ID   DOCK9_HUMAN             Reviewed;        2069 AA.
AC   Q9BZ29; B3KX25; E9PFM9; Q5JUD4; Q5JUD6; Q5T2Q1; Q5TAN8; Q9BZ25; Q9BZ26;
AC   Q9BZ27; Q9BZ28; Q9UPU4;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 2.
DT   24-JAN-2024, entry version 185.
DE   RecName: Full=Dedicator of cytokinesis protein 9 {ECO:0000305};
DE   AltName: Full=Cdc42 guanine nucleotide exchange factor zizimin-1 {ECO:0000305};
DE            Short=Zizimin-1 {ECO:0000305};
GN   Name=DOCK9 {ECO:0000312|HGNC:HGNC:14132};
GN   Synonyms=KIAA1058, ZIZ1 {ECO:0000305};
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 (ISOFORM 1), FUNCTION, INTERACTION WITH CDC42, GEF
RP   ACTIVITY, AND TISSUE SPECIFICITY.
RX   PubMed=12172552; DOI=10.1038/ncb835;
RA   Meller N., Irani-Tehrani M., Kiosses W.B., Del Pozo M.A., Schwartz M.A.;
RT   "Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho
RT   proteins.";
RL   Nat. Cell Biol. 4:639-647(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA   Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:197-205(1999).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   TISSUE=Uterus;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1; 2; 3 AND 4).
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1551-2069 (ISOFORM 4).
RC   TISSUE=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   [7]
RP   NOMENCLATURE, AND GEF ACTIVITY.
RX   PubMed=12432077; DOI=10.1242/jcs.00219;
RA   Cote J.-F., Vuori K.;
RT   "Identification of an evolutionarily conserved superfamily of DOCK180-
RT   related proteins with guanine nucleotide exchange activity.";
RL   J. Cell Sci. 115:4901-4913(2002).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1241, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1235 AND THR-1241, 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   [11]
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-32; SER-927; SER-1255
RP   AND SER-1264, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167 AND SER-170, 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   [14]
RP   STRUCTURE BY NMR OF 165-301.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of pleckstrin homology domain from human KIAA1058
RT   protein.";
RL   Submitted (NOV-2004) to the PDB data bank.
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1605-2069 IN COMPLEX WITH CDC42,
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=19745154; DOI=10.1126/science.1174468;
RA   Yang J., Zhang Z., Roe S.M., Marshall C.J., Barford D.;
RT   "Activation of Rho GTPases by DOCK exchange factors is mediated by a
RT   nucleotide sensor.";
RL   Science 325:1398-1402(2009).
CC   -!- FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates CDC42
CC       by exchanging bound GDP for free GTP. Overexpression induces filopodia
CC       formation. {ECO:0000269|PubMed:12172552, ECO:0000269|PubMed:19745154}.
CC   -!- SUBUNIT: Homodimer (Probable). Interacts preferentially with
CC       nucleotide-depleted CDC42. {ECO:0000269|PubMed:12172552,
CC       ECO:0000269|PubMed:19745154, ECO:0000305}.
CC   -!- INTERACTION:
CC       Q9BZ29; Q15796: SMAD2; NbExp=3; IntAct=EBI-2695893, EBI-1040141;
CC       Q9BZ29; P84022: SMAD3; NbExp=3; IntAct=EBI-2695893, EBI-347161;
CC   -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000305}.
CC       Note=Associated with membranes. {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q9BZ29-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BZ29-5; Sequence=VSP_017128;
CC       Name=3;
CC         IsoId=Q9BZ29-3; Sequence=VSP_004024;
CC       Name=4;
CC         IsoId=Q9BZ29-4; Sequence=VSP_007709, VSP_007710;
CC       Name=5;
CC         IsoId=Q9BZ29-6; Sequence=VSP_017128, VSP_045683, VSP_045684;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in heart
CC       and placenta. Expressed at intermediate level in kidney, brain, lung
CC       and skeletal muscle. {ECO:0000269|PubMed:12172552}.
CC   -!- DOMAIN: The DOCKER domain is necessary and sufficient for the GEF
CC       activity.
