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Q16658

- FSCN1_HUMAN

UniProt

Q16658 - FSCN1_HUMAN

Protein

Fascin

Gene

FSCN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Organizes filamentous actin into bundles with a minimum of 4.1:1 actin/fascin ratio. Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration.4 Publications

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. actin filament binding Source: UniProtKB
    3. drug binding Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: IntAct

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. actin filament bundle assembly Source: UniProtKB
    3. cell migration Source: UniProtKB
    4. cell motility Source: UniProtKB
    5. cell proliferation Source: ProtInc

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fascin
    Alternative name(s):
    55 kDa actin-bundling protein
    Singed-like protein
    p55
    Gene namesi
    Name:FSCN1
    Synonyms:FAN1, HSN, SNL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:11148. FSCN1.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cell projectionfilopodium. Cell projectioninvadopodium. Cytoplasmcytosol
    Note: In glioma cells, partially colocalizes with F-actin stress fibers in the cytosol.

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. cytoplasm Source: HPA
    4. cytosol Source: UniProtKB-SubCell
    5. extracellular vesicular exosome Source: UniProt
    6. filopodium Source: UniProtKB
    7. invadopodium Source: UniProtKB
    8. stress fiber Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi39 – 391S → A: Loss of phosphorylation. 1 Publication
    Mutagenesisi392 – 3921H → A: Decreased actin-bundling activity. 1 Publication
    Mutagenesisi471 – 4711K → A: Decreased actin-bundling activity. 1 Publication
    Mutagenesisi488 – 4881A → W: Decreased actin-bundling activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA128394534.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 493492FascinPRO_0000219379Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine2 Publications
    Modified residuei38 – 381Phosphoserine2 Publications
    Modified residuei39 – 391Phosphoserine; by PKC2 Publications
    Modified residuei74 – 741N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylation on Ser-39 inhibits the actin-binding ability of fascin.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ16658.
    PaxDbiQ16658.
    PRIDEiQ16658.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00163187.
    Q16658.
    UCD-2DPAGEQ16658.

    PTM databases

    PhosphoSiteiQ16658.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ16658.
    BgeeiQ16658.
    CleanExiHS_FSCN1.
    GenevestigatoriQ16658.

    Organism-specific databases

    HPAiCAB000121.
    CAB035991.
    HPA005723.

    Interactioni

    Subunit structurei

    Associates with beta-catenin. Interacts with PLXNB3.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FANCD2Q9BXW96EBI-351076,EBI-359343
    MLH1P406927EBI-351076,EBI-744248
    PLXNB3Q9ULL42EBI-351076,EBI-311073
    YWHAZP631043EBI-351076,EBI-347088

    Protein-protein interaction databases

    BioGridi112508. 24 interactions.
    DIPiDIP-33171N.
    IntActiQ16658. 25 interactions.
    MINTiMINT-3033029.
    STRINGi9606.ENSP00000371798.

    Structurei

    Secondary structure

    1
    493
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 175
    Beta strandi23 – 264
    Helixi29 – 313
    Beta strandi33 – 397
    Helixi42 – 443
    Beta strandi46 – 494
    Helixi53 – 553
    Beta strandi60 – 634
    Beta strandi69 – 724
    Beta strandi78 – 847
    Helixi87 – 893
    Beta strandi91 – 955
    Beta strandi97 – 993
    Beta strandi101 – 1055
    Turni106 – 1083
    Beta strandi111 – 1166
    Beta strandi118 – 1258
    Helixi128 – 1303
    Beta strandi132 – 1365
    Beta strandi141 – 1466
    Turni147 – 1504
    Beta strandi151 – 1566
    Beta strandi162 – 1698
    Helixi173 – 1753
    Beta strandi177 – 1815
    Beta strandi183 – 1897
    Beta strandi202 – 2054
    Helixi208 – 2103
    Beta strandi212 – 2165
    Beta strandi221 – 2244
    Beta strandi230 – 2345
    Turni235 – 2384
    Beta strandi239 – 2424
    Helixi250 – 2523
    Beta strandi254 – 2585
    Beta strandi262 – 2665
    Beta strandi272 – 2743
    Beta strandi277 – 2804
    Beta strandi282 – 2865
    Helixi290 – 2923
    Beta strandi294 – 2985
    Turni300 – 3023
    Beta strandi305 – 3084
    Turni310 – 3123
    Beta strandi314 – 3174
    Beta strandi321 – 3299
    Helixi332 – 3343
    Beta strandi336 – 3416
    Beta strandi344 – 3485
    Beta strandi354 – 3574
    Beta strandi361 – 3699
    Helixi372 – 3743
    Beta strandi376 – 3805
    Beta strandi384 – 3863
    Beta strandi393 – 3975
    Turni399 – 4013
    Beta strandi403 – 4108
    Beta strandi414 – 4196
    Beta strandi422 – 4265
    Beta strandi432 – 4354
    Beta strandi439 – 4479
    Beta strandi451 – 4566
    Turni457 – 4593
    Beta strandi460 – 4656
    Beta strandi468 – 4725
    Beta strandi476 – 4849
    Helixi487 – 4893
    Beta strandi490 – 4923

