WIPF1_HUMAN
ID WIPF1_HUMAN Reviewed; 503 AA.
AC O43516; B8ZZM1; D3DPE4; Q15220; Q53TA9; Q6MZU9; Q9BU37; Q9UNP1;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=WAS/WASL-interacting protein family member 1;
DE AltName: Full=Protein PRPL-2;
DE AltName: Full=Wiskott-Aldrich syndrome protein-interacting protein;
DE Short=WASP-interacting protein;
GN Name=WIPF1; Synonyms=WASPIP, WIP;
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), VARIANTS LEU-198 AND GLY-495,
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH WASP; PROFILIN AND
RP ACTIN.
RX PubMed=9405671; DOI=10.1073/pnas.94.26.14671;
RA Ramesh N., Anton I.M., Hartwig J.H., Geha R.S.;
RT "WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces
RT actin polymerization and redistribution in lymphoid cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14671-14676(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS LEU-198 AND GLY-495.
RC TISSUE=Tonsil;
RA Kreideweiss S., Delany-Heiken P., Nordheim A., Ruhlmann A.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT LEU-198.
RC TISSUE=Endometrial tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-198.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT LEU-198.
RC TISSUE=Skin;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 192-503 (ISOFORM 1), INTERACTION WITH WASP,
RP AND VARIANT LEU-198.
RX PubMed=10202051;
RA Stewart D.M., Tian L., Nelson D.L.;
RT "Mutations that cause the Wiskott-Aldrich syndrome impair the interaction
RT of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein.";
RL J. Immunol. 162:5019-5024(1999).
RN [8]
RP FUNCTION.
RX PubMed=10878810; DOI=10.1038/35017080;
RA Moreau V., Frischknecht F., Reckmann I., Vincentelli R., Rabut G.,
RA Stewart D.M., Way M.;
RT "A complex of N-WASP and WIP integrates signalling cascades that lead to
RT actin polymerization.";
RL Nat. Cell Biol. 2:441-448(2000).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-345 AND SER-350, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DBNL.
RX PubMed=19910490; DOI=10.1091/mbc.e09-02-0106;
RA Cortesio C.L., Perrin B.J., Bennin D.A., Huttenlocher A.;
RT "Actin-binding protein-1 interacts with WASp-interacting protein to
RT regulate growth factor-induced dorsal ruffle formation.";
RL Mol. Biol. Cell 21:186-197(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340; THR-345 AND SER-350, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP INVOLVEMENT IN WAS2.
RX PubMed=22231303; DOI=10.1084/jem.20110896;
RA Lanzi G., Moratto D., Vairo D., Masneri S., Delmonte O., Paganini T.,
RA Parolini S., Tabellini G., Mazza C., Savoldi G., Montin D., Martino S.,
RA Tovo P., Pessach I.M., Massaad M.J., Ramesh N., Porta F., Plebani A.,
RA Notarangelo L.D., Geha R.S., Giliani S.;
RT "A novel primary human immunodeficiency due to deficiency in the WASP-
RT interacting protein WIP.";
RL J. Exp. Med. 209:29-34(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234; SER-340 AND SER-350, AND
RP IDENTIFICATION BY 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, AND IDENTIFICATION BY
RP 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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 29-60 IN COMPLEX WITH ACTIN.
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: Plays a role in the reorganization of the actin cytoskeleton.
CC Contributes with NCK1 and GRB2 in the recruitment and activation of
CC WASL. May participate in regulating the subcellular localization of
CC WASL, resulting in the disassembly of stress fibers in favor of
CC filopodia formation. Plays a role in the formation of cell ruffles (By
CC similarity). Plays an important role in the intracellular motility of
CC vaccinia virus by functioning as an adapter for recruiting WASL to
CC vaccinia virus. {ECO:0000250, ECO:0000269|PubMed:10878810,
CC ECO:0000269|PubMed:19910490, ECO:0000269|PubMed:9405671}.