CC   -!- MISCELLANEOUS: 'Zizim' means 'spike' in Hebrew. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 4]: Produced by exon skipping that results in a
CC       frameshift. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00983}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA83010.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF527605; AAM90306.1; -; mRNA.
DR   EMBL; AB028981; BAA83010.2; ALT_INIT; mRNA.
DR   EMBL; AK126492; BAG54337.1; -; mRNA.
DR   EMBL; AL139084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL161420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL391122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC043506; AAH43506.1; -; mRNA.
DR   CCDS; CCDS45062.1; -. [Q9BZ29-5]
DR   CCDS; CCDS45063.1; -. [Q9BZ29-6]
DR   CCDS; CCDS91829.1; -. [Q9BZ29-1]
DR   RefSeq; NP_001123520.1; NM_001130048.1. [Q9BZ29-5]
DR   RefSeq; NP_001123521.1; NM_001130049.1.
DR   RefSeq; NP_001123522.1; NM_001130050.1. [Q9BZ29-6]
DR   RefSeq; NP_001305778.1; NM_001318849.1.
DR   RefSeq; NP_056111.1; NM_015296.2. [Q9BZ29-1]
DR   PDB; 1WG7; NMR; -; A=165-301.
DR   PDB; 2WM9; X-ray; 2.20 A; A=1605-2067.
DR   PDB; 2WMN; X-ray; 2.39 A; A=1605-2067.
DR   PDB; 2WMO; X-ray; 2.20 A; A=1605-2067.
DR   PDBsum; 1WG7; -.
DR   PDBsum; 2WM9; -.
DR   PDBsum; 2WMN; -.
DR   PDBsum; 2WMO; -.
DR   AlphaFoldDB; Q9BZ29; -.
DR   SMR; Q9BZ29; -.
DR   BioGRID; 116930; 59.
DR   IntAct; Q9BZ29; 28.
DR   MINT; Q9BZ29; -.
DR   STRING; 9606.ENSP00000365643; -.
DR   GlyGen; Q9BZ29; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BZ29; -.
DR   PhosphoSitePlus; Q9BZ29; -.
DR   BioMuta; DOCK9; -.
DR   DMDM; 24212635; -.
DR   EPD; Q9BZ29; -.
DR   jPOST; Q9BZ29; -.
DR   MassIVE; Q9BZ29; -.
DR   MaxQB; Q9BZ29; -.
DR   PaxDb; 9606-ENSP00000365643; -.
DR   PeptideAtlas; Q9BZ29; -.
DR   ProteomicsDB; 20137; -.
DR   ProteomicsDB; 79758; -. [Q9BZ29-1]
DR   ProteomicsDB; 79759; -. [Q9BZ29-3]
DR   ProteomicsDB; 79760; -. [Q9BZ29-4]
DR   ProteomicsDB; 79761; -. [Q9BZ29-5]
DR   Pumba; Q9BZ29; -.
DR   Antibodypedia; 25029; 79 antibodies from 17 providers.
DR   DNASU; 23348; -.
DR   Ensembl; ENST00000376460.5; ENSP00000365643.1; ENSG00000088387.22. [Q9BZ29-5]
DR   Ensembl; ENST00000627024.2; ENSP00000487551.1; ENSG00000088387.22. [Q9BZ29-6]
DR   Ensembl; ENST00000652315.1; ENSP00000498761.1; ENSG00000088387.22. [Q9BZ29-1]
DR   GeneID; 23348; -.
DR   KEGG; hsa:23348; -.
DR   UCSC; uc058xyj.1; human. [Q9BZ29-1]
DR   AGR; HGNC:14132; -.
DR   CTD; 23348; -.
DR   DisGeNET; 23348; -.
DR   GeneCards; DOCK9; -.
DR   HGNC; HGNC:14132; DOCK9.
DR   HPA; ENSG00000088387; Low tissue specificity.
DR   MIM; 607325; gene.
DR   neXtProt; NX_Q9BZ29; -.
DR   OpenTargets; ENSG00000088387; -.
DR   PharmGKB; PA134877754; -.
DR   VEuPathDB; HostDB:ENSG00000088387; -.
