DOCK2_MOUSE
ID DOCK2_MOUSE Reviewed; 1828 AA.
AC Q8C3J5; Q5SRI4; Q99M79;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Dedicator of cytokinesis protein 2;
DE AltName: Full=Protein Hch;
GN Name=Dock2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=11518968; DOI=10.1038/35090591;
RA Fukui Y., Hashimoto O., Sanui T., Oono T., Koga H., Abe M., Inayoshi A.,
RA Noda M., Oike M., Shirai T., Sasazuki T.;
RT "Haematopoietic cell-specific CDM family protein DOCK2 is essential for
RT lymphocyte migration.";
RL Nature 412:826-831(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1501-1828.
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588; SER-1704 AND SER-1729,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in cytoskeletal rearrangements required for
CC lymphocyte migration in response of chemokines. Activates RAC1 and
CC RAC2, but not CDC42, by functioning as a guanine nucleotide exchange
CC factor (GEF), which exchanges bound GDP for free GTP. May also
CC participate in IL2 transcriptional activation via the activation of
CC RAC2. {ECO:0000269|PubMed:11518968}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with RAC1 and RAC2. Interacts
CC with CRKL and VAV. Interacts with CD3Z (By similarity). {ECO:0000250,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Colocalizes with F-actin. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in hematopoietic cells.
CC {ECO:0000269|PubMed:11518968}.
CC -!- DOMAIN: The DOCKER domain probably mediates the GEF activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000255|PROSITE-
CC ProRule:PRU00983}.
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DR EMBL; AY027438; AAK13045.1; -; mRNA.
DR EMBL; AK085708; BAC39514.2; -; mRNA.
DR EMBL; AL669849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR392356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR762384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS83791.1; -.
DR RefSeq; NP_203538.2; NM_033374.3.
DR AlphaFoldDB; Q8C3J5; -.
DR SMR; Q8C3J5; -.
DR BioGRID; 220457; 3.
DR IntAct; Q8C3J5; 5.
DR STRING; 10090.ENSMUSP00000090884; -.
DR iPTMnet; Q8C3J5; -.
DR MetOSite; Q8C3J5; -.
DR PhosphoSitePlus; Q8C3J5; -.
DR EPD; Q8C3J5; -.
DR jPOST; Q8C3J5; -.
DR MaxQB; Q8C3J5; -.
DR PaxDb; Q8C3J5; -.
DR PeptideAtlas; Q8C3J5; -.
DR PRIDE; Q8C3J5; -.
DR ProteomicsDB; 279754; -.
DR Antibodypedia; 28772; 247 antibodies from 32 providers.
DR DNASU; 94176; -.
DR Ensembl; ENSMUST00000093193; ENSMUSP00000090884; ENSMUSG00000020143.
DR GeneID; 94176; -.
DR KEGG; mmu:94176; -.
DR UCSC; uc029rle.2; mouse.
DR CTD; 1794; -.
DR MGI; MGI:2149010; Dock2.
DR VEuPathDB; HostDB:ENSMUSG00000020143; -.
DR eggNOG; KOG1998; Eukaryota.
DR GeneTree; ENSGT00940000154903; -.
DR HOGENOM; CLU_000595_2_1_1; -.
DR InParanoid; Q8C3J5; -.
DR OMA; MEECFKS; -.
DR OrthoDB; 102580at2759; -.
DR PhylomeDB; Q8C3J5; -.
DR TreeFam; TF300423; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 94176; 4 hits in 53 CRISPR screens.
DR ChiTaRS; Dock2; mouse.
DR PRO; PR:Q8C3J5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C3J5; protein.
DR Bgee; ENSMUSG00000020143; Expressed in peripheral lymph node and 118 other tissues.
DR ExpressionAtlas; Q8C3J5; baseline and differential.
DR Genevisible; Q8C3J5; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IMP:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0042608; F:T cell receptor binding; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0046631; P:alpha-beta T cell activation; IMP:MGI.
DR GO; GO:0046633; P:alpha-beta T cell proliferation; IMP:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IMP:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:MGI.
DR GO; GO:0001768; P:establishment of T cell polarity; IMP:MGI.
DR GO; GO:0001771; P:immunological synapse formation; IMP:MGI.
DR GO; GO:0044351; P:macropinocytosis; IMP:UniProtKB.
DR GO; GO:0001766; P:membrane raft polarization; IMP:MGI.
DR GO; GO:0002277; P:myeloid dendritic cell activation involved in immune response; IMP:UniProtKB.
DR GO; GO:0007520; P:myoblast fusion; IBA:GO_Central.
DR GO; GO:0045060; P:negative thymic T cell selection; IMP:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:UniProtKB.
DR GO; GO:0035022; P:positive regulation of Rac protein signal transduction; IC:MGI.
DR GO; GO:0045059; P:positive thymic T cell selection; IMP:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0042110; P:T cell activation; IMP:MGI.
DR GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR Gene3D; 1.20.1270.350; -; 1.
DR Gene3D; 1.20.58.740; -; 1.
DR Gene3D; 1.25.40.410; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027007; C2_DOCK-type_domain.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR026791; DOCK.
DR InterPro; IPR026799; DOCK_2.
DR InterPro; IPR043161; DOCK_C_lobe_A.
DR InterPro; IPR043162; DOCK_C_lobe_C.
DR InterPro; IPR032376; DOCK_N.
DR InterPro; IPR042455; DOCK_N_sub1.
DR InterPro; IPR027357; DOCKER_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR45653; PTHR45653; 1.
