Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P23528

- COF1_HUMAN

UniProt

P23528 - COF1_HUMAN

Protein

Cofilin-1

Gene

CFL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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 1 Publication. Cytoplasmcytoskeleton 1 Publication. Cell projectionruffle membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cell projectionlamellipodium membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
    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.

    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. membrane Source: UniProtKB
    7. nuclear matrix Source: UniProtKB-SubCell
    8. nucleus Source: UniProtKB
    9. ruffle membrane Source: UniProtKB-SubCell
    10. vesicle Source: UniProtKB

    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 – 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 NRK7 Publications
    Modified residuei8 – 81PhosphoserineBy similarity
    Modified residuei13 – 131N6-acetyllysine1 Publication
    Modified residuei25 – 251Phosphothreonine2 Publications
    Modified residuei68 – 681Phosphotyrosine2 Publications
    Modified residuei73 – 731N6-acetyllysine1 Publication
    Modified residuei140 – 1401Phosphotyrosine2 Publications
    Modified residuei144 – 1441N6-acetyllysine1 Publication
    Modified residuei156 – 1561Phosphoserine4 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 similarity9 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.
    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

    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

    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: October 1, 2014
    This is version 167 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