ID   DOC11_HUMAN             Reviewed;        2073 AA.
AC   Q5JSL3; A6NMF0; Q66M66; Q6ZUJ5; Q86VU8; Q96MN3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Dedicator of cytokinesis protein 11 {ECO:0000305};
DE   AltName: Full=Activated Cdc42-associated guanine nucleotide exchange factor;
DE            Short=ACG;
DE   AltName: Full=Zizimin-2 {ECO:0000305};
GN   Name=DOCK11 {ECO:0000312|HGNC:HGNC:23483};
GN   Synonyms=ZIZ2 {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 [MRNA].
RC   TISSUE=Brain;
RX   PubMed=16968698; DOI=10.1074/jbc.m606248200;
RA   Lin Q., Yang W., Baird D., Feng Q., Cerione R.A.;
RT   "Identification of a DOCK180-related guanine nucleotide exchange factor
RT   that is capable of mediating a positive feedback activation of Cdc42.";
RL   J. Biol. Chem. 281:35253-35262(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 811-2073.
RC   TISSUE=Synovium;
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 MRNA] OF 1283-2073.
RC   TISSUE=Testis;
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-248 AND SER-440, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [8]
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   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-16; SER-23; SER-306;
RP   SER-440; SER-1237 AND SER-1240, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND IDENTIFICATION BY
RP   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   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [13]
RP   VARIANTS SER-275; TYR-414; ARG-1298; ARG-1336; GLN-1366; SER-1706 AND
RP   CYS-1885, AND INVOLVEMENT IN AUTOIMMUNE DISEASE.
RX   PubMed=36952639; DOI=10.1182/blood.2022018486;
RA   Boussard C., Delage L., Gajardo T., Kauskot A., Batignes M., Goudin N.,
RA   Stolzenberg M.C., Brunaud C., Panikulam P., Riller Q., Moya-Nilges M.,
RA   Solarz J., Reperant C., Durel B., Bordet J.C., Pelle O., Lebreton C.,
RA   Magerus A., Pirabakaran V., Vargas P., Dupichaud S., Jeanpierre M.,
RA   Vinit A., Zarhrate M., Masson C., Aladjidi N., Arkwright P.D.,
RA   Bader-Meunier B., Baron Joly S., Benadiba J., Bernard E., Berrebi D.,
RA   Bodemer C., Castelle M., Charbit-Henrion F., Chbihi M., Debray A.,
RA   Drabent P., Fraitag S., Hie M., Landman-Parker J., Lhermitte L.,
RA   Moshous D., Rohrlich P., Ruemmele F., Welfringer-Morin A., Tusseau M.,
RA   Belot A., Cerf-Bensussan N., Roelens M., Picard C., Neven B., Fischer A.,
RA   Callebaut I., Menager M.M., Sepulveda F.E., Adam F., Rieux-Laucat F.;
RT   "DOCK11 deficiency in patients with X-linked actinopathy and
RT   autoimmunity.";
RL   Blood 141:2713-2726(2023).
CC   -!- FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates CDC42
CC       by exchanging bound GDP for free GTP. Required for marginal zone (MZ)
CC       B-cell development, is associated with early bone marrow B-cell
CC       development, MZ B-cell formation, MZ B-cell number and marginal
CC       metallophilic macrophages morphology. Facilitates filopodia formation
CC       through the activation of CDC42. {ECO:0000250|UniProtKB:A2AF47}.
CC   -!- SUBUNIT: Interacts with CDC42. {ECO:0000250|UniProtKB:A2AF47}.
CC   -!- DOMAIN: The DOCKER domain is necessary for the GEF activity. The DOCKER
CC       domain mediates interaction with activated CDC42 in conjunction with
CC       residues 66-126. {ECO:0000250|UniProtKB:A2AF47}.
CC   -!- DISEASE: Note=DOCK11 variants have been found in several patients with
CC       an early-onset autoimmune disease characterized by cytopenia, systemic
CC       lupus erythematosus, inflammatory bowel disease, and immune-related
CC       skin manifestations. {ECO:0000269|PubMed:36952639}.
