ID   DOK1_MOUSE              Reviewed;         482 AA.
AC   P97465; Q9R213;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   17-JAN-2003, sequence version 2.
DT   24-JAN-2024, entry version 191.
DE   RecName: Full=Docking protein 1;
DE   AltName: Full=Downstream of tyrosine kinase 1;
DE   AltName: Full=p62(dok);
GN   Name=Dok1; Synonyms=Dok;
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], AND PROTEIN SEQUENCE OF 25-46; 122-160; 257-276
RP   AND 424-453.
RC   STRAIN=C57BL/6J; TISSUE=B-cell, and Spleen;
RX   PubMed=9008161; DOI=10.1016/s0092-8674(00)81841-3;
RA   Yamanashi Y., Baltimore D.;
RT   "Identification of the Abl- and rasGAP-associated 62 kDa protein as a
RT   docking protein, Dok.";
RL   Cell 88:205-211(1997).
RN   [2]
RP   SEQUENCE REVISION TO 381 AND 384.
RA   Yamanashi Y., Baltimore D.;
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=9927484;
RA   Jang W., Hua A., Spilson S.V., Miller W., Roe B.A., Meisler M.H.;
RT   "Comparative sequence of human and mouse BAC clones from the mnd2 region of
RT   chromosome 2p13.";
RL   Genome Res. 9:53-61(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   PHOSPHORYLATION BY TEC.
RX   PubMed=9872994; DOI=10.1074/jbc.274.2.607;
RA   Yang W.C., Ghiotto M., Barbarat B., Olive D.;
RT   "The role of Tec protein-tyrosine kinase in T cell signaling.";
RL   J. Biol. Chem. 274:607-617(1999).
RN   [6]
RP   INTERACTION WITH INPP5D.
RX   PubMed=10822173; DOI=10.1016/s0898-6568(00)00073-5;
RA   Dunant N.M., Wisniewski D., Strife A., Clarkson B., Resh M.D.;
RT   "The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with
RT   the dok1 phosphoprotein in bcr-Abl transformed cells.";
RL   Cell. Signal. 12:317-326(2000).
RN   [7]
RP   DISRUPTION PHENOTYPE, AND PHOSPHORYLATION BY LYN.
RX   PubMed=10640270;
RA   Yamanashi Y., Tamura T., Kanamori T., Yamane H., Nariuchi H., Yamamoto T.,
RA   Baltimore D.;
RT   "Role of the rasGAP-associated docking protein p62(dok) in negative
RT   regulation of B cell receptor-mediated signaling.";
RL   Genes Dev. 14:11-16(2000).
RN   [8]
RP   INTERACTION WITH INPP5D.
RX   PubMed=11031258; DOI=10.1074/jbc.m006250200;
RA   Sattler M., Verma S., Pride Y.B., Salgia R., Rohrschneider L.R.,
RA   Griffin J.D.;
RT   "SHIP1, an SH2 domain containing polyinositol-5-phosphatase, regulates
RT   migration through two critical tyrosine residues and forms a novel
RT   signaling complex with DOK1 and CRKL.";
RL   J. Biol. Chem. 276:2451-2458(2001).
RN   [9]
RP   CRYSTALLIZATION.
RX   PubMed=14747716; DOI=10.1107/s0907444903026696;
RA   Shi N., Liu Y., Ni M., Yang M., Wu J., Peng Y., Gao F., Sun F., Peng X.,
RA   Qiang B., Rao Z., Yuan J.;
RT   "Expression, crystallization and preliminary X-ray studies of the
RT   recombinant PTB domain of mouse dok1 protein.";
RL   Acta Crystallogr. D 60:334-336(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-295; TYR-336; TYR-340 AND
RP   TYR-361, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-361; TYR-408 AND TYR-450, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-376, AND IDENTIFICATION BY
RP   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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 AND TYR-450, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, and Spleen;
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).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 152-266.
RX   PubMed=14607833; DOI=10.1074/jbc.m311030200;
RA   Shi N., Ye S., Bartlam M., Yang M., Wu J., Liu Y., Sun F., Han X., Peng X.,
RA   Qiang B., Yuan J., Rao Z.;
RT   "Structural basis for the specific recognition of RET by the Dok1
RT   phosphotyrosine binding domain.";
RL   J. Biol. Chem. 279:4962-4969(2004).
