ID DBNL_HUMAN Reviewed; 430 AA.
AC Q9UJU6; A4D2I9; B4DDP6; B4DEM2; C9J7P1; P84070; Q6IAI8; Q96F30; Q96K74;
AC Q9HBN8; Q9NR72;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 202.
DE RecName: Full=Drebrin-like protein;
DE AltName: Full=Cervical SH3P7;
DE AltName: Full=Cervical mucin-associated protein;
DE AltName: Full=Drebrin-F;
DE AltName: Full=HPK1-interacting protein of 55 kDa;
DE Short=HIP-55;
DE AltName: Full=SH3 domain-containing protein 7;
GN Name=DBNL; Synonyms=CMAP, SH3P7; ORFNames=PP5423;
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), AND INTERACTION WITH MAP4K1.
RX PubMed=10567356; DOI=10.1074/jbc.274.48.33945;
RA Ensenat D., Yao Z., Wang X.-S., Kori R., Zhou G., Lee S.C., Tan T.-H.;
RT "A novel src homology 3 domain-containing adaptor protein, HIP-55, that
RT interacts with hematopoietic progenitor kinase 1.";
RL J. Biol. Chem. 274:33945-33950(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhang W., Yuan Z., Wan T., He L., Cao X.;
RT "Molecular cloning of cDNA encoding drebrin F.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
RA Toribara N.W., Ho S.B., Wang R., Arthur M., Shekels L.L., Spurr-Michaud S.,
RA Keutmann H.T., Hill J.A., Gipson I.K.;
RT "Expression cloning of a novel cervical mucin-associated protein (CMAP).";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 5 AND 6).
RC TISSUE=Cerebellum, and Mammary gland;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [9]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Eye;
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 [11]
RP IDENTIFICATION.
RX PubMed=9891087; DOI=10.1128/mcb.19.2.1539;
RA Larbolette O., Wollscheid B., Schweikert J., Nielsen P.J., Wienands J.;
RT "SH3P7 is a cytoskeleton adapter protein and is coupled to signal
RT transduction from lymphocyte antigen receptors.";
RL Mol. Cell. Biol. 19:1539-1546(1999).
RN [12]
RP DEGRADATION BY CASPASES.
RX PubMed=11689006; DOI=10.1006/bbrc.2001.5862;
RA Chen Y.-R., Kori R., John B., Tan T.-H.;
RT "Caspase-mediated cleavage of actin-binding and SH3-domain-containing
RT proteins cortactin, HS1, and HIP-55 during apoptosis.";
RL Biochem. Biophys. Res. Commun. 288:981-989(2001).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14729663; DOI=10.1074/jbc.m312659200;
RA Le Bras S., Foucault I., Foussat A., Brignone C., Acuto O., Deckert M.;
RT "Recruitment of the actin-binding protein HIP-55 to the immunological
RT synapse regulates T cell receptor signaling and endocytosis.";
RL J. Biol. Chem. 279:15550-15560(2004).
RN [15]
RP INTERACTION WITH PRAM1, CLEAVAGE BY CASPASES, AND MUTAGENESIS OF ASP-361.
RX PubMed=15637062; DOI=10.1074/jbc.m413564200;
RA Denis F.M., Benecke A., Di Gioia Y., Touw I.P., Cayre Y.E., Lutz P.G.;
RT "PRAM-1 potentiates arsenic trioxide-induced JNK activation.";
RL J. Biol. Chem. 280:9043-9048(2005).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-232 (ISOFORMS 2 AND 3), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-137 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-183 (ISOFORM 6), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269, 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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269, 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 [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-176 AND LYS-288, AND
RP IDENTIFICATION BY MASS 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 (ISOFORMS 2 AND 3),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 (ISOFORM 4),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 (ISOFORM 6), 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 [25]
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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION BY
RP 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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-232; SER-269;
RP SER-272; SER-275; SER-283 AND THR-291, AND IDENTIFICATION BY MASS
RP 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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 AND SER-275, 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 [29]
RP STRUCTURE BY NMR OF 1-133.
RX PubMed=19768801; DOI=10.1002/pro.248;
RA Goroncy A.K., Koshiba S., Tochio N., Tomizawa T., Sato M., Inoue M.,
RA Watanabe S., Hayashizaki Y., Tanaka A., Kigawa T., Yokoyama S.;
RT "NMR solution structures of actin depolymerizing factor homology domains.";
RL Protein Sci. 18:2384-2392(2009).
