WASF2_HUMAN
ID WASF2_HUMAN Reviewed; 498 AA.
AC Q9Y6W5; B4DZN0; O60794; Q9UDY7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Actin-binding protein WASF2 {ECO:0000305};
DE AltName: Full=Protein WAVE-2;
DE AltName: Full=Verprolin homology domain-containing protein 2;
DE AltName: Full=Wiskott-Aldrich syndrome protein family member 2;
DE Short=WASP family protein member 2;
GN Name=WASF2 {ECO:0000312|HGNC:HGNC:12733};
GN Synonyms=WAVE2 {ECO:0000312|HGNC:HGNC:12733};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ACTIN
RP AND THE ARP2/3 COMPLEX, SUBUNIT, DOMAIN, AND TISSUE SPECIFICITY.
RC TISSUE=T-cell lymphoma;
RX PubMed=10381382; DOI=10.1006/bbrc.1999.0894;
RA Suetsugu S., Miki H., Takenawa T.;
RT "Identification of two human WAVE/SCAR homologues as general actin
RT regulatory molecules which associate with the Arp2/3 complex.";
RL Biochem. Biophys. Res. Commun. 260:296-302(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH BAIAP2.
RX PubMed=11130076; DOI=10.1038/35047107;
RA Miki H., Yamaguchi H., Suetsugu S., Takenawa T.;
RT "IRSp53 is an essential intermediate between Rac and WAVE in the regulation
RT of membrane ruffling.";
RL Nature 408:732-735(2000).
RN [6]
RP INTERACTION WITH C3ORF10.
RX PubMed=15070726; DOI=10.1073/pnas.0400628101;
RA Gautreau A., Ho H.-Y., Li J., Steen H., Gygi S.P., Kirschner M.W.;
RT "Purification and architecture of the ubiquitous Wave complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4379-4383(2004).
RN [7]
RP IDENTIFICATION IN THE WAVE2 COMPLEX.
RX PubMed=16417406; DOI=10.1371/journal.pbio.0040038;
RA Weiner O.D., Rentel M.C., Ott A., Brown G.E., Jedrychowski M., Yaffe M.B.,
RA Gygi S.P., Cantley L.C., Bourne H.R., Kirschner M.W.;
RT "Hem-1 complexes are essential for Rac activation, actin polymerization,
RT and myosin regulation during neutrophil chemotaxis.";
RL PLoS Biol. 4:E38-E38(2006).
RN [8]
RP INTERACTION WITH FNBP1L.
RX PubMed=19798448; DOI=10.1371/journal.pgen.1000675;
RA Giuliani C., Troglio F., Bai Z., Patel F.B., Zucconi A., Malabarba M.G.,
RA Disanza A., Stradal T.B., Cassata G., Confalonieri S., Hardin J.D.,
RA Soto M.C., Grant B.D., Scita G.;
RT "Requirements for F-BAR proteins TOCA-1 and TOCA-2 in actin dynamics and
RT membrane trafficking during Caenorhabditis elegans oocyte growth and
RT embryonic epidermal morphogenesis.";
RL PLoS Genet. 5:E1000675-E1000675(2009).
RN [9]
RP MUTAGENESIS OF LEU-40; ILE-50; PHE-51 AND LEU-54, AND SUBUNIT.
RX PubMed=21107423; DOI=10.1038/nature09623;
RA Chen Z., Borek D., Padrick S.B., Gomez T.S., Metlagel Z., Ismail A.M.,
RA Umetani J., Billadeau D.D., Otwinowski Z., Rosen M.K.;
RT "Structure and control of the actin regulatory WAVE complex.";
RL Nature 468:533-538(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL135 (MICROBIAL INFECTION).