DR   eggNOG; KOG1997; Eukaryota.
DR   GeneTree; ENSGT00940000155972; -.
DR   InParanoid; Q9BZ29; -.
DR   OrthoDB; 5480873at2759; -.
DR   PhylomeDB; Q9BZ29; -.
DR   TreeFam; TF313629; -.
DR   PathwayCommons; Q9BZ29; -.
DR   Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR   Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR   Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR   SignaLink; Q9BZ29; -.
DR   BioGRID-ORCS; 23348; 10 hits in 1155 CRISPR screens.
DR   ChiTaRS; DOCK9; human.
DR   EvolutionaryTrace; Q9BZ29; -.
DR   GeneWiki; Dock9; -.
DR   GenomeRNAi; 23348; -.
DR   Pharos; Q9BZ29; Tbio.
DR   PRO; PR:Q9BZ29; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q9BZ29; Protein.
DR   Bgee; ENSG00000088387; Expressed in calcaneal tendon and 207 other cell types or tissues.
DR   ExpressionAtlas; Q9BZ29; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd08697; C2_Dock-D; 1.
DR   CDD; cd11698; DHR2_DOCK9; 1.
DR   CDD; cd13267; PH_DOCK-D; 1.
DR   Gene3D; 1.20.58.740; -; 1.
DR   Gene3D; 1.25.40.410; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR037809; C2_Dock-D.
DR   InterPro; IPR027007; C2_DOCK-type_domain.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR026791; DOCK.
DR   InterPro; IPR021816; DOCK_C/D_N.
DR   InterPro; IPR043161; DOCK_C_lobe_A.
DR   InterPro; IPR043162; DOCK_C_lobe_C.
DR   InterPro; IPR027357; DOCKER_dom.
DR   InterPro; IPR046769; DOCKER_Lobe_A.
DR   InterPro; IPR046770; DOCKER_Lobe_B.
DR   InterPro; IPR046773; DOCKER_Lobe_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR23317; DEDICATOR OF CYTOKINESIS DOCK; 1.
DR   PANTHER; PTHR23317:SF77; DEDICATOR OF CYTOKINESIS PROTEIN 9; 1.
DR   Pfam; PF06920; DHR-2_Lobe_A; 1.
DR   Pfam; PF20422; DHR-2_Lobe_B; 1.
DR   Pfam; PF20421; DHR-2_Lobe_C; 1.
DR   Pfam; PF14429; DOCK-C2; 1.
DR   Pfam; PF11878; DOCK_C-D_N; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS51650; C2_DOCK; 1.
DR   PROSITE; PS51651; DOCKER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   Genevisible; Q9BZ29; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil;
KW   Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..2069
FT                   /note="Dedicator of cytokinesis protein 9"
FT                   /id="PRO_0000189999"
FT   DOMAIN          174..281
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          640..818
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00983"
FT   DOMAIN          1605..2069
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT   REGION          290..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1241..1282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1693..2069
FT                   /note="Interaction with CDC42"
FT                   /evidence="ECO:0000269|PubMed:12172552"
FT   COILED          1948..1982
FT                   /evidence="ECO:0000255"
FT   COILED          2034..2067
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        290..306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         170
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         433
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BIK4"
FT   MOD_RES         443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BIK4"
FT   MOD_RES         927
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1235
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         1241
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         1255
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1261
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BIK4"
FT   MOD_RES         1264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..43
FT                   /note="MSQPPLLPASAETRKFTRALSKPGTAAELRQSVSEVVRGSVLL -> MQADK