CC -!- FUNCTION: Adapter protein that binds F-actin and DNM1, and thereby
CC plays a role in receptor-mediated endocytosis. Plays a role in the
CC reorganization of the actin cytoskeleton, formation of cell
CC projections, such as neurites, in neuron morphogenesis and synapse
CC formation via its interaction with WASL and COBL. Does not bind G-actin
CC and promote actin polymerization by itself. Required for the formation
CC of organized podosome rosettes (By similarity). May act as a common
CC effector of antigen receptor-signaling pathways in leukocytes. Acts as
CC a key component of the immunological synapse that regulates T-cell
CC activation by bridging TCRs and the actin cytoskeleton to gene
CC activation and endocytic processes. {ECO:0000250,
CC ECO:0000269|PubMed:14729663}.
CC -!- SUBUNIT: Interacts with SHANK2, SHANK3 and SYN1. Interacts with FGD1
CC and DNM1. Interacts with ANKRD54. Interacts with COBL. Interacts with
CC WASL and WIPF1 (By similarity). Interacts with MAP4K1 and PRAM1.
CC {ECO:0000250, ECO:0000269|PubMed:10567356,
CC ECO:0000269|PubMed:15637062}.
CC -!- INTERACTION:
CC Q9UJU6; Q96AP0: ACD; NbExp=2; IntAct=EBI-751783, EBI-717666;
CC Q9UJU6; P46379-2: BAG6; NbExp=3; IntAct=EBI-751783, EBI-10988864;
CC Q9UJU6; O14645: DNALI1; NbExp=3; IntAct=EBI-751783, EBI-395638;
CC Q9UJU6; P22607: FGFR3; NbExp=3; IntAct=EBI-751783, EBI-348399;
CC Q9UJU6; Q14957: GRIN2C; NbExp=3; IntAct=EBI-751783, EBI-8285963;
CC Q9UJU6; P06396: GSN; NbExp=3; IntAct=EBI-751783, EBI-351506;
CC Q9UJU6; P42858: HTT; NbExp=3; IntAct=EBI-751783, EBI-466029;
CC Q9UJU6; O14901: KLF11; NbExp=3; IntAct=EBI-751783, EBI-948266;
CC Q9UJU6; Q9H788: SH2D4A; NbExp=6; IntAct=EBI-751783, EBI-747035;
CC Q9UJU6; Q9H788-2: SH2D4A; NbExp=3; IntAct=EBI-751783, EBI-10308083;
CC Q9UJU6; P78314: SH3BP2; NbExp=7; IntAct=EBI-751783, EBI-727062;
CC Q9UJU6; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-751783, EBI-741480;
CC Q9UJU6-2; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-12192777, EBI-747035;
CC Q9UJU6-2; P78314-3: SH3BP2; NbExp=3; IntAct=EBI-12192777, EBI-12304031;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q62418}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q62418}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:Q62418}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q62418}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9JHL4}. Synapse {ECO:0000250|UniProtKB:Q62418}.
CC Perikaryon {ECO:0000250|UniProtKB:Q62418}. Cell projection, neuron
CC projection {ECO:0000250|UniProtKB:Q62418}. Cell membrane
CC {ECO:0000269|PubMed:14729663}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q62418}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q62418}. Cytoplasmic vesicle, clathrin-coated
CC vesicle membrane {ECO:0000250|UniProtKB:Q62418}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q62418}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q62418}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q62418}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q62418}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q62418}. Cell projection, podosome
CC {ECO:0000250|UniProtKB:Q62418}. Early endosome
CC {ECO:0000269|PubMed:14729663}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9JHL4}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q9JHL4}. Note=Associates with lamellipodial
CC actin and membrane ruffles. Colocalizes with actin and cortactin at
CC podosome dots and podosome rosettes. {ECO:0000250|UniProtKB:Q62418,
CC ECO:0000250|UniProtKB:Q9JHL4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9UJU6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJU6-2; Sequence=VSP_011398;
CC Name=3;
CC IsoId=Q9UJU6-3; Sequence=VSP_011398, VSP_011399;
CC Name=4;
CC IsoId=Q9UJU6-4; Sequence=VSP_054779, VSP_011398;
CC Name=5;
CC IsoId=Q9UJU6-5; Sequence=VSP_054780;
CC Name=6;
CC IsoId=Q9UJU6-6; Sequence=VSP_057346, VSP_011398;
CC -!- DOMAIN: The SH3 domain mediates interaction with SHANK2, SHANK3 and
CC PRAM1.
CC -!- PTM: Degraded by caspases during apoptosis.
CC -!- SIMILARITY: Belongs to the ABP1 family. {ECO:0000305}.
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DR EMBL; AF197060; AAF13701.1; -; mRNA.
DR EMBL; AF077353; AAF80228.1; -; mRNA.
DR EMBL; AF250287; AAF81273.1; -; mRNA.
DR EMBL; AF151364; AAG13120.1; -; mRNA.
DR EMBL; AF218020; AAG17262.2; -; mRNA.
DR EMBL; AK027367; BAB55065.1; -; mRNA.
DR EMBL; AK293279; BAG56807.1; -; mRNA.
