Rho protein signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_19236. Sema3A PAK dependent Axon repulsion.
REACT_263952. EPHB-mediated forward signaling.
REACT_318. Platelet degranulation.
SignaLinkiP23528.

Names & Taxonomyi

Protein namesi
Recommended name:
Cofilin-1
Alternative name(s):
18 kDa phosphoprotein
Short name:
p18
Cofilin, non-muscle isoform
Gene namesi
Name:CFL1
Synonyms:CFL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:1874. CFL1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell junction Source: Ensembl
  • cortical actin cytoskeleton Source: Ensembl
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • lamellipodium membrane Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • nuclear matrix Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
  • ruffle membrane Source: UniProtKB-SubCell
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26423.

Polymorphism and mutation databases

BioMutaiCFL1.
DMDMi116848.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed9 Publications
Chaini2 – 166165Cofilin-1PRO_0000214898Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine8 Publications
Modified residuei3 – 31Phosphoserine; by NRK6 Publications
Modified residuei8 – 81PhosphoserineBy similarity
Modified residuei13 – 131N6-acetyllysine1 Publication
Modified residuei25 – 251Phosphothreonine1 Publication
Modified residuei68 – 681Phosphotyrosine1 Publication
Modified residuei73 – 731N6-acetyllysine1 Publication
Modified residuei140 – 1401Phosphotyrosine1 Publication
Modified residuei144 – 1441N6-acetyllysine1 Publication
Modified residuei156 – 1561Phosphoserine3 Publications

Post-translational modificationi

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.By similarity2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP23528.
PRIDEiP23528.

2D gel databases

DOSAC-COBS-2DPAGEP23528.
OGPiP23528.
REPRODUCTION-2DPAGEIPI00012011.
SWISS-2DPAGEP23528.
UCD-2DPAGEP23528.

PTM databases

PhosphoSiteiP23528.

Miscellaneous databases

PMAP-CutDBP23528.

Expressioni

Tissue specificityi

Widely distributed in various tissues.

Inductioni

Up-regulated in response to enterovirus 71 (EV71) infection (at protein level).1 Publication

Gene expression databases

BgeeiP23528.
ExpressionAtlasiP23528. baseline and differential.
GenevisibleiP23528. HS.

Organism-specific databases

HPAiCAB037077.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTBP607094EBI-352733,EBI-353944
ACTG1P632616EBI-352733,EBI-351292
ATXN1P542535EBI-352733,EBI-930964
CFL2Q549N03EBI-352733,EBI-10201319
PLD1Q133934EBI-352733,EBI-2827556
PLD2O149392EBI-352733,EBI-1053996
PS1TP5BP1Q1KLZ03EBI-352733,EBI-9978131
SSH1Q8WYL52EBI-352733,EBI-1222387
YWHAZP631043EBI-352733,EBI-347088

Protein-protein interaction databases

BioGridi107499. 60 interactions.
DIPiDIP-33000N.
IntActiP23528. 49 interactions.
MINTiMINT-4999473.
STRINGi9606.ENSP00000309629.

Structurei

Secondary structure

1
166
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1810Combined sources
Turni28 – 303Combined sources
Beta strandi31 – 4010Combined sources
Beta strandi42 – 454Combined sources
Beta strandi46 – 5611Combined sources
Helixi57 – 593Combined sources
Helixi60 – 645Combined sources
Helixi67 – 748Combined sources
Beta strandi77 – 793Combined sources
Beta strandi81 – 9010Combined sources
Beta strandi95 – 10410Combined sources
Helixi111 – 1199Combined sources
Helixi121 – 1255Combined sources
Beta strandi133 – 1375Combined sources
Helixi140 – 1434Combined sources
Helixi146 – 1549Combined sources
Helixi155 – 1573Combined sources
Beta strandi161 – 1644Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP23528.
SMRiP23528. Positions 1-166.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23528.

