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P23528

- COF1_HUMAN

UniProt

P23528 - COF1_HUMAN

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Protein

Cofilin-1

Gene
CFL1, CFL
Organism
Homo sapiens (Human)
Status
Reviewed - 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 - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. actin cytoskeleton organization Source: ProtInc
  2. actin filament depolymerization Source: InterPro
  3. axon guidance Source: Reactome
  4. blood coagulation Source: Reactome
  5. cytoskeleton organization Source: UniProtKB
  6. establishment of cell polarity Source: Ensembl
  7. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  8. innate immune response Source: Reactome
  9. negative regulation of apoptotic process Source: UniProtKB
  10. negative regulation of cell size Source: Ensembl
  11. neural crest cell migration Source: Ensembl
  12. neural fold formation Source: Ensembl
  13. platelet activation Source: Reactome
  14. platelet degranulation Source: Reactome
  15. positive regulation of actin filament depolymerization Source: Ensembl
  16. protein import into nucleus Source: Ensembl
  17. protein phosphorylation Source: Ensembl
  18. regulation of cell morphogenesis Source: UniProtKB
  19. response to amino acid Source: Ensembl
  20. response to virus Source: UniProtKB
  21. 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.
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: Chromosome 11

Organism-specific databases

HGNCiHGNC:1874. CFL1.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. cortical actin cytoskeleton Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. extracellular space Source: UniProt
  4. extracellular vesicular exosome Source: UniProt
  5. lamellipodium membrane Source: UniProtKB-SubCell
  6. nuclear matrix Source: UniProtKB-SubCell
  7. nucleus Source: UniProtKB
  8. ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26423.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 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 – 81Phosphoserine By 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 ACKR2.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP23528.
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

ArrayExpressiP23528.
BgeeiP23528.
GenevestigatoriP23528.

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
ATXN1P542535EBI-352733,EBI-930964
PLD1Q133934EBI-352733,EBI-2827556
PLD2O149392EBI-352733,EBI-1053996
SSH1Q8WYL52EBI-352733,EBI-1222387
YWHAZP631043EBI-352733,EBI-347088

Protein-protein interaction databases

BioGridi107499. 56 interactions.
DIPiDIP-33000N.
IntActiP23528. 44 interactions.
MINTiMINT-4999473.
STRINGi9606.ENSP00000309629.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP23528.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 153150ADF-HAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi30 – 345Nuclear localization signal Reviewed prediction

Sequence similaritiesi

Contains 1 ADF-H domain.

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

MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE    50
EGKEILVGDV GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV 100
FIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA 150
EKLGGSAVIS LEGKPL 166
Length:166
Mass (Da):18,502
Last modified:January 23, 2007 - v3
Checksum:i589EF8FC1EC13719
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi116848.

Cross-referencesi

Web resourcesi

Wikipedia

Cofilin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS8114.1.
PIRi S12632.
RefSeqi NP_005498.1. NM_005507.2.
UniGenei Hs.170622.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4BEX X-ray 2.80 1 1-166 [» ]
ProteinModelPortali P23528.
SMRi P23528. Positions 1-166.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107499. 56 interactions.
DIPi DIP-33000N.
IntActi P23528. 44 interactions.
MINTi MINT-4999473.
STRINGi 9606.ENSP00000309629.

Chemistry

ChEMBLi CHEMBL1075129.

PTM databases

PhosphoSitei P23528.

Polymorphism databases

DMDMi 116848.

2D gel databases

DOSAC-COBS-2DPAGE P23528.
OGPi P23528.
REPRODUCTION-2DPAGE IPI00012011.
SWISS-2DPAGE P23528.
UCD-2DPAGE P23528.

Proteomic databases

MaxQBi P23528.
PaxDbi P23528.
PRIDEi P23528.

Protocols and materials databases

DNASUi 1072.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308162 ; ENSP00000309629 ; ENSG00000172757 .
ENST00000525451 ; ENSP00000432660 ; ENSG00000172757 .
GeneIDi 1072.
KEGGi hsa:1072.
UCSCi uc001ofs.3. human.

Organism-specific databases

CTDi 1072.
GeneCardsi GC11M065622.
H-InvDB HIX0009009.
HGNCi HGNC:1874. CFL1.
HPAi CAB037077.
MIMi 601442. gene.
neXtProti NX_P23528.
PharmGKBi PA26423.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG286948.
HOGENOMi HOG000039697.
HOVERGENi HBG000381.
InParanoidi P23528.
KOi K05765.
OrthoDBi EOG7353Z9.
PhylomeDBi P23528.
TreeFami TF328601.

Enzyme and pathway databases

Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_19236. Sema3A PAK dependent Axon repulsion.
SignaLinki P23528.

Miscellaneous databases

ChiTaRSi CFL1. human.
EvolutionaryTracei P23528.
GeneWikii Cofilin_1.
GenomeRNAii 1072.
NextBioi 4476.
PMAP-CutDB P23528.
PROi P23528.
SOURCEi Search...

Gene expression databases

ArrayExpressi P23528.
Bgeei P23528.
Genevestigatori P23528.

Family and domain databases

Gene3Di 3.40.20.10. 1 hit.
InterProi IPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin/Destrin.
IPR027234. Cofilin_1.
[Graphical view ]
PANTHERi PTHR11913. PTHR11913. 1 hit.
PTHR11913:SF17. PTHR11913:SF17. 1 hit.
Pfami PF00241. Cofilin_ADF. 1 hit.
[Graphical view ]
PRINTSi PR00006. COFILIN.
SMARTi SM00102. ADF. 1 hit.
[Graphical view ]
PROSITEi PS51263. ADF_H. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].
  19. 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. 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. 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.

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: September 3, 2014
This is version 166 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

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