CC -!- SUBUNIT: Binds to WAS, profilin and actin. Binds to WASL (By
CC similarity). Interacts with DBNL. Interacts with FNBP1L (via the SH3
CC domain) (PubMed:19798448). {ECO:0000250, ECO:0000269|PubMed:10202051,
CC ECO:0000269|PubMed:16275905, ECO:0000269|PubMed:19798448,
CC ECO:0000269|PubMed:19910490, ECO:0000269|PubMed:9405671}.
CC -!- INTERACTION:
CC O43516; Q9NYB9: ABI2; NbExp=4; IntAct=EBI-346356, EBI-743598;
CC O43516; P13196: ALAS1; NbExp=3; IntAct=EBI-346356, EBI-3905054;
CC O43516; Q14296: FASTK; NbExp=3; IntAct=EBI-346356, EBI-1754067;
CC O43516; P62993: GRB2; NbExp=4; IntAct=EBI-346356, EBI-401755;
CC O43516; P08631: HCK; NbExp=3; IntAct=EBI-346356, EBI-346340;
CC O43516; P14317: HCLS1; NbExp=2; IntAct=EBI-346356, EBI-750369;
CC O43516; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-346356, EBI-748420;
CC O43516; P16333: NCK1; NbExp=2; IntAct=EBI-346356, EBI-389883;
CC O43516; P53992: SEC24C; NbExp=3; IntAct=EBI-346356, EBI-81134;
CC O43516; P42768: WAS; NbExp=25; IntAct=EBI-346356, EBI-346375;
CC O43516; O00401: WASL; NbExp=8; IntAct=EBI-346356, EBI-957615;
CC O43516; O00308: WWP2; NbExp=4; IntAct=EBI-346356, EBI-743923;
CC O43516; Q60598: Cttn; Xeno; NbExp=4; IntAct=EBI-346356, EBI-397955;
CC O43516-4; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-12052927, EBI-11096309;
CC O43516-4; Q9Y698: CACNG2; NbExp=3; IntAct=EBI-12052927, EBI-6659211;
CC O43516-4; O43639: NCK2; NbExp=3; IntAct=EBI-12052927, EBI-713635;
CC O43516-4; O15258: RER1; NbExp=3; IntAct=EBI-12052927, EBI-716910;
CC O43516-4; P42768: WAS; NbExp=3; IntAct=EBI-12052927, EBI-346375;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Cell projection, ruffle
CC {ECO:0000269|PubMed:19910490}. Note=Vesicle surfaces and along actin
CC tails. Colocalizes with actin stress fibers. When coexpressed with
CC WASL, no longer associated with actin filaments but accumulated in
CC perinuclear and cortical areas like WASL (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O43516-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43516-2; Sequence=VSP_012965;
CC Name=3;
CC IsoId=O43516-3; Sequence=VSP_012966;
CC Name=4;
CC IsoId=O43516-4; Sequence=VSP_012964;
CC -!- TISSUE SPECIFICITY: Highly expressed in peripheral blood mononuclear
CC cells, spleen, placenta, small intestine, colon and thymus. Lower
CC expression in ovary, heart, brain, lung, liver, skeletal muscle,
CC kidney, pancreas, prostate and testis. {ECO:0000269|PubMed:9405671}.
CC -!- DOMAIN: Binds to WAS within the N-terminal region 170, at a site
CC distinct from the CDC42-binding site.
CC -!- DISEASE: Wiskott-Aldrich syndrome 2 (WAS2) [MIM:614493]: An
CC immunodeficiency disorder characterized by eczema, thrombocytopenia,
CC recurrent infections, defective T-cell proliferation, and impaired
CC natural killer cell function. {ECO:0000269|PubMed:22231303}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Recruited to PIP5K-induced vesicle surfaces in the
CC absence of functional WASL. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the verprolin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC03767.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA60014.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF031588; AAC03767.1; ALT_FRAME; mRNA.
DR EMBL; X86019; CAA60014.1; ALT_FRAME; mRNA.
DR EMBL; BX640870; CAE45928.1; -; mRNA.
