ID   DNMBP_HUMAN             Reviewed;        1577 AA.
AC   Q6XZF7; Q8IVY3; Q9Y2L3;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Dynamin-binding protein {ECO:0000312|HGNC:HGNC:30373};
DE   AltName: Full=Scaffold protein Tuba {ECO:0000305|PubMed:14506234};
GN   Name=DNMBP {ECO:0000312|HGNC:HGNC:30373};
GN   Synonyms=ARHGEF36 {ECO:0000312|HGNC:HGNC:30373}, KIAA1010
GN   {ECO:0000303|PubMed:10231032}, TUBA {ECO:0000303|PubMed:14506234};
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), ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain, and Skeletal muscle;
RX   PubMed=14506234; DOI=10.1074/jbc.m308104200;
RA   Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H.,
RA   Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.;
RT   "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology
RT   domains, links dynamin to regulation of the actin cytoskeleton.";
RL   J. Biol. Chem. 278:49031-49043(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 263-1577 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:63-70(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT TRP-1413.
RC   TISSUE=Uterus;
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   [4]
RP   INTERACTION WITH TJP1 AND WASL, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=17015620; DOI=10.1083/jcb.200605012;
RA   Otani T., Ichii T., Aono S., Takeichi M.;
RT   "Cdc42 GEF Tuba regulates the junctional configuration of simple epithelial
RT   cells.";
RL   J. Cell Biol. 175:135-146(2006).
RN   [5]
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   [6]
RP   INTERACTION WITH FASLG.
RX   PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA   Voss M., Lettau M., Janssen O.;
RT   "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT   phage display screening.";
RL   BMC Immunol. 10:53-53(2009).
RN   [7]
RP   FUNCTION, INTERACTION WITH WASL, INTERACTION WITH L.MONOCYTOGENES INLC, AND
RP   SUBUNIT (MICROBIAL INFECTION).
RX   PubMed=19767742; DOI=10.1038/ncb1964;
RA   Rajabian T., Gavicherla B., Heisig M., Mueller-Altrock S., Goebel W.,
RA   Gray-Owen S.D., Ireton K.;
RT   "The bacterial virulence factor InlC perturbs apical cell junctions and
RT   promotes cell-to-cell spread of Listeria.";
RL   Nat. Cell Biol. 11:1212-1218(2009).
RN   [8]
RP   FUNCTION.
RX   PubMed=20479467; DOI=10.1083/jcb.201002097;
RA   Qin Y., Meisen W.H., Hao Y., Macara I.G.;
RT   "Tuba, a Cdc42 GEF, is required for polarized spindle orientation during
RT   epithelial cyst formation.";
RL   J. Cell Biol. 189:661-669(2010).
RN   [9]
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   [10]
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   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496 AND SER-684, AND
RP   IDENTIFICATION BY MASS 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   [13]
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   [14]
RP   VARIANT CTRCT48 271-ARG--THR-1577 DEL, AND INVOLVEMENT IN CTRCT48.
RX   PubMed=30290152; DOI=10.1016/j.ajhg.2018.09.004;
RA   Ansar M., Chung H.L., Taylor R.L., Nazir A., Imtiaz S., Sarwar M.T.,
RA   Manousopoulou A., Makrythanasis P., Saeed S., Falconnet E., Guipponi M.,
RA   Pournaras C.J., Ansari M.A., Ranza E., Santoni F.A., Ahmed J., Shah I.,
RA   Gul K., Black G.C., Bellen H.J., Antonarakis S.E.;
RT   "Bi-allelic loss-of-function variants in DNMBP cause infantile cataracts.";
RL   Am. J. Hum. Genet. 103:568-578(2018).
RN   [15]
RP   STRUCTURE BY NMR OF 1278-1353 AND 1510-1575.
RG   RIKEN structural genomics initiative (RSGI);
RT   "NMR structure of SH3 domain of hypothetical protein BAA76854.1.";
RL   Submitted (DEC-2003) to the PDB data bank.
RN   [16] {ECO:0007744|PDB:1UHC}
RP   STRUCTURE BY NMR OF 1510-1575.
