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Q12792

- TWF1_HUMAN

UniProt

Q12792 - TWF1_HUMAN

Protein

Twinfilin-1

Gene

TWF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 3 (22 Sep 2009)
      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 By similarity.By similarity

    GO - Molecular functioni

    1. actin monomer binding Source: BHF-UCL
    2. ATP binding Source: BHF-UCL
    3. phosphatidylinositol-4,5-bisphosphate binding Source: BHF-UCL

    GO - Biological processi

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

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Twinfilin-1
    Alternative name(s):
    Protein A6
    Protein tyrosine kinase 9
    Gene namesi
    Name:TWF1
    Synonyms:PTK9
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9620. TWF1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. cell-cell junction Source: BHF-UCL
    3. cytoplasm Source: HPA
    4. filopodium Source: BHF-UCL
    5. myofibril Source: BHF-UCL
    6. perinuclear region of cytoplasm Source: BHF-UCL
    7. ruffle membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162407406.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 350349Twinfilin-1PRO_0000214950Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei143 – 1431Phosphoserine2 Publications
    Modified residuei309 – 3091Phosphotyrosine3 Publications
    Modified residuei349 – 3491Phosphothreonine2 Publications

    Post-translational modificationi

    Phosphorylated on serine and threonine residues.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ12792.
    PaxDbiQ12792.
    PRIDEiQ12792.

    2D gel databases

    OGPiQ12792.

    PTM databases

    PhosphoSiteiQ12792.

    Expressioni

    Tissue specificityi

    Expressed at high levels in the colon, testis, ovary, prostate and lung. Expressed at lower levels in the brain, bladder and heart. Not detected in liver.1 Publication

    Gene expression databases

    ArrayExpressiQ12792.
    BgeeiQ12792.
    GenevestigatoriQ12792.

    Organism-specific databases

    HPAiHPA018116.

    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 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi111723. 23 interactions.
    IntActiQ12792. 3 interactions.
    MINTiMINT-3026525.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12792.
    SMRiQ12792. Positions 7-139, 176-316.
    ModBaseiSearch...
    MobiDBiSearch...

    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.
    HOVERGENiHBG000848.
    KOiK08870.
    OrthoDBiEOG79GT6W.
    PhylomeDBiQ12792.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1Curated (identifier: Q12792-2) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSHQTGIQAS EDVKEIFARA RNGKYRLLKI SIENEQLVIG SYSQPSDSWD    50
    KDYDSFVLPL LEDKQPCYIL FRLDSQNAQG YEWIFIAWSP DHSHVRQKML 100
    YAATRATLKK EFGGGHIKDE VFGTVKEDVS LHGYKKYLLS QSSPAPLTAA 150
    EEELRQIKIN EVQTDVGVDT KHQTLQGVAF PISREAFQAL EKLNNRQLNY 200
    VQLEIDIKNE IIILANTTNT ELKDLPKRIP KDSARYHFFL YKHSHEGDYL 250
    ESIVFIYSMP GYTCSIRERM LYSSCKSRLL EIVERQLQMD VIRKIEIDNG 300
    DELTADFLYE EVHPKQHAHK QSFAKPKGPA GKRGIRRLIR GPAETEATTD 350
    Length:350
    Mass (Da):40,283
    Last modified:September 22, 2009 - v3
    Checksum:i5F68A6946E969A80
    GO
    Isoform 3 (identifier: Q12792-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         161-161: E → ESPEDHIG

    Show »
    Length:357
    Mass (Da):41,018
    Checksum:i826E95A7D995033B
    GO
    Isoform 4 (identifier: Q12792-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-98: Missing.

    Show »
    Length:252
    Mass (Da):28,823
    Checksum:iCCE0A5A82BBE109D
    GO

    Sequence cautioni

    The sequence AAH43148.2 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH68548.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAD92539.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121D → Y in CAG46561. 1 PublicationCurated
    Sequence conflicti246 – 2461E → V in BAG54588. (PubMed:14702039)Curated
    Sequence conflicti269 – 2691R → W in CAG46536. 1 PublicationCurated
    Sequence conflicti302 – 3021E → G in BAF83912. (PubMed:14702039)Curated
    Sequence conflicti329 – 3291P → H in BAG59691. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9898Missing in isoform 4. 2 PublicationsVSP_038075Add
    BLAST
    Alternative sequencei161 – 1611E → ESPEDHIG in isoform 3. 1 PublicationVSP_017899

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U02680 mRNA. Translation: AAC50062.1.
    AK127868 mRNA. Translation: BAG54588.1.
    AK291223 mRNA. Translation: BAF83912.1.
    AK297206 mRNA. Translation: BAG59691.1.
    CR541736 mRNA. Translation: CAG46536.1.
    CR541761 mRNA. Translation: CAG46561.1.
    BT019691 mRNA. Translation: AAV38497.1.
    AB209302 mRNA. Translation: BAD92539.1. Different initiation.
    BC022344 mRNA. Translation: AAH22344.1.
    BC043148 mRNA. Translation: AAH43148.2. Different initiation.
    BC068548 mRNA. Translation: AAH68548.1. Different initiation.
    CCDSiCCDS31780.2. [Q12792-2]
    CCDS55818.1. [Q12792-3]
    PIRiA55922.
    RefSeqiNP_001229326.1. NM_001242397.1. [Q12792-3]
    NP_002813.3. NM_002822.4. [Q12792-2]
    UniGeneiHs.189075.
    Hs.313056.