DR EMBL; AC010894; AAY14708.1; -; Genomic_DNA.
DR EMBL; AC104595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471058; EAX11131.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11132.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11133.1; -; Genomic_DNA.
DR EMBL; BC002914; AAH02914.1; -; mRNA.
DR EMBL; AF106062; AAD45972.1; -; mRNA.
DR CCDS; CCDS2260.1; -. [O43516-1]
DR RefSeq; NP_001070737.1; NM_001077269.1. [O43516-1]
DR RefSeq; NP_003378.3; NM_003387.4. [O43516-1]
DR RefSeq; XP_011510082.1; XM_011511780.2.
DR PDB; 2A41; X-ray; 2.60 A; C=29-60.
DR PDBsum; 2A41; -.
DR AlphaFoldDB; O43516; -.
DR SMR; O43516; -.
DR BioGRID; 113295; 35.
DR CORUM; O43516; -.
DR DIP; DIP-17015N; -.
DR ELM; O43516; -.
DR IntAct; O43516; 28.
DR MINT; O43516; -.
DR STRING; 9606.ENSP00000376330; -.
DR GlyGen; O43516; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43516; -.
DR PhosphoSitePlus; O43516; -.
DR BioMuta; WIPF1; -.
DR EPD; O43516; -.
DR jPOST; O43516; -.
DR MassIVE; O43516; -.
DR MaxQB; O43516; -.
DR PaxDb; O43516; -.
DR PeptideAtlas; O43516; -.
DR PRIDE; O43516; -.
DR ProteomicsDB; 49004; -. [O43516-1]
DR ProteomicsDB; 49005; -. [O43516-2]
DR ProteomicsDB; 49006; -. [O43516-3]
DR ProteomicsDB; 49007; -. [O43516-4]
DR Antibodypedia; 4053; 157 antibodies from 34 providers.
DR DNASU; 7456; -.
DR Ensembl; ENST00000272746.9; ENSP00000272746.5; ENSG00000115935.18. [O43516-3]
DR Ensembl; ENST00000359761.7; ENSP00000352802.3; ENSG00000115935.18. [O43516-1]
DR Ensembl; ENST00000392546.6; ENSP00000376329.2; ENSG00000115935.18. [O43516-1]
DR Ensembl; ENST00000392547.6; ENSP00000376330.2; ENSG00000115935.18. [O43516-1]
DR Ensembl; ENST00000409891.5; ENSP00000386431.1; ENSG00000115935.18. [O43516-2]
DR Ensembl; ENST00000679041.1; ENSP00000503603.1; ENSG00000115935.18. [O43516-1]
DR GeneID; 7456; -.
DR KEGG; hsa:7456; -.
DR MANE-Select; ENST00000679041.1; ENSP00000503603.1; NM_001375834.1; NP_001362763.1.
DR UCSC; uc002uiz.4; human. [O43516-1]
DR CTD; 7456; -.
DR DisGeNET; 7456; -.
DR GeneCards; WIPF1; -.
DR HGNC; HGNC:12736; WIPF1.
DR HPA; ENSG00000115935; Tissue enhanced (lymphoid).
DR MalaCards; WIPF1; -.
DR MIM; 602357; gene.
DR MIM; 614493; phenotype.
DR neXtProt; NX_O43516; -.
DR OpenTargets; ENSG00000115935; -.
DR Orphanet; 906; Wiskott-Aldrich syndrome.
DR PharmGKB; PA162409189; -.
DR VEuPathDB; HostDB:ENSG00000115935; -.
DR eggNOG; KOG4462; Eukaryota.
DR GeneTree; ENSGT00910000144296; -.
DR HOGENOM; CLU_041032_0_0_1; -.
DR InParanoid; O43516; -.
DR OMA; NTPRPVQ; -.
DR PhylomeDB; O43516; -.
DR TreeFam; TF332135; -.
DR PathwayCommons; O43516; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; O43516; -.
DR SIGNOR; O43516; -.