DR EMBL; AK293698; BAG57133.1; -; mRNA.
DR EMBL; CR457167; CAG33448.1; -; mRNA.
DR EMBL; AC017116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236960; EAL23770.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61132.1; -; Genomic_DNA.
DR EMBL; BC011677; AAH11677.1; -; mRNA.
DR EMBL; BC031687; AAH31687.1; -; mRNA.
DR CCDS; CCDS34622.1; -. [Q9UJU6-2]
DR CCDS; CCDS34623.1; -. [Q9UJU6-1]
DR CCDS; CCDS47579.1; -. [Q9UJU6-3]
DR CCDS; CCDS64633.1; -. [Q9UJU6-4]
DR CCDS; CCDS64634.1; -. [Q9UJU6-5]
DR RefSeq; NP_001014436.1; NM_001014436.2. [Q9UJU6-1]
DR RefSeq; NP_001116428.1; NM_001122956.1. [Q9UJU6-3]
DR RefSeq; NP_001271242.1; NM_001284313.1. [Q9UJU6-5]
DR RefSeq; NP_001271244.1; NM_001284315.1. [Q9UJU6-4]
DR RefSeq; NP_054782.2; NM_014063.6. [Q9UJU6-2]
DR PDB; 1X67; NMR; -; A=1-133.
DR PDBsum; 1X67; -.
DR AlphaFoldDB; Q9UJU6; -.
DR SMR; Q9UJU6; -.
DR BioGRID; 118809; 178.
DR IntAct; Q9UJU6; 37.
DR MINT; Q9UJU6; -.
DR STRING; 9606.ENSP00000417653; -.
DR GlyGen; Q9UJU6; 7 sites, 1 O-linked glycan (7 sites).
DR iPTMnet; Q9UJU6; -.
DR MetOSite; Q9UJU6; -.
DR PhosphoSitePlus; Q9UJU6; -.
DR SwissPalm; Q9UJU6; -.
DR BioMuta; DBNL; -.
DR DMDM; 51316115; -.
DR OGP; Q9UJU6; -.
DR EPD; Q9UJU6; -.
DR jPOST; Q9UJU6; -.
DR MassIVE; Q9UJU6; -.
DR MaxQB; Q9UJU6; -.
DR PaxDb; 9606-ENSP00000417653; -.
DR PeptideAtlas; Q9UJU6; -.
DR ProteomicsDB; 3878; -.
DR ProteomicsDB; 3970; -.
DR ProteomicsDB; 84659; -. [Q9UJU6-1]
DR ProteomicsDB; 84660; -. [Q9UJU6-2]
DR ProteomicsDB; 84661; -. [Q9UJU6-3]
DR ProteomicsDB; 8938; -.
DR Pumba; Q9UJU6; -.
DR TopDownProteomics; Q9UJU6-2; -. [Q9UJU6-2]
DR ABCD; Q9UJU6; 5 sequenced antibodies.
DR Antibodypedia; 13203; 295 antibodies from 35 providers.
DR DNASU; 28988; -.
DR Ensembl; ENST00000440166.5; ENSP00000415173.1; ENSG00000136279.21. [Q9UJU6-5]
DR Ensembl; ENST00000448521.6; ENSP00000411701.1; ENSG00000136279.21. [Q9UJU6-1]
DR Ensembl; ENST00000456905.5; ENSP00000416421.1; ENSG00000136279.21. [Q9UJU6-6]
DR Ensembl; ENST00000468694.5; ENSP00000417653.1; ENSG00000136279.21. [Q9UJU6-3]
DR Ensembl; ENST00000490734.6; ENSP00000417749.2; ENSG00000136279.21. [Q9UJU6-4]
DR Ensembl; ENST00000494774.5; ENSP00000419992.1; ENSG00000136279.21. [Q9UJU6-2]
DR GeneID; 28988; -.
DR KEGG; hsa:28988; -.
DR MANE-Select; ENST00000448521.6; ENSP00000411701.1; NM_001014436.3; NP_001014436.1.
DR UCSC; uc003tjo.5; human. [Q9UJU6-1]
DR AGR; HGNC:2696; -.
DR CTD; 28988; -.
DR DisGeNET; 28988; -.
DR GeneCards; DBNL; -.
DR HGNC; HGNC:2696; DBNL.
DR HPA; ENSG00000136279; Low tissue specificity.
DR MalaCards; DBNL; -.
DR MIM; 610106; gene.
DR neXtProt; NX_Q9UJU6; -.
DR OpenTargets; ENSG00000136279; -.
DR PharmGKB; PA27164; -.
DR VEuPathDB; HostDB:ENSG00000136279; -.
DR eggNOG; KOG3655; Eukaryota.
DR GeneTree; ENSGT00940000156732; -.
DR HOGENOM; CLU_013085_0_1_1; -.
