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Q16658

- FSCN1_HUMAN

UniProt

Q16658 - FSCN1_HUMAN

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Protein

Fascin

Gene

FSCN1

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

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

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
Complete GO annotation...

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. extracellular vesicular exosome Source: UniProt
  5. filopodium Source: UniProtKB
  6. invadopodium Source: UniProtKB
  7. stress fiber Source: UniProtKB
Complete GO annotation...

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 – 381Phosphoserine1 Publication
Modified residuei39 – 391Phosphoserine; by PKC1 Publication
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

BgeeiQ16658.
CleanExiHS_FSCN1.
ExpressionAtlasiQ16658. baseline and differential.
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. 25 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 – 175Combined sources
Beta strandi23 – 264Combined sources
Helixi29 – 313Combined sources
Beta strandi33 – 397Combined sources
Helixi42 – 443Combined sources
Beta strandi46 – 494Combined sources
Helixi53 – 553Combined sources
Beta strandi60 – 634Combined sources
Beta strandi69 – 724Combined sources
Beta strandi78 – 847Combined sources
Helixi87 – 893Combined sources
Beta strandi91 – 955Combined sources
Beta strandi97 – 993Combined sources
Beta strandi101 – 1055Combined sources
Turni106 – 1083Combined sources
Beta strandi111 – 1166Combined sources
Beta strandi118 – 1258Combined sources
Helixi128 – 1303Combined sources
Beta strandi132 – 1365Combined sources
Beta strandi141 – 1466Combined sources
Turni147 – 1504Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi162 – 1698Combined sources
Helixi173 – 1753Combined sources
Beta strandi177 – 1815Combined sources
Beta strandi183 – 1897Combined sources
Beta strandi202 – 2054Combined sources
Helixi208 – 2103Combined sources
Beta strandi212 – 2165Combined sources
Beta strandi221 – 2244Combined sources
Beta strandi230 – 2345Combined sources
Turni235 – 2384Combined sources
Beta strandi239 – 2424Combined sources
Helixi250 – 2523Combined sources
Beta strandi254 – 2585Combined sources
Beta strandi262 – 2665Combined sources
Beta strandi272 – 2743Combined sources
Beta strandi277 – 2804Combined sources
Beta strandi282 – 2865Combined sources
Helixi290 – 2923Combined sources
Beta strandi294 – 2985Combined sources
Turni300 – 3023Combined sources
Beta strandi305 – 3084Combined sources
Turni310 – 3123Combined sources
Beta strandi314 – 3174Combined sources
Beta strandi321 – 3299Combined sources
Helixi332 – 3343Combined sources
Beta strandi336 – 3416Combined sources
Beta strandi344 – 3485Combined sources
Beta strandi354 – 3574Combined sources
Beta strandi361 – 3699Combined sources
Helixi372 – 3743Combined sources
Beta strandi376 – 3805Combined sources
Beta strandi384 – 3863Combined sources
Beta strandi393 – 3975Combined sources
Turni399 – 4013Combined sources
Beta strandi403 – 4108Combined sources
Beta strandi414 – 4196Combined sources
Beta strandi422 – 4265Combined sources
Beta strandi432 – 4354Combined sources
Beta strandi439 – 4479Combined sources
Beta strandi451 – 4566Combined sources
Turni457 – 4593Combined sources
Beta strandi460 – 4656Combined sources
Beta strandi468 – 4725Combined sources
Beta strandi476 – 4849Combined sources
Helixi487 – 4893Combined sources
Beta strandi490 – 4923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000063373.
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

        10         20         30         40         50
MTANGTAEAV QIQFGLINCG NKYLTAEAFG FKVNASASSL KKKQIWTLEQ
60 70 80 90 100
PPDEAGSAAV CLRSHLGRYL AADKDGNVTC EREVPGPDCR FLIVAHDDGR
110 120 130 140 150
WSLQSEAHRR YFGGTEDRLS CFAQTVSPAE KWSVHIAMHP QVNIYSVTRK
160 170 180 190 200
RYAHLSARPA DEIAVDRDVP WGVDSLITLA FQDQRYSVQT ADHRFLRHDG
210 220 230 240 250
RLVARPEPAT GYTLEFRSGK VAFRDCEGRY LAPSGPSGTL KAGKATKVGK
260 270 280 290 300
DELFALEQSC AQVVLQAANE RNVSTRQGMD LSANQDEETD QETFQLEIDR
310 320 330 340 350
DTKKCAFRTH TGKYWTLTAT GGVQSTASSK NASCYFDIEW RDRRITLRAS
360 370 380 390 400
NGKFVTSKKN GQLAASVETA GDSELFLMKL INRPIIVFRG EHGFIGCRKV
410 420 430 440 450
TGTLDANRSS YDVFQLEFND GAYNIKDSTG KYWTVGSDSA VTSSGDTPVD
460 470 480 490
FFFEFCDYNK VAIKVGGRYL KGDHAGVLKA SAETVDPASL WEY
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.Curated

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 25 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.
GeneTreei ENSGT00530000063373.
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

Bgeei Q16658.
CleanExi HS_FSCN1.
ExpressionAtlasi Q16658. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 154 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