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

eggNOGiNOG286948.
HOGENOMiHOG000039697.
HOVERGENiHBG000381.
InParanoidiP23528.
KOiK05765.
OrthoDBiEOG7353Z9.
PhylomeDBiP23528.
TreeFamiTF328601.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin/Destrin.
IPR027234. Cofilin_1.
[Graphical view]
PANTHERiPTHR11913. PTHR11913. 1 hit.
PTHR11913:SF17. PTHR11913:SF17. 1 hit.
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
PRINTSiPR00006. COFILIN.
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P23528-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE
60 70 80 90 100
EGKEILVGDV GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV
110 120 130 140 150
FIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA
160
EKLGGSAVIS LEGKPL
Length:166
Mass (Da):18,502
Last modified:January 23, 2007 - v3
Checksum:i589EF8FC1EC13719
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8114.1.
PIRiS12632.
RefSeqiNP_005498.1. NM_005507.2.
UniGeneiHs.170622.

Genome annotation databases

EnsembliENST00000308162; ENSP00000309629; ENSG00000172757.
ENST00000525451; ENSP00000432660; ENSG00000172757.
GeneIDi1072.
KEGGihsa:1072.
UCSCiuc001ofs.3. human.

Cross-referencesi

Web resourcesi

Wikipedia

Cofilin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8114.1.
PIRiS12632.
RefSeqiNP_005498.1. NM_005507.2.
UniGeneiHs.170622.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP23528.
SMRiP23528. Positions 1-166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107499. 60 interactions.
DIPiDIP-33000N.
IntActiP23528. 49 interactions.
MINTiMINT-4999473.
STRINGi9606.ENSP00000309629.

Chemistry

ChEMBLiCHEMBL1075129.

PTM databases

PhosphoSiteiP23528.

Polymorphism and mutation databases

BioMutaiCFL1.
DMDMi116848.

2D gel databases

DOSAC-COBS-2DPAGEP23528.
OGPiP23528.
REPRODUCTION-2DPAGEIPI00012011.
SWISS-2DPAGEP23528.
UCD-2DPAGEP23528.

Proteomic databases

PaxDbiP23528.
PRIDEiP23528.

Protocols and materials databases

DNASUi1072.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308162; ENSP00000309629; ENSG00000172757.
ENST00000525451; ENSP00000432660; ENSG00000172757.
GeneIDi1072.
KEGGihsa:1072.
UCSCiuc001ofs.3. human.

Organism-specific databases

CTDi1072.
GeneCardsiGC11M065622.
H-InvDBHIX0009009.
HGNCiHGNC:1874. CFL1.
HPAiCAB037077.
MIMi601442. gene.
neXtProtiNX_P23528.
PharmGKBiPA26423.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG286948.
HOGENOMiHOG000039697.
HOVERGENiHBG000381.
InParanoidiP23528.
KOiK05765.
OrthoDBiEOG7353Z9.
PhylomeDBiP23528.
TreeFamiTF328601.

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_19236. Sema3A PAK dependent Axon repulsion.
REACT_263952. EPHB-mediated forward signaling.
REACT_318. Platelet degranulation.
SignaLinkiP23528.

Miscellaneous databases

ChiTaRSiCFL1. human.
EvolutionaryTraceiP23528.
GeneWikiiCofilin_1.
GenomeRNAii1072.
NextBioi4476.
PMAP-CutDBP23528.
PROiP23528.
SOURCEiSearch...

Gene expression databases

BgeeiP23528.
ExpressionAtlasiP23528. baseline and differential.
GenevisibleiP23528. HS.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin/Destrin.
IPR027234. Cofilin_1.
[Graphical view]
PANTHERiPTHR11913. PTHR11913. 1 hit.
PTHR11913:SF17. PTHR11913:SF17. 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. 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. 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. 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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  19. 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].
  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], CLEAVAGE OF INITIATOR METHIONINE [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], CLEAVAGE OF INITIATOR METHIONINE [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. 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], CLEAVAGE OF INITIATOR METHIONINE [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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  27. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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. "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(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  30. "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.

Entry informationi

Entry nameiCOF1_HUMAN
AccessioniPrimary (citable) accession number: P23528
Secondary accession number(s): B3KUQ1, Q53Y87, Q9UCA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 176 of the entry and version 3 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.