DR PANTHER; PTHR45653:SF6; PTHR45653:SF6; 1.
DR Pfam; PF06920; DHR-2; 1.
DR Pfam; PF14429; DOCK-C2; 1.
DR Pfam; PF16172; DOCK_N; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Guanine-nucleotide releasing factor;
KW Membrane; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..1828
FT /note="Dedicator of cytokinesis protein 2"
FT /id="PRO_0000189987"
FT DOMAIN 8..69
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 423..607
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00983"
FT DOMAIN 1210..1621
FT /note="DOCKER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT REGION 1652..1703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 304
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92608"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92608"
FT MOD_RES 738
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92608"
FT MOD_RES 1683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92608"
FT MOD_RES 1704
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92608"
FT CONFLICT 936
FT /note="V -> E (in Ref. 1; AAK13045)"
FT /evidence="ECO:0000305"
FT CONFLICT 1722
FT /note="S -> F (in Ref. 2; BAC39514)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1828 AA; 211704 MW; 7EB3200A7CD04AA7 CRC64;
MAPWRKTDKE RHGVAIYNFQ GSEAQHLTLQ IGDVVRIQET CGDWYRGYLI KHKLSQGIFP
TSFIHLKEVT VEKRRNIENI IPAEIPLAQE VTTTLWEWGS IWKQLYVASK KERFLQVQSM
MYDLMEWRSQ LLSGTLPKDE LKELKQKVTS KIDYGNKILE LDLIVRDEDG NILDPDKTSV
ISLFHAHEEA TYKITERIKE EMSKDQPDYG VYSRISSSPT HSLYVFVRNF VCRIGEDAEL
FMSLYDPHKQ TVISENYLVR WGSKGFPKEI EMLNNLKVVF TDLGNKDLNR DKIFLICQIV
RIGKMDLKDI NAKKCTQGLR RPFGVAVMDI TDIIKGKAES DEEKQHFIPF HPVSAENDFL
HSLLGKVIAS KGDSGGQGLW VTMKMLVGDI IQIRKDYPHL VDRTTVVARK LGFPEIIMPG
DVRNDIYITL LQGDFDKYTK TTQRNVEVIM CVCTEDGKVL PNAICVGAGD KAMNEYHSVV
YYQVKQPRWM ETVKVAVPIE DMQRIHLRFM FRHRSSLESK DKGEKNFAMS YVKLMKEDGT
TLHDGYHELV VLKGDSKKME DASAYLTLPS YRHPVENKGA TLSRSSSSVG GLSVSSRDVF
SISTLVCSTK LTQNVGLLGL LKWRMKPQLL QENLEKLKIV DGEEVVKFLQ DTLDALFNIM
MEHSQSNEYD ILVFDALIYI IGLIADRKFQ HFNTVLEAYI QQHFSATLAY KKLMTVLKTY
LDTSSRGEQC EPILRTLKAL EYVFKFIVRS RTLFSQLYEG KEQMEFEESM RRLFESINNL
MKSQYKTTIL LQVAALKYIP SVLHDVETVF DAKLLSQLLY EFYTCIPPVK LQKQKVQSMN
EIVQSNLFKK QECRDILLPV ITKELKELLE QRDDGQHQAE KKHCVELLNS ILEVLSCQDA
AFTYDHIQEI MVQLLRTVNR TVITMGRDHA LISHFVACMT AILDQMGDQH YSFYIETFQT
SSDLVDFLME TFIMFKDLIG KNVYPGDWMA MSMVQNRVFL RAINKFAETM NQKFLEHTSF
EFQLWNNYFH LAVAFITQDS LQLEQFTHAK YNKILNKYGD MRRLIGFSIR DMWYKLGQNK
ICFIPGMVGP ILEMTLIPEA ELRKATIPIF FDMMLCEYQR TGAFKKFENE IILKLDHEVE
GGRGDEQYMQ LLESILMECT AEHPTIAKSV ENFVSLVKGL LEKLLDYRGV MTDESKDNRM
SCTVNLLNFY KDNNREEMYI RYLYKLRDLH LDCENYTEAA YTLLLHTWLL KWSDEQCASQ
VMQTGQQHPQ THRQLKETLY ETIIGYFDKG KMWEEAISLC KELAEQYEME IFDYELLSQN
LTQQAKFYEN IMKILRTKPD YFAVGYYGQG FPSFLRNKVF IYRGKEYERR EDFQMQLLSQ
FPNAEKMNTT SAPGDDVRNA PGQYIQCFTV QPVLDEHPRF KNKPVPDQII NFYKSNYVQK
FHYSRPVRRG KVDPENEFAS MWIERTSFLT AYKLPGILRW FEVVHMSQTT ISPLENAIET
MSTVNEKILM MINQYQSDES LPINPLSMLL NGIVDPAVMG GFAKYEKAFF TEEYSREHPE
DQDKLSHLKD LIAWQIPFLG AGIKIHEKRV SDNLRPFHDR MEECFKNLKM KVEKEYGVRE
MPDFEDRRVG RPRSMLRSYR QMSVISLASM HSDCSTPSKV PAESFDLESA PPKTPKVEEE
PISPGSTLPE VKLRRSKKRT KRSSVVFADE KAATESDLKR LSRKQEFMSD TNLSEHAAIP
ARVSILSQMS FASQSMPTIP ALTLSVAGVP GLDEANTSPR LSQTFFQVSD GDKKTLKKKK
VNQFFKTMLA SKSSEESKQI PDFLSTNM
