DREB_HUMAN
ID DREB_HUMAN Reviewed; 649 AA.
AC Q16643; A8MV58; B2RBG0; Q9UFZ5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 4.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Drebrin;
DE AltName: Full=Developmentally-regulated brain protein;
GN Name=DBN1; Synonyms=D0S117E;
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), TISSUE SPECIFICITY, AND VARIANTS
RP VAL-446 AND PRO-553.
RC TISSUE=Fetal brain;
RX PubMed=8216329; DOI=10.1006/bbrc.1993.2273;
RA Toda M., Shirao T., Minoshima S., Shimizu N., Toya S., Uyemura K.;
RT "Molecular cloning of cDNA encoding human drebrin E and chromosomal mapping
RT of its gene.";
RL Biochem. Biophys. Res. Commun. 196:468-472(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP VAL-446 AND PRO-553.
RC TISSUE=Osteoblast;
RA Fisher L.W., McBride O.W., Filpula D., Ibaraki K., Young M.F.;
RT "Human drebrin: cDNA sequence, mRNA tissue distribution and chromosomal
RT localization.";
RL Neurosci. Res. Commun. 14:35-42(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS VAL-446
RP AND PRO-553.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 37-521 (ISOFORM 3), AND VARIANTS VAL-446 AND PRO-553.
RC TISSUE=Eye, and Muscle;
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 [7]
RP PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
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 [8]
RP PROTEIN SEQUENCE OF 2-10; 43-62; 140-147; 150-165; 272-299 AND 328-390,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT
RP SER-142, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Dozynkiewicz M., Norman J.C.;
RL Submitted (JUN-2009) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 80-94, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INVOLVEMENT IN AD.
RX PubMed=8838578; DOI=10.1002/jnr.490430111;
RA Harigaya Y., Shoji M., Shirao T., Hirai S.;
RT "Disappearance of actin-binding protein, drebrin, from hippocampal synapses
RT in Alzheimer's disease.";
RL J. Neurosci. Res. 43:87-92(1996).
RN [11]
RP IDENTIFICATION BY 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [13]
RP IDENTIFICATION BY 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; THR-331; THR-335;
RP SER-337 AND THR-346, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-331 AND THR-346, 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 [17]
RP FUNCTION, INTERACTION WITH CXCR4, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=20215400; DOI=10.1242/jcs.064238;
RA Perez-Martinez M., Gordon-Alonso M., Cabrero J.R., Barrero-Villar M.,
RA Rey M., Mittelbrunn M., Lamana A., Morlino G., Calabia C., Yamazaki H.,
RA Shirao T., Vazquez J., Gonzalez-Amaro R., Veiga E., Sanchez-Madrid F.;
RT "F-actin-binding protein drebrin regulates CXCR4 recruitment to the immune
RT synapse.";
RL J. Cell Sci. 123:1160-1170(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-142, 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 [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-142; SER-337 AND
RP SER-339, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-142; THR-331;
RP SER-337; SER-339 AND THR-346, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416 AND THR-497, 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 [23]
RP VARIANTS [LARGE SCALE ANALYSIS] LYS-278 AND GLN-640.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [24] {ECO:0007744|PDB:5Y1Z}
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 1-135 IN COMPLEX WITH ZMYND8,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-10 AND CYS-96.
RX PubMed=28966017; DOI=10.1016/j.str.2017.08.014;
RA Yao N., Li J., Liu H., Wan J., Liu W., Zhang M.;
RT "The Structure of the ZMYND8/Drebrin Complex Suggests a Cytoplasmic
RT Sequestering Mechanism of ZMYND8 by Drebrin.";
RL Structure 25:1657-1666(2017).
CC -!- FUNCTION: Actin cytoskeleton-organizing protein that plays a role in
CC the formation of cell projections (PubMed:20215400). Required for actin
CC polymerization at immunological synapses (IS) and for the recruitment
CC of the chemokine receptor CXCR4 to IS (PubMed:20215400). Plays a role
CC in dendritic spine morphogenesis and organization, including the
CC localization of the dopamine receptor DRD1 to the dendritic spines (By
CC similarity). Involved in memory-related synaptic plasticity in the
CC hippocampus (By similarity). {ECO:0000250|UniProtKB:Q9QXS6,
CC ECO:0000269|PubMed:20215400}.
CC -!- SUBUNIT: Interacts with RUFY3 (By similarity). Interacts with CXCR4;
CC this interaction is enhanced by antigenic stimulation
CC (PubMed:20215400). Interacts (via ADF-H domain) with ZMYND8 (via PHD-
CC type Zinc finger, Bromo and PWWP domains); the interaction leads to
CC sequestering of ZMYND8 in the cytoplasm (PubMed:28966017).
