DOC10_HUMAN
ID DOC10_HUMAN Reviewed; 2186 AA.
AC Q96BY6; B3FL70; O75178; Q68DA4; Q9NW06; Q9NXI8;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Dedicator of cytokinesis protein 10 {ECO:0000305};
DE AltName: Full=Zizimin-3;
GN Name=DOCK10 {ECO:0000312|HGNC:HGNC:23479}; Synonyms=KIAA0694, ZIZ3;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INDUCTION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18499258; DOI=10.1016/j.molimm.2008.04.003;
RA Yelo E., Bernardo M.V., Gimeno L., Alcaraz-Garcia M.J., Majado M.J.,
RA Parrado A.;
RT "Dock10, a novel CZH protein selectively induced by interleukin-4 in human
RT B lymphocytes.";
RL Mol. Immunol. 45:3411-3418(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=21514340; DOI=10.1016/j.humimm.2011.03.024;
RA Alcaraz-Garcia M.J., Ruiz-Lafuente N., Sebastian-Ruiz S., Majado M.J.,
RA Gonzalez-Garcia C., Bernardo M.V., Alvarez-Lopez M.R., Parrado A.;
RT "Human and mouse DOCK10 splicing isoforms with alternative first coding
RT exon usage are differentially expressed in T and B lymphocytes.";
RL Hum. Immunol. 72:531-537(2011).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1599-2186 (ISOFORM 1).
RC TISSUE=Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1599-2186 (ISOFORM 1).
RC TISSUE=Colon mucosa, and Teratocarcinoma;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 977-2186.
RC TISSUE=Bone marrow;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [9]
RP NOMENCLATURE.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1292; SER-1295 AND SER-1318,
RP AND 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1292 AND SER-1295, AND
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1232; SER-1292; SER-1295;
RP SER-1318 AND THR-1440, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-834, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
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).
CC -!- FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates CDC42
CC and RAC1 by exchanging bound GDP for free GTP. Essential for dendritic
CC spine morphogenesis in Purkinje cells and in hippocampal neurons, via a
CC CDC42-mediated pathway. Sustains B-cell lymphopoiesis in secondary
CC lymphoid tissues and regulates FCER2/CD23 expression.
CC {ECO:0000250|UniProtKB:Q8BZN6}.
CC -!- INTERACTION:
CC Q96BY6; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-748520, EBI-10171570;
CC Q96BY6; P43364: MAGEA11; NbExp=3; IntAct=EBI-748520, EBI-739552;
CC Q96BY6; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-748520, EBI-5280197;
CC Q96BY6; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-748520, EBI-2623095;
CC Q96BY6-3; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-10282566, EBI-10178634;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18499258}. Cytoplasm
CC {ECO:0000269|PubMed:18499258}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q8BZN6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=DOCK10.1;
CC IsoId=Q96BY6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96BY6-2; Sequence=VSP_007716, VSP_007717;
CC Name=3; Synonyms=DOCK10.2;
CC IsoId=Q96BY6-3; Sequence=VSP_047731;
CC -!- TISSUE SPECIFICITY: Expressed at low level in brain and lung. Isoform 1
CC is enriched in normal T-cells, isoform 3 is enriched in normal B-cells
CC and chronic lymphocytic leukemia (CLL) B-cells.
CC {ECO:0000269|PubMed:18499258, ECO:0000269|PubMed:21514340,
CC ECO:0000269|PubMed:9734811}.
CC -!- INDUCTION: Isoforms 1 and 2 are up-regulated in response to IL4 in B-
CC cells but not T-cells. {ECO:0000269|PubMed:18499258,
CC ECO:0000269|PubMed:21514340}.
CC -!- DOMAIN: The DOCKER domain may mediate some GEF activity.
CC {ECO:0000250|UniProtKB:Q8BZN6}.
CC -!- MISCELLANEOUS: 'Zizim' means 'spike' in Hebrew. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000255|PROSITE-
CC ProRule:PRU00983}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15018.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA31669.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91022.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA91583.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH18316.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB014594; BAA31669.2; ALT_INIT; mRNA.
DR EMBL; EU236710; ABY70713.2; -; mRNA.
DR EMBL; AC011739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC017095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015018; AAH15018.1; ALT_INIT; mRNA.
DR EMBL; AK000227; BAA91022.1; ALT_FRAME; mRNA.
DR EMBL; AK001253; BAA91583.1; ALT_INIT; mRNA.
DR EMBL; CR749492; CAH18316.1; ALT_INIT; mRNA.