RX PubMed=25121749; DOI=10.1016/j.chom.2014.07.005;
RA Stanton R.J., Prod'homme V., Purbhoo M.A., Moore M., Aicheler R.J.,
RA Heinzmann M., Bailer S.M., Haas J., Antrobus R., Weekes M.P., Lehner P.J.,
RA Vojtesek B., Miners K.L., Man S., Wilkie G.S., Davison A.J., Wang E.C.,
RA Tomasec P., Wilkinson G.W.;
RT "HCMV pUL135 remodels the actin cytoskeleton to impair immune recognition
RT of infected cells.";
RL Cell Host Microbe 16:201-214(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=30250061; DOI=10.1038/s41556-018-0198-9;
RA Fort L., Batista J.M., Thomason P.A., Spence H.J., Whitelaw J.A.,
RA Tweedy L., Greaves J., Martin K.J., Anderson K.I., Brown P., Lilla S.,
RA Neilson M.P., Tafelmeyer P., Zanivan S., Ismail S., Bryant D.M.,
RA Tomkinson N.C.O., Chamberlain L.H., Mastick G.S., Insall R.H.,
RA Machesky L.M.;
RT "Fam49/CYRI interacts with Rac1 and locally suppresses protrusions.";
RL Nat. Cell Biol. 20:1159-1171(2018).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 433-464 IN COMPLEX WITH ACTIN,
RP FUNCTION, DOMAIN, MUTAGENESIS OF TYR-124; TYR-150 AND 160-TRP-LYS-161, AND
RP SUBUNIT.
RX PubMed=16275905; DOI=10.1073/pnas.0507021102;
RA Chereau D., Kerff F., Graceffa P., Grabarek Z., Langsetmo K., Dominguez R.;
RT "Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology
RT domain 2 and the implications for filament assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16644-16649(2005).
CC -!- FUNCTION: Downstream effector molecule involved in the transmission of
CC signals from tyrosine kinase receptors and small GTPases to the actin
CC cytoskeleton. Promotes formation of actin filaments. Part of the WAVE
CC complex that regulates lamellipodia formation. The WAVE complex
CC regulates actin filament reorganization via its interaction with the
CC Arp2/3 complex. {ECO:0000269|PubMed:10381382,
CC ECO:0000269|PubMed:16275905}.
CC -!- SUBUNIT: Binds actin and the Arp2/3 complex. Interacts with BAIAP2.
CC Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1,
CC NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic cells) and WASF2/WAVE2
CC (PubMed:16417406). Directly interacts with BRK1. Interacts with FNBP1L
CC (via the SH3 domain) (PubMed:19798448). {ECO:0000269|PubMed:10381382,
CC ECO:0000269|PubMed:11130076, ECO:0000269|PubMed:15070726,
CC ECO:0000269|PubMed:16275905, ECO:0000269|PubMed:16417406,
CC ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:21107423}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC protein UL135. {ECO:0000269|PubMed:25121749}.
CC -!- INTERACTION:
CC Q9Y6W5; Q9UQB8-4: BAIAP2; NbExp=5; IntAct=EBI-4290615, EBI-6174091;
CC Q9Y6W5; O60504-2: SORBS3; NbExp=3; IntAct=EBI-4290615, EBI-1222956;
CC Q9Y6W5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-4290615, EBI-5235340;
CC Q9Y6W5; Q8IUH5: ZDHHC17; NbExp=2; IntAct=EBI-4290615, EBI-524753;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC projection, lamellipodium {ECO:0000250}. Basolateral cell membrane
CC {ECO:0000269|PubMed:30250061}. Note=At the interface between the
CC lamellipodial actin meshwork and the membrane. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y6W5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y6W5-2; Sequence=VSP_042514, VSP_042515;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues with strongest expression
CC in placenta, lung, and peripheral blood leukocytes, but not in skeletal
CC muscle. {ECO:0000269|PubMed:10381382}.
CC -!- DOMAIN: Binds and activates the Arp2/3 complex via the C-terminal
CC domain. Interacts with actin via the WH2 domain.
CC {ECO:0000269|PubMed:10381382, ECO:0000269|PubMed:16275905}.
CC -!- SIMILARITY: Belongs to the SCAR/WAVE family. {ECO:0000305}.