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=BAB71253.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC86230.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY692226; AAU04438.1; -; mRNA.
DR   EMBL; AC007021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL391237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL391280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471161; EAW89895.1; -; Genomic_DNA.
DR   EMBL; AK056684; BAB71253.1; ALT_INIT; mRNA.
DR   EMBL; AK125641; BAC86230.1; ALT_INIT; mRNA.
DR   EMBL; BC047713; AAH47713.1; -; mRNA.
DR   CCDS; CCDS35373.1; -.
DR   RefSeq; NP_653259.3; NM_144658.3.
DR   AlphaFoldDB; Q5JSL3; -.
DR   SMR; Q5JSL3; -.
DR   BioGRID; 126589; 43.
DR   IntAct; Q5JSL3; 21.
DR   MINT; Q5JSL3; -.
DR   STRING; 9606.ENSP00000276202; -.
DR   GlyCosmos; Q5JSL3; 1 site, 2 glycans.
DR   GlyGen; Q5JSL3; 1 site, 2 O-linked glycans (1 site).
DR   iPTMnet; Q5JSL3; -.
DR   MetOSite; Q5JSL3; -.
DR   PhosphoSitePlus; Q5JSL3; -.
DR   BioMuta; DOCK11; -.
DR   DMDM; 158563857; -.
DR   EPD; Q5JSL3; -.
DR   jPOST; Q5JSL3; -.
DR   MassIVE; Q5JSL3; -.
DR   MaxQB; Q5JSL3; -.
DR   PaxDb; 9606-ENSP00000276202; -.
DR   PeptideAtlas; Q5JSL3; -.
DR   ProteomicsDB; 63163; -.
DR   Pumba; Q5JSL3; -.
DR   Antibodypedia; 29701; 67 antibodies from 17 providers.
DR   DNASU; 139818; -.
DR   Ensembl; ENST00000276202.9; ENSP00000276202.7; ENSG00000147251.16.
DR   GeneID; 139818; -.
DR   KEGG; hsa:139818; -.
DR   MANE-Select; ENST00000276202.9; ENSP00000276202.7; NM_144658.4; NP_653259.3.
DR   UCSC; uc004eqp.3; human.
DR   AGR; HGNC:23483; -.
DR   CTD; 139818; -.
DR   DisGeNET; 139818; -.
DR   GeneCards; DOCK11; -.
DR   HGNC; HGNC:23483; DOCK11.
DR   HPA; ENSG00000147251; Tissue enhanced (adipose).
DR   MalaCards; DOCK11; -.
DR   MIM; 300681; gene.
DR   neXtProt; NX_Q5JSL3; -.
DR   OpenTargets; ENSG00000147251; -.
DR   PharmGKB; PA128394757; -.
DR   VEuPathDB; HostDB:ENSG00000147251; -.
DR   eggNOG; KOG1997; Eukaryota.
DR   GeneTree; ENSGT00940000155658; -.
DR   InParanoid; Q5JSL3; -.
DR   OrthoDB; 5480873at2759; -.
DR   PhylomeDB; Q5JSL3; -.
DR   TreeFam; TF313629; -.
DR   PathwayCommons; Q5JSL3; -.
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; Q5JSL3; -.
DR   BioGRID-ORCS; 139818; 13 hits in 778 CRISPR screens.
DR   ChiTaRS; DOCK11; human.
DR   GeneWiki; Dock11; -.
DR   GenomeRNAi; 139818; -.
DR   Pharos; Q5JSL3; Tdark.
DR   PRO; PR:Q5JSL3; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q5JSL3; Protein.
DR   Bgee; ENSG00000147251; Expressed in parietal pleura and 179 other cell types or tissues.
DR   ExpressionAtlas; Q5JSL3; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR   GO; GO:0001782; P:B cell homeostasis; ISS:UniProtKB.