DR CCDS; CCDS46528.1; -. [Q96BY6-1]
DR CCDS; CCDS74661.1; -. [Q96BY6-3]
DR RefSeq; NP_001277192.1; NM_001290263.1. [Q96BY6-3]
DR RefSeq; NP_055504.2; NM_014689.2. [Q96BY6-1]
DR PDB; 6TKY; X-ray; 2.55 A; A=1694-2151, B=1694-2150.
DR PDB; 6TKZ; X-ray; 2.64 A; A/B=1694-2151.
DR PDB; 6TM1; X-ray; 3.71 A; B=1694-2150, C=1694-2151.
DR PDBsum; 6TKY; -.
DR PDBsum; 6TKZ; -.
DR PDBsum; 6TM1; -.
DR AlphaFoldDB; Q96BY6; -.
DR SMR; Q96BY6; -.
DR BioGRID; 120758; 18.
DR IntAct; Q96BY6; 9.
DR STRING; 9606.ENSP00000258390; -.
DR GlyGen; Q96BY6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96BY6; -.
DR PhosphoSitePlus; Q96BY6; -.
DR BioMuta; DOCK10; -.
DR DMDM; 332278210; -.
DR EPD; Q96BY6; -.
DR jPOST; Q96BY6; -.
DR MassIVE; Q96BY6; -.
DR MaxQB; Q96BY6; -.
DR PaxDb; Q96BY6; -.
DR PeptideAtlas; Q96BY6; -.
DR PRIDE; Q96BY6; -.
DR ProteomicsDB; 3476; -.
DR ProteomicsDB; 76127; -. [Q96BY6-1]
DR ProteomicsDB; 76128; -. [Q96BY6-2]
DR Antibodypedia; 34369; 65 antibodies from 15 providers.
DR DNASU; 55619; -.
DR Ensembl; ENST00000258390.12; ENSP00000258390.7; ENSG00000135905.20. [Q96BY6-1]
DR Ensembl; ENST00000409592.7; ENSP00000386694.3; ENSG00000135905.20. [Q96BY6-3]
DR GeneID; 55619; -.
DR KEGG; hsa:55619; -.
DR MANE-Select; ENST00000258390.12; ENSP00000258390.7; NM_014689.3; NP_055504.2.
DR UCSC; uc002vob.3; human. [Q96BY6-1]
DR CTD; 55619; -.
DR DisGeNET; 55619; -.
DR GeneCards; DOCK10; -.
DR HGNC; HGNC:23479; DOCK10.
DR HPA; ENSG00000135905; Tissue enhanced (brain, lymphoid tissue).
DR MIM; 611518; gene.
DR neXtProt; NX_Q96BY6; -.
DR OpenTargets; ENSG00000135905; -.
DR PharmGKB; PA134983197; -.
DR VEuPathDB; HostDB:ENSG00000135905; -.
DR eggNOG; KOG1997; Eukaryota.
DR GeneTree; ENSGT00940000157469; -.
DR HOGENOM; CLU_000624_1_0_1; -.
DR InParanoid; Q96BY6; -.
DR OMA; FEIMIKS; -.
DR OrthoDB; 20156at2759; -.
DR PhylomeDB; Q96BY6; -.
DR TreeFam; TF313629; -.
DR PathwayCommons; Q96BY6; -.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q96BY6; -.
DR SIGNOR; Q96BY6; -.
DR BioGRID-ORCS; 55619; 19 hits in 1071 CRISPR screens.
DR ChiTaRS; DOCK10; human.
DR GeneWiki; Dock10; -.
DR GenomeRNAi; 55619; -.
DR Pharos; Q96BY6; Tbio.
DR PRO; PR:Q96BY6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96BY6; protein.
DR Bgee; ENSG00000135905; Expressed in corpus callosum and 163 other tissues.
DR ExpressionAtlas; Q96BY6; baseline and differential.
DR Genevisible; Q96BY6; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0001782; P:B cell homeostasis; ISS:UniProtKB.
DR GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0002315; P:marginal zone B cell differentiation; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IDA: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; 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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR23317; PTHR23317; 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 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; Acetylation; Alternative splicing; Cell projection;
KW Cytoplasm; Guanine-nucleotide releasing factor; Nucleus; Phosphoprotein;
KW Reference proteome; Synapse.
