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Q9Y6W5 (WASF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Wiskott-Aldrich syndrome protein family member 2

Short name=WASP family protein member 2
Alternative name(s):
Protein WAVE-2
Verprolin homology domain-containing protein 2
Gene names
Name:WASF2
Synonyms:WAVE2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length498 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. Ref.1 Ref.9

Subunit structure

Binds actin and the Arp2/3 complex. Interacts with BAIAP2. Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1, NCKAP1/NAP1 and WASF2/WAVE2. Directly interacts with BRK1. Ref.1 Ref.5 Ref.6 Ref.7 Ref.9

Subcellular location

Cytoplasmcytoskeleton By similarity. Cell projectionlamellipodium By similarity. Note: At the interface between the lamellipodial actin meshwork and the membrane By similarity.

Tissue specificity

Expressed in all tissues with strongest expression in placenta, lung, and peripheral blood leukocytes, but not in skeletal muscle. Ref.1

Domain

Binds and activates the Arp2/3 complex via the C-terminal domain. Interacts with actin via the WH2 domain. Ref.1 Ref.9

Sequence similarities

Belongs to the SCAR/WAVE family.

Contains 1 WH2 domain.

Ontologies

Keywords
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   LigandActin-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

Rac protein signal transduction

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton organization

Traceable author statement PubMed 9732292. Source: ProtInc

actin filament-based movement

Inferred from electronic annotation. Source: Ensembl

adenylate cyclase-modulating G-protein coupled receptor signaling pathway

Traceable author statement PubMed 9732292. Source: ProtInc

ameboidal cell migration

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

lamellipodium assembly

Inferred from electronic annotation. Source: Ensembl

lamellipodium morphogenesis

Inferred from electronic annotation. Source: Ensembl

megakaryocyte development

Inferred from electronic annotation. Source: Ensembl

negative regulation of stress fiber assembly

Inferred from mutant phenotype Ref.7. Source: UniProt

positive regulation of lamellipodium assembly

Inferred from mutant phenotype PubMed 18560548Ref.7. Source: UniProt

   Cellular_componentSCAR complex

Inferred from mutant phenotype Ref.7. Source: UniProt

actin cytoskeleton

Traceable author statement PubMed 10970852. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

early endosome

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

intracellular

Inferred from direct assay PubMed 17101133. Source: MGI

lamellipodium

Inferred from direct assay PubMed 17101133. Source: MGI

ruffle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionactin binding

Traceable author statement PubMed 10970852. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 16417406. Source: UniProtKB

protein complex binding

Inferred from direct assay PubMed 18560548. Source: UniProt

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y6W5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9Y6W5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     275-281: SYPVDNQ → RFSAAQG
     282-498: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 498498Wiskott-Aldrich syndrome protein family member 2
PRO_0000188994

Regions

Domain436 – 45318WH2
Compositional bias268 – 2714Poly-Pro
Compositional bias318 – 32811Poly-Pro
Compositional bias333 – 3386Poly-Pro
Compositional bias347 – 3504Poly-Pro
Compositional bias364 – 3718Poly-Pro
Compositional bias379 – 3824Poly-Pro
Compositional bias391 – 40616Poly-Pro

Natural variations

Alternative sequence275 – 2817SYPVDNQ → RFSAAQG in isoform 2.
VSP_042514
Alternative sequence282 – 498217Missing in isoform 2.
VSP_042515

Experimental info

Mutagenesis401L → D: Decreased interaction with WAVE complex; when associated with D-51. Ref.7
Mutagenesis501I → D: Decreased interaction with WAVE complex; when associated with D-54. Ref.7
Mutagenesis511F → D: Decreased interaction with WAVE complex; when associated with D-40. Ref.7
Mutagenesis541L → D: Decreased interaction with WAVE complex; when associated with D-50. Ref.7
Mutagenesis1241Y → D: Constitutive induction of the formation of actin filaments. Strongly enhances formation of lamellipodia. Ref.9
Mutagenesis1501Y → D: Constitutive induction of the formation of actin filaments. Strongly enhances formation of lamellipodia. Ref.9
Mutagenesis160 – 1612WK → ED: Constitutive induction of the formation of actin filaments. Strongly enhances formation of lamellipodia.

Secondary structure

... 498
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 2005. Version 3.
Checksum: C737CE963016DE94

FASTA49854,284
        10         20         30         40         50         60 
MPLVTRNIEP RHLCRQTLPS VRSELECVTN ITLANVIRQL GSLSKYAEDI FGELFTQANT 

        70         80         90        100        110        120 
FASRVSSLAE RVDRLQVKVT QLDPKEEEVS LQGINTRKAF RSSTIQDQKL FDRNSLPVPV 

       130        140        150        160        170        180 
LETYNTCDTP PPLNNLTPYR DDGKEALKFY TDPSYFFDLW KEKMLQDTKD IMKEKRKHRK 

       190        200        210        220        230        240 
EKKDNPNRGN VNPRKIKTRK EEWEKMKMGQ EFVESKEKLG TSGYPPTLVY QNGSIGCVEN 

       250        260        270        280        290        300 
VDASSYPPPP QSDSASSPSP SFSEDNLPPP PAEFSYPVDN QRGSGLAGPK RSSVVSPSHP 

       310        320        330        340        350        360 
PPAPPLGSPP GPKPGFAPPP APPPPPPPMI GIPPPPPPVG FGSPGTPPPP SPPSFPPHPD 

       370        380        390        400        410        420 
FAAPPPPPPP PAADYPTLPP PPLSQPTGGA PPPPPPPPPP GPPPPPFTGA DGQPAIPPPL 

       430        440        450        460        470        480 
SDTTKPKSSL PAVSDARSDL LSAIRQGFQL RRVEEQREQE KRDVVGNDVA TILSRRIAVE 

       490 
YSDSEDDSSE FDEDDWSD 

« Hide

Isoform 2 [UniParc].