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DFCX-ray2.90A/B1-493[»]
    3LLPX-ray1.80A/B1-493[»]
    3O8KX-ray2.70A/B1-493[»]
    3P53X-ray2.00A/B1-493[»]
    4GOVX-ray2.20A/B1-493[»]
    4GOYX-ray2.30A/B1-493[»]
    4GP0X-ray2.50A/B1-493[»]
    4GP3X-ray2.25A/B1-493[»]
    ProteinModelPortaliQ16658.
    SMRiQ16658. Positions 8-493.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16658.

    Family & Domainsi

    Domaini

    Composed of four beta-trefoil domains.2 Publications

    Sequence similaritiesi

    Belongs to the fascin family.Curated

    Phylogenomic databases

    eggNOGiNOG85029.
    HOGENOMiHOG000267034.
    HOVERGENiHBG000968.
    InParanoidiQ16658.
    KOiK17455.
    OMAiPATLWEY.
    OrthoDBiEOG7VQJCP.
    PhylomeDBiQ16658.
    TreeFamiTF323992.

    Family and domain databases

    InterProiIPR008999. Actin_cross-linking.
    IPR010431. Fascin.
    IPR022768. Fascin-domain.
    IPR024703. Fascin_metazoans.
    [Graphical view]
    PANTHERiPTHR10551. PTHR10551. 1 hit.
    PfamiPF06268. Fascin. 4 hits.
    [Graphical view]
    PIRSFiPIRSF005682. Fascin. 1 hit.
    SUPFAMiSSF50405. SSF50405. 4 hits.

    Sequencei

    Sequence statusi: Complete.

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

    Q16658-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTANGTAEAV QIQFGLINCG NKYLTAEAFG FKVNASASSL KKKQIWTLEQ    50
    PPDEAGSAAV CLRSHLGRYL AADKDGNVTC EREVPGPDCR FLIVAHDDGR 100
    WSLQSEAHRR YFGGTEDRLS CFAQTVSPAE KWSVHIAMHP QVNIYSVTRK 150
    RYAHLSARPA DEIAVDRDVP WGVDSLITLA FQDQRYSVQT ADHRFLRHDG 200
    RLVARPEPAT GYTLEFRSGK VAFRDCEGRY LAPSGPSGTL KAGKATKVGK 250
    DELFALEQSC AQVVLQAANE RNVSTRQGMD LSANQDEETD QETFQLEIDR 300
    DTKKCAFRTH TGKYWTLTAT GGVQSTASSK NASCYFDIEW RDRRITLRAS 350
    NGKFVTSKKN GQLAASVETA GDSELFLMKL INRPIIVFRG EHGFIGCRKV 400
    TGTLDANRSS YDVFQLEFND GAYNIKDSTG KYWTVGSDSA VTSSGDTPVD 450
    FFFEFCDYNK VAIKVGGRYL KGDHAGVLKA SAETVDPASL WEY 493
    Length:493
    Mass (Da):54,530
    Last modified:January 23, 2007 - v3
    Checksum:iC1453714BED6109A
    GO

    Sequence cautioni

    The sequence AAH07539.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti440 – 4401A → V in AAH06304. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03057 mRNA. Translation: AAA86442.1.
    U09873 mRNA. Translation: AAA62201.1.
    AY044229 Genomic DNA. Translation: AAL01526.1.
    AK316607 mRNA. Translation: BAG38194.1.
    BT006636 mRNA. Translation: AAP35282.1.
    AC006483 Genomic DNA. No translation available.
    CH471144 Genomic DNA. Translation: EAW87346.1.
    BC000521 mRNA. Translation: AAH00521.1.
    BC006304 mRNA. Translation: AAH06304.1.
    BC007539 mRNA. Translation: AAH07539.1. Different initiation.
    BC007643 mRNA. Translation: AAH07643.1.
    BC007948 mRNA. Translation: AAH07948.1.
    BC007988 mRNA. Translation: AAH07988.1.
    CCDSiCCDS5342.1.
    PIRiI38621.
    RefSeqiNP_003079.1. NM_003088.3.
    UniGeneiHs.118400.