RA   Abe T., Hirota H., Kobayashi N., Hayashi F., Yokoyama S.;
RT   "Solution structure of RSGI RUH-002, a SH3 domain of KIAA1010 protein [Homo
RT   sapiens].";
RL   Submitted (JUN-2003) to the PDB data bank.
RN   [17] {ECO:0007744|PDB:4GLM}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 246-301.
RA   Guan X., Dong A., Huang H., Tempel W., Gu J., Sidhu S., Bountra C.,
RA   Arrowsmith C.H., Edwards A.M., Tong Y.;
RT   "Crystal structure of the SH3 Domain of DNMBP protein [Homo sapiens].";
RL   Submitted (AUG-2012) to the PDB data bank.
RN   [18] {ECO:0007744|PDB:4CC2, ECO:0007744|PDB:4CC3, ECO:0007744|PDB:4CC4, ECO:0007744|PDB:4CC7}
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1513-1577 IN COMPLEX WITH WASL;
RP   MURINE ENAH AND L.MONOCYTOGENES INLC, SUBUNIT, AND MUTAGENESIS OF VAL-1521;
RP   PRO-1529 AND ASN-1569.
RX   PubMed=24332715; DOI=10.1016/j.str.2013.10.017;
RA   Polle L., Rigano L.A., Julian R., Ireton K., Schubert W.D.;
RT   "Structural details of human tuba recruitment by InlC of Listeria
RT   monocytogenes elucidate bacterial cell-cell spreading.";
RL   Structure 22:304-314(2014).
CC   -!- FUNCTION: Plays a critical role as a guanine nucleotide exchange factor
CC       (GEF) for CDC42 in several intracellular processes associated with the
CC       actin and microtubule cytoskeleton. Regulates the structure of apical
CC       junctions through F-actin organization in epithelial cells
CC       (PubMed:19767742, PubMed:17015620). Participates in the normal
CC       lumenogenesis of epithelial cell cysts by regulating spindle
CC       orientation (PubMed:20479467). Plays a role in ciliogenesis (By
CC       similarity). May play a role in membrane trafficking between the cell
CC       surface and the Golgi (By similarity). {ECO:0000250|UniProtKB:E2RP94,
CC       ECO:0000250|UniProtKB:Q6TXD4, ECO:0000269|PubMed:17015620,
CC       ECO:0000269|PubMed:19767742, ECO:0000269|PubMed:20479467}.
CC   -!- SUBUNIT: Binds DNM1 via its N-terminal SH3 domains. The C-terminal SH3
CC       domain binds a complex containing actin, tubulin, Hsp70 and actin-
CC       regulatory proteins, such as ENAH, EVL, WIRE, CR16, WAVE1 and NAP1L1
CC       (By similarity). Interacts with FASLG (PubMed:19807924). Interacts (via
CC       SH3 domain 6) with WASL (PubMed:19767742, PubMed:24332715,
CC       PubMed:17015620). Interacts (via SH3 domain 6) interacts with ENAH
CC       (PubMed:24332715). Interacts (via C-terminal domain) with TJP1;
CC       required for the apical cell-cell junction localization of DNMBP
CC       (PubMed:17015620). {ECO:0000250, ECO:0000250|UniProtKB:Q6TXD4,
CC       ECO:0000269|PubMed:17015620, ECO:0000269|PubMed:19767742,
CC       ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:24332715}.
CC   -!- SUBUNIT: (Microbial infection) Interacts (via SH3 domain 6) with
CC       L.monocytogenes InlC. {ECO:0000269|PubMed:19767742,
CC       ECO:0000269|PubMed:24332715}.