Checksum: C5E79110854FAF56
Show »

FASTA28131,979

References

« Hide 'large scale' references
[1]"Identification of two human WAVE/SCAR homologues as general actin regulatory molecules which associate with the Arp2/3 complex."
Suetsugu S., Miki H., Takenawa T.
Biochem. Biophys. Res. Commun. 260:296-302(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ACTIN AND THE ARP2/3 COMPLEX, SUBUNIT, DOMAIN, TISSUE SPECIFICITY.
Tissue: T-cell lymphoma.
[2]"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] (ISOFORM 2).
Tissue: Testis.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 1).
Tissue: Lymph.
[5]"IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling."
Miki H., Yamaguchi H., Suetsugu S., Takenawa T.
Nature 408:732-735(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAIAP2.
[6]"Purification and architecture of the ubiquitous Wave complex."
Gautreau A., Ho H.-Y., Li J., Steen H., Gygi S.P., Kirschner M.W.
Proc. Natl. Acad. Sci. U.S.A. 101:4379-4383(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH C3ORF10.
[7]"Structure and control of the actin regulatory WAVE complex."
Chen Z., Borek D., Padrick S.B., Gomez T.S., Metlagel Z., Ismail A.M., Umetani J., Billadeau D.D., Otwinowski Z., Rosen M.K.
Nature 468:533-538(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LEU-40; ILE-50; PHE-51 AND LEU-54, SUBUNIT.
[8]"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].
[9]"Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly."
Chereau D., Kerff F., Graceffa P., Grabarek Z., Langsetmo K., Dominguez R.
Proc. Natl. Acad. Sci. U.S.A. 102:16644-16649(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 433-464 IN COMPLEX WITH ACTIN, FUNCTION, DOMAIN, MUTAGENESIS OF TYR-124; TYR-150 AND 160-TRP-LYS-161, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB026542 mRNA. Translation: BAA81795.1.
AK303011 mRNA. Translation: BAG64142.1.
AL096774 Genomic DNA. Translation: CAC18518.1.
AL663122 Genomic DNA. No translation available.
BX293535 Genomic DNA. No translation available.
BC040943 mRNA. Translation: AAH40943.1.
CCDSCCDS304.1. [Q9Y6W5-1]
CCDS55582.1. [Q9Y6W5-2]
RefSeqNP_001188333.1. NM_001201404.1. [Q9Y6W5-2]
NP_008921.1. NM_006990.3. [Q9Y6W5-1]
UniGeneHs.469244.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A40X-ray1.80C/F433-464[»]
ProteinModelPortalQ9Y6W5.
SMRQ9Y6W5. Positions 21-197, 435-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115465. 13 interactions.
DIPDIP-41817N.
IntActQ9Y6W5. 7 interactions.
MINTMINT-5005787.
STRING9606.ENSP00000396211.

PTM databases

PhosphoSiteQ9Y6W5.

Polymorphism databases

DMDM59800456.

Proteomic databases

MaxQBQ9Y6W5.
PaxDbQ9Y6W5.
PeptideAtlasQ9Y6W5.
PRIDEQ9Y6W5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000430629; ENSP00000396211; ENSG00000158195. [Q9Y6W5-1]
ENST00000536657; ENSP00000439883; ENSG00000158195. [Q9Y6W5-2]
GeneID10163.
KEGGhsa:10163.
UCSCuc001bof.2. human. [Q9Y6W5-1]
uc010ofl.2. human. [Q9Y6W5-2]

Organism-specific databases

CTD10163.
GeneCardsGC01M027730.
HGNCHGNC:12733. WASF2.
HPACAB022632.
HPA045288.
MIM605875. gene.
neXtProtNX_Q9Y6W5.
PharmGKBPA37344.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG299696.
HOGENOMHOG000021456.
HOVERGENHBG058482.
InParanoidQ9Y6W5.
KOK05748.
OMADTSELEC.
OrthoDBEOG7VHSXK.
PhylomeDBQ9Y6W5.
TreeFamTF315031.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ9Y6W5.

Gene expression databases

ArrayExpressQ9Y6W5.
BgeeQ9Y6W5.
CleanExHS_WASF2.
GenevestigatorQ9Y6W5.

Family and domain databases

InterProIPR028288. SCAR/WAVE_fam.
IPR003124. WH2_dom.
[Graphical view]
PANTHERPTHR12902. PTHR12902. 1 hit.
PfamPF02205. WH2. 1 hit.
[Graphical view]
SMARTSM00246. WH2. 1 hit.
[Graphical view]
PROSITEPS51082. WH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSWASF2. human.
EvolutionaryTraceQ9Y6W5.
GeneWikiWASF2.
GenomeRNAi10163.
NextBio38478.
PMAP-CutDBQ9Y6W5.
PROQ9Y6W5.
SOURCESearch...

Entry information

Entry nameWASF2_HUMAN
AccessionPrimary (citable) accession number: Q9Y6W5
Secondary accession number(s): B4DZN0, O60794, Q9UDY7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: February 1, 2005
Last modified: July 9, 2014
This is version 129 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 1

Human chromosome 1: entries, gene names and cross-references to MIM