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DR EMBL; AB026542; BAA81795.1; -; mRNA.
DR EMBL; AK303011; BAG64142.1; -; mRNA.
DR EMBL; AL096774; CAC18518.1; -; Genomic_DNA.
DR EMBL; AL663122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX293535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040943; AAH40943.1; -; mRNA.
DR CCDS; CCDS304.1; -. [Q9Y6W5-1]
DR CCDS; CCDS55582.1; -. [Q9Y6W5-2]
DR RefSeq; NP_001188333.1; NM_001201404.2. [Q9Y6W5-2]
DR RefSeq; NP_008921.1; NM_006990.4. [Q9Y6W5-1]
DR PDB; 2A40; X-ray; 1.80 A; C/F=433-464.
DR PDBsum; 2A40; -.
DR AlphaFoldDB; Q9Y6W5; -.
DR SMR; Q9Y6W5; -.
DR BioGRID; 115465; 106.
DR CORUM; Q9Y6W5; -.
DR DIP; DIP-41817N; -.
DR ELM; Q9Y6W5; -.
DR IntAct; Q9Y6W5; 36.
DR MINT; Q9Y6W5; -.
DR STRING; 9606.ENSP00000483313; -.
DR GlyGen; Q9Y6W5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y6W5; -.
DR PhosphoSitePlus; Q9Y6W5; -.
DR BioMuta; WASF2; -.
DR DMDM; 59800456; -.
DR EPD; Q9Y6W5; -.
DR jPOST; Q9Y6W5; -.
DR MassIVE; Q9Y6W5; -.
DR MaxQB; Q9Y6W5; -.
DR PaxDb; Q9Y6W5; -.
DR PeptideAtlas; Q9Y6W5; -.
DR PRIDE; Q9Y6W5; -.
DR ProteomicsDB; 86801; -. [Q9Y6W5-1]
DR ProteomicsDB; 86802; -. [Q9Y6W5-2]
DR Antibodypedia; 30784; 353 antibodies from 32 providers.
DR DNASU; 10163; -.
DR Ensembl; ENST00000536657.1; ENSP00000439883.1; ENSG00000158195.11. [Q9Y6W5-2]
DR Ensembl; ENST00000618852.5; ENSP00000483313.1; ENSG00000158195.11. [Q9Y6W5-1]
DR GeneID; 10163; -.
DR KEGG; hsa:10163; -.
DR MANE-Select; ENST00000618852.5; ENSP00000483313.1; NM_006990.5; NP_008921.1.
DR UCSC; uc057dvq.1; human. [Q9Y6W5-1]
DR CTD; 10163; -.
DR DisGeNET; 10163; -.
DR GeneCards; WASF2; -.
DR HGNC; HGNC:12733; WASF2.
DR HPA; ENSG00000158195; Low tissue specificity.
DR MIM; 605875; gene.
DR neXtProt; NX_Q9Y6W5; -.
DR OpenTargets; ENSG00000158195; -.
DR PharmGKB; PA37344; -.
DR VEuPathDB; HostDB:ENSG00000158195; -.
DR eggNOG; KOG1830; Eukaryota.
DR GeneTree; ENSGT00950000182962; -.
DR HOGENOM; CLU_036022_2_0_1; -.
DR InParanoid; Q9Y6W5; -.
DR OMA; WEKIKMG; -.
DR OrthoDB; 1183697at2759; -.
DR PhylomeDB; Q9Y6W5; -.
DR TreeFam; TF315031; -.
DR PathwayCommons; Q9Y6W5; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; Q9Y6W5; -.
DR SIGNOR; Q9Y6W5; -.
DR BioGRID-ORCS; 10163; 88 hits in 1078 CRISPR screens.
DR ChiTaRS; WASF2; human.
DR EvolutionaryTrace; Q9Y6W5; -.
DR GeneWiki; WASF2; -.
DR GenomeRNAi; 10163; -.
DR Pharos; Q9Y6W5; Tbio.