CC   -!- INTERACTION:
CC       Q6XZF7; Q9NQY0: BIN3; NbExp=2; IntAct=EBI-2483419, EBI-2653038;
CC       Q6XZF7; P21575: Dnm1; Xeno; NbExp=3; IntAct=EBI-2483419, EBI-80070;
CC       Q6XZF7-1; O00401: WASL; NbExp=2; IntAct=EBI-16085546, EBI-957615;
CC       Q6XZF7-1; Q03173-1: Enah; Xeno; NbExp=2; IntAct=EBI-16085546, EBI-16085647;
CC       Q6XZF7-1; P71451: inlC; Xeno; NbExp=6; IntAct=EBI-16085546, EBI-21019720;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17015620}. Golgi
CC       apparatus, Golgi stack {ECO:0000250|UniProtKB:Q6TXD4}. Cytoplasm,
CC       cytoskeleton {ECO:0000250|UniProtKB:Q6TXD4}. Synapse
CC       {ECO:0000250|UniProtKB:M0R4F8}. Cell junction
CC       {ECO:0000269|PubMed:17015620}. Note=Localizes to the apical junction,
CC       colocalizes with TJP1. {ECO:0000269|PubMed:17015620}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6XZF7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6XZF7-2; Sequence=VSP_012079;
CC   -!- TISSUE SPECIFICITY: Detected in heart, brain, lung, liver, skeletal
CC       muscle, kidney and pancreas. {ECO:0000269|PubMed:14506234}.
CC   -!- DISEASE: Cataract 48 (CTRCT48) [MIM:618415]: A form of cataract, an
CC       opacification of the crystalline lens of the eye that frequently
CC       results in visual impairment or blindness. Opacities vary in
CC       morphology, are often confined to a portion of the lens, and may be
CC       static or progressive. In general, the more posteriorly located and
CC       dense an opacity, the greater the impact on visual function. CTRCT48 is
CC       an autosomal recessive form characterized by infantile or early-
CC       childhood onset. {ECO:0000269|PubMed:30290152}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
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; AY196211; AAP34307.1; -; mRNA.
DR   EMBL; AB023227; BAA76854.1; -; mRNA.
DR   EMBL; BC041628; AAH41628.1; -; mRNA.
DR   CCDS; CCDS7485.1; -. [Q6XZF7-1]
DR   RefSeq; NP_001305255.1; NM_001318326.1.
DR   RefSeq; NP_001305256.1; NM_001318327.1.
DR   RefSeq; NP_056036.1; NM_015221.3. [Q6XZF7-1]
DR   RefSeq; XP_011537861.1; XM_011539559.2. [Q6XZF7-1]
DR   PDB; 1UG1; NMR; -; A=1278-1355.
DR   PDB; 1UHC; NMR; -; A=1510-1575.
DR   PDB; 4CC2; X-ray; 1.55 A; A/C=1513-1577.
DR   PDB; 4CC3; X-ray; 1.97 A; A/C/E/G=1513-1577.
DR   PDB; 4CC4; X-ray; 2.60 A; B/D/F=1513-1577.
DR   PDB; 4CC7; X-ray; 1.97 A; A/C/E/G/I/K/M=1513-1577.
DR   PDB; 4GLM; X-ray; 1.90 A; A/B/C/D=246-301.
DR   PDBsum; 1UG1; -.
DR   PDBsum; 1UHC; -.
DR   PDBsum; 4CC2; -.
DR   PDBsum; 4CC3; -.
DR   PDBsum; 4CC4; -.
DR   PDBsum; 4CC7; -.
DR   PDBsum; 4GLM; -.
DR   AlphaFoldDB; Q6XZF7; -.
DR   SMR; Q6XZF7; -.
DR   BioGRID; 116869; 124.
DR   DIP; DIP-53822N; -.
DR   IntAct; Q6XZF7; 38.
DR   MINT; Q6XZF7; -.
DR   STRING; 9606.ENSP00000315659; -.
DR   ChEMBL; CHEMBL4295871; -.
DR   GlyGen; Q6XZF7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6XZF7; -.
DR   MetOSite; Q6XZF7; -.
DR   PhosphoSitePlus; Q6XZF7; -.
DR   BioMuta; DNMBP; -.
DR   DMDM; 56404535; -.
DR   EPD; Q6XZF7; -.
DR   jPOST; Q6XZF7; -.
DR   MassIVE; Q6XZF7; -.
DR   MaxQB; Q6XZF7; -.
DR   PaxDb; 9606-ENSP00000315659; -.
DR   PeptideAtlas; Q6XZF7; -.
DR   ProteomicsDB; 67829; -. [Q6XZF7-1]
DR   ProteomicsDB; 67830; -. [Q6XZF7-2]
DR   Pumba; Q6XZF7; -.