FT                   CRTSSRSVKKELVIESPLQYKDAAQGEVEAESPGPVP (in isoform 2 and
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10470851,
FT                   ECO:0000303|PubMed:14702039"
FT                   /id="VSP_017128"
FT   VAR_SEQ         1234..1254
FT                   /note="ASPYTTSTPNINSVRNADSRG -> GNAPCSCGLLSTITLKVSWSQ (in
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045683"
FT   VAR_SEQ         1255..2069
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045684"
FT   VAR_SEQ         1355..1378
FT                   /note="RTGMMHARLQQLGSLDNSLTFNHS -> SVRKISSVLGISVDNG (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_004024"
FT   VAR_SEQ         1791..1804
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_007709"
FT   VAR_SEQ         2068..2069
FT                   /note="LG -> ICPLEEKTSVLPNSLHIFNAISGTPTSTMVHGMTSSSSVV (in
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_007710"
FT   VARIANT         455
FT                   /note="A -> T (in dbSNP:rs56010605)"
FT                   /id="VAR_062000"
FT   VARIANT         1416
FT                   /note="K -> E (in dbSNP:rs16955934)"
FT                   /id="VAR_053067"
FT   CONFLICT        170
FT                   /note="S -> P (in Ref. 4; BAG54337)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        296
FT                   /note="S -> P (in Ref. 4; BAG54337)"
FT                   /evidence="ECO:0000305"
FT   STRAND          178..183
FT                   /evidence="ECO:0007829|PDB:1WG7"
FT   HELIX           190..194
FT                   /evidence="ECO:0007829|PDB:1WG7"
FT   STRAND          198..206
FT                   /evidence="ECO:0007829|PDB:1WG7"
FT   STRAND          208..210
FT                   /evidence="ECO:0007829|PDB:1WG7"
FT   STRAND          212..220
FT                   /evidence="ECO:0007829|PDB:1WG7"
FT   STRAND          227..230
FT                   /evidence="ECO:0007829|PDB:1WG7"
FT   TURN            232..234
FT                   /evidence="ECO:0007829|PDB:1WG7"
FT   STRAND          248..252
FT                   /evidence="ECO:0007829|PDB:1WG7"
FT   STRAND          254..256
FT                   /evidence="ECO:0007829|PDB:1WG7"
FT   STRAND          258..262
FT                   /evidence="ECO:0007829|PDB:1WG7"
FT   HELIX           266..291
FT                   /evidence="ECO:0007829|PDB:1WG7"
FT   HELIX           1610..1628
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1631..1651
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   STRAND          1677..1679
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1682..1685
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   TURN            1686..1688
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1690..1695
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   STRAND          1708..1710
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1711..1727
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1731..1733
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1734..1738
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   TURN            1739..1741
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1742..1747
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1751..1774
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   STRAND          1781..1788
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1808..1810
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   STRAND          1814..1820
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1825..1840
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1842..1844
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   STRAND          1845..1848
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1856..1858
