DOCK9_HUMAN
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 03-AUG-2022, entry version 178.
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 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; 55.
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; Q9BZ29; -.
DR PeptideAtlas; Q9BZ29; -.
DR PRIDE; 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 Antibodypedia; 25029; 57 antibodies from 17 providers.
DR DNASU; 23348; -.
DR Ensembl; ENST00000376460.5; ENSP00000365643.1; ENSG00000088387.21. [Q9BZ29-5]
DR Ensembl; ENST00000627024.2; ENSP00000487551.1; ENSG00000088387.21. [Q9BZ29-6]
DR Ensembl; ENST00000652315.1; ENSP00000498761.1; ENSG00000088387.21. [Q9BZ29-1]
DR GeneID; 23348; -.
DR KEGG; hsa:23348; -.
DR UCSC; uc058xyj.1; human. [Q9BZ29-1]
DR CTD; 23348; -.
DR DisGeNET; 23348; -.
DR GeneCards; DOCK9; -.
DR HGNC; HGNC:14132; DOCK9.
DR HPA; ENSG00000088387; Tissue enhanced (brain).
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; 20156at2759; -.
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 1077 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 205 other tissues.
DR ExpressionAtlas; Q9BZ29; baseline and differential.
DR Genevisible; Q9BZ29; HS.
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 Gene3D; 1.20.58.740; -; 1.
DR Gene3D; 1.25.40.410; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 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; IPR026796; DOCK9.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR23317; PTHR23317; 1.
DR PANTHER; PTHR23317:SF77; PTHR23317:SF77; 1.
DR Pfam; PF06920; DHR-2; 1.
DR Pfam; PF14429; DOCK-C2; 1.
DR Pfam; PF11878; DUF3398; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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