CC {ECO:0000250|UniProtKB:Q9QXS6, ECO:0000269|PubMed:20215400,
CC ECO:0000269|PubMed:28966017}.
CC -!- INTERACTION:
CC Q16643; P55196: AFDN; NbExp=4; IntAct=EBI-351394, EBI-365875;
CC Q16643; P61073: CXCR4; NbExp=5; IntAct=EBI-351394, EBI-489411;
CC Q16643; Q16643-1: DBN1; NbExp=2; IntAct=EBI-351394, EBI-8757328;
CC Q16643; P62993: GRB2; NbExp=4; IntAct=EBI-351394, EBI-401755;
CC Q16643; P28799: GRN; NbExp=5; IntAct=EBI-351394, EBI-747754;
CC Q16643; P60484: PTEN; NbExp=5; IntAct=EBI-351394, EBI-696162;
CC Q16643; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-351394, EBI-717399;
CC Q16643; Q9ULU4: ZMYND8; NbExp=4; IntAct=EBI-351394, EBI-765834;
CC Q16643; O35889: Afdn; Xeno; NbExp=3; IntAct=EBI-351394, EBI-6654073;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20215400,
CC ECO:0000269|PubMed:28966017, ECO:0000269|PubMed:8838578}. Cell
CC projection, dendrite {ECO:0000269|PubMed:8838578}. Cytoplasm, cell
CC cortex {ECO:0000269|PubMed:20215400}. Cell junction
CC {ECO:0000269|PubMed:20215400}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q9QXS6}. Note=In the absence of antigen, evenly
CC distributed throughout subcortical regions of the T-cell membrane and
CC cytoplasm (PubMed:20215400). In the presence of antigen, distributes to
CC the immunological synapse forming at the T-cell-APC contact area, where
CC it localizes at the peripheral and distal supramolecular activation
CC clusters (SMAC) (PubMed:20215400). Colocalized with RUFY3 and F-actin
CC at the transitional domain of the axonal growth cone (By similarity).
CC {ECO:0000250|UniProtKB:Q9QXS6, ECO:0000269|PubMed:20215400}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Drebrin E, drebrin E2, Embryonic drebrin;
CC IsoId=Q16643-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16643-2; Sequence=VSP_028175;
CC Name=3; Synonyms=Drebrin A;
CC IsoId=Q16643-3; Sequence=VSP_053443;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, with expression in the
CC molecular layer of the dentate gyrus, stratum pyramidale, and stratum
CC radiatum of the hippocampus (at protein level) (PubMed:8838578). Also
CC expressed in the terminal varicosities distributed along dendritic
CC trees of pyramidal cells in CA4 and CA3 of the hippocampus (at protein
CC level) (PubMed:8838578). Expressed in pyramidal cells in CA2, CA1 and
CC the subiculum of the hippocampus (at protein level) (PubMed:8838578).
CC Expressed in peripheral blood lymphocytes, including T-cells (at
CC protein level) (PubMed:20215400). Expressed in the brain
CC (PubMed:8216329, Ref.2). Expressed in the heart, placenta, lung,
CC skeletal muscle, kidney, pancreas, skin fibroblasts, gingival
CC fibroblasts and bone-derived cells (Ref.2).
CC {ECO:0000269|PubMed:20215400, ECO:0000269|PubMed:8216329,
CC ECO:0000269|PubMed:8838578, ECO:0000269|Ref.2}.
CC -!- DISEASE: Alzheimer disease (AD) [MIM:104300]: Alzheimer disease is a
CC neurodegenerative disorder characterized by progressive dementia, loss
CC of cognitive abilities, and deposition of fibrillar amyloid proteins as
CC intraneuronal neurofibrillary tangles, extracellular amyloid plaques
CC and vascular amyloid deposits. The major constituents of these plaques
CC are neurotoxic amyloid-beta protein 40 and amyloid-beta protein 42,
CC that are produced by the proteolysis of the transmembrane APP protein.
CC The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved
CC products, such as C31, are also implicated in neuronal death.
CC {ECO:0000269|PubMed:8838578}. Note=The protein represented in this
CC entry may be involved in disease pathogenesis. In brains of patients
CC with AD, decreased expression and absence from dystrophic neurites in
CC amyloid plaques. Disappearance of debrin from the hippocampus may
CC contribute to the pathogenesis of memory disturbance in AD.
CC {ECO:0000269|PubMed:8838578}.
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; D17530; BAA04480.1; -; mRNA.
DR EMBL; U00802; AAA16256.1; -; mRNA.
DR EMBL; AK314645; BAG37207.1; -; mRNA.