    Genome annotation databases

    EnsembliENST00000382361; ENSP00000371798; ENSG00000075618.
    GeneIDi6624.
    KEGGihsa:6624.
    UCSCiuc003sou.3. human.

    Polymorphism databases

    DMDMi2498357.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03057 mRNA. Translation: AAA86442.1 .
    U09873 mRNA. Translation: AAA62201.1 .
    AY044229 Genomic DNA. Translation: AAL01526.1 .
    AK316607 mRNA. Translation: BAG38194.1 .
    BT006636 mRNA. Translation: AAP35282.1 .
    AC006483 Genomic DNA. No translation available.
    CH471144 Genomic DNA. Translation: EAW87346.1 .
    BC000521 mRNA. Translation: AAH00521.1 .
    BC006304 mRNA. Translation: AAH06304.1 .
    BC007539 mRNA. Translation: AAH07539.1 . Different initiation.
    BC007643 mRNA. Translation: AAH07643.1 .
    BC007948 mRNA. Translation: AAH07948.1 .
    BC007988 mRNA. Translation: AAH07988.1 .
    CCDSi CCDS5342.1.
    PIRi I38621.
    RefSeqi NP_003079.1. NM_003088.3.
    UniGenei Hs.118400.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DFC X-ray 2.90 A/B 1-493 [» ]
    3LLP X-ray 1.80 A/B 1-493 [» ]
    3O8K X-ray 2.70 A/B 1-493 [» ]
    3P53 X-ray 2.00 A/B 1-493 [» ]
    4GOV X-ray 2.20 A/B 1-493 [» ]
    4GOY X-ray 2.30 A/B 1-493 [» ]
    4GP0 X-ray 2.50 A/B 1-493 [» ]
    4GP3 X-ray 2.25 A/B 1-493 [» ]
    ProteinModelPortali Q16658.
    SMRi Q16658. Positions 8-493.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112508. 24 interactions.
    DIPi DIP-33171N.
    IntActi Q16658. 25 interactions.
    MINTi MINT-3033029.
    STRINGi 9606.ENSP00000371798.

    PTM databases

    PhosphoSitei Q16658.

    Polymorphism databases

    DMDMi 2498357.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00163187.
    Q16658.
    UCD-2DPAGE Q16658.

    Proteomic databases

    MaxQBi Q16658.
    PaxDbi Q16658.
    PRIDEi Q16658.

    Protocols and materials databases

    DNASUi 6624.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000382361 ; ENSP00000371798 ; ENSG00000075618 .
    GeneIDi 6624.
    KEGGi hsa:6624.
    UCSCi uc003sou.3. human.

    Organism-specific databases

    CTDi 6624.
    GeneCardsi GC07P005632.
    H-InvDB HIX0033686.
    HGNCi HGNC:11148. FSCN1.
    HPAi CAB000121.
    CAB035991.
    HPA005723.
    MIMi 602689. gene.
    neXtProti NX_Q16658.
    PharmGKBi PA128394534.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG85029.
    HOGENOMi HOG000267034.
    HOVERGENi HBG000968.
    InParanoidi Q16658.
    KOi K17455.
    OMAi PATLWEY.
    OrthoDBi EOG7VQJCP.
    PhylomeDBi Q16658.
    TreeFami TF323992.

    Miscellaneous databases

    ChiTaRSi FSCN1. human.
    EvolutionaryTracei Q16658.
    GeneWikii FSCN1.
    GenomeRNAii 6624.
    NextBioi 25801.
    PROi Q16658.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16658.
    Bgeei Q16658.
    CleanExi HS_FSCN1.
    Genevestigatori Q16658.

