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)

Q91YR1

- TWF1_MOUSE

UniProt

Q91YR1 - TWF1_MOUSE

Protein

Twinfilin-1

Gene

Twf1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (04 Apr 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.4 Publications

    GO - Molecular functioni

    1. actin monomer binding Source: BHF-UCL
    2. ATP binding Source: Ensembl
    3. phosphatidylinositol-4,5-bisphosphate binding Source: BHF-UCL
    4. protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. barbed-end actin filament capping Source: BHF-UCL
    2. negative regulation of actin filament polymerization Source: BHF-UCL
    3. peptidyl-tyrosine phosphorylation Source: GOC
    4. regulation of actin phosphorylation Source: Ensembl
    5. sequestering of actin monomers Source: BHF-UCL

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Twinfilin-1
    Alternative name(s):
    Protein A6
    Gene namesi
    Name:Twf1
    Synonyms:Ptk9
    OrganismiMus musculus (Mouse)Imported
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1100520. Twf1.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytoskeleton 1 Publication
    Note: Diffuse cytoplasmic localization with perinuclear and G-actin-rich cortical actin structures sublocalization. Also found at membrane ruffles and cell-cell contacts.

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. cell-cell junction Source: BHF-UCL
    3. filopodium Source: BHF-UCL
    4. myofibril Source: BHF-UCL
    5. perinuclear region of cytoplasm Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 350349Twinfilin-1PRO_0000214951Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei143 – 1431PhosphoserineBy similarity
    Modified residuei309 – 3091Phosphotyrosine2 Publications
    Modified residuei349 – 3491Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylated on serine and threonine residues.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ91YR1.
    PaxDbiQ91YR1.
    PRIDEiQ91YR1.

    PTM databases

    PhosphoSiteiQ91YR1.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels in brain, liver and kidney. Also expressed in heart, lung and testis. Not detected in spleen or skeletal muscle.3 Publications

    Developmental stagei

    Expression was widespread throughout the embryonic stages analyzed; E10.5, E12.5, E14.5 and E18.5. At E14.5, strongest expression was observed in the developing central and peripheral nervous system (CNS and PNS, respectively) and in the olfactory sensory epithelium. In the CNS, the proliferating neuronal precursors in the ventricular zone expressed it more than the postmitotic neurons. At E18.5, highest expression levels were detected in the mechanosensory hair cells of the inner ear and in the differentiated keratinocytes of the skin.1 Publication

    Gene expression databases

    ArrayExpressiQ91YR1.
    BgeeiQ91YR1.
    GenevestigatoriQ91YR1.

    Interactioni

    Subunit structurei

    Interacts with G-actin; ADP-actin form and capping protein (CP). May also be able to interact with TWF2 and phosphoinositides, PI(4,5)P2. When bound to PI(4,5)P2, it is down-regulated.4 Publications

    Protein-protein interaction databases

    BioGridi202468. 1 interaction.
    DIPiDIP-33923N.
    IntActiQ91YR1. 3 interactions.
    MINTiMINT-1869546.

    Structurei

    Secondary structure

    1
    350
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 2111
    Turni22 – 243
    Beta strandi26 – 327
    Beta strandi34 – 4310
    Helixi49 – 579
    Helixi58 – 603
    Beta strandi67 – 7711
    Beta strandi80 – 889
    Helixi95 – 11218
    Helixi114 – 1163
    Beta strandi117 – 1259
    Helixi126 – 1294
    Helixi131 – 1388
    Helixi184 – 19411
    Beta strandi199 – 2068
    Turni207 – 2104
    Beta strandi211 – 2166
    Helixi222 – 2243
    Helixi226 – 2283
    Beta strandi231 – 2333
    Beta strandi235 – 24511
    Beta strandi248 – 25811
    Beta strandi262 – 2643
    Helixi266 – 2749
    Helixi276 – 28712
    Beta strandi291 – 30212
    Helixi305 – 3128

