true2001-04-272024-03-27222WASL_HUMANIdentification of N-WASP homologs in human and rat brain.Fukuoka M.Miki H.Takenawa T.doi:10.1016/s0378-1119(97)00184-41997Gene19643-48NUCLEOTIDE SEQUENCE [MRNA]BrainAnalysis of the anti-tumor T cell repertoire of melanoma patients vaccinated with a mixed tumor cell/DC vaccine.Lennerz V.Fatho M.Eberts D.Woelfel C.Schreiber S.Huber C.van der Bruggen P.Schmidt C.W.Woelfel T.2006-07EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [MRNA]MelanomaThe 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.doi:10.1038/nature017822003Nature424157-164NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project Teamdoi:10.1101/gr.25965042004Genome Res.142121-2127NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP.Miki H.Sasaki T.Takai Y.Takenawa T.doi:10.1038/342081998Nature39193-96FUNCTIONSUBCELLULAR LOCATIONINTERACTION WITH CDC42Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri.Suzuki T.Miki H.Takenawa T.Sasakawa C.doi:10.1093/emboj/17.10.27671998EMBO J.172767-2776INTERACTION WITH SHIGELLA FLEXNERI ICSA (MICROBIAL INFECTION)Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility.Egile C.Loisel T.P.Laurent V.Li R.Pantaloni D.Sansonetti P.J.Carlier M.-F.doi:10.1083/jcb.146.6.13191999J. Cell Biol.1461319-1332INTERACTION WITH SHIGELLA FLEXNERI ICSA (MICROBIAL INFECTION)Phosphorylation of WASP by the Cdc42-associated kinase ACK1: dual hydroxyamino acid specificity in a tyrosine kinase.Yokoyama N.Lougheed J.Miller W.T.doi:10.1074/jbc.m5069962002005J. Biol. Chem.28042219-42226PHOSPHORYLATION AT SER-242 AND TYR-256 BY TNK2INTERACTION WITH TNK2NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS.Icking A.Matt S.Opitz N.Wiesenthal A.Mueller-Esterl W.Schilling K.doi:10.1242/jcs.026202005J. Cell Sci.1185059-5069INTERACTION WITH NOSTRINRegulation of RNA-polymerase-II-dependent transcription by N-WASP and its nuclear-binding partners.Wu X.Yoo Y.Okuhama N.N.Tucker P.W.Liu G.Guan J.L.doi:10.1038/ncb14332006Nat. Cell Biol.8756-763FUNCTIONSUBCELLULAR LOCATIONIDENTIFICATION IN A COMPLEX WITH NONO AND SFPQINTERACTION WITH NONOCdc42 GEF Tuba regulates the junctional configuration of simple epithelial cells.Otani T.Ichii T.Aono S.Takeichi M.doi:10.1083/jcb.2006050122006J. Cell Biol.175135-146INTERACTION WITH DNMBPA quantitative atlas of mitotic phosphorylation.Dephoure N.Zhou C.Villen J.Beausoleil S.A.Bakalarski C.E.Elledge S.J.Gygi S.P.doi:10.1073/pnas.08051391052008Proc. Natl. Acad. Sci. U.S.A.10510762-10767IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Cervix carcinomaLys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S.Helbig A.O.Slijper M.Krijgsveld J.Heck A.J.Mohammed S.doi:10.1021/ac90043092009Anal. Chem.814493-4501ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Sorting nexin 33 induces mammalian cell micronucleated phenotype and actin polymerization by interacting with Wiskott-Aldrich syndrome protein.Zhang J.Zhang X.Guo Y.Xu L.Pei D.doi:10.1074/jbc.m109.0072782009J. Biol. Chem.28421659-21669FUNCTIONINTERACTION WITH SNX33The bacterial virulence factor InlC perturbs apical cell junctions and promotes cell-to-cell spread of Listeria.Rajabian T.Gavicherla B.Heisig M.Mueller-Altrock S.Goebel W.Gray-Owen S.D.Ireton K.doi:10.1038/ncb19642009Nat. Cell Biol.111212-1218FUNCTIONINTERACTION WITH DNMBPInsulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin assembly effectors Tir and EspF(U) during pedestal formation.Vingadassalom D.Kazlauskas A.Skehan B.Cheng H.C.Magoun L.Robbins D.Rosen M.K.Saksela K.Leong J.M.doi:10.1073/pnas.08091311062009Proc. Natl. Acad. Sci. U.S.A.1066754-6759FUNCTIONINTERACTION WITH E.COLI EFFECTOR PROTEIN ESPF(U) (MICROBIAL INFECTION)IDENTIFICATION IN A COMPLEX WITH BAIAP2L1 AND E.COLI EFFECTOR PROTEIN