DR InParanoid; Q9UJU6; -.
DR OMA; FKEPRGA; -.
DR OrthoDB; 101008at2759; -.
DR PhylomeDB; Q9UJU6; -.
DR TreeFam; TF318935; -.
DR PathwayCommons; Q9UJU6; -.
DR Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9UJU6; -.
DR SIGNOR; Q9UJU6; -.
DR BioGRID-ORCS; 28988; 16 hits in 1152 CRISPR screens.
DR ChiTaRS; DBNL; human.
DR EvolutionaryTrace; Q9UJU6; -.
DR GeneWiki; Drebrin-like; -.
DR GenomeRNAi; 28988; -.
DR Pharos; Q9UJU6; Tbio.
DR PRO; PR:Q9UJU6; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UJU6; Protein.
DR Bgee; ENSG00000136279; Expressed in lower esophagus mucosa and 164 other cell types or tissues.
DR ExpressionAtlas; Q9UJU6; baseline and differential.
DR Genevisible; Q9UJU6; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0002102; C:podosome; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0071800; P:podosome assembly; ISS:UniProtKB.
DR GO; GO:0016601; P:Rac protein signal transduction; ISS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
DR CDD; cd11281; ADF_drebrin_like; 1.
DR CDD; cd11960; SH3_Abp1_eu; 1.
DR Gene3D; 3.40.20.10; Severin; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR035717; Drebrin-like_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10829; CORTACTIN AND DREBRIN; 1.
DR PANTHER; PTHR10829:SF12; DREBRIN-LIKE PROTEIN; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00102; ADF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF55753; Actin depolymerizing proteins; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51263; ADF_H; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Adaptive immunity;
KW Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endocytosis;
KW Endosome; Golgi apparatus; Immunity; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain; Synapse; Transport.
FT CHAIN 1..430
FT /note="Drebrin-like protein"
FT /id="PRO_0000079793"
FT DOMAIN 4..133
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT DOMAIN 371..430
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 219..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 176..231
FT /evidence="ECO:0000255"
FT COMPBIAS 227..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 361..362
FT /note="Cleavage; by caspase-3"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62418"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 176
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:23186163"
FT MOD_RES 288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 291
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 334
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62418"
FT MOD_RES 344
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62418"
FT VAR_SEQ 1..109
FT /note="MAANLSRNGPALQEAYVRVVTEKSPTDWALFTYEGNSNDIRVAGTGEGGLEE
FT MVEELNSGKVMYAFCRVKDPNSGLPKFVLINWTGEGVNDVRKGACASHVSTMASFLK
FT -> MKATAMTSAWLAQG (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_054779"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054780"
FT VAR_SEQ 110..158
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057346"
FT VAR_SEQ 234
FT /note="Q -> QS (in isoform 2, isoform 3, isoform 4 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011398"
FT VAR_SEQ 251
FT /note="Q -> QGSTCASLQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011399"
FT MUTAGEN 361
FT /note="D->A: Abolishes cleavage by caspase-3."
FT /evidence="ECO:0000269|PubMed:15637062"
FT CONFLICT 8
FT /note="N -> K (in Ref. 4; AAG17262)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="A -> S (in Ref. 3; AAF81273/AAG13120)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="R -> S (in Ref. 3; AAF81273/AAG13120)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="E -> D (in Ref. 6; CAG33448)"
FT /evidence="ECO:0000305"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:1X67"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1X67"
FT STRAND 27..38
FT /evidence="ECO:0007829|PDB:1X67"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:1X67"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:1X67"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:1X67"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1X67"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:1X67"
FT HELIX 91..107
FT /evidence="ECO:0007829|PDB:1X67"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1X67"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:1X67"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:1X67"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:1X67"
FT MOD_RES Q9UJU6-2:232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q9UJU6-3:232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q9UJU6-4:137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q9UJU6-6:183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231"
SQ SEQUENCE 430 AA; 48207 MW; 7E8C42ED047257AE CRC64;
MAANLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL EEMVEELNSG
KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACASH VSTMASFLKG AHVTINARAE
EDVEPECIME KVAKASGANY SFHKESGRFQ DVGPQAPVGS VYQKTNAVSE IKRVGKDSFW
AKAEKEEENR RLEEKRRAEE AQRQLEQERR ERELREAARR EQRYQEQGGE ASPQRTWEQQ
QEVVSRNRNE QESAVHPREI FKQKERAMST TSISSPQPGK LRSPFLQKQL TQPETHFGRE
PAAAISRPRA DLPAEEPAPS TPPCLVQAEE EAVYEEPPEQ ETFYEQPPLV QQQGAGSEHI
DHHIQGQGLS GQGLCARALY DYQAADDTEI SFDPENLITG IEVIDEGWWR GYGPDGHFGM
FPANYVELIE
//