DR   GO; GO:0002315; P:marginal zone B cell differentiation; ISS:UniProtKB.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IMP: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; cd11700; DHR2_DOCK11; 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:SF81; DEDICATOR OF CYTOKINESIS PROTEIN 11; 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; Q5JSL3; HS.
PE   1: Evidence at protein level;
KW   Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome.
FT   CHAIN           1..2073
FT                   /note="Dedicator of cytokinesis protein 11"
FT                   /id="PRO_0000299558"
FT   DOMAIN          165..272
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          1609..2036
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT   REGION          1226..1267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1251..1267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         16
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   MOD_RES         248
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         306
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         440
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         445
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A2AF47"
FT   MOD_RES         1237
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1240
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         275
FT                   /note="T -> S (found in a patient with autoimmune
FT                   manifestations; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36952639"
FT                   /id="VAR_088240"
FT   VARIANT         414
FT                   /note="D -> Y (found in a patient with autoimmune
FT                   manifestations; uncertain significance; decreased
FT                   expression in patient platelets and activated T-cells;
FT                   decreased CDC42 activation in patient platelets)"
FT                   /evidence="ECO:0000269|PubMed:36952639"
FT                   /id="VAR_088241"
FT   VARIANT         813
FT                   /note="I -> F (in dbSNP:rs16995229)"
FT                   /id="VAR_034854"
FT   VARIANT         1298
FT                   /note="L -> R (found in a patient with autoimmune
FT                   manifestations; uncertain significance; decreased
FT                   expression in patient platelets and activated T-cells;
FT                   impaired CDC42 activation in patient platelets)"
FT                   /evidence="ECO:0000269|PubMed:36952639"
FT                   /id="VAR_088242"
FT   VARIANT         1336
FT                   /note="H -> R (found in a patient with autoimmune
FT                   manifestations; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36952639"
FT                   /id="VAR_088243"
FT   VARIANT         1366
FT                   /note="R -> Q (found in a patient with autoimmune
FT                   manifestations; uncertain significance; decreased CDC42
FT                   activation in patient platelets)"
FT                   /evidence="ECO:0000269|PubMed:36952639"
FT                   /id="VAR_088244"
FT   VARIANT         1706
FT                   /note="L -> S (found in a patient with autoimmune
FT                   manifestations; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36952639"