ESPF(U)Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V.Vermeulen M.Santamaria A.Kumar C.Miller M.L.Jensen L.J.Gnad F.Cox J.Jensen T.S.Nigg E.A.Brunak S.Mann M.doi:10.1126/scisignal.20004752010Sci. Signal.3RA3PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-256; SER-484 AND SER-485IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]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.doi:10.1186/1752-0509-5-172011BMC Syst. Biol.517IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]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.doi:10.1126/scisignal.20015702011Sci. Signal.4RS3PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND SER-485IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]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.doi:10.1074/mcp.m111.0151312012Mol. Cell. Proteomics11M111.015131ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P.Lasa M.Polevoda B.Gazquez C.Elosegui-Artola A.Kim D.S.De Juan-Pardo E.Demeyer K.Hole K.Larrea E.Timmerman E.Prieto J.Arnesen T.Sherman F.Gevaert K.Aldabe R.doi:10.1073/pnas.12103031092012Proc. Natl. Acad. Sci. U.S.A.10912449-12454ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.Guo A.Gu H.Zhou J.Mulhern D.Wang Y.Lee K.A.Yang V.Aguiar M.Kornhauser J.Jia X.Ren J.Beausoleil S.A.Silva J.C.Vemulapalli V.Bedford M.T.Comb M.J.doi:10.1074/mcp.o113.0278702014Mol. Cell. Proteomics13372-387METHYLATION [LARGE SCALE ANALYSIS] AT ARG-307IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Colon carcinomaA Flat BAR Protein Promotes Actin Polymerization at the Base of Clathrin-Coated Pits.Almeida-Souza L.Frank R.A.W.Garcia-Nafria J.Colussi A.Gunawardana N.Johnson C.M.Yu M.Howard G.Andrews B.Vallis Y.McMahon H.T.doi:10.1016/j.cell.2018.05.0202018Cell174325-337INTERACTION WITH FCHSD2The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins.Aguda A.H.Xue B.Irobi E.Preat T.Robinson R.C.doi:10.1016/j.str.2005.12.0112006Structure14469-476X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 451-465Interactions of isolated C-terminal fragments of neural Wiskott-Aldrich syndrome protein (N-WASP) with actin and Arp2/3 complex.Gaucher J.F.Mauge C.Didry D.Guichard B.Renault L.Carlier M.F.doi:10.1074/jbc.m112.3943612012J. Biol. Chem.28734646-34659X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 392-484 IN COMPLEX WITH ACTINFUNCTIONSUBUNITINTERACTION WITH THE ARP2/3 COMPLEXACTIN-BINDINGEnterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly.Aitio O.Hellman M.Skehan B.Kesti T.Leong J.M.Saksela K.Permi P.doi:10.1016/j.str.2012.07.0152012Structure201692-1703STRUCTURE BY NMR OF 207-270 IN COMPLEX WITH BAIAP2L1 AND THE E.COLI SECRETED EFFECTOR PROTEIN ESPF(U) (MICROBIAL INFECTION)IDENTIFICATION IN A COMPLEX WITH BAIAP2L1 AND E.COLI EFFECTOR PROTEIN ESPF(U)FUNCTIONStructural details of human tuba recruitment by InlC of Listeria monocytogenes elucidate bacterial cell-cell spreading.Polle L.Rigano L.A.Julian R.Ireton K.Schubert W.D.doi:10.1016/j.str.2013.10.0172014Structure22304-314X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 346-357 IN COMPLEX WITH DNMBPSUBUNIT2.00C=451-465A=207-2703.20D/E=392-4841.55B/D=346-3571.97B/D/F/H/J/L/N=346-357125722 sites, 1 O-linked glycan (2 sites)298 antibodies from 37 providershumanWASLLow tissue specificitygeneEukaryotaRegulation of actin dynamics for phagocytic cup formationNOSTRIN mediated eNOS traffickingNephrin family interactionsEPHB-mediated forward signalingDCC mediated attractive signalingRHO GTPases Activate WASPs and WAVEsClathrin-mediated endocytosisCDC42 GTPase cycleRAC1 GTPase cycleRHOQ GTPase cycleRHOJ GTPase cycleRHOV GTPase cycleFCGR3A-mediated phagocytosis35 hits in 1169 CRISPR screenshumanTbioProteinExpressed in middle temporal gyrus and 205 other cell types or