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M4JX-ray1.60A/B1-142[»]
    2D8BNMR-A161-313[»]
    2HD7NMR-A176-316[»]
    3DAWX-ray2.55B167-322[»]
    ProteinModelPortaliQ91YR1.
    SMRiQ91YR1. Positions 7-139, 161-313.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ91YR1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 139138ADF-H 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini175 – 313139ADF-H 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 ADF-H domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG263290.
    GeneTreeiENSGT00530000063868.
    HOGENOMiHOG000168296.
    HOVERGENiHBG000848.
    InParanoidiQ91YR1.
    KOiK08870.
    OMAiTVFIYSM.
    OrthoDBiEOG79GT6W.
    PhylomeDBiQ91YR1.
    TreeFamiTF352598.

    Family and domain databases

    Gene3Di3.40.20.10. 2 hits.
    InterProiIPR002108. ADF-H.
    IPR029006. ADF-H/Gelsolin-like_dom.
    IPR028458. Twinfilin.
    [Graphical view]
    PANTHERiPTHR13759. PTHR13759. 1 hit.
    PfamiPF00241. Cofilin_ADF. 2 hits.
    [Graphical view]
    SMARTiSM00102. ADF. 2 hits.
    [Graphical view]
    PROSITEiPS51263. ADF_H. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q91YR1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHQTGIQAS EDVKEIFARA RNGKYRLLKI SIENEQLVVG SCSPPSDSWE    50
    QDYDSFVLPL LEDKQPCYVL FRLDSQNAQG YEWIFIAWSP DHSHVRQKML 100
    YAATRATLKK EFGGGHIKDE VFGTVKEDVS LHGYKKYLLS QSSPAPLTAA 150
    EEELRQIKIN EVQTDVSVDT KHQTLQGVAF PISRDAFQAL EKLSKKQLNY 200
    VQLEIDIKNE TIILANTENT ELRDLPKRIP KDSARYHFFL YKHSHEGDYL 250
    ESVVFIYSMP GYTCSIRERM LYSSCKSPLL EIVERQLQMD VIRKIEIDNG 300
    DELTADFLYD EVHPKQHAHK QSFAKPKGPA GKRGIRRLIR GPAEAEATTD 350
    Length:350
    Mass (Da):40,079
    Last modified:April 4, 2006 - v2
    Checksum:i643CBBA18D38D4E0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti345 – 3451A → R in AAB66592. (PubMed:9249064)Curated
    Sequence conflicti345 – 3451A → R in AAP31404. (PubMed:12807912)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti51 – 511Q → H.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82324 mRNA. Translation: AAB66592.1.
    AY267188 mRNA. Translation: AAP31404.1.
    AK147990 mRNA. Translation: BAE28272.1.
    AK150852 mRNA. Translation: BAE29908.1.
    BC015081 mRNA. Translation: AAH15081.1.
    BC094034 mRNA. Translation: AAH94034.1.
    CCDSiCCDS27773.1.
    RefSeqiNP_032997.3. NM_008971.4.
    UniGeneiMm.490250.

    Genome annotation databases

    EnsembliENSMUST00000023087; ENSMUSP00000023087; ENSMUSG00000022451.
    GeneIDi19230.
    KEGGimmu:19230.
    UCSCiuc007xjl.1. mouse.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Molecular embrace - Issue 73 of August 2006

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82324 mRNA. Translation: AAB66592.1 .
    AY267188 mRNA. Translation: AAP31404.1 .
    AK147990 mRNA. Translation: BAE28272.1 .
    AK150852 mRNA. Translation: BAE29908.1 .
    BC015081 mRNA. Translation: AAH15081.1 .
    BC094034 mRNA. Translation: AAH94034.1 .
    CCDSi CCDS27773.1.
    RefSeqi NP_032997.3. NM_008971.4.
    UniGenei Mm.490250.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M4J X-ray 1.60 A/B 1-142 [» ]
    2D8B NMR - A 161-313 [» ]
    2HD7 NMR - A 176-316 [» ]
    3DAW X-ray 2.55 B 167-322 [» ]
    ProteinModelPortali Q91YR1.
    SMRi Q91YR1. Positions 7-139, 161-313.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202468. 1 interaction.
    DIPi DIP-33923N.
    IntActi Q91YR1. 3 interactions.
    MINTi MINT-1869546.