DR BioGRID-ORCS; 7456; 21 hits in 1074 CRISPR screens.
DR ChiTaRS; WIPF1; human.
DR EvolutionaryTrace; O43516; -.
DR GeneWiki; WIPF1; -.
DR GenomeRNAi; 7456; -.
DR Pharos; O43516; Tbio.
DR PRO; PR:O43516; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O43516; protein.
DR Bgee; ENSG00000115935; Expressed in blood and 200 other tissues.
DR ExpressionAtlas; O43516; baseline and differential.
DR Genevisible; O43516; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0005522; F:profilin binding; TAS:ProtInc.
DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
DR GO; GO:0030048; P:actin filament-based movement; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; TAS:ProtInc.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR GO; GO:0051707; P:response to other organism; IEA:Ensembl.
DR DisProt; DP01172; -.
DR Gene3D; 2.30.29.30; -; 1.
DR IDEAL; IID00258; -.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR003124; WH2_dom.
DR InterPro; IPR028295; WIP.
DR PANTHER; PTHR23202:SF32; PTHR23202:SF32; 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 projection;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Methylation; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..503
FT /note="WAS/WASL-interacting protein family member 1"
FT /id="PRO_0000065941"
FT DOMAIN 32..49
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REPEAT 352..361
FT /note="XRSGPXPPXP motif 1"
FT REPEAT 374..383
FT /note="XRSGPXPPXP motif 2"
FT REPEAT 410..419
FT /note="XRSGPXPPXP motif 3"
FT REGION 1..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..48
FT /note="Binds actin"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..326
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..387
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..436
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1I7"
FT MOD_RES 125
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1I7"
FT MOD_RES 134
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1I7"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1I7"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 345
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 220..364
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012964"
FT VAR_SEQ 487..503
FT /note="GSNRRERGAPPLPPIPR -> EYFCQGF (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_012965"
FT VAR_SEQ 503
FT /note="R -> RPPKQAAE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_012966"
FT VARIANT 198
FT /note="P -> L (in dbSNP:rs4972450)"
FT /evidence="ECO:0000269|PubMed:10202051,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:9405671, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.5"
FT /id="VAR_046526"
FT VARIANT 495
FT /note="A -> G"
FT /evidence="ECO:0000269|PubMed:9405671, ECO:0000269|Ref.2"
FT /id="VAR_010295"
FT CONFLICT 119
FT /note="N -> D (in Ref. 3; CAE45928)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="D -> H (in Ref. 6; AAH02914)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="P -> PV (in Ref. 2; CAA60014)"
FT /evidence="ECO:0000305"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:2A41"
SQ SEQUENCE 503 AA; 51258 MW; 09B7A95E6808A46D CRC64;
MPVPPPPAPP PPPTFALANT EKPTLNKTEQ AGRNALLSDI SKGKKLKKTV TNDRSAPILD
KPKGAGAGGG GGGFGGGGGF GGGGGGGGGG SFGGGGPPGL GGLFQAGMPK LRSTANRDND
SGGSRPPLLP PGGRSTSAKP FSPPSGPGRF PVPSPGHRSG PPEPQRNRMP PPRPDVGSKP
DSIPPPVPST PRPIQSSPHN RGSPPVPGGP RQPSPGPTPP PFPGNRGTAL GGGSIRQSPL
SSSSPFSNRP PLPPTPSRAL DDKPPPPPPP VGNRPSIHRE AVPPPPPQNN KPPVPSTPRP
SASSQAPPPP PPPSRPGPPP LPPSSSGNDE TPRLPQRNLS LSSSTPPLPS PGRSGPLPPP
PSERPPPPVR DPPGRSGPLP PPPPVSRNGS TSRALPATPQ LPSRSGVDSP RSGPRPPLPP
DRPSAGAPPP PPPSTSIRNG FQDSPCEDEW ESRFYFHPIS DLPPPEPYVQ TTKSYPSKLA
RNESRSGSNR RERGAPPLPP IPR