tissuesCRIBEVH1_WASP-likeWH2_hN-WASP_r2_likeWH2_N-WASP_r1CRIB domainPleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)CRIB_domCRIB_dom_sfPH-like_dom_sfWAS_CWASPfam_EVH1WH1/EVH1_domWH2_domNEURAL WISKOTT-ALDRICH SYNDROME PROTEINSPROUTY-RELATED, EVH1 DOMAIN-CONTAINING PROTEIN FAMILY MEMBERPBDWH1WH2PBDWH1WH2PH domain-likeWiscott-Aldrich syndrome protein, WASP, C-terminal domainCRIBWH1WH2HSActin nucleation-promoting factor WASLNeural Wiskott-Aldrich syndrome proteinN-WASPWASLRegulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex (PubMed:9422512, PubMed:16767080, PubMed:19366662, PubMed:19487689, PubMed:22847007, PubMed:22921828). Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization (PubMed:9422512, PubMed:19366662, PubMed:19487689, PubMed:22847007, PubMed:22921828). Together with CDC42, involved in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia (PubMed:9422512). In addition to its role in the cytoplasm, also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization (PubMed:16767080). Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression (By similarity). Plays a role in dendrite spine morphogenesis (By similarity). Decreasing levels of DNMBP (using antisense RNA) alters apical junction morphology in cultured enterocytes, junctions curve instead of being nearly linear (PubMed:19767742).Binds actin and the Arp2/3 complex (PubMed:22847007). Interacts with CDC42 (PubMed:9422512). Interacts with FCHSD1 (By similarity). Interacts with FCHSD2 (PubMed:29887380). Binds to SH3 domains of GRB2. Interacts with the C-terminal SH3 domain of DNMBP (PubMed:19767742, PubMed:24332715, PubMed:17015620). Interacts with SNX9 (By similarity). Interacts with the WW domains of PRPF40A/FBP11 (By similarity). Interacts with PTK2/FAK1 (By similarity). Interacts with PACSIN1, PACSIN2 and PACSIN3 (By similarity). Interacts with NOSTRIN (PubMed:16234328). Binds to TNK2 (PubMed:16257963). Interacts with SNX33 (PubMed:19487689). Interacts with NONO (via second RRM domain); the interaction is direct (PubMed:16767080). Component of a multiprotein complex with NONO and SFPQ; associates with the complex via direct interaction with NONO (PubMed:16767080).(Microbial infection) Interacts with E.coli effector protein EspF(U) (PubMed:19366662, PubMed:22921828). Identified in a complex containing at least WASL, BAIAP2L1 and E.coli EspF(U) (PubMed:22921828).(Microbial infection) Interacts with Shigella flexneri protein IcsA (PubMed:9582270, PubMed:10491394). The interaction with IcsA enhances the affinity of WASL for Arp2/3, thus assembling a tight complex which has maximal activity in actin assembly (PubMed:9582270, PubMed:10491394).Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated (By similarity). Exported from the nucleus by an nuclear export signal (NES)-dependent mechanism to the cytoplasm (By similarity).Phosphorylation at Ser-242, Tyr-256, Ser-484 and Ser-485 enhances actin polymerization activity.Removed1Actin nucleation-promoting factor WASL546962505WH134141CRIB203216WH2 1405422WH2 2433450Disordered138163Disordered184205Disordered266406Disordered476Pro residues274394Acidic residues486N-acetylserinePhosphoserine; by TNK2242Phosphotyrosine; by FAK1 and TNK2256Omega-N-methylarginine307Phosphoserine484Phosphoserine485H76G201S223LE248L252S296E333L351219221225227232239243246249251262265269435443false5false3false6false3false3false7false2false11false3false2false2false3false7false3false3false8false3false6false8false6false2false3false3false5false3false3false8false5true2true3true2true5true2ABI2ARHGAP12ARPC3ARPC4CDC42CIB1DNMBPGRB2NCK1NCK1NCK1NCK2NCK2PACSIN2PACSIN3PAK4PTK6RHOJRNF8SDCBPSNX9SORBS2SORBS3TRIP10UBASH3AUBASH3BWIPF1WIPF2ACTA1ACTR3espF(U)espF(U)Fnbp12005-02-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