Q16658 (FSCN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fascin

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

Gene names

Name:	FSCN1
Synonyms:	FAN1, HSN, SNL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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. 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. Ref.13 Ref.14 Ref.17 Ref.22
Subunit structure	Associates with beta-catenin. Interacts with PLXNB3. Ref.20
Subcellular location	Cytoplasm › cytoskeleton. Cell projection › filopodium. Cell projection › invadopodium. Cytoplasm › cytosol. Note: In glioma cells, partially colocalizes with F-actin stress fibers in the cytosol. Ref.11 Ref.14 Ref.17 Ref.20
Tissue specificity	Ubiquitous.
Domain	Composed of four beta-trefoil domains. Ref.21 Ref.22
Post-translational modification	Phosphorylation on Ser-39 inhibits the actin-binding ability of fascin.
Sequence similarities	Belongs to the fascin family.

Ontologies

Keywords
Cellular component	Cell junction Cell projection Cytoplasm Cytoskeleton
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin filament bundle assembly Inferred from direct assay Ref.22. Source: UniProtKB cell migration Inferred from mutant phenotype Ref.22. Source: UniProtKB cell proliferation Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell filopodium Inferred from direct assay Ref.11. Source: UniProtKB invadopodium Inferred from direct assay Ref.17. Source: UniProtKB stress fiber Inferred from direct assay Ref.11. Source: UniProtKB
Molecular_function	actin filament binding Inferred from direct assay PubMed 96218192. Source: UniProtKB drug binding Inferred from direct assay Ref.22. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FANCD2	Q9BXW9	6	EBI-351076,EBI-359343
MLH1	P40692	7	EBI-351076,EBI-744248
PLXNB3	Q9ULL4	2	EBI-351076,EBI-311073

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9

Chain

2 – 493

492

Fascin

PRO_0000219379

Amino acid modifications

Modified residue

2

1

N-acetylthreonine Ref.9

Modified residue

38

1

Phosphoserine Ref.16

Modified residue

39

1

Phosphoserine; by PKC Ref.15

Experimental info

Mutagenesis

39

1

S → A: Loss of phosphorylation. Ref.15

Mutagenesis

392

1

H → A: Decreased actin-bundling activity. Ref.22

Mutagenesis

471

1

K → A: Decreased actin-bundling activity. Ref.22

Mutagenesis

488

1

A → W: Decreased actin-bundling activity. Ref.22

Sequence conflict

440

1

A → V in AAH06304. Ref.8

Secondary structure

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493

Helix Strand Turn

Details...

Beta strand

13 – 17

5

Beta strand

23 – 26

4

Helix

29 – 31

3

Beta strand

33 – 39

7

Helix

42 – 44

3

Beta strand

46 – 49

4

Helix

53 – 55

3

Beta strand

60 – 63

4

Beta strand

69 – 72

4

Beta strand

78 – 84

7

Helix

87 – 89

3

Beta strand

91 – 95

5

Beta strand

97 – 99

3

Beta strand

101 – 105

5

Turn

106 – 108

3

Beta strand

111 – 116

6

Beta strand

118 – 125

8

Helix

128 – 130

3

Beta strand

132 – 136

5

Beta strand

141 – 146

6

Turn

147 – 150

4

Beta strand

151 – 156

6

Beta strand

162 – 169

8

Helix

173 – 175

3

Beta strand

177 – 181

5

Beta strand

183 – 189

7

Beta strand

202 – 205

4

Helix

208 – 210

3

Beta strand

212 – 216

5

Beta strand

221 – 224

4

Beta strand

230 – 234

5

Turn

235 – 238

4

Beta strand

239 – 242

4

Helix

250 – 252

3

Beta strand

254 – 258

5

Beta strand

262 – 266

5

Beta strand

272 – 274

3

Beta strand

277 – 280

4

Beta strand

282 – 286

5

Helix

290 – 292

3

Beta strand

294 – 298

5

Turn

300 – 302

3

Beta strand

305 – 308

4

Turn

310 – 312

3

Beta strand

314 – 317

4

Beta strand

321 – 329

9

Helix

332 – 334

3

Beta strand

336 – 341

6

Beta strand

344 – 348

5

Beta strand

354 – 357

4

Beta strand

361 – 369

9

Helix

372 – 374

3

Beta strand

376 – 380

5

Beta strand

384 – 386

3

Beta strand

393 – 397

5

Turn

399 – 401

3

Beta strand

403 – 410

8

Beta strand

414 – 419

6

Beta strand

422 – 426

5

Beta strand

432 – 435

4

Beta strand

439 – 447

9

Beta strand

451 – 456

6

Turn

457 – 459

3

Beta strand

460 – 465

6

Beta strand

468 – 472

5

Beta strand

476 – 484

9

Helix

487 – 489

3

Beta strand

490 – 492

3

Sequences

	Sequence		Length	Mass (Da)
	Q16658 [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] [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]	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] [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, 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, 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]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, MASS SPECTROMETRY. 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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]	"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.
[21]	"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.
[22]	"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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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. NM_003088.3.

UniGene

Hs.118400.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q16658.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33171N.

IntAct

Q16658. 24 interactions.

MINT

MINT-3033029.

STRING

9606.ENSP00000371798.

PTM databases

PhosphoSite

Q16658.

Polymorphism databases

DMDM

2498357.

2D gel databases

REPRODUCTION-2DPAGE

IPI00163187.
Q16658.

UCD-2DPAGE

Q16658.

Proteomic databases

PaxDb

Q16658.

PRIDE

Q16658.

Protocols and materials databases

DNASU

6624.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000382361; ENSP00000371798; ENSG00000075618.

GeneID

6624.

KEGG

hsa:6624.

UCSC

uc003sou.3. human.

Organism-specific databases

CTD

6624.

GeneCards

GC07P005632.

H-InvDB

HIX0033686.

HGNC

HGNC:11148. FSCN1.

HPA

CAB000121.
CAB035991.
HPA005723.

MIM

602689. gene.

neXtProt

NX_Q16658.

PharmGKB

PA128394534.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG85029.

HOGENOM

HOG000267034.

HOVERGEN

HBG000968.

InParanoid

Q16658.

OMA

GADCRFL.

OrthoDB

EOG41NTKS.

PhylomeDB

Q16658.

Gene expression databases

ArrayExpress

Q16658.

Bgee

Q16658.

CleanEx

HS_FSCN1.

Genevestigator

Q16658.

GermOnline

ENSG00000075618. Homo sapiens.

Family and domain databases

InterPro

IPR008999. Actin_cross-linking.
IPR010431. Fascin.
IPR022768. Fascin-domain.
IPR024703. Fascin_metazoans.
[Graphical view]

PANTHER

PTHR10551. PTHR10551. 1 hit.

Pfam

PF06268. Fascin. 4 hits.
[Graphical view]

PIRSF

PIRSF005682. Fascin. 1 hit.

SUPFAM

SSF50405. Actin_crosslink. 4 hits.

ProtoNet

Search...

Other

ChiTaRS

FSCN1. human.

EvolutionaryTrace

Q16658.

GenomeRNAi

6624.

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:	May 1, 2013
This is version 139 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.