Reviewed, UniProtKB/Swiss-Prot Q16658 (FSCN1_HUMAN)

Names and origin

Protein names

Recommended name:
    Fascin
Alternative name(s):
    Singed-like protein
    55 kDa actin-bundling protein
    p55

Gene names

Name:	FSCN1
Synonyms:	FAN1, HSN, SNL

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Organizes filamentous actin into bundles with a minimum of 4.1:1 actin/fascin ratio. Probably involved in the assembly of actin filament bundles present in microspikes, membrane ruffles, and stress fibers.
Subunit structure	Associates with beta-catenin.
Tissue specificity	Ubiquitous.
Post-translational modification	Phosphorylation on Ser-39 inhibits the actin-binding ability of fascin.
Involvement in disease	Marks and mediates breast cancer metastasis to the lungs. FSCN1 is not functionally validated but achieves the highest statistical significance (P less than 0.000001). Those subjects expressing the lung metastasis signature have a significantly poorer lung metastasis-free survival, but not bone metastasis-free survival, compared to subjects without the signature. Ref.12
Sequence similarities	Belongs to the fascin family.

Ontologies

Keywords
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	actin filament bundle formation Ref.10 Traceable author statement. Source: ProtInc cell proliferation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	actin cytoskeleton Ref.10 Traceable author statement. Source: ProtInc cytoplasm Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular function	actin filament binding Inferred from electronic annotation. Source: InterPro protein binding, bridging Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GNAS	P63092	1	EBI-351076,EBI-1047114
VHL	P40337	1	EBI-351076,EBI-301246

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 493

492

Fascin

PRO_0000219379

Amino acid modifications

Modified residue

2

1

N-acetylthreonine Probable

Modified residue

38

1

Phosphoserine Ref.13

Modified residue

39

1

Phosphoserine; by PKC Ref.11

Experimental info

Mutagenesis

39

1

S → A: Loss of phosphorylation. Ref.11

Sequence conflict

440

1

A → V in AAH06304. Ref.8

Secondary structure

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493

Helix Strand Turn

Details...