DR EMBL; AL110225; CAB53683.1; -; mRNA.
DR EMBL; AC145098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000283; AAH00283.1; -; mRNA.
DR EMBL; BC007281; AAH07281.1; -; mRNA.
DR EMBL; BC007567; AAH07567.1; -; mRNA.
DR EMBL; BC114553; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS4420.1; -. [Q16643-1]
DR CCDS; CCDS4421.1; -. [Q16643-2]
DR CCDS; CCDS87354.1; -. [Q16643-3]
DR PIR; JN0809; JN0809.
DR PIR; T14763; T14763.
DR RefSeq; NP_004386.2; NM_004395.3. [Q16643-1]
DR RefSeq; NP_543157.1; NM_080881.2. [Q16643-2]
DR RefSeq; XP_005265884.1; XM_005265827.3.
DR RefSeq; XP_016864629.1; XM_017009140.1. [Q16643-2]
DR PDB; 5Y1Z; X-ray; 2.68 A; A/B=1-135.
DR PDB; 5ZZ9; X-ray; 2.30 A; D/E/F=530-551.
DR PDBsum; 5Y1Z; -.
DR PDBsum; 5ZZ9; -.
DR AlphaFoldDB; Q16643; -.
DR SMR; Q16643; -.
DR BioGRID; 107995; 336.
DR IntAct; Q16643; 275.
DR MINT; Q16643; -.
DR STRING; 9606.ENSP00000292385; -.
DR GlyGen; Q16643; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16643; -.
DR MetOSite; Q16643; -.
DR PhosphoSitePlus; Q16643; -.
DR SwissPalm; Q16643; -.
DR BioMuta; DBN1; -.
DR DMDM; 215274247; -.
DR OGP; Q16643; -.
DR CPTAC; CPTAC-347; -.
DR CPTAC; CPTAC-348; -.
DR EPD; Q16643; -.
DR jPOST; Q16643; -.
DR MassIVE; Q16643; -.
DR MaxQB; Q16643; -.
DR PaxDb; Q16643; -.
DR PeptideAtlas; Q16643; -.
DR PRIDE; Q16643; -.
DR ProteomicsDB; 2155; -.
DR ProteomicsDB; 60996; -. [Q16643-1]
DR ProteomicsDB; 60997; -. [Q16643-2]
DR Antibodypedia; 3641; 343 antibodies from 37 providers.
DR DNASU; 1627; -.
DR Ensembl; ENST00000292385.9; ENSP00000292385.5; ENSG00000113758.14. [Q16643-2]
DR Ensembl; ENST00000309007.9; ENSP00000308532.5; ENSG00000113758.14. [Q16643-1]
DR Ensembl; ENST00000393565.6; ENSP00000377195.1; ENSG00000113758.14. [Q16643-3]
DR GeneID; 1627; -.
DR KEGG; hsa:1627; -.
DR MANE-Select; ENST00000393565.6; ENSP00000377195.1; NM_001363541.2; NP_001350470.2. [Q16643-3]
DR UCSC; uc003mgx.3; human. [Q16643-1]
DR CTD; 1627; -.
DR DisGeNET; 1627; -.
DR GeneCards; DBN1; -.
DR HGNC; HGNC:2695; DBN1.
DR HPA; ENSG00000113758; Low tissue specificity.
DR MIM; 104300; phenotype.
DR MIM; 126660; gene.
DR neXtProt; NX_Q16643; -.
DR NIAGADS; ENSG00000113758; -.
DR OpenTargets; ENSG00000113758; -.
DR PharmGKB; PA27163; -.
DR VEuPathDB; HostDB:ENSG00000113758; -.
DR eggNOG; KOG3655; Eukaryota.
DR GeneTree; ENSGT00940000159431; -.
DR HOGENOM; CLU_013085_3_0_1; -.
DR InParanoid; Q16643; -.
DR OMA; FAQSDEC; -.
DR OrthoDB; 885776at2759; -.
DR PhylomeDB; Q16643; -.
DR TreeFam; TF318935; -.
DR PathwayCommons; Q16643; -.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013407; RHOH GTPase cycle.
DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle.
DR SignaLink; Q16643; -.
DR BioGRID-ORCS; 1627; 13 hits in 1077 CRISPR screens.
DR ChiTaRS; DBN1; human.
DR GeneWiki; DBN1; -.
DR GenomeRNAi; 1627; -.
DR Pharos; Q16643; Tbio.
DR PRO; PR:Q16643; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q16643; protein.
DR Bgee; ENSG00000113758; Expressed in ganglionic eminence and 197 other tissues.
DR ExpressionAtlas; Q16643; baseline and differential.
