ID LASP1_HUMAN Reviewed; 261 AA. AC Q14847; B4DGQ0; Q96ED2; Q96IG0; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 2. DT 27-MAR-2024, entry version 214. DE RecName: Full=LIM and SH3 domain protein 1; DE Short=LASP-1; DE AltName: Full=Metastatic lymph node gene 50 protein; DE Short=MLN 50; GN Name=LASP1; Synonyms=MLN50; 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). RC TISSUE=Mammary carcinoma; RX PubMed=7490069; DOI=10.1006/geno.1995.1163; RA Tomasetto C.L., Regnier C.H., Moog-Lutz C., Mattei M.-G., Chenard M.-P., RA Lidereau R., Basset P., Rio M.-C.; RT "Identification of four novel human genes amplified and overexpressed in RT breast carcinoma and localized to the q11-q21.3 region of chromosome 17."; RL Genomics 28:367-376(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; 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=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Liver, and 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 [5] RP PROTEIN SEQUENCE OF 1-7, AND ACETYLATION AT MET-1. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [6] RP DOMAINS. RX PubMed=7589475; DOI=10.1016/0014-5793(95)01040-l; RA Tomasetto C., Moog-Lutz C., Regnier C.H., Schreiber V., Basset P., RA Rio M.-C.; RT "Lasp-1 (MLN 50) defines a new LIM protein subfamily characterized by the RT association of LIM and SH3 domains."; RL FEBS Lett. 373:245-249(1995). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68; THR-104 AND SER-146, 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 [10] RP INTERACTION WITH KBTBD10. RX PubMed=19726686; DOI=10.1074/jbc.m109.023259; RA Gray C.H., McGarry L.C., Spence H.J., Riboldi-Tunnicliffe A., Ozanne B.W.; RT "Novel beta-propeller of the BTB-Kelch protein Krp1 provides a binding site RT for Lasp-1 that is necessary for pseudopodial extension."; RL J. Biol. Chem. 284:30498-30507(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68 AND THR-104, 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 [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68; THR-104; SER-118 AND RP SER-146, AND 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 [14] 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68; SER-99; THR-104; SER-134 RP AND SER-146, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, 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 [17] RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-75, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [18] 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). CC -!- FUNCTION: Plays an important role in the regulation of dynamic actin- CC based, cytoskeletal activities. Agonist-dependent changes in LASP1 CC phosphorylation may also serve to regulate actin-associated ion CC transport activities, not only in the parietal cell but also in certain CC other F-actin-rich secretory epithelial cell types (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Interacts with F-actin (By similarity). Interacts with ANKRD54 CC (By similarity). Interacts with KBTBD10. {ECO:0000250, CC ECO:0000269|PubMed:19726686}. CC -!- INTERACTION: CC Q14847; D3DTR7: ARHGEF15; NbExp=3; IntAct=EBI-742828, EBI-10176602; CC Q14847; P51116: FXR2; NbExp=3; IntAct=EBI-742828, EBI-740459; CC Q14847; Q08379: GOLGA2; NbExp=3; IntAct=EBI-742828, EBI-618309; CC Q14847; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-742828, EBI-10172511; CC Q14847; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-742828, EBI-741037; CC Q14847; Q99750: MDFI; NbExp=3; IntAct=EBI-742828, EBI-724076; CC Q14847; P25788: PSMA3; NbExp=3; IntAct=EBI-742828, EBI-348380; CC Q14847; Q04864: REL; NbExp=3; IntAct=EBI-742828, EBI-307352; CC Q14847; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-742828, EBI-372094; CC Q14847; Q9UH03: SEPTIN3; NbExp=3; IntAct=EBI-742828, EBI-727037; CC Q14847; Q9NP31: SH2D2A; NbExp=2; IntAct=EBI-742828, EBI-490630; CC Q14847; O43597: SPRY2; NbExp=3; IntAct=EBI-742828, EBI-742487; CC Q14847; P15884: TCF4; NbExp=3; IntAct=EBI-742828, EBI-533224; CC Q14847; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-742828, EBI-741515; CC Q14847; Q9UDY2: TJP2; NbExp=9; IntAct=EBI-742828, EBI-1042602; CC Q14847; P14373: TRIM27; NbExp=3; IntAct=EBI-742828, EBI-719493; CC Q14847; Q15645: TRIP13; NbExp=7; IntAct=EBI-742828, EBI-358993; CC Q14847; Q96C00: ZBTB9; NbExp=4; IntAct=EBI-742828, EBI-395708; CC Q14847; Q96GY0: ZC2HC1A; NbExp=3; IntAct=EBI-742828, EBI-5458880; CC Q14847-2; Q5BKX5-3: ACTMAP; NbExp=3; IntAct=EBI-9088686, EBI-11976299; CC Q14847-2; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-9088686, EBI-11954519; CC Q14847-2; Q5VV41: ARHGEF16; NbExp=3; IntAct=EBI-9088686, EBI-1057448; CC Q14847-2; Q03989: ARID5A; NbExp=3; IntAct=EBI-9088686, EBI-948603; CC Q14847-2; Q86V38: ATN1; NbExp=3; IntAct=EBI-9088686, EBI-11954292; CC Q14847-2; P54253: ATXN1; NbExp=9; IntAct=EBI-9088686, EBI-930964; CC Q14847-2; Q9Y5Z0: BACE2; NbExp=3; IntAct=EBI-9088686, EBI-11282723; CC Q14847-2; O95429: BAG4; NbExp=3; IntAct=EBI-9088686, EBI-2949658; CC Q14847-2; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-9088686, EBI-742750; CC Q14847-2; O14503: BHLHE40; NbExp=3; IntAct=EBI-9088686, EBI-711810; CC Q14847-2; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-9088686, EBI-11983447; CC Q14847-2; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-9088686, EBI-725606; CC Q14847-2; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-9088686, EBI-1383687; CC Q14847-2; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-9088686, EBI-744545; CC Q14847-2; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-9088686, EBI-12261896; CC Q14847-2; P28329-3: CHAT; NbExp=3; IntAct=EBI-9088686, EBI-25837549; CC Q14847-2; Q8IWX8: CHERP; NbExp=3; IntAct=EBI-9088686, EBI-2555370; CC Q14847-2; P02489: CRYAA; NbExp=3; IntAct=EBI-9088686, EBI-6875961; CC Q14847-2; P05813: CRYBA1; NbExp=3; IntAct=EBI-9088686, EBI-7043337; CC Q14847-2; P53672: CRYBA2; NbExp=4; IntAct=EBI-9088686, EBI-750444; CC Q14847-2; Q9H0L4: CSTF2T; NbExp=3; IntAct=EBI-9088686, EBI-747012; CC Q14847-2; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-9088686, EBI-11962928; CC Q14847-2; A8MQ03: CYSRT1; NbExp=8; IntAct=EBI-9088686, EBI-3867333; CC Q14847-2; Q15038: DAZAP2; NbExp=5; IntAct=EBI-9088686, EBI-724310; CC Q14847-2; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-9088686, EBI-9679045; CC Q14847-2; Q6PKX4: DOK6; NbExp=3; IntAct=EBI-9088686, EBI-2880244; CC Q14847-2; Q86UW9: DTX2; NbExp=3; IntAct=EBI-9088686, EBI-740376; CC Q14847-2; Q03828: EVX2; NbExp=3; IntAct=EBI-9088686, EBI-17280301; CC Q14847-2; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-9088686, EBI-11978259; CC Q14847-2; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-9088686, EBI-12193763; CC Q14847-2; Q96EF6: FBXO17; NbExp=5; IntAct=EBI-9088686, EBI-2510157; CC Q14847-2; P22607: FGFR3; NbExp=3; IntAct=EBI-9088686, EBI-348399; CC Q14847-2; O75593: FOXH1; NbExp=3; IntAct=EBI-9088686, EBI-1759806; CC Q14847-2; O95995: GAS8; NbExp=3; IntAct=EBI-9088686, EBI-1052570; CC Q14847-2; O75603: GCM2; NbExp=3; IntAct=EBI-9088686, EBI-10188645; CC Q14847-2; P14136: GFAP; NbExp=3; IntAct=EBI-9088686, EBI-744302; CC Q14847-2; Q14957: GRIN2C; NbExp=3; IntAct=EBI-9088686, EBI-8285963; CC Q14847-2; P28799: GRN; NbExp=3; IntAct=EBI-9088686, EBI-747754; CC Q14847-2; P06396: GSN; NbExp=3; IntAct=EBI-9088686, EBI-351506; CC Q14847-2; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-9088686, EBI-11978177; CC Q14847-2; O14964: HGS; NbExp=3; IntAct=EBI-9088686, EBI-740220; CC Q14847-2; P52597: HNRNPF; NbExp=3; IntAct=EBI-9088686, EBI-352986; CC Q14847-2; P49639: HOXA1; NbExp=3; IntAct=EBI-9088686, EBI-740785; CC Q14847-2; P01112: HRAS; NbExp=3; IntAct=EBI-9088686, EBI-350145; CC Q14847-2; P04792: HSPB1; NbExp=3; IntAct=EBI-9088686, EBI-352682; CC Q14847-2; P10809: HSPD1; NbExp=3; IntAct=EBI-9088686, EBI-352528; CC Q14847-2; Q5TA45: INTS11; NbExp=3; IntAct=EBI-9088686, EBI-748258; CC Q14847-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-9088686, EBI-10975473; CC Q14847-2; Q92876: KLK6; NbExp=3; IntAct=EBI-9088686, EBI-2432309; CC Q14847-2; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-9088686, EBI-10171774; CC Q14847-2; P60329: KRTAP12-4; NbExp=3; IntAct=EBI-9088686, EBI-10176396; CC Q14847-2; Q7Z4W3: KRTAP19-3; NbExp=3; IntAct=EBI-9088686, EBI-12020132; CC Q14847-2; Q3LI73: KRTAP19-4; NbExp=3; IntAct=EBI-9088686, EBI-12958461; CC Q14847-2; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-9088686, EBI-12805508; CC Q14847-2; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-9088686, EBI-3957672; CC Q14847-2; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-9088686, EBI-751260; CC Q14847-2; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-9088686, EBI-3957694; CC Q14847-2; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-9088686, EBI-11962084; CC Q14847-2; Q96PV6: LENG8; NbExp=3; IntAct=EBI-9088686, EBI-739546; CC Q14847-2; P61968: LMO4; NbExp=3; IntAct=EBI-9088686, EBI-2798728; CC Q14847-2; Q99750: MDFI; NbExp=3; IntAct=EBI-9088686, EBI-724076; CC Q14847-2; Q71SY5: MED25; NbExp=3; IntAct=EBI-9088686, EBI-394558; CC Q14847-2; Q13064: MKRN3; NbExp=3; IntAct=EBI-9088686, EBI-2340269; CC Q14847-2; P07196: NEFL; NbExp=3; IntAct=EBI-9088686, EBI-475646; CC Q14847-2; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-9088686, EBI-12025760; CC Q14847-2; P61970: NUTF2; NbExp=3; IntAct=EBI-9088686, EBI-591778; CC Q14847-2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-9088686, EBI-748974; CC Q14847-2; P32242: OTX1; NbExp=3; IntAct=EBI-9088686, EBI-740446; CC Q14847-2; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-9088686, EBI-12813389; CC Q14847-2; Q13153: PAK1; NbExp=3; IntAct=EBI-9088686, EBI-1307; CC Q14847-2; P16284: PECAM1; NbExp=3; IntAct=EBI-9088686, EBI-716404; CC Q14847-2; P78337: PITX1; NbExp=5; IntAct=EBI-9088686, EBI-748265; CC Q14847-2; P28340: POLD1; NbExp=3; IntAct=EBI-9088686, EBI-716569; CC Q14847-2; P28069: POU1F1; NbExp=5; IntAct=EBI-9088686, EBI-8673859; CC Q14847-2; P86480: PRR20D; NbExp=3; IntAct=EBI-9088686, EBI-12754095; CC Q14847-2; P0CG20: PRR35; NbExp=3; IntAct=EBI-9088686, EBI-11986293; CC Q14847-2; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-9088686, EBI-2798044; CC Q14847-2; Q9NWB1-5: RBFOX1; NbExp=3; IntAct=EBI-9088686, EBI-12123390; CC Q14847-2; Q93062-3: RBPMS; NbExp=8; IntAct=EBI-9088686, EBI-740343; CC Q14847-2; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-9088686, EBI-11987469; CC Q14847-2; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-9088686, EBI-372094; CC Q14847-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-9088686, EBI-396669; CC Q14847-2; Q9H0F5: RNF38; NbExp=3; IntAct=EBI-9088686, EBI-2341200; CC Q14847-2; Q7Z5V6-2: SAXO4; NbExp=3; IntAct=EBI-9088686, EBI-12000762; CC Q14847-2; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-9088686, EBI-11959123; CC Q14847-2; Q9BXF9: TEKT3; NbExp=3; IntAct=EBI-9088686, EBI-8644516; CC Q14847-2; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-9088686, EBI-750487; CC Q14847-2; Q96M29: TEKT5; NbExp=3; IntAct=EBI-9088686, EBI-10239812; CC Q14847-2; Q92734: TFG; NbExp=3; IntAct=EBI-9088686, EBI-357061; CC Q14847-2; O43711: TLX3; NbExp=5; IntAct=EBI-9088686, EBI-3939165; CC Q14847-2; Q63HR2: TNS2; NbExp=3; IntAct=EBI-9088686, EBI-949753; CC Q14847-2; Q15645: TRIP13; NbExp=3; IntAct=EBI-9088686, EBI-358993; CC Q14847-2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-9088686, EBI-947187; CC Q14847-2; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-9088686, EBI-12068150; CC Q14847-2; Q08AM6: VAC14; NbExp=3; IntAct=EBI-9088686, EBI-2107455; CC Q14847-2; Q14119: VEZF1; NbExp=3; IntAct=EBI-9088686, EBI-11980193; CC Q14847-2; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-9088686, EBI-11957216; CC Q14847-2; P08670: VIM; NbExp=3; IntAct=EBI-9088686, EBI-353844; CC Q14847-2; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-9088686, EBI-2559305; CC Q14847-2; O76024: WFS1; NbExp=3; IntAct=EBI-9088686, EBI-720609; CC Q14847-2; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-9088686, EBI-12040603; CC Q14847-2; P07947: YES1; NbExp=3; IntAct=EBI-9088686, EBI-515331; CC Q14847-2; Q9BYJ9: YTHDF1; NbExp=3; IntAct=EBI-9088686, EBI-1051237; CC Q14847-2; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-9088686, EBI-742550; CC Q14847-2; Q8IUH5: ZDHHC17; NbExp=3; IntAct=EBI-9088686, EBI-524753; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, CC cytoskeleton {ECO:0000250}. Note=Associated with the F-actin rich CC cortical cytoskeleton. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q14847-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14847-2; Sequence=VSP_016554; CC Name=3; CC IsoId=Q14847-3; Sequence=VSP_054611; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/203/Lasp1"; 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; X82456; CAA57833.1; -; mRNA. DR EMBL; AK294704; BAG57861.1; -; mRNA. DR EMBL; AC006441; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC110749; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC007560; AAH07560.1; -; mRNA. DR EMBL; BC012460; AAH12460.1; -; mRNA. DR CCDS; CCDS11331.1; -. [Q14847-1] DR CCDS; CCDS62164.1; -. [Q14847-3] DR PIR; S68234; S68234. DR RefSeq; NP_001258537.1; NM_001271608.1. [Q14847-3] DR RefSeq; NP_006139.1; NM_006148.3. [Q14847-1] DR PDB; 3I35; X-ray; 1.40 A; A=202-261. DR PDBsum; 3I35; -. DR AlphaFoldDB; Q14847; -. DR SMR; Q14847; -. DR BioGRID; 110120; 234. DR IntAct; Q14847; 170. DR MINT; Q14847; -. DR STRING; 9606.ENSP00000325240; -. DR GlyCosmos; Q14847; 4 sites, 2 glycans. DR GlyGen; Q14847; 6 sites, 2 O-linked glycans (6 sites). DR iPTMnet; Q14847; -. DR MetOSite; Q14847; -. DR PhosphoSitePlus; Q14847; -. DR SwissPalm; Q14847; -. DR BioMuta; LASP1; -. DR DMDM; 3122342; -. DR OGP; Q14847; -. DR CPTAC; CPTAC-86; -. DR CPTAC; CPTAC-87; -. DR CPTAC; CPTAC-928; -. DR EPD; Q14847; -. DR jPOST; Q14847; -. DR MassIVE; Q14847; -. DR MaxQB; Q14847; -. DR PaxDb; 9606-ENSP00000325240; -. DR PeptideAtlas; Q14847; -. DR ProteomicsDB; 4149; -. DR ProteomicsDB; 60206; -. [Q14847-1] DR ProteomicsDB; 60207; -. [Q14847-2] DR Pumba; Q14847; -. DR ABCD; Q14847; 6 sequenced antibodies. DR Antibodypedia; 1894; 444 antibodies from 38 providers. DR DNASU; 3927; -. DR Ensembl; ENST00000318008.11; ENSP00000325240.6; ENSG00000002834.19. [Q14847-1] DR Ensembl; ENST00000433206.6; ENSP00000401048.2; ENSG00000002834.19. [Q14847-3] DR GeneID; 3927; -. DR KEGG; hsa:3927; -. DR MANE-Select; ENST00000318008.11; ENSP00000325240.6; NM_006148.4; NP_006139.1. DR UCSC; uc002hra.3; human. [Q14847-1] DR AGR; HGNC:6513; -. DR CTD; 3927; -. DR DisGeNET; 3927; -. DR GeneCards; LASP1; -. DR HGNC; HGNC:6513; LASP1. DR HPA; ENSG00000002834; Low tissue specificity. DR MIM; 602920; gene. DR neXtProt; NX_Q14847; -. DR OpenTargets; ENSG00000002834; -. DR PharmGKB; PA30298; -. DR VEuPathDB; HostDB:ENSG00000002834; -. DR eggNOG; KOG1702; Eukaryota. DR GeneTree; ENSGT00940000154775; -. DR HOGENOM; CLU_026811_0_1_1; -. DR InParanoid; Q14847; -. DR OMA; KSRMGTP; -. DR OrthoDB; 4243at2759; -. DR PhylomeDB; Q14847; -. DR TreeFam; TF319104; -. DR PathwayCommons; Q14847; -. DR SignaLink; Q14847; -. DR SIGNOR; Q14847; -. DR BioGRID-ORCS; 3927; 16 hits in 1156 CRISPR screens. DR ChiTaRS; LASP1; human. DR EvolutionaryTrace; Q14847; -. DR GeneWiki; LASP1; -. DR GenomeRNAi; 3927; -. DR Pharos; Q14847; Tbio. DR PRO; PR:Q14847; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q14847; Protein. DR Bgee; ENSG00000002834; Expressed in lower lobe of lung and 208 other cell types or tissues. DR ExpressionAtlas; Q14847; baseline and differential. DR GO; GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015075; F:monoatomic ion transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0006811; P:monoatomic ion transport; ISS:UniProtKB. DR CDD; cd09447; LIM_LASP; 1. DR CDD; cd11934; SH3_Lasp1_C; 1. DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR035630; Lasp1_SH3. DR InterPro; IPR000900; Nebulin_repeat. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR001781; Znf_LIM. DR PANTHER; PTHR46218; LASP; 1. DR PANTHER; PTHR46218:SF2; LIM AND SH3 DOMAIN PROTEIN 1; 1. DR Pfam; PF00412; LIM; 1. DR Pfam; PF00880; Nebulin; 2. DR Pfam; PF14604; SH3_9; 1. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00132; LIM; 1. DR SMART; SM00227; NEBU; 2. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS00478; LIM_DOMAIN_1; 1. DR PROSITE; PS50023; LIM_DOMAIN_2; 1. DR PROSITE; PS51216; NEBULIN; 2. DR PROSITE; PS50002; SH3; 1. DR SWISS-2DPAGE; Q14847; -. DR Genevisible; Q14847; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; Ion transport; LIM domain; KW Metal-binding; Methylation; Phosphoprotein; Reference proteome; Repeat; KW SH3 domain; Transport; Zinc. FT CHAIN 1..261 FT /note="LIM and SH3 domain protein 1" FT /id="PRO_0000075761" FT DOMAIN 5..56 FT /note="LIM zinc-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT REPEAT 61..95 FT /note="Nebulin 1" FT REPEAT 97..131 FT /note="Nebulin 2" FT DOMAIN 202..261 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 111..186 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 116..151 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 152..182 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:12665801" FT MOD_RES 42 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 68 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 75 FT /note="N6-methyllysine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 99 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 104 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17924679, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 112 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q61792" FT MOD_RES 118 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 134 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 146 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..83 FT /note="MNPNCARCGKIVYPTEKVNCLDKFWHKACFHCETCKMTLNMKNYKGYEKKPY FT CNAHYPKQSFTMVADTPENLRLKQQSELQSQ -> MLPLRDLQDDTEHEELQGLREEAL FT LQR (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054611" FT VAR_SEQ 201..261 FT /note="GGGGKRYRAVYDYSAADEDEVSFQDGDTIVNVQQIDDGWMYGTVERTGDTGM FT LPANYVEAI -> ICLQHIPRHRIRPGRDPSILQCLCFLKPATACDSYPSSSFFCQLKP FT SSATSAGSLLWQASPLIDFLVFSLDGTGMGLSGGGRGPWGRAGMGDLLACGPHLPLCSL FT PSHPPAQLLTYPHIPGLG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_016554" FT CONFLICT 79 FT /note="E -> R (in Ref. 4; AAH12460)" FT /evidence="ECO:0000305" FT CONFLICT 210 FT /note="V -> A (in Ref. 4; AAH12460)" FT /evidence="ECO:0000305" FT CONFLICT 220 FT /note="E -> A (in Ref. 4; AAH12460)" FT /evidence="ECO:0000305" FT STRAND 207..211 FT /evidence="ECO:0007829|PDB:3I35" FT STRAND 228..236 FT /evidence="ECO:0007829|PDB:3I35" FT STRAND 239..244 FT /evidence="ECO:0007829|PDB:3I35" FT TURN 245..248 FT /evidence="ECO:0007829|PDB:3I35" FT STRAND 249..254 FT /evidence="ECO:0007829|PDB:3I35" FT HELIX 255..257 FT /evidence="ECO:0007829|PDB:3I35" FT STRAND 258..260 FT /evidence="ECO:0007829|PDB:3I35" SQ SEQUENCE 261 AA; 29717 MW; 3B89B988605B3639 CRC64; MNPNCARCGK IVYPTEKVNC LDKFWHKACF HCETCKMTLN MKNYKGYEKK PYCNAHYPKQ SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGKGFSV VADTPELQRI KKTQDQISNI KYHEEFEKSR MGPSGGEGME PERRDSQDGS SYRRPLEQQQ PHHIPTSAPV YQQPQQQPVA QSYGGYKEPA APVSIQRSAP GGGGKRYRAV YDYSAADEDE VSFQDGDTIV NVQQIDDGWM YGTVERTGDT GMLPANYVEA I //