DR   ABCD; Q6XZF7; 6 sequenced antibodies.
DR   Antibodypedia; 31117; 176 antibodies from 25 providers.
DR   DNASU; 23268; -.
DR   Ensembl; ENST00000324109.9; ENSP00000315659.4; ENSG00000107554.17. [Q6XZF7-1]
DR   GeneID; 23268; -.
DR   KEGG; hsa:23268; -.
DR   MANE-Select; ENST00000324109.9; ENSP00000315659.4; NM_015221.4; NP_056036.1.
DR   UCSC; uc001kqg.3; human. [Q6XZF7-1]
DR   AGR; HGNC:30373; -.
DR   CTD; 23268; -.
DR   DisGeNET; 23268; -.
DR   GeneCards; DNMBP; -.
DR   HGNC; HGNC:30373; DNMBP.
DR   HPA; ENSG00000107554; Low tissue specificity.
DR   MalaCards; DNMBP; -.
DR   MIM; 611282; gene.
DR   MIM; 618415; phenotype.
DR   neXtProt; NX_Q6XZF7; -.
DR   OpenTargets; ENSG00000107554; -.
DR   Orphanet; 98994; Total early-onset cataract.
DR   PharmGKB; PA134950706; -.
DR   VEuPathDB; HostDB:ENSG00000107554; -.
DR   eggNOG; KOG3519; Eukaryota.
DR   eggNOG; KOG4225; Eukaryota.
DR   GeneTree; ENSGT00950000183088; -.
DR   HOGENOM; CLU_252350_0_0_1; -.
DR   InParanoid; Q6XZF7; -.
DR   OrthoDB; 25601at2759; -.
DR   PhylomeDB; Q6XZF7; -.
DR   TreeFam; TF330015; -.
DR   PathwayCommons; Q6XZF7; -.
DR   Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR   SignaLink; Q6XZF7; -.
DR   SIGNOR; Q6XZF7; -.
DR   BioGRID-ORCS; 23268; 15 hits in 1154 CRISPR screens.
DR   ChiTaRS; DNMBP; human.
DR   EvolutionaryTrace; Q6XZF7; -.
DR   GenomeRNAi; 23268; -.
DR   Pharos; Q6XZF7; Tbio.
DR   PRO; PR:Q6XZF7; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q6XZF7; Protein.
DR   Bgee; ENSG00000107554; Expressed in jejunal mucosa and 201 other cell types or tissues.
DR   ExpressionAtlas; Q6XZF7; baseline and differential.
DR   GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR   CDD; cd07589; BAR_DNMBP; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd11798; SH3_DNMBP_C1; 1.
DR   CDD; cd12141; SH3_DNMBP_C2; 1.
DR   CDD; cd11794; SH3_DNMBP_N1; 1.
DR   CDD; cd11795; SH3_DNMBP_N2; 1.
DR   CDD; cd11796; SH3_DNMBP_N3; 1.
DR   CDD; cd11797; SH3_DNMBP_N4; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 6.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR035820; DNMBP_SH3_C1.
DR   InterPro; IPR035817; DNMBP_SH3_N1.
DR   InterPro; IPR035818; DNMBP_SH3_N2.
DR   InterPro; IPR035819; DNMBP_SH3_N3.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR22834:SF19; DYNAMIN-BINDING PROTEIN; 1.
DR   PANTHER; PTHR22834; NUCLEAR FUSION PROTEIN FUS2; 1.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00018; SH3_1; 2.
DR   Pfam; PF07653; SH3_2; 2.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   SMART; SM00721; BAR; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00326; SH3; 6.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50044; SH3-domain; 6.
DR   PROSITE; PS51021; BAR; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50002; SH3; 6.
DR   Genevisible; Q6XZF7; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cataract; Cell junction;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; Golgi apparatus;
KW   Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome;
KW   Repeat; SH3 domain; Synapse.
