ID EVL_HUMAN Reviewed; 416 AA. AC Q9UI08; A8K105; B7Z3I5; O95884; Q7Z522; Q8TBV1; Q9UF25; Q9UIC2; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 15-NOV-2002, sequence version 2. DT 27-MAR-2024, entry version 204. DE RecName: Full=Ena/VASP-like protein; DE AltName: Full=Ena/vasodilator-stimulated phosphoprotein-like; GN Name=EVL; Synonyms=RNB6; 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 2). RA Ohta S., Mineta T., Kimoto M., Tabuchi K.; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Wan Y.Z., Yu L., Yue P., Tu Q., Fu S.N., Zhao S.Y.; RT "Cloning of a new human cDNA homologous to R.norvegicus RNB6 mRNA."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Adrenal gland; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., RA Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis RT and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Brain, and Substantia nigra; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Lung, and Pancreas; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-416. RC TISSUE=Brain; RA Mei G., Yu W., Gibbs R.A.; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 163-364. RC TISSUE=Uterus; 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 [10] RP INTERACTION WITH FYB1. RX PubMed=10747096; DOI=10.1083/jcb.149.1.181; RA Krause M., Sechi A.S., Konradt M., Monner D., Gertler F.B., Wehland J.; RT "Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), RT Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 RT complex link T cell receptor (TCR) signaling to the actin cytoskeleton."; RL J. Cell Biol. 149:181-194(2000). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349 AND SER-369, AND 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-304; SER-306; RP SER-329; SER-331 AND SER-349, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-341 AND SER-354, AND RP IDENTIFICATION BY 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 [14] 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-331 AND SER-369, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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-349 AND SER-369, AND 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 [19] RP IDENTIFICATION (ISOFORM 5). RC TISSUE=Fetal brain; RA Lemonidis K.; RL Submitted (NOV-2016) to UniProtKB. RN [20] RP INTERACTION WITH SEMA6A. RX PubMed=10993894; DOI=10.1074/jbc.m006316200; RA Klostermann A., Lutz B., Gertler F., Behl C.; RT "The orthologous human and murine semaphorin 6A-1 proteins (SEMA6A- RT 1/Sema6A-1) bind to the enabled/vasodilator-stimulated phosphoprotein-like RT protein (EVL) via a novel carboxyl-terminal zyxin-like domain."; RL J. Biol. Chem. 275:39647-39653(2000). RN [21] RP INTERACTION WITH RAPH1. RX PubMed=15469845; DOI=10.1016/j.devcel.2004.07.024; RA Krause M., Leslie J.D., Stewart M., Lafuente E.M., Valderrama F., RA Jagannathan R., Strasser G.A., Rubinson D.A., Liu H., Way M., Yaffe M.B., RA Boussiotis V.A., Gertler F.B.; RT "Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of RT lamellipodial dynamics."; RL Dev. Cell 7:571-583(2004). RN [22] RP INTERACTION WITH ZYX. RX PubMed=18158903; DOI=10.1016/j.molcel.2007.10.033; RA Boeda B., Briggs D.C., Higgins T., Garvalov B.K., Fadden A.J., RA McDonald N.Q., Way M.; RT "Tes, a specific Mena interacting partner, breaks the rules for EVH1 RT binding."; RL Mol. Cell 28:1071-1082(2007). RN [23] RP INTERACTION WITH ZDHHC17. RX PubMed=28882895; DOI=10.1074/jbc.m117.799650; RA Lemonidis K., MacLeod R., Baillie G.S., Chamberlain L.H.; RT "Peptide array based screening reveals a large number of proteins RT interacting with the ankyrin repeat domain of the zDHHC17 S- RT acyltransferase."; RL J. Biol. Chem. 292:17190-17202(2017). RN [24] RP VARIANTS [LARGE SCALE ANALYSIS] LEU-188 AND LEU-247. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a CC range of processes dependent on cytoskeleton remodeling and cell CC polarity such as axon guidance and lamellipodial and filopodial CC dynamics in migrating cells. EVL enhances actin nucleation and CC polymerization. CC -!- SUBUNIT: Homotetramer (By similarity). Binds to the SH3 domains of CC ABL1, LYN and SRC. Also binds to profilin, with preference for isoform CC IIa of PFN2, and the WW domain of APBB1/FE65. Binds to SEMA6A. CC Interacts, via the Pro-rich region, with the C-terminal SH3 domain of CC DNMBP. Interacts with RAPH1. Binds, via the EVH1 domain, the Pro-rich CC domain of Listeria monocytogenes actA (By similarity). Binds, via the CC EVH1 domain, the Pro-rich domain of ZYX. Interacts with FYB1 CC (PubMed:10747096). Interacts with ZDHHC17 (PubMed:28882895). CC {ECO:0000250|UniProtKB:P70429, ECO:0000269|PubMed:10747096, CC ECO:0000269|PubMed:10993894, ECO:0000269|PubMed:15469845, CC ECO:0000269|PubMed:18158903, ECO:0000269|PubMed:28882895}. CC -!- INTERACTION: CC Q9UI08; Q9P2A4: ABI3; NbExp=4; IntAct=EBI-346653, EBI-742038; CC Q9UI08; Q13813: SPTAN1; NbExp=4; IntAct=EBI-346653, EBI-351450; CC Q9UI08; Q9C026: TRIM9; NbExp=3; IntAct=EBI-346653, EBI-720828; CC Q9UI08-2; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-6448852, EBI-742038; CC Q9UI08-2; P50570-2: DNM2; NbExp=3; IntAct=EBI-6448852, EBI-10968534; CC Q9UI08-2; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-6448852, EBI-11110431; CC Q9UI08-2; P42858: HTT; NbExp=20; IntAct=EBI-6448852, EBI-466029; CC Q9UI08-2; O14656-2: TOR1A; NbExp=3; IntAct=EBI-6448852, EBI-25847109; CC Q9UI08-2; Q9C026: TRIM9; NbExp=3; IntAct=EBI-6448852, EBI-720828; CC Q9UI08-2; P09936: UCHL1; NbExp=3; IntAct=EBI-6448852, EBI-714860; CC Q9UI08-2; O76024: WFS1; NbExp=3; IntAct=EBI-6448852, EBI-720609; CC Q9UI08-2; Q8IUH5: ZDHHC17; NbExp=2; IntAct=EBI-6448852, EBI-524753; CC Q9UI08-2; Q8N720: ZNF655; NbExp=3; IntAct=EBI-6448852, EBI-625509; CC Q9UI08-2; Q15942: ZYX; NbExp=5; IntAct=EBI-6448852, EBI-444225; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P70429}. Cytoplasm, cytoskeleton, stress fiber CC {ECO:0000250|UniProtKB:P70429}. Cell projection, lamellipodium CC {ECO:0000250|UniProtKB:P70429}. Note=Targeted to the leading edge of CC lamellipodia and the distal tip of stress fibers through interaction CC with a number of proteins. In activated T-cells, localizes to the F- CC actin collar and the distal tip of microspikes. CC {ECO:0000250|UniProtKB:P70429}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=2; Synonyms=EVL-I; CC IsoId=Q9UI08-1; Sequence=Displayed; CC Name=1; CC IsoId=Q9UI08-2; Sequence=VSP_004044; CC Name=3; CC IsoId=Q9UI08-3; Sequence=VSP_057322, VSP_057323; CC Name=4; CC IsoId=Q9UI08-4; Sequence=VSP_058779; CC Name=5; CC IsoId=Q9UI08-5; Sequence=VSP_004044, VSP_058778; CC -!- DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a CC thymosin-like domain required for G-actin binding. The KLKR motif CC within this block is essential for the G-actin binding and for actin CC polymerization. Block B is required for F-actin binding and subcellular CC location, and Block C for tetramerization. CC -!- PTM: Phosphorylated by PKA; phosphorylation abolishes binding to SH3 CC domains of ABL and SRC. {ECO:0000250}. CC -!- MISCELLANEOUS: Required to transform actin polymerization into active CC movement for the propulsive force of Listeria monocytogenes. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF052504; AAF21709.1; -; mRNA. DR EMBL; AF087843; AAP97156.1; -; mRNA. DR EMBL; AF112209; AAF17197.1; -; mRNA. DR EMBL; AK289720; BAF82409.1; -; mRNA. DR EMBL; AK295919; BAH12221.1; -; mRNA. DR EMBL; AL133368; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL133523; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL157912; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF456005; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF456007; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF456010; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471061; EAW81684.1; -; Genomic_DNA. DR EMBL; BC023997; AAH23997.1; -; mRNA. DR EMBL; BC032358; AAH32358.1; -; mRNA. DR EMBL; AF131766; AAD20040.1; -; mRNA. DR EMBL; AL133642; CAB63763.2; -; mRNA. DR CCDS; CCDS81851.1; -. [Q9UI08-1] DR CCDS; CCDS9955.1; -. [Q9UI08-2] DR RefSeq; NP_001317150.1; NM_001330221.1. [Q9UI08-1] DR RefSeq; NP_057421.1; NM_016337.2. [Q9UI08-2] DR AlphaFoldDB; Q9UI08; -. DR SMR; Q9UI08; -. DR BioGRID; 119556; 66. DR ELM; Q9UI08; -. DR IntAct; Q9UI08; 46. DR MINT; Q9UI08; -. DR STRING; 9606.ENSP00000376652; -. DR GlyGen; Q9UI08; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UI08; -. DR MetOSite; Q9UI08; -. DR PhosphoSitePlus; Q9UI08; -. DR BioMuta; EVL; -. DR DMDM; 25090276; -. DR EPD; Q9UI08; -. DR jPOST; Q9UI08; -. DR MassIVE; Q9UI08; -. DR MaxQB; Q9UI08; -. DR PaxDb; 9606-ENSP00000376652; -. DR PeptideAtlas; Q9UI08; -. DR ProteomicsDB; 6523; -. DR ProteomicsDB; 84445; -. [Q9UI08-1] DR ProteomicsDB; 84446; -. [Q9UI08-2] DR Pumba; Q9UI08; -. DR Antibodypedia; 14371; 172 antibodies from 33 providers. DR DNASU; 51466; -. DR Ensembl; ENST00000392920.8; ENSP00000376652.3; ENSG00000196405.13. [Q9UI08-2] DR Ensembl; ENST00000402714.6; ENSP00000384720.2; ENSG00000196405.13. [Q9UI08-1] DR Ensembl; ENST00000544450.6; ENSP00000437904.2; ENSG00000196405.13. [Q9UI08-3] DR GeneID; 51466; -. DR KEGG; hsa:51466; -. DR MANE-Select; ENST00000392920.8; ENSP00000376652.3; NM_016337.3; NP_057421.1. [Q9UI08-2] DR UCSC; uc001ygt.4; human. [Q9UI08-1] DR AGR; HGNC:20234; -. DR CTD; 51466; -. DR DisGeNET; 51466; -. DR GeneCards; EVL; -. DR HGNC; HGNC:20234; EVL. DR HPA; ENSG00000196405; Low tissue specificity. DR neXtProt; NX_Q9UI08; -. DR OpenTargets; ENSG00000196405; -. DR PharmGKB; PA134890866; -. DR VEuPathDB; HostDB:ENSG00000196405; -. DR eggNOG; KOG4590; Eukaryota. DR GeneTree; ENSGT00940000157826; -. DR InParanoid; Q9UI08; -. DR OMA; RTHFGIN; -. DR OrthoDB; 2884005at2759; -. DR PhylomeDB; Q9UI08; -. DR TreeFam; TF321411; -. DR PathwayCommons; Q9UI08; -. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-376176; Signaling by ROBO receptors. DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins. DR SignaLink; Q9UI08; -. DR SIGNOR; Q9UI08; -. DR BioGRID-ORCS; 51466; 12 hits in 1157 CRISPR screens. DR ChiTaRS; EVL; human. DR GeneWiki; Enah/Vasp-like; -. DR GenomeRNAi; 51466; -. DR Pharos; Q9UI08; Tbio. DR PRO; PR:Q9UI08; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q9UI08; Protein. DR Bgee; ENSG00000196405; Expressed in granulocyte and 193 other cell types or tissues. DR ExpressionAtlas; Q9UI08; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB. DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0001725; C:stress fiber; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005522; F:profilin binding; ISS:UniProtKB. DR GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB. DR GO; GO:0007015; P:actin filament organization; TAS:ProtInc. DR GO; GO:0008154; P:actin polymerization or depolymerization; ISS:UniProtKB. DR GO; GO:0009887; P:animal organ morphogenesis; NAS:UniProtKB. DR GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:UniProtKB. DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:UniProtKB. DR GO; GO:1900028; P:negative regulation of ruffle assembly; IMP:UniProtKB. DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB. DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central. DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:UniProtKB. DR GO; GO:0051289; P:protein homotetramerization; IEA:InterPro. DR CDD; cd01207; EVH1_Ena_VASP-like; 1. DR CDD; cd22185; WH2_hVASP-like; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR017354; VASP/EVL. DR InterPro; IPR038023; VASP_sf. DR InterPro; IPR014885; VASP_tetra. DR InterPro; IPR000697; WH1/EVH1_dom. DR PANTHER; PTHR11202:SF4; ENA_VASP-LIKE PROTEIN; 1. DR PANTHER; PTHR11202; SPROUTY-RELATED, EVH1 DOMAIN-CONTAINING PROTEIN FAMILY MEMBER; 1. DR Pfam; PF08776; VASP_tetra; 1. DR Pfam; PF00568; WH1; 1. DR PIRSF; PIRSF038010; Vasodilator_Phospo; 1. DR SMART; SM00461; WH1; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF118370; Vasodilator-stimulated phosphoprotein, VASP, tetramerisation domain; 1. DR PROSITE; PS50229; WH1; 1. DR Genevisible; Q9UI08; HS. PE 1: Evidence at protein level; KW Actin-binding; Alternative splicing; Cell projection; Cytoplasm; KW Cytoskeleton; Phosphoprotein; Reference proteome; SH3-binding. FT CHAIN 1..416 FT /note="Ena/VASP-like protein" FT /id="PRO_0000087104" FT DOMAIN 1..112 FT /note="WH1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410" FT REGION 114..133 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 141..369 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 222..413 FT /note="EVH2" FT REGION 222..242 FT /note="EVH2 block A" FT REGION 265..282 FT /note="EVH2 block B" FT REGION 342..362 FT /note="Required for interaction with ZDHHC17" FT /evidence="ECO:0000269|PubMed:28882895" FT REGION 379..413 FT /note="EVH2 block C" FT MOTIF 231..234 FT /note="KLKR" FT COMPBIAS 178..208 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 241..258 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 272..299 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 300..365 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 130 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O08719" FT MOD_RES 246 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 259 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O08719" FT MOD_RES 304 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 306 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 329 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 331 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 341 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 349 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:24275569" FT MOD_RES 354 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 369 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19367720, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 1 FT /note="M -> MAT (in isoform 1 and isoform 5)" FT /evidence="ECO:0000303|PubMed:10931946, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.19, FT ECO:0000303|Ref.2" FT /id="VSP_004044" FT VAR_SEQ 1 FT /note="M -> MFAFEEF (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057322" FT VAR_SEQ 342..362 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.19" FT /id="VSP_058778" FT VAR_SEQ 364..416 FT /note="MKPAGSVNDMALDAFDLDRMKQEILEEVVRELHKVKEEIIDAIRQELSGIST FT T -> YRTTLLLTCPPGFGAPLSPVP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057323" FT VAR_SEQ 368..397 FT /note="Missing (in isoform 4)" FT /id="VSP_058779" FT VARIANT 188 FT /note="P -> L (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs367737727)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036464" FT VARIANT 247 FT /note="P -> L (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036465" FT CONFLICT 201 FT /note="P -> S (in Ref. 3; AAF17197)" FT /evidence="ECO:0000305" FT CONFLICT 329 FT /note="S -> N (in Ref. 2; AAP97156)" FT /evidence="ECO:0000305" FT CONFLICT 364 FT /note="M -> Y (in Ref. 9; CAB63763)" FT /evidence="ECO:0000305" SQ SEQUENCE 416 AA; 44620 MW; AD5B67458755D659 CRC64; MSEQSICQAR ASVMVYDDTS KKWVPIKPGQ QGFSRINIYH NTASNTFRVV GVKLQDQQVV INYSIVKGLK YNQATPTFHQ WRDARQVYGL NFASKEEATT FSNAMLFALN IMNSQEGGPS SQRQVQNGPS PDEMDIQRRQ VMEQHQQQRQ ESLERRTSAT GPILPPGHPS SAASAPVSCS GPPPPPPPPV PPPPTGATPP PPPPLPAGGA QGSSHDESSM SGLAAAIAGA KLRRVQRPED ASGGSSPSGT SKSDANRASS GGGGGGLMEE MNKLLAKRRK AASQSDKPAE KKEDESQMED PSTSPSPGTR AASQPPNSSE AGRKPWERSN SVEKPVSSIL SRTPSVAKSP EAKSPLQSQP HSRMKPAGSV NDMALDAFDL DRMKQEILEE VVRELHKVKE EIIDAIRQEL SGISTT //