DR Genevisible; Q16643; HS.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0042641; C:actomyosin; NAS:UniProtKB.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030863; C:cortical cytoskeleton; TAS:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:ARUK-UCL.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005921; C:gap junction; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005522; F:profilin binding; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0010643; P:cell communication by chemical coupling; IEA:Ensembl.
DR GO; GO:0010644; P:cell communication by electrical coupling; IEA:Ensembl.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0032507; P:maintenance of protein location in cell; IEA:Ensembl.
DR GO; GO:0061351; P:neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0045773; P:positive regulation of axon extension; IBA:GO_Central.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:1902685; P:positive regulation of receptor localization to synapse; ISS:UniProtKB.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0050773; P:regulation of dendrite development; NAS:UniProtKB.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; NAS:UniProtKB.
DR Gene3D; 3.40.20.10; -; 1.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR028438; Drebrin.
DR PANTHER; PTHR10829:SF1; PTHR10829:SF1; 2.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR SMART; SM00102; ADF; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Alzheimer disease; Amyloidosis; Cell junction; Cell projection; Cytoplasm;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Neurodegeneration; Neurogenesis; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.8,
FT ECO:0007744|PubMed:19413330"
FT CHAIN 2..649
FT /note="Drebrin"
FT /id="PRO_0000080008"
FT DOMAIN 3..134
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT REGION 208..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..378
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.8,
FT ECO:0007744|PubMed:19413330"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS6"
FT MOD_RES 346
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 497
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS6"
FT VAR_SEQ 4..29
FT /note="VSFSGHRLELLAAYEEVIREESAADW -> HPWHGTAALASSQAWRDGRERQ
FT ALVSCR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028175"
FT VAR_SEQ 319
FT /note="G -> GRPYCPFIKASDSGPSSSSSSSSSPPRTPFPYITCHRTPNLSSSLPC
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053443"
FT VARIANT 278
FT /note="E -> K (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035910"
FT VARIANT 446
FT /note="I -> V (in dbSNP:rs2544809)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:8216329,
FT ECO:0000269|Ref.2"
FT /id="VAR_047365"
FT VARIANT 553
FT /note="S -> P (in dbSNP:rs28538572)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:8216329,
FT ECO:0000269|Ref.2"
FT /id="VAR_047366"
FT VARIANT 640
FT /note="E -> Q (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035911"
FT MUTAGEN 10
FT /note="R->D,G: Loss of binding to ZMYND8. Loss of ZMYND8
FT cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:28966017"
FT MUTAGEN 96
FT /note="C->Q: Decreased binding to ZMYND8."
FT /evidence="ECO:0000269|PubMed:28966017"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:5Y1Z"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:5Y1Z"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:5Y1Z"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:5Y1Z"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:5Y1Z"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5Y1Z"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:5Y1Z"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5Y1Z"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:5Y1Z"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:5Y1Z"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:5Y1Z"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:5Y1Z"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:5Y1Z"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:5Y1Z"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:5ZZ9"
SQ SEQUENCE 649 AA; 71429 MW; A7DF1AE3776C0BEA CRC64;
MAGVSFSGHR LELLAAYEEV IREESAADWA LYTYEDGSDD LKLAASGEGG LQELSGHFEN
QKVMYGFCSV KDSQAALPKY VLINWVGEDV PDARKCACAS HVAKVAEFFQ GVDVIVNASS
VEDIDAGAIG QRLSNGLARL SSPVLHRLRL REDENAEPVG TTYQKTDAAV EMKRINREQF
WEQAKKEEEL RKEEERKKAL DERLRFEQER MEQERQEQEE RERRYREREQ QIEEHRRKQQ
TLEAEEAKRR LKEQSIFGDH RDEEEETHMK KSESEVEEAA AIIAQRPDNP REFFKQQERV
ASASAGSCDV PSPFNHRPGS HLDSHRRMAP TPIPTRSPSD SSTASTPVAE QIERALDEVT
SSQPPPLPPP PPPAQETQEP SPILDSEETR AAAPQAWAGP MEEPPQAQAP PRGPGSPAED
LMFMESAEQA VLAAPVEPAT ADATEIHDAA DTIETDTATA DTTVANNVPP AATSLIDLWP
GNGEGASTLQ GEPRAPTPPS GTEVTLAEVP LLDEVAPEPL LPAGEGCATL LNFDELPEPP
ATFCDPEEVE GESLAAPQTP TLPSALEELE QEQEPEPHLL TNGETTQKEG TQASEGYFSQ
SQEEEFAQSE ELCAKAPPPV FYNKPPEIDI TCWDADPVPE EEEGFEGGD