FT                   /id="VAR_088245"
FT   VARIANT         1885
FT                   /note="R -> C (found in a patient with autoimmune
FT                   manifestations; uncertain significance; decreased CDC42
FT                   activation in patient platelets)"
FT                   /evidence="ECO:0000269|PubMed:36952639"
FT                   /id="VAR_088246"
FT   CONFLICT        376
FT                   /note="F -> L (in Ref. 1; AAU04438)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        740
FT                   /note="N -> K (in Ref. 1; AAU04438)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1984
FT                   /note="K -> E (in Ref. 1; AAU04438 and 4; BAB71253)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2073 AA;  237671 MW;  558FC01EE5D23B6E CRC64;
     MAEVRKFTKR LSKPGTAAEL RQSVSEAVRG SVVLEKAKVV EPLDYENVIA QRKTQIYSDP
     LRDLLMFPME DISISVIGRQ RRTVQSTVPE DAEKRAQSLF VKECIKTYST DWHVVNYKYE
     DFSGDFRMLP CKSLRPEKIP NHVFEIDEDC EKDEDSSSLC SQKGGVIKQG WLHKANVNST
     ITVTMKVFKR RYFYLTQLPD GSYILNSYKD EKNSKESKGC IYLDACIDVV QCPKMRRHAF
     ELKMLDKYSH YLAAETEQEM EEWLITLKKI IQINTDSLVQ EKKETVETAQ DDETSSQGKA
     ENIMASLERS MHPELMKYGR ETEQLNKLSR GDGRQNLFSF DSEVQRLDFS GIEPDIKPFE
     EKCNKRFLVN CHDLTFNILG QIGDNAKGPP TNVEPFFINL ALFDVKNNCK ISADFHVDLN
     PPSVREMLWG SSTQLASDGS PKGSSPESYI HGIAESQLRY IQQGIFSVTN PHPEIFLVAR
     IEKVLQGNIT HCAEPYIKNS DPVKTAQKVH RTAKQVCSRL GQYRMPFAWA ARPIFKDTQG
     SLDLDGRFSP LYKQDSSKLS SEDILKLLSE YKKPEKTKLQ IIPGQLNITV ECVPVDLSNC
     ITSSYVPLKP FEKNCQNITV EVEEFVPEMT KYCYPFTIYK NHLYVYPLQL KYDSQKTFAK
     ARNIAVCVEF RDSDESDASA LKCIYGKPAG SVFTTNAYAV VSHHNQNPEF YDEIKIELPI
     HLHQKHHLLF TFYHVSCEIN TKGTTKKQDT VETPVGFAWV PLLKDGRIIT FEQQLPVSAN
     LPPGYLNLND AESRRQCNVD IKWVDGAKPL LKIKSHLEST IYTQDLHVHK FFHHCQLIQS
     GSKEVPGELI KYLKCLHAME IQVMIQFLPV ILMQLFRVLT NMTHEDDVPI NCTMVLLHIV
     SKCHEEGLDS YLRSFIKYSF RPEKPSAPQA QLIHETLATT MIAILKQSAD FLSINKLLKY
     SWFFFEIIAK SMATYLLEEN KIKLPRGQRF PETYHHVLHS LLLAIIPHVT IRYAEIPDES
     RNVNYSLASF LKRCLTLMDR GFIFNLINDY ISGFSPKDPK VLAEYKFEFL QTICNHEHYI
     PLNLPMAFAK PKLQRVQDSN LEYSLSDEYC KHHFLVGLLL RETSIALQDN YEIRYTAISV
     IKNLLIKHAF DTRYQHKNQQ AKIAQLYLPF VGLLLENIQR LAGRDTLYSC AAMPNSASRD
     EFPCGFTSPA NRGSLSTDKD TAYGSFQNGH GIKREDSRGS LIPEGATGFP DQGNTGENTR
     QSSTRSSVSQ YNRLDQYEIR SLLMCYLYIV KMISEDTLLT YWNKVSPQEL INILILLEVC
     LFHFRYMGKR NIARVHDAWL SKHFGIDRKS QTMPALRNRS GVMQARLQHL SSLESSFTLN
     HSSTTTEADI FHQALLEGNT ATEVSLTVLD TISFFTQCFK TQLLNNDGHN PLMKKVFDIH
     LAFLKNGQSE VSLKHVFASL RAFISKFPSA FFKGRVNMCA AFCYEVLKCC TSKISSTRNE
     ASALLYLLMR NNFEYTKRKT FLRTHLQIII AVSQLIADVA LSGGSRFQES LFIINNFANS
     DRPMKATAFP AEVKDLTKRI RTVLMATAQM KEHEKDPEML IDLQYSLAKS YASTPELRKT
     WLDSMAKIHV KNGDFSEAAM CYVHVAALVA EFLHRKKLFP NGCSAFKKIT PNIDEEGAMK
     EDAGMMDVHY SEEVLLELLE QCVDGLWKAE RYEIISEISK LIVPIYEKRR EFEKLTQVYR
     TLHGAYTKIL EVMHTKKRLL GTFFRVAFYG QSFFEEEDGK EYIYKEPKLT GLSEISLRLV
     KLYGEKFGTE NVKIIQDSDK VNAKELDPKY AHIQVTYVKP YFDDKELTER KTEFERNHNI
     SRFVFEAPYT LSGKKQGCIE EQCKRRTILT TSNSFPYVKK RIPINCEQQI NLKPIDVATD
     EIKDKTAELQ KLCSSTDVDM IQLQLKLQGC VSVQVNAGPL AYARAFLNDS QASKYPPKKV
     SELKDMFRKF IQACSIALEL NERLIKEDQV EYHEGLKSNF RDMVKELSDI IHEQILQEDT
     MHSPWMSNTL HVFCAISGTS SDRGYGSPRY AEV
//