FT CHAIN 1..2186
FT /note="Dedicator of cytokinesis protein 10"
FT /id="PRO_0000190002"
FT DOMAIN 181..290
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 672..850
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00983"
FT DOMAIN 1690..2150
FT /note="DOCKER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT REGION 158..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZN6"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZN6"
FT MOD_RES 368
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZN6"
FT MOD_RES 834
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 877
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZN6"
FT MOD_RES 1232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZN6"
FT MOD_RES 1292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:19690332"
FT MOD_RES 1295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:19690332"
FT MOD_RES 1318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 1406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZN6"
FT MOD_RES 1440
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..41
FT /note="MAGERTRRFTRSLLRPGQAAELRHSAASAAAVAVSSRQQQR -> MSFRGKV
FT FKREPSEFWKKRRTVRRVNQEEIHRFSS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:21514340"
FT /id="VSP_047731"
FT VAR_SEQ 565..593
FT /note="FKDNQGNVDRDSRFSPLFRQESSKISTED -> DSCSQQTRNTFNGGIGSFS
FT FERFCVAYYF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9734811"
FT /id="VSP_007716"
FT VAR_SEQ 594..2186
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9734811"
FT /id="VSP_007717"
FT CONFLICT 563
FT /note="S -> Y (in Ref. 1; BAA31669)"
FT /evidence="ECO:0000305"
FT CONFLICT 1833
FT /note="N -> D (in Ref. 7; BAA91583)"
FT /evidence="ECO:0000305"
FT CONFLICT 1966
FT /note="T -> S (in Ref. 7; BAA91022)"
FT /evidence="ECO:0000305"
FT CONFLICT 2062
FT /note="Q -> R (in Ref. 8; CAH18316)"
FT /evidence="ECO:0000305"
FT CONFLICT 2093
FT /note="Q -> R (in Ref. 8; CAH18316)"
FT /evidence="ECO:0000305"
FT HELIX 1696..1713
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 1716..1736
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 1773..1775
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 1777..1780
FT /evidence="ECO:0007829|PDB:6TKY"
FT TURN 1781..1783
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 1785..1791
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 1806..1822
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 1826..1828
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 1829..1843
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 1846..1864
FT /evidence="ECO:0007829|PDB:6TKY"
FT TURN 1865..1868
FT /evidence="ECO:0007829|PDB:6TKY"
FT STRAND 1876..1883
FT /evidence="ECO:0007829|PDB:6TKY"
FT TURN 1885..1887
FT /evidence="ECO:0007829|PDB:6TKY"
FT TURN 1890..1893
FT /evidence="ECO:0007829|PDB:6TKY"
FT STRAND 1895..1901
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 1906..1921
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 1923..1925
FT /evidence="ECO:0007829|PDB:6TKY"
FT STRAND 1926..1929
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 1937..1939
FT /evidence="ECO:0007829|PDB:6TKY"
FT STRAND 1944..1954
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 1958..1961
FT /evidence="ECO:0007829|PDB:6TKY"
FT TURN 1967..1970