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   STRAND          1863..1873
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1877..1882
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1887..1889
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   STRAND          1890..1902
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   STRAND          1904..1909
FT                   /evidence="ECO:0007829|PDB:2WMO"
FT   TURN            1912..1914
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   STRAND          1916..1929
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   STRAND          1931..1945
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1947..1967
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1973..1984
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   STRAND          1987..1989
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           1993..1999
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           2013..2037
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   TURN            2041..2043
FT                   /evidence="ECO:0007829|PDB:2WM9"
FT   HELIX           2044..2064
FT                   /evidence="ECO:0007829|PDB:2WM9"
SQ   SEQUENCE   2069 AA;  236446 MW;  95073CD751745AAE CRC64;
     MSQPPLLPAS AETRKFTRAL SKPGTAAELR QSVSEVVRGS VLLAKPKLIE PLDYENVIVQ
     KKTQILNDCL REMLLFPYDD FQTAILRRQG RYICSTVPAK AEEEAQSLFV TECIKTYNSD
     WHLVNYKYED YSGEFRQLPN KVVKLDKLPV HVYEVDEEVD KDEDAASLGS QKGGITKHGW
     LYKGNMNSAI SVTMRSFKRR FFHLIQLGDG SYNLNFYKDE KISKEPKGSI FLDSCMGVVQ
     NNKVRRFAFE LKMQDKSSYL LAADSEVEME EWITILNKIL QLNFEAAMQE KRNGDSHEDD
     EQSKLEGSGS GLDSYLPELA KSAREAEIKL KSESRVKLFY LDPDAQKLDF SSAEPEVKSF
     EEKFGKRILV KCNDLSFNLQ CCVAENEEGP TTNVEPFFVT LSLFDIKYNR KISADFHVDL
     NHFSVRQMLA TTSPALMNGS GQSPSVLKGI LHEAAMQYPK QGIFSVTCPH PDIFLVARIE
     KVLQGSITHC AEPYMKSSDS SKVAQKVLKN AKQACQRLGQ YRMPFAWAAR TLFKDASGNL
     DKNARFSAIY RQDSNKLSND DMLKLLADFR KPEKMAKLPV ILGNLDITID NVSSDFPNYV
     NSSYIPTKQF ETCSKTPITF EVEEFVPCIP KHTQPYTIYT NHLYVYPKYL KYDSQKSFAK
     ARNIAICIEF KDSDEEDSQP LKCIYGRPGG PVFTRSAFAA VLHHHQNPEF YDEIKIELPT
     QLHEKHHLLL TFFHVSCDNS SKGSTKKRDV VETQVGYSWL PLLKDGRVVT SEQHIPVSAN
     LPSGYLGYQE LGMGRHYGPE IKWVDGGKPL LKISTHLVST VYTQDQHLHN FFQYCQKTES
     GAQALGNELV KYLKSLHAME GHVMIAFLPT ILNQLFRVLT RATQEEVAVN VTRVIIHVVA
     QCHEEGLESH LRSYVKYAYK AEPYVASEYK TVHEELTKSM TTILKPSADF LTSNKLLKYS
     WFFFDVLIKS MAQHLIENSK VKLLRNQRFP ASYHHAVETV VNMLMPHITQ KFRDNPEASK
     NANHSLAVFI KRCFTFMDRG FVFKQINNYI SCFAPGDPKT LFEYKFEFLR VVCNHEHYIP
     LNLPMPFGKG RIQRYQDLQL DYSLTDEFCR NHFLVGLLLR EVGTALQEFR EVRLIAISVL
     KNLLIKHSFD DRYASRSHQA RIATLYLPLF GLLIENVQRI NVRDVSPFPV NAGMTVKDES
     LALPAVNPLV TPQKGSTLDN SLHKDLLGAI SGIASPYTTS TPNINSVRNA DSRGSLISTD
     SGNSLPERNS EKSNSLDKHQ QSSTLGNSVV RCDKLDQSEI KSLLMCFLYI LKSMSDDALF
     TYWNKASTSE LMDFFTISEV CLHQFQYMGK RYIARTGMMH ARLQQLGSLD NSLTFNHSYG
     HSDADVLHQS LLEANIATEV CLTALDTLSL FTLAFKNQLL ADHGHNPLMK KVFDVYLCFL
     QKHQSETALK NVFTALRSLI YKFPSTFYEG RADMCAALCY EILKCCNSKL SSIRTEASQL
     LYFLMRNNFD YTGKKSFVRT HLQVIISVSQ LIADVVGIGG TRFQQSLSII NNCANSDRLI
     KHTSFSSDVK DLTKRIRTVL MATAQMKEHE NDPEMLVDLQ YSLAKSYAST PELRKTWLDS
     MARIHVKNGD LSEAAMCYVH VTALVAEYLT RKEAVQWEPP LLPHSHSACL RRSRGGVFRQ
     GCTAFRVITP NIDEEASMME DVGMQDVHFN EDVLMELLEQ CADGLWKAER YELIADIYKL
     IIPIYEKRRD FERLAHLYDT LHRAYSKVTE VMHSGRRLLG TYFRVAFFGQ AAQYQFTDSE
     TDVEGFFEDE DGKEYIYKEP KLTPLSEISQ RLLKLYSDKF GSENVKMIQD SGKVNPKDLD
     SKYAYIQVTH VIPFFDEKEL QERKTEFERS HNIRRFMFEM PFTQTGKRQG GVEEQCKRRT
     ILTAIHCFPY VKKRIPVMYQ HHTDLNPIEV AIDEMSKKVA ELRQLCSSAE VDMIKLQLKL
     QGSVSVQVNA GPLAYARAFL DDTNTKRYPD NKVKLLKEVF RQFVEACGQA LAVNERLIKE
     DQLEYQEEMK ANYREMAKEL SEIMHEQLG
//