Beta strand

28 – 31

4

Turn

42 – 44

3

Beta strand

69 – 72

4

Beta strand

78 – 84

7

Helix

87 – 89

3

Beta strand

97 – 99

3

Turn

106 – 108

3

Beta strand

111 – 115

5

Beta strand

118 – 125

8

Helix

128 – 130

3

Beta strand

132 – 134

3

Beta strand

140 – 146

7

Turn

147 – 149

3

Beta strand

152 – 155

4

Beta strand

160 – 169

10

Turn

172 – 175

4

Beta strand

177 – 181

5

Beta strand

183 – 190

8

Beta strand

202 – 205

4

Helix

208 – 210

3

Beta strand

212 – 216

5

Beta strand

221 – 228

8

Beta strand

230 – 233

4

Beta strand

235 – 237

3

Beta strand

240 – 242

3

Beta strand

254 – 258

5

Beta strand

262 – 266

5

Beta strand

272 – 274

3

Beta strand

282 – 285

4

Helix

290 – 292

3

Beta strand

294 – 298

5

Turn

300 – 302

3

Beta strand

305 – 309

5

Turn

310 – 312

3

Beta strand

313 – 317

5

Beta strand

321 – 329

9

Helix

332 – 334

3

Beta strand

336 – 341

6

Beta strand

344 – 348

5

Beta strand

352 – 354

3

Beta strand

359 – 365

7

Beta strand

372 – 380

9

Beta strand

384 – 386

3

Beta strand

393 – 397

5

Beta strand

399 – 401

3

Beta strand

403 – 410

8

Beta strand

414 – 419

6

Beta strand

422 – 426

5

Beta strand

440 – 443

4

Beta strand

451 – 457

7

Beta strand

460 – 465

6

Beta strand

468 – 472

5

Helix

474 – 476

3

Beta strand

477 – 484

8

Helix

487 – 489

3

Sequences

	Sequence		Length	Mass (Da)
	Q16658-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C1453714BED6109A	FASTA	493	54,530
	10 20 30 40 50 60 MTANGTAEAV QIQFGLINCG NKYLTAEAFG FKVNASASSL KKKQIWTLEQ PPDEAGSAAV 70 80 90 100 110 120 CLRSHLGRYL AADKDGNVTC EREVPGPDCR FLIVAHDDGR WSLQSEAHRR YFGGTEDRLS 130 140 150 160 170 180 CFAQTVSPAE KWSVHIAMHP QVNIYSVTRK RYAHLSARPA DEIAVDRDVP WGVDSLITLA 190 200 210 220 230 240 FQDQRYSVQT ADHRFLRHDG RLVARPEPAT GYTLEFRSGK VAFRDCEGRY LAPSGPSGTL 250 260 270 280 290 300 KAGKATKVGK DELFALEQSC AQVVLQAANE RNVSTRQGMD LSANQDEETD QETFQLEIDR 310 320 330 340 350 360 DTKKCAFRTH TGKYWTLTAT GGVQSTASSK NASCYFDIEW RDRRITLRAS NGKFVTSKKN 370 380 390 400 410 420 GQLAASVETA GDSELFLMKL INRPIIVFRG EHGFIGCRKV TGTLDANRSS YDVFQLEFND 430 440 450 460 470 480 GAYNIKDSTG KYWTVGSDSA VTSSGDTPVD FFFEFCDYNK VAIKVGGRYL KGDHAGVLKA 490 SAETVDPASL WEY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8068206] [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: 7933116] [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: 14702039] [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: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Eye, Lung and Muscle.
[9]	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, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[10]	"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: 8647875] [Abstract] Cited for: PHOSPHORYLATION.
[11]	"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: 8999969] [Abstract] Cited for: PHOSPHORYLATION AT SER-39, MUTAGENESIS OF SER-39.
[12]	"Genes that mediate breast cancer metastasis to lung." Minn A.J., Gupta G.P., Siegel P.M., Bos P.D., Shu W., Giri D.D., Viale A., Olshen A.B., Gerald W.L., Massague J. Nature 436:518-524(2005) [PubMed: 16049480] [Abstract] Cited for: DISEASE.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, MASS SPECTROMETRY.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
BC007643 mRNA. Translation: AAH07643.1.
BC007948 mRNA. Translation: AAH07948.1.
BC007988 mRNA. Translation: AAH07988.1.

IPI

IPI00163187.

PIR

I38621.

RefSeq

NP_003079.1.

UniGene

Hs.118400

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DFC	X-ray	2.90	A/B	1-493	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q16658. 19 interactions.

PTM databases

PhosphoSite

Q16658.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00163187.
Q16658.

Proteomic databases

PRIDE

Q16658.

Genome annotation databases

Ensembl

ENSG00000075618. Homo sapiens. [Contig view]

GeneID

6624.

KEGG

hsa:6624.

Organism-specific databases

GeneCards

GC07P005598.

H-InvDB

HIX0006455.

HGNC

HGNC:11148. FSCN1.

HPA

CAB000121.
HPA005723.

MIM

602689. gene.

PharmGKB

PA128394534.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q16658.

Gene expression databases

ArrayExpress

Q16658.

Bgee

Q16658.

CleanEx

HS_FSCN1.

GermOnline

ENSG00000075618. Homo sapiens.

Family and domain databases

InterPro

IPR010431. Fascin.
[Graphical view]

PANTHER

PTHR10551. Fascin. 1 hit.

Pfam

PF06268. Fascin. 4 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

25801.

SOURCE

Search...

Entry information

Entry name

FSCN1_HUMAN

Accession

Primary (citable) accession number: Q16658
Secondary accession number(s): A6NI89 , B2RE97, Q96IC5, Q9BRF1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 97 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)