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Q6IBS0

- TWF2_HUMAN

UniProt

Q6IBS0 - TWF2_HUMAN

Protein

Twinfilin-2

Gene

TWF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 2 (02 May 2006)
      Previous versions | rss
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    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. May play a role in regulating the mature length of the middle and short rows of stereocilia By similarity.By similarity

    GO - Molecular functioni

    1. actin monomer binding Source: BHF-UCL
    2. ATP binding Source: UniProtKB
    3. phosphatidylinositol-4,5-bisphosphate binding Source: BHF-UCL
    4. poly(A) RNA binding Source: UniProtKB
    5. protein kinase C binding Source: BHF-UCL

    GO - Biological processi

    1. barbed-end actin filament capping Source: BHF-UCL
    2. cell projection organization Source: UniProtKB-KW
    3. cellular response to growth factor stimulus Source: BHF-UCL
    4. cellular response to retinoic acid Source: BHF-UCL
    5. negative regulation of actin filament polymerization Source: BHF-UCL
    6. positive regulation of axon extension Source: BHF-UCL
    7. positive regulation of lamellipodium assembly Source: BHF-UCL
    8. positive regulation of neuron projection development Source: BHF-UCL
    9. regulation of actin cytoskeleton organization Source: BHF-UCL
    10. regulation of microvillus length Source: BHF-UCL
    11. sequestering of actin monomers Source: BHF-UCL

    Keywords - Biological processi

    Cilium biogenesis/degradation

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Twinfilin-2
    Alternative name(s):
    A6-related protein
    Short name:
    hA6RP
    Protein tyrosine kinase 9-like
    Twinfilin-1-like protein
    Gene namesi
    Name:TWF2
    Synonyms:PTK9L
    ORF Names:MSTP011
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9621. TWF2.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cytoplasmperinuclear region 1 Publication. Cell projectionstereocilium By similarity
    Note: Perinuclear and G-actin-rich cortical actin structure sublocalization.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB-SubCell
    3. extracellular vesicular exosome Source: UniProt
    4. filopodium Source: BHF-UCL
    5. growth cone Source: BHF-UCL
    6. lamellipodium Source: BHF-UCL
    7. myofibril Source: BHF-UCL
    8. perinuclear region of cytoplasm Source: BHF-UCL
    9. stereocilium Source: BHF-UCL

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162407429.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 349348Twinfilin-2PRO_0000233136Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei14 – 141N6-acetyllysine1 Publication
    Modified residuei309 – 3091Phosphotyrosine3 Publications
    Modified residuei349 – 3491Phosphoserine3 Publications

    Post-translational modificationi

    In vitro, phosphorylated by PRKCZ, CK2 and SRC.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ6IBS0.
    PaxDbiQ6IBS0.
    PeptideAtlasiQ6IBS0.
    PRIDEiQ6IBS0.

    2D gel databases

    OGPiQ9Y3F5.

    PTM databases

    PhosphoSiteiQ6IBS0.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ6IBS0.
    BgeeiQ6IBS0.
    CleanExiHS_TWF2.
    GenevestigatoriQ6IBS0.

    Organism-specific databases

    HPAiHPA053874.

    Interactioni

    Subunit structurei

    Interacts with G-actin; ADP-actin form and capping protein (CP). May also be able to interact with TWF1 and phosphoinositides, PI(4,5)P2. When bound to PI(4,5)P2, it is down-regulated. Interacts with MYO7A By similarity.By similarity

    Protein-protein interaction databases

    BioGridi116472. 51 interactions.
    IntActiQ6IBS0. 6 interactions.
    MINTiMINT-1414584.
    STRINGi9606.ENSP00000303908.

    Structurei

    Secondary structure

    1
    349
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 2212
    Beta strandi26 – 338
    Beta strandi36 – 438
    Helixi49 – 579
    Helixi58 – 603
    Beta strandi67 – 7711
    Beta strandi80 – 889
    Helixi95 – 11218
    Helixi114 – 1163
    Beta strandi117 – 1259
    Helixi126 – 1294
    Helixi131 – 1366
    Helixi184 – 19411
    Beta strandi199 – 2068
    Turni207 – 2104
    Beta strandi211 – 2166
    Helixi222 – 2287
    Beta strandi231 – 2333
    Beta strandi235 – 24511
    Beta strandi248 – 25811
    Helixi261 – 2633
    Helixi266 – 28520
    Beta strandi291 – 2988
    Helixi300 – 3023
    Helixi305 – 3128

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VACX-ray1.70A6-137[»]
    2W0IX-ray1.80A181-313[»]
    ProteinModelPortaliQ6IBS0.
    SMRiQ6IBS0. Positions 6-137, 181-313.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6IBS0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 139136ADF-H 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini177 – 313137ADF-H 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 ADF-H domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG263290.
    HOGENOMiHOG000168296.
    HOVERGENiHBG000848.
    InParanoidiQ6IBS0.
    KOiK08870.
    OMAiHATPELK.
    OrthoDBiEOG79GT6W.
    PhylomeDBiQ6IBS0.
    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.