FT /evidence="ECO:0007829|PDB:6TKY"
FT STRAND 1971..1983
FT /evidence="ECO:0007829|PDB:6TKY"
FT STRAND 1985..1987
FT /evidence="ECO:0007829|PDB:6TKY"
FT TURN 1993..1995
FT /evidence="ECO:0007829|PDB:6TKY"
FT STRAND 1997..2010
FT /evidence="ECO:0007829|PDB:6TKY"
FT STRAND 2012..2026
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 2028..2048
FT /evidence="ECO:0007829|PDB:6TKY"
FT STRAND 2049..2051
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 2054..2065
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 2074..2080
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 2083..2086
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 2091..2116
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 2121..2123
FT /evidence="ECO:0007829|PDB:6TKY"
FT HELIX 2124..2145
FT /evidence="ECO:0007829|PDB:6TKY"
SQ SEQUENCE 2186 AA; 249531 MW; 955ABC03DE2270AF CRC64;
MAGERTRRFT RSLLRPGQAA ELRHSAASAA AVAVSSRQQQ RQEKPRLLEP LDYETVIEEL
EKTYRNDPLQ DLLFFPSDDF SAATVSWDIR TLYSTVPEDA EHKAENLLVK EACKFYSSQW
HVVNYKYEQY SGDIRQLPRA EYKPEKLPSH SFEIDHEDAD KDEDTTSHSS SKGGGGAGGT
GVFKSGWLYK GNFNSTVNNT VTVRSFKKRY FQLTQLPDNS YIMNFYKDEK ISKEPKGCIF
LDSCTGVVQN NRLRKYAFEL KMNDLTYFVL AAETESDMDE WIHTLNRILQ ISPEGPLQGR
RSTELTDLGL DSLDNSVTCE CTPEETDSSE NNLHADFAKY LTETEDTVKT TRNMERLNLF
SLDPDIDTLK LQKKDLLEPE SVIKPFEEKA AKRIMIICKA LNSNLQGCVT ENENDPITNI
EPFFVSVALY DLRDSRKISA DFHVDLNHAA VRQMLLGASV ALENGNIDTI TPRQSEEPHI
KGLPEEWLKF PKQAVFSVSN PHSEIVLVAK IEKVLMGNIA SGAEPYIKNP DSNKYAQKIL
KSNRQFCSKL GKYRMPFAWA VRSVFKDNQG NVDRDSRFSP LFRQESSKIS TEDLVKLVSD
YRRADRISKM QTIPGSLDIA VDNVPLEHPN CVTSSFIPVK PFNMMAQTEP TVEVEEFVYD
STKYCRPYRV YKNQIYIYPK HLKYDSQKCF NKARNITVCI EFKNSDEESA KPLKCIYGKP
GGPLFTSAAY TAVLHHSQNP DFSDEVKIEL PTQLHEKHHI LFSFYHVTCD INAKANAKKK
EALETSVGYA WLPLMKHDQI ASQEYNIPIA TSLPPNYLSF QDSASGKHGG SDIKWVDGGK
PLFKVSTFVV STVNTQDPHV NAFFQECQKR EKDMSQSPTS NFIRSCKNLL NVEKIHAIMS
FLPIILNQLF KVLVQNEEDE ITTTVTRVLT DIVAKCHEEQ LDHSVQSYIK FVFKTRACKE
RTVHEELAKN VTGLLKSNDS TTVKHVLKHS WFFFAIILKS MAQHLIDTNK IQLPRPQRFP
ESYQNELDNL VMVLSDHVIW KYKDALEETR RANHSVARFL KRCFTFMDRG YVFKMVNNYI
SMFSSGDLKT LCQYKFDFLQ EVCQHEHFIP LCLPIRSANI PDPLTPSEST QELHASDMPE
YSVTNEFCRK HFLIGILLRE VGFALQEDQD VRHLALAVLK NLMAKHSFDD RYREPRKQAQ
IASLYMPLYG MLLDNMPRIY LKDLYPFTVN TSNQGSRDDL STNGGFQSQT AIKHANSVDT
SFSKDVLNSI AAFSSIAIST VNHADSRASL ASLDSNPSTN EKSSEKTDNC EKIPRPLSLI
GSTLRFDKLD QAETRSLLMC FLHIMKTISY ETLIAYWQRA PSPEVSDFFS ILDVCLQNFR
YLGKRNIIRK IAAAFKFVQS TQNNGTLKGS NPSCQTSGLL SQWMHSTSSH EGHKQHRSQT
LPIIRGKNAL SNPKLLQMLD NTMTSNSNEI DIVHHVDTEA NIATEVCLTI LDLLSLFTQT
HQRQLQQCDC QNSLMKRVFD TYMLFFQVNQ SATALKHVFA SLRLFVCKFP SAFFQGPADL
CGSFCYEVLK CCNHRSRSTQ TEASALLYFF MRKNFEFNKQ KSIVRSHLQL IKAVSQLIAD
AGIGGSRFQH SLAITNNFAN GDKQMKNSNF PAEVKDLTKR IRTVLMATAQ MKEHEKDPEM
LVDLQYSLAN SYASTPELRR TWLESMAKIH ARNGDLSEAA MCYIHIAALI AEYLKRKGYW
KVEKICTASL LSEDTHPCDS NSLLTTPSGG SMFSMGWPAF LSITPNIKEE GAMKEDSGMQ
DTPYNENILV EQLYMCVEFL WKSERYELIA DVNKPIIAVF EKQRDFKKLS DLYYDIHRSY
LKVAEVVNSE KRLFGRYYRV AFYGQGFFEE EEGKEYIYKE PKLTGLSEIS QRLLKLYADK
FGADNVKIIQ DSNKVNPKDL DPKYAYIQVT YVTPFFEEKE IEDRKTDFEM HHNINRFVFE
TPFTLSGKKH GGVAEQCKRR TILTTSHLFP YVKKRIQVIS QSSTELNPIE VAIDEMSKKV
SELNQLCTME EVDMIRLQLK LQGSVSVKVN AGPMAYARAF LEETNAKKYP DNQVKLLKEI
FRQFADACGQ ALDVNERLIK EDQLEYQEEL RSHYKDMLSE LSTVMNEQIT GRDDLSKRGV
DQTCTRVISK ATPALPTVSI SSSAEV