    PTM databases

    PhosphoSitei Q91YR1.

    Proteomic databases

    MaxQBi Q91YR1.
    PaxDbi Q91YR1.
    PRIDEi Q91YR1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023087 ; ENSMUSP00000023087 ; ENSMUSG00000022451 .
    GeneIDi 19230.
    KEGGi mmu:19230.
    UCSCi uc007xjl.1. mouse.

    Organism-specific databases

    CTDi 5756.
    MGIi MGI:1100520. Twf1.

    Phylogenomic databases

    eggNOGi NOG263290.
    GeneTreei ENSGT00530000063868.
    HOGENOMi HOG000168296.
    HOVERGENi HBG000848.
    InParanoidi Q91YR1.
    KOi K08870.
    OMAi TVFIYSM.
    OrthoDBi EOG79GT6W.
    PhylomeDBi Q91YR1.
    TreeFami TF352598.

    Miscellaneous databases

    ChiTaRSi TWF1. mouse.
    EvolutionaryTracei Q91YR1.
    NextBioi 296036.
    PROi Q91YR1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q91YR1.
    Bgeei Q91YR1.
    Genevestigatori Q91YR1.

    Family and domain databases

    Gene3Di 3.40.20.10. 2 hits.
    InterProi IPR002108. ADF-H.
    IPR029006. ADF-H/Gelsolin-like_dom.
    IPR028458. Twinfilin.
    [Graphical view ]
    PANTHERi PTHR13759. PTHR13759. 1 hit.
    Pfami PF00241. Cofilin_ADF. 2 hits.
    [Graphical view ]
    SMARTi SM00102. ADF. 2 hits.
    [Graphical view ]
    PROSITEi PS51263. ADF_H. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the mouse homolog of the human A6 gene."
      Beeler J.F., Patel B.K.R., Chedid M., LaRochelle W.J.
      Gene 193:31-37(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    2. "Mammals have two twinfilin isoforms whose subcellular localizations and tissue distributions are differentially regulated."
      Vartiainen M.K., Sarkkinen E.M., Matilainen T., Salminen M., Lappalainen P.
      J. Biol. Chem. 278:34347-34355(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH TWF2 AND PHOSPHOINOSITIDE, DEVELOPMENTAL STAGE.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow.
    4. "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], VARIANT HIS-51.
      Strain: NMRI.
      Tissue: Mammary gland and Mammary tumor.
    5. "Mouse A6/twinfilin is an actin monomer-binding protein that localizes to the regions of rapid actin dynamics."
      Vartiainen M., Ojala P.J., Auvinen P., Peranen J., Lappalainen P.
      Mol. Cell. Biol. 20:1772-1783(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "Biological role and structural mechanism of twinfilin-capping protein interaction."
      Falck S., Paavilainen V.O., Wear M.A., Grossmann J.G., Cooper J.A., Lappalainen P.
      EMBO J. 23:3010-3019(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH G-ACTIN AND CAPPING PROTEINS.
    7. "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-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Mammalian twinfilin sequesters ADP-G-actin and caps filament barbed ends: implications in motility."
      Helfer E., Nevalainen E.M., Naumanen P., Romero S., Didry D., Pantaloni D., Lappalainen P., Carlier M.-F.
      EMBO J. 25:1184-1195(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH G-ACTIN AND CAPPING PROTEINS.
    9. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    10. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    11. "Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin."
      Paavilainen V.O., Merckel M.C., Falck S., Ojala P.J., Pohl E., Wilmanns M., Lappalainen P.
      J. Biol. Chem. 277:43089-43095(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-142.
    12. Cited for: STRUCTURE BY NMR OF 161-313.

    Entry informationi

    Entry nameiTWF1_MOUSE
    AccessioniPrimary (citable) accession number: Q91YR1
    Secondary accession number(s): O09132, Q52L77, Q80X09
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 2, 2004
    Last sequence update: April 4, 2006
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3