    Q6IBS0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAHQTGIHAT EELKEFFAKA RAGSVRLIKV VIEDEQLVLG ASQEPVGRWD    50
    QDYDRAVLPL LDAQQPCYLL YRLDSQNAQG FEWLFLAWSP DNSPVRLKML 100
    YAATRATVKK EFGGGHIKDE LFGTVKDDLS FAGYQKHLSS CAAPAPLTSA 150
    ERELQQIRIN EVKTEISVES KHQTLQGLAF PLQPEAQRAL QQLKQKMVNY 200
    IQMKLDLERE TIELVHTEPT DVAQLPSRVP RDAARYHFFL YKHTHEGDPL 250
    ESVVFIYSMP GYKCSIKERM LYSSCKSRLL DSVEQDFHLE IAKKIEIGDG 300
    AELTAEFLYD EVHPKQHAFK QAFAKPKGPG GKRGHKRLIR GPGENGDDS 349
    Length:349
    Mass (Da):39,548
    Last modified:May 2, 2006 - v2
    Checksum:i635EF8C04EFCE92B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti110 – 1101K → R in CAG33013. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721R → C.1 Publication
    Corresponds to variant rs35114109 [ dbSNP | Ensembl ].
    VAR_042407
    Natural varianti76 – 761Q → R.1 Publication
    Corresponds to variant rs35711542 [ dbSNP | Ensembl ].
    VAR_042408
    Natural varianti103 – 1031A → T in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
    VAR_042409

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y17169 mRNA. Translation: CAB38055.1.
    AL136773 mRNA. Translation: CAB66707.1.
    AF109365 mRNA. Translation: AAQ13513.1.
    CR456732 mRNA. Translation: CAG33013.1.
    CR533520 mRNA. Translation: CAG38551.1.
    BC000327 mRNA. Translation: AAH00327.1.
    BC003161 mRNA. Translation: AAH03161.1.
    BC016452 mRNA. Translation: AAH16452.1.
    CCDSiCCDS2849.1.
    PIRiT46362.
    RefSeqiNP_009215.1. NM_007284.3.
    UniGeneiHs.436439.

    Genome annotation databases

    EnsembliENST00000305533; ENSP00000303908; ENSG00000247596.
    GeneIDi11344.
    KEGGihsa:11344.
    UCSCiuc003ddd.3. human.

    Polymorphism databases

    DMDMi94730596.

    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
    Y17169 mRNA. Translation: CAB38055.1 .
    AL136773 mRNA. Translation: CAB66707.1 .
    AF109365 mRNA. Translation: AAQ13513.1 .
    CR456732 mRNA. Translation: CAG33013.1 .
    CR533520 mRNA. Translation: CAG38551.1 .
    BC000327 mRNA. Translation: AAH00327.1 .
    BC003161 mRNA. Translation: AAH03161.1 .
    BC016452 mRNA. Translation: AAH16452.1 .
    CCDSi CCDS2849.1.
    PIRi T46362.
    RefSeqi NP_009215.1. NM_007284.3.
    UniGenei Hs.436439.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VAC X-ray 1.70 A 6-137 [» ]
    2W0I X-ray 1.80 A 181-313 [» ]
    ProteinModelPortali Q6IBS0.
    SMRi Q6IBS0. Positions 6-137, 181-313.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116472. 51 interactions.
    IntActi Q6IBS0. 6 interactions.
    MINTi MINT-1414584.
    STRINGi 9606.ENSP00000303908.

    PTM databases

    PhosphoSitei Q6IBS0.

    Polymorphism databases

    DMDMi 94730596.

    2D gel databases

    OGPi Q9Y3F5.

    Proteomic databases

    MaxQBi Q6IBS0.
    PaxDbi Q6IBS0.
    PeptideAtlasi Q6IBS0.
    PRIDEi Q6IBS0.

    Protocols and materials databases

    DNASUi 11344.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000305533 ; ENSP00000303908 ; ENSG00000247596 .
    GeneIDi 11344.
    KEGGi hsa:11344.
    UCSCi uc003ddd.3. human.

    Organism-specific databases

    CTDi 11344.
    GeneCardsi GC03M052262.
    HGNCi HGNC:9621. TWF2.
    HPAi HPA053874.
    MIMi 607433. gene.
    neXtProti NX_Q6IBS0.
    PharmGKBi PA162407429.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263290.
    HOGENOMi HOG000168296.
    HOVERGENi HBG000848.
    InParanoidi Q6IBS0.
    KOi K08870.
    OMAi HATPELK.
    OrthoDBi EOG79GT6W.
    PhylomeDBi Q6IBS0.
    TreeFami TF352598.

    Miscellaneous databases

    EvolutionaryTracei Q6IBS0.
    GeneWikii TWF2.
    GenomeRNAii 11344.
    NextBioi 43112.
    PROi Q6IBS0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6IBS0.
    Bgeei Q6IBS0.
    CleanExi HS_TWF2.
    Genevestigatori Q6IBS0.

    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, expression and characterization of an A6 related protein."
      Rohwer A., Kittstein W., Marks F., Gschwendt M.
      Eur. J. Biochem. 263:518-525(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION.
      Tissue: Keratinocyte.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Aorta.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney, Lung and Placenta.
    6. Bienvenut W.V., Vousden K.H., Lukashchuk N.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-19 AND 279-293, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Lung carcinoma.
    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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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].
    10. "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-309 AND SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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 AND LYS-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-72; ARG-76 AND THR-103.

    Entry informationi

    Entry nameiTWF2_HUMAN
    AccessioniPrimary (citable) accession number: Q6IBS0
    Secondary accession number(s): Q9Y3F5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2006
    Last sequence update: May 2, 2006
    Last modified: October 1, 2014
    This is version 100 of the entry and version 2 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 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3