    Genome annotation databases

    EnsembliENST00000395510; ENSP00000378886; ENSG00000151239. [Q12792-2]
    ENST00000548315; ENSP00000449428; ENSG00000151239. [Q12792-3]
    ENST00000552521; ENSP00000448750; ENSG00000151239. [Q12792-4]
    GeneIDi5756.
    KEGGihsa:5756.
    UCSCiuc001roa.4. human. [Q12792-2]
    uc001rob.3. human. [Q12792-3]

    Polymorphism databases

    DMDMi259016376.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Molecular embrace - Issue 73 of August 2006

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U02680 mRNA. Translation: AAC50062.1 .
    AK127868 mRNA. Translation: BAG54588.1 .
    AK291223 mRNA. Translation: BAF83912.1 .
    AK297206 mRNA. Translation: BAG59691.1 .
    CR541736 mRNA. Translation: CAG46536.1 .
    CR541761 mRNA. Translation: CAG46561.1 .
    BT019691 mRNA. Translation: AAV38497.1 .
    AB209302 mRNA. Translation: BAD92539.1 . Different initiation.
    BC022344 mRNA. Translation: AAH22344.1 .
    BC043148 mRNA. Translation: AAH43148.2 . Different initiation.
    BC068548 mRNA. Translation: AAH68548.1 . Different initiation.
    CCDSi CCDS31780.2. [Q12792-2 ]
    CCDS55818.1. [Q12792-3 ]
    PIRi A55922.
    RefSeqi NP_001229326.1. NM_001242397.1. [Q12792-3 ]
    NP_002813.3. NM_002822.4. [Q12792-2 ]
    UniGenei Hs.189075.
    Hs.313056.

    3D structure databases

    ProteinModelPortali Q12792.
    SMRi Q12792. Positions 7-139, 176-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111723. 23 interactions.
    IntActi Q12792. 3 interactions.
    MINTi MINT-3026525.

    PTM databases

    PhosphoSitei Q12792.

    Polymorphism databases

    DMDMi 259016376.

    2D gel databases

    OGPi Q12792.

    Proteomic databases

    MaxQBi Q12792.
    PaxDbi Q12792.
    PRIDEi Q12792.

    Protocols and materials databases

    DNASUi 5756.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000395510 ; ENSP00000378886 ; ENSG00000151239 . [Q12792-2 ]
    ENST00000548315 ; ENSP00000449428 ; ENSG00000151239 . [Q12792-3 ]
    ENST00000552521 ; ENSP00000448750 ; ENSG00000151239 . [Q12792-4 ]
    GeneIDi 5756.
    KEGGi hsa:5756.
    UCSCi uc001roa.4. human. [Q12792-2 ]
    uc001rob.3. human. [Q12792-3 ]

    Organism-specific databases

    CTDi 5756.
    GeneCardsi GC12M044187.
    HGNCi HGNC:9620. TWF1.
    HPAi HPA018116.
    MIMi 610932. gene.
    neXtProti NX_Q12792.
    PharmGKBi PA162407406.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263290.
    HOVERGENi HBG000848.
    KOi K08870.
    OrthoDBi EOG79GT6W.
    PhylomeDBi Q12792.
    TreeFami TF352598.

    Miscellaneous databases

    GeneWikii TWF1.
    GenomeRNAii 5756.
    NextBioi 22400.
    PROi Q12792.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12792.
    Bgeei Q12792.
    Genevestigatori Q12792.

    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. "Prokaryotic expression cloning of a novel human tyrosine kinase."
      Beeler J.F., LaRochelle W.J., Chedid M., Tronick S.R., Aaronson S.A.
      Mol. Cell. Biol. 14:982-988(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), COFACTOR, TISSUE SPECIFICITY, PHOSPHORYLATION.
      Tissue: Lung fibroblast.
    2. "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] (ISOFORMS 1 AND 4).
      Tissue: Brain, Placenta and Teratocarcinoma.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    6. "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] (ISOFORMS 1 AND 4).
      Tissue: Prostate and Testis.
    7. Bienvenut W.V., Calvo F., Kolch W.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-37 (ISOFORMS 1/3), PROTEIN SEQUENCE OF 65-72; 99-105; 111-155; 172-192; 236-242 AND 279-285 (ISOFORMS 1/3), PROTEIN SEQUENCE OF 159-171 (ISOFORM 1), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    8. "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].
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTWF1_HUMAN
    AccessioniPrimary (citable) accession number: Q12792
    Secondary accession number(s): A8K5A8
    , B3KXS6, B4DLX9, Q59G07, Q5U0B1, Q6FHJ1, Q6FHL6, Q6NUK9, Q86XL6, Q8TCD3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 2, 2004
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 132 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

    Caution

    Was originally thought to have protein tyrosine kinase activity.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3