DR PRO; PR:Q9Y6W5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y6W5; protein.
DR Bgee; ENSG00000158195; Expressed in nipple and 198 other tissues.
DR Genevisible; Q9Y6W5; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR GO; GO:0031209; C:SCAR complex; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0071933; F:Arp2/3 complex binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0051018; F:protein kinase A binding; IPI:UniProtKB.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030048; P:actin filament-based movement; IEA:Ensembl.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0001667; P:ameboidal-type cell migration; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0072673; P:lamellipodium morphogenesis; IEA:Ensembl.
DR GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:UniProtKB.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:UniProtKB.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0016601; P:Rac protein signal transduction; IEA:Ensembl.
DR InterPro; IPR028288; SCAR/WAVE_fam.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR12902; PTHR12902; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00246; WH2; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Host-virus interaction; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..498
FT /note="Actin-binding protein WASF2"
FT /id="PRO_0000188994"
FT DOMAIN 436..453
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 173..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..413
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 275..281
FT /note="SYPVDNQ -> RFSAAQG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042514"
FT VAR_SEQ 282..498
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042515"
FT MUTAGEN 40
FT /note="L->D: Decreased interaction with WAVE complex; when
FT associated with D-51."
FT /evidence="ECO:0000269|PubMed:21107423"
FT MUTAGEN 50
FT /note="I->D: Decreased interaction with WAVE complex; when
FT associated with D-54."
FT /evidence="ECO:0000269|PubMed:21107423"
FT MUTAGEN 51
FT /note="F->D: Decreased interaction with WAVE complex; when
FT associated with D-40."
FT /evidence="ECO:0000269|PubMed:21107423"
FT MUTAGEN 54
FT /note="L->D: Decreased interaction with WAVE complex; when
FT associated with D-50."
FT /evidence="ECO:0000269|PubMed:21107423"
FT MUTAGEN 124
FT /note="Y->D: Constitutive induction of the formation of
FT actin filaments. Strongly enhances formation of
FT lamellipodia."
FT /evidence="ECO:0000269|PubMed:16275905"
FT MUTAGEN 150
FT /note="Y->D: Constitutive induction of the formation of
FT actin filaments. Strongly enhances formation of
FT lamellipodia."
FT /evidence="ECO:0000269|PubMed:16275905"
FT MUTAGEN 160..161
FT /note="WK->ED: Constitutive induction of the formation of
FT actin filaments. Strongly enhances formation of
FT lamellipodia."
FT /evidence="ECO:0000269|PubMed:16275905"
FT HELIX 436..446
FT /evidence="ECO:0007829|PDB:2A40"
SQ SEQUENCE 498 AA; 54284 MW; C737CE963016DE94 CRC64;
MPLVTRNIEP RHLCRQTLPS VRSELECVTN ITLANVIRQL GSLSKYAEDI FGELFTQANT
FASRVSSLAE RVDRLQVKVT QLDPKEEEVS LQGINTRKAF RSSTIQDQKL FDRNSLPVPV
LETYNTCDTP PPLNNLTPYR DDGKEALKFY TDPSYFFDLW KEKMLQDTKD IMKEKRKHRK
EKKDNPNRGN VNPRKIKTRK EEWEKMKMGQ EFVESKEKLG TSGYPPTLVY QNGSIGCVEN
VDASSYPPPP QSDSASSPSP SFSEDNLPPP PAEFSYPVDN QRGSGLAGPK RSSVVSPSHP
PPAPPLGSPP GPKPGFAPPP APPPPPPPMI GIPPPPPPVG FGSPGTPPPP SPPSFPPHPD
FAAPPPPPPP PAADYPTLPP PPLSQPTGGA PPPPPPPPPP GPPPPPFTGA DGQPAIPPPL
SDTTKPKSSL PAVSDARSDL LSAIRQGFQL RRVEEQREQE KRDVVGNDVA TILSRRIAVE
YSDSEDDSSE FDEDDWSD