FT   CHAIN           1..1577
FT                   /note="Dynamin-binding protein"
FT                   /id="PRO_0000079959"
FT   DOMAIN          2..61
FT                   /note="SH3 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          66..126
FT                   /note="SH3 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          145..204
FT                   /note="SH3 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          243..302
FT                   /note="SH3 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          784..967
FT                   /note="DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT   DOMAIN          1008..1217
FT                   /note="BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT   DOMAIN          1285..1348
FT                   /note="SH3 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          1513..1576
FT                   /note="SH3 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          211..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          639..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1348..1487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          693..757
FT                   /evidence="ECO:0000255"
FT   COILED          1136..1173
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        335..351
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..610
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1352..1405
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1414..1448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         496
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         684
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..754
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012079"
FT   VARIANT         81
FT                   /note="E -> D (in dbSNP:rs12267912)"
FT                   /id="VAR_050955"
FT   VARIANT         271..1577
FT                   /note="Missing (in CTRCT48)"
FT                   /evidence="ECO:0000269|PubMed:30290152"
FT                   /id="VAR_081450"
FT   VARIANT         373
FT                   /note="N -> K (in dbSNP:rs35924554)"
FT                   /id="VAR_050956"
FT   VARIANT         914
FT                   /note="N -> K (in dbSNP:rs7919507)"
FT                   /id="VAR_050957"
FT   VARIANT         1413
FT                   /note="C -> W (in dbSNP:rs11190305)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_024339"
FT   MUTAGEN         1521
FT                   /note="V->R: Decreased interaction of SH3 domain 6 with
FT                   L.monocytogenes InlC."
FT                   /evidence="ECO:0000269|PubMed:24332715"
FT   MUTAGEN         1529
FT                   /note="P->A: Wild-type interaction of SH3 domain 6 with
FT                   L.monocytogenes InlC."
FT                   /evidence="ECO:0000269|PubMed:24332715"
FT   MUTAGEN         1569
FT                   /note="N->R: Decreased interaction of SH3 domain 6 with
FT                   L.monocytogenes InlC."
FT                   /evidence="ECO:0000269|PubMed:24332715"
FT   CONFLICT        831
FT                   /note="M -> T (in Ref. 3; AAH41628)"
FT                   /evidence="ECO:0000305"
FT   STRAND          247..252
FT                   /evidence="ECO:0007829|PDB:4GLM"
FT   STRAND          269..275
FT                   /evidence="ECO:0007829|PDB:4GLM"
FT   STRAND          280..285
FT                   /evidence="ECO:0007829|PDB:4GLM"
FT   STRAND          288..293
