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}. 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; 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 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. DR Genevisible; Q9UJU6; HS. 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 //