    Family and domain databases

    InterProi IPR008999. Actin_cross-linking.
    IPR010431. Fascin.
    IPR022768. Fascin-domain.
    IPR024703. Fascin_metazoans.
    [Graphical view ]
    PANTHERi PTHR10551. PTHR10551. 1 hit.
    Pfami PF06268. Fascin. 4 hits.
    [Graphical view ]
    PIRSFi PIRSF005682. Fascin. 1 hit.
    SUPFAMi SSF50405. SSF50405. 4 hits.
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning and expression of the human homolog of the sea urchin fascin and Drosophila singed genes which encodes an actin-bundling protein."
      Duh F.-M., Latif F., Weng Y., Geil L., Modi W., Stackhouse T., Matsumura F., Duan D.R., Linehan W.M., Lerman M.I., Gnarra J.R.
      DNA Cell Biol. 13:821-827(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Teratocarcinoma.
    2. "Epstein-Barr virus infection induces expression in B lymphocytes of a novel gene encoding an evolutionarily conserved 55-kilodalton actin-bundling protein."
      Mosialos G., Yamashiro S., Baughman R.W., Matsudaira P., Vara L., Matsumura F., Kieff E., Birkenbach M.
      J. Virol. 68:7320-7328(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Human fascin gene sequence."
      Bros M., Ross X.L., Reske-Kunz A.B., Ross R.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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.
    5. "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].
    6. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Brain, Eye, Lung and Muscle.
    9. Bienvenut W.V.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-32; 44-63; 69-82; 111-149; 159-185; 202-217; 230-241; 248-271; 314-341; 409-426 AND 469-493, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    10. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 119-149; 202-217; 230-241; 314-330 AND 380-389, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    11. "Intracellular localization of the 55-kD actin-bundling protein in cultured cells: spatial relationships with actin, alpha-actinin, tropomyosin, and fimbrin."
      Yamashiro-Matsumura S., Matsumura F.
      J. Cell Biol. 103:631-640(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Phosphorylation of human fascin inhibits its actin binding and bundling activities."
      Yamakita Y., Ono S., Matsumura F., Yamashiro S.
      J. Biol. Chem. 271:12632-12638(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    13. "Characterization of cell-matrix adhesion requirements for the formation of fascin microspikes."
      Adams J.C.
      Mol. Biol. Cell 8:2345-2363(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Fascin, an actin-bundling protein, induces membrane protrusions and increases cell motility of epithelial cells."
      Yamashiro S., Yamakita Y., Ono S., Matsumura F.
      Mol. Biol. Cell 9:993-1006(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    15. "Identification of an actin binding region and a protein kinase C phosphorylation site on human fascin."
      Ono S., Yamakita Y., Yamashiro S., Matsudaira P.T., Gnarra J.R., Obinata T., Matsumura F.
      J. Biol. Chem. 272:2527-2533(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-39, MUTAGENESIS OF SER-39.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "The actin-bundling protein fascin stabilizes actin in invadopodia and potentiates protrusive invasion."
      Li A., Dawson J.C., Forero-Vargas M., Spence H.J., Yu X., Konig I., Anderson K., Machesky L.M.
      Curr. Biol. 20:339-345(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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 THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Semaphorin 5A and plexin-B3 regulate human glioma cell motility and morphology through Rac1 and the actin cytoskeleton."
      Li X., Law J.W., Lee A.Y.
      Oncogene 31:595-610(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLXNB3, SUBCELLULAR LOCATION.
    22. "Structure, evolutionary conservation, and conformational dynamics of Homo sapiens fascin-1, an F-actin crosslinking protein."
      Sedeh R.S., Fedorov A.A., Fedorov E.V., Ono S., Matsumura F., Almo S.C., Bathe M.
      J. Mol. Biol. 400:589-604(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), DOMAIN.
    23. "Migrastatin analogues target fascin to block tumour metastasis."
      Chen L., Yang S., Jakoncic J., Zhang J.J., Huang X.Y.
      Nature 464:1062-1066(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), FUNCTION, MUTAGENESIS OF HIS-392; LYS-471 AND ALA-488, DOMAIN.

    Entry informationi

    Entry nameiFSCN1_HUMAN
    AccessioniPrimary (citable) accession number: Q16658
    Secondary accession number(s): A6NI89
    , B2RE97, Q96IC5, Q96IH1, Q9BRF1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 152 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 7
      Human chromosome 7: 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