Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q16658 (FSCN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fascin
Alternative name(s):
55 kDa actin-bundling protein
Singed-like protein
p55
Gene names
Name:FSCN1
Synonyms:FAN1, HSN, SNL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.23

Subunit structure

Associates with beta-catenin. Interacts with PLXNB3. Ref.21

Subcellular location

Cytoplasmcytoskeleton. Cell projectionfilopodium. Cell projectioninvadopodium. Cytoplasmcytosol. Note: In glioma cells, partially colocalizes with F-actin stress fibers in the cytosol. Ref.11 Ref.14 Ref.17 Ref.21

Tissue specificity

Ubiquitous.

Domain

Composed of four beta-trefoil domains. Ref.22 Ref.23

Post-translational modification

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

Sequence similarities

Belongs to the fascin family.

Ontologies

Keywords
   Cellular componentCell junction
Cell projection
Cytoplasm
Cytoskeleton
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from direct assay Ref.14. Source: UniProtKB

actin filament bundle assembly

Inferred from direct assay Ref.23. Source: UniProtKB

cell migration

Inferred from mutant phenotype Ref.23. Source: UniProtKB

cell motility

Inferred from direct assay Ref.14. Source: UniProtKB

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentactin cytoskeleton

Inferred from direct assay Ref.11. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

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_functionactin binding

Inferred from direct assay Ref.23PubMed 96218192. Source: UniProtKB

actin filament binding

Inferred from direct assay PubMed 96218192. Source: UniProtKB

drug binding

Inferred from direct assay Ref.23. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 493492Fascin
PRO_0000219379

Amino acid modifications

Modified residue21N-acetylthreonine Ref.9 Ref.20
Modified residue381Phosphoserine Ref.16
Modified residue391Phosphoserine; by PKC Ref.15
Modified residue741N6-acetyllysine By similarity

Experimental info

Mutagenesis391S → A: Loss of phosphorylation. Ref.15
Mutagenesis3921H → A: Decreased actin-bundling activity. Ref.23
Mutagenesis4711K → A: Decreased actin-bundling activity. Ref.23
Mutagenesis4881A → W: Decreased actin-bundling activity. Ref.23
Sequence conflict4401A → V in AAH06304. Ref.8

Secondary structure

................................................................................................................................. 493
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16658 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C1453714BED6109A

FASTA49354,530
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, 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]"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, 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]"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]"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.
+Additional computationally mapped references.

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.
PIRI38621.
RefSeqNP_003079.1. NM_003088.3.
UniGeneHs.118400.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ16658.
SMRQ16658. Positions 8-493.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112508. 24 interactions.
DIPDIP-33171N.
IntActQ16658. 25 interactions.
MINTMINT-3033029.
STRING9606.ENSP00000371798.

PTM databases

PhosphoSiteQ16658.

Polymorphism databases

DMDM2498357.

2D gel databases

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

Proteomic databases

PaxDbQ16658.
PRIDEQ16658.

Protocols and materials databases

DNASU6624.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000382361; ENSP00000371798; ENSG00000075618.
GeneID6624.
KEGGhsa:6624.
UCSCuc003sou.3. human.

Organism-specific databases

CTD6624.
GeneCardsGC07P005632.
H-InvDBHIX0033686.
HGNCHGNC:11148. FSCN1.
HPACAB000121.
CAB035991.
HPA005723.
MIM602689. gene.
neXtProtNX_Q16658.
PharmGKBPA128394534.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG85029.
HOGENOMHOG000267034.
HOVERGENHBG000968.
InParanoidQ16658.
KOK17455.
OMAPATLWEY.
OrthoDBEOG7VQJCP.
PhylomeDBQ16658.
TreeFamTF323992.

Gene expression databases

ArrayExpressQ16658.
BgeeQ16658.
CleanExHS_FSCN1.
GenevestigatorQ16658.

Family and domain databases

InterProIPR008999. Actin_cross-linking.
IPR010431. Fascin.
IPR022768. Fascin-domain.
IPR024703. Fascin_metazoans.
[Graphical view]
PANTHERPTHR10551. PTHR10551. 1 hit.
PfamPF06268. Fascin. 4 hits.
[Graphical view]
PIRSFPIRSF005682. Fascin. 1 hit.
SUPFAMSSF50405. SSF50405. 4 hits.
ProtoNetSearch...

Other

ChiTaRSFSCN1. human.
EvolutionaryTraceQ16658.
GeneWikiFSCN1.
GenomeRNAi6624.
NextBio25801.
PROQ16658.
SOURCESearch...

Entry information

Entry nameFSCN1_HUMAN
AccessionPrimary (citable) accession number: Q16658
Secondary accession number(s): A6NI89 expand/collapse secondary AC list , B2RE97, Q96IC5, Q9BRF1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM