LASP1_HUMAN
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 03-AUG-2022, entry version 205.
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; 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; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-9088686, EBI-11976299;
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; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-9088686, EBI-12000762;
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; 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="http://atlasgeneticsoncology.org/Genes/Lasp1ID203.html";
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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; 208.
DR IntAct; Q14847; 167.
DR MINT; Q14847; -.
DR STRING; 9606.ENSP00000325240; -.
DR GlyGen; Q14847; 4 sites, 2 O-linked glycans (4 sites).
DR iPTMnet; Q14847; -.
DR MetOSite; Q14847; -.
DR PhosphoSitePlus; Q14847; -.
DR SwissPalm; Q14847; -.
DR BioMuta; LASP1; -.
DR DMDM; 3122342; -.
DR OGP; Q14847; -.
DR SWISS-2DPAGE; 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; Q14847; -.
DR PeptideAtlas; Q14847; -.
DR PRIDE; Q14847; -.
DR ProteomicsDB; 4149; -.
DR ProteomicsDB; 60206; -. [Q14847-1]
DR ProteomicsDB; 60207; -. [Q14847-2]
DR ABCD; Q14847; 6 sequenced antibodies.
DR Antibodypedia; 1894; 408 antibodies from 38 providers.
DR DNASU; 3927; -.
DR Ensembl; ENST00000318008.11; ENSP00000325240.6; ENSG00000002834.18. [Q14847-1]
DR Ensembl; ENST00000433206.6; ENSP00000401048.2; ENSG00000002834.18. [Q14847-3]
DR Ensembl; ENST00000435347.7; ENSP00000392853.3; ENSG00000002834.18. [Q14847-1]
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 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; QIEYVEY; -.
DR PhylomeDB; Q14847; -.
DR TreeFam; TF319104; -.
DR PathwayCommons; Q14847; -.
DR SignaLink; Q14847; -.
DR SIGNOR; Q14847; -.
DR BioGRID-ORCS; 3927; 13 hits in 1076 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 206 other tissues.
DR ExpressionAtlas; Q14847; baseline and differential.
DR Genevisible; Q14847; HS.
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:0015075; F:ion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; ISS:UniProtKB.
DR CDD; cd11934; SH3_Lasp1_C; 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 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; SSF50044; SSF50044; 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.
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