FT                   /evidence="ECO:0007829|PDB:4GLM"
FT   HELIX           294..296
FT                   /evidence="ECO:0007829|PDB:4GLM"
FT   STRAND          297..300
FT                   /evidence="ECO:0007829|PDB:4GLM"
FT   HELIX           1278..1283
FT                   /evidence="ECO:0007829|PDB:1UG1"
FT   HELIX           1286..1288
FT                   /evidence="ECO:0007829|PDB:1UG1"
FT   STRAND          1289..1294
FT                   /evidence="ECO:0007829|PDB:1UG1"
FT   STRAND          1300..1302
FT                   /evidence="ECO:0007829|PDB:1UG1"
FT   STRAND          1311..1317
FT                   /evidence="ECO:0007829|PDB:1UG1"
FT   STRAND          1324..1330
FT                   /evidence="ECO:0007829|PDB:1UG1"
FT   STRAND          1332..1339
FT                   /evidence="ECO:0007829|PDB:1UG1"
FT   HELIX           1340..1342
FT                   /evidence="ECO:0007829|PDB:1UG1"
FT   STRAND          1343..1345
FT                   /evidence="ECO:0007829|PDB:1UG1"
FT   STRAND          1517..1522
FT                   /evidence="ECO:0007829|PDB:4CC2"
FT   STRAND          1528..1531
FT                   /evidence="ECO:0007829|PDB:1UHC"
FT   STRAND          1539..1546
FT                   /evidence="ECO:0007829|PDB:4CC2"
FT   STRAND          1554..1559
FT                   /evidence="ECO:0007829|PDB:4CC2"
FT   STRAND          1562..1567
FT                   /evidence="ECO:0007829|PDB:4CC2"
FT   HELIX           1568..1570
FT                   /evidence="ECO:0007829|PDB:4CC2"
FT   STRAND          1571..1574
FT                   /evidence="ECO:0007829|PDB:4CC2"
SQ   SEQUENCE   1577 AA;  177347 MW;  5A1FDCB06124F627 CRC64;
     MEAGSVVRAI FDFCPSVSEE LPLFVGDIIE VLAVVDEFWL LGKKEDVTGQ FPSSFVEIVT
     IPSLKEGERL FVCICEFTSQ ELDNLPLHRG DLVILDGIPT AGWLQGRSCW GARGFFPSSC
     VRELCLSSQS RQWHSQSALF QIPEYSMGQA RALMGLSAQL DEELDFREGD VITIIGVPEP
     GWFEGELEGR RGIFPEGFVE LLGPLRTVDE SVSSGNQDDC IVNGEVDTPV GEEEIGPDED
     EEEPGTYGVA LYRFQALEPN ELDFEVGDKI RILATLEDGW LEGSLKGRTG IFPYRFVKLC
     PDTRVEETMA LPQEGSLARI PETSLDCLEN TLGVEEQRHE TSDHEAEEPD CIISEAPTSP
     LGHLTSEYDT DRNSYQDEDT AGGPPRSPGV EWEMPLATDS PTSDPTEVVN GISSQPQVPF
     HPNLQKSQYY STVGGSHPHS EQYPDLLPLE ARTRDYASLP PKRMYSQLKT LQKPVLPLYR
     GSSVSASRVV KPRQSSPQLH NLASYTKKHH TSSVYSISER LEMKPGPQAQ GLVMEAATHS
     QGDGSTDLDS KLTQQLIEFE KSLAGPGTEP DKILRHFSIM DFNSEKDIVR GSSKLITEQE
     LPERRKALRP PPPRPCTPVS TSPHLLVDQN LKPAPPLVVR PSRPAPLPPS AQQRTNAVSP
     KLLSRHRPTC ETLEKEGPGH MGRSLDQTSP CPLVLVRIEE MERDLDMYSR AQEELNLMLE
     EKQDESSRAE TLEDLKFCES NIESLNMELQ QLREMTLLSS QSSSLVAPSG SVSAENPEQR
     MLEKRAKVIE ELLQTERDYI RDLEMCIERI MVPMQQAQVP NIDFEGLFGN MQMVIKVSKQ
     LLAALEISDA VGPVFLGHRD ELEGTYKIYC QNHDEAIALL EIYEKDEKIQ KHLQDSLADL
     KSLYNEWGCT NYINLGSFLI KPVQRVMRYP LLLMELLNST PESHPDKVPL TNAVLAVKEI
     NVNINEYKRR KDLVLKYRKG DEDSLMEKIS KLNIHSIIKK SNRVSSHLKH LTGFAPQIKD
     EVFEETEKNF RMQERLIKSF IRDLSLYLQH IRESACVKVV AAVSMWDVCM ERGHRDLEQF
     ERVHRYISDQ LFTNFKERTE RLVISPLNQL LSMFTGPHKL VQKRFDKLLD FYNCTERAEK
     LKDKKTLEEL QSARNNYEAL NAQLLDELPK FHQYAQGLFT NCVHGYAEAH CDFVHQALEQ
     LKPLLSLLKV AGREGNLIAI FHEEHSRVLQ QLQVFTFFPE SLPATKKPFE RKTIDRQSAR
     KPLLGLPSYM LQSEELRASL LARYPPEKLF QAERNFNAAQ DLDVSLLEGD LVGVIKKKDP
     MGSQNRWLID NGVTKGFVYS SFLKPYNPRR SHSDASVGSH SSTESEHGSS SPRFPRQNSG
     STLTFNPSSM AVSFTSGSCQ KQPQDASPPP KECDQGTLSA SLNPSNSESS PSRCPSDPDS
     TSQPRSGDSA DVARDVKQPT ATPRSYRNFR HPEIVGYSVP GRNGQSQDLV KGCARTAQAP
     EDRSTEPDGS EAEGNQVYFA VYTFKARNPN ELSVSANQKL KILEFKDVTG NTEWWLAEVN
     GKKGYVPSNY IRKTEYT
//