CC   -!- FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding
CC       proteins. They provide a docking platform for the assembly of
CC       multimolecular signaling complexes. DOK1 appears to be a negative
CC       regulator of the insulin signaling pathway. Modulates integrin
CC       activation by competing with talin for the same binding site on ITGB3
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RasGAP, INPP5D/SHIP1 and ABL1. Interacts
CC       directly with phosphorylated ITGB3 (By similarity). Interacts with SRMS
CC       (via the SH2 and SH3 domains) (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P97465; P00520: Abl1; NbExp=4; IntAct=EBI-914917, EBI-914519;
CC       P97465; Q99M51: Nck1; NbExp=5; IntAct=EBI-914917, EBI-642202;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in lung, spleen, skeletal muscle and
CC       kidney.
CC   -!- DOMAIN: PTB domain mediates receptor interaction.
CC   -!- PTM: Constitutively tyrosine-phosphorylated. Phosphorylated by TEC.
CC       Phosphorylated on tyrosine residues by the insulin receptor kinase.
CC       Results in the negative regulation of the insulin signaling pathway (By
CC       similarity). Phosphorylated by LYN. Phosphorylated on tyrosine residues
CC       by SRMS (By similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice appear healthy and are
CC       fertile. {ECO:0000269|PubMed:10640270}.
CC   -!- SIMILARITY: Belongs to the DOK family. Type A subfamily. {ECO:0000305}.
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DR   EMBL; U78818; AAB48827.2; -; mRNA.
DR   EMBL; AF084363; AAC95339.1; -; Genomic_DNA.
DR   EMBL; BC013066; AAH13066.1; -; mRNA.
DR   CCDS; CCDS20265.1; -.
DR   RefSeq; NP_001278728.1; NM_001291799.1.
DR   RefSeq; NP_034200.4; NM_010070.4.
DR   PDB; 1P5T; X-ray; 2.35 A; A/B=152-266.
DR   PDB; 1UEF; X-ray; 2.50 A; A/B=152-266.
DR   PDBsum; 1P5T; -.
DR   PDBsum; 1UEF; -.
DR   AlphaFoldDB; P97465; -.
DR   SMR; P97465; -.
DR   BioGRID; 199267; 35.
DR   CORUM; P97465; -.
DR   IntAct; P97465; 13.
DR   MINT; P97465; -.
DR   STRING; 10090.ENSMUSP00000087079; -.
DR   iPTMnet; P97465; -.
DR   PhosphoSitePlus; P97465; -.
DR   EPD; P97465; -.
DR   jPOST; P97465; -.
DR   MaxQB; P97465; -.
DR   PaxDb; 10090-ENSMUSP00000087079; -.
DR   PeptideAtlas; P97465; -.
DR   ProteomicsDB; 279468; -.
DR   Pumba; P97465; -.
DR   Antibodypedia; 3784; 970 antibodies from 42 providers.
DR   DNASU; 13448; -.
DR   Ensembl; ENSMUST00000089651.6; ENSMUSP00000087079.6; ENSMUSG00000068335.7.
DR   GeneID; 13448; -.
DR   KEGG; mmu:13448; -.
DR   UCSC; uc009clr.2; mouse.
DR   AGR; MGI:893587; -.
DR   CTD; 1796; -.
DR   MGI; MGI:893587; Dok1.
DR   VEuPathDB; HostDB:ENSMUSG00000068335; -.
DR   eggNOG; KOG4047; Eukaryota.
DR   GeneTree; ENSGT00940000155980; -.
DR   HOGENOM; CLU_030101_3_1_1; -.
DR   InParanoid; P97465; -.
DR   OMA; KPQGLAF; -.
DR   OrthoDB; 2996885at2759; -.
DR   PhylomeDB; P97465; -.
DR   TreeFam; TF324994; -.
DR   Reactome; R-MMU-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
DR   Reactome; R-MMU-8853659; RET signaling.
DR   BioGRID-ORCS; 13448; 3 hits in 81 CRISPR screens.
DR   ChiTaRS; Dok1; mouse.
DR   EvolutionaryTrace; P97465; -.
DR   PRO; PR:P97465; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P97465; Protein.
DR   Bgee; ENSMUSG00000068335; Expressed in stroma of bone marrow and 160 other cell types or tissues.
DR   ExpressionAtlas; P97465; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IPI:MGI.
DR   GO; GO:0038145; P:macrophage colony-stimulating factor signaling pathway; IPI:MGI.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; TAS:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IBA:GO_Central.
DR   GO; GO:0007265; P:Ras protein signal transduction; IPI:MGI.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IPI:MGI.
DR   CDD; cd01203; PTB_DOK1_DOK2_DOK3; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   IDEAL; IID50286; -.
DR   InterPro; IPR037751; Dok1/2/3_PTB.
DR   InterPro; IPR002404; IRS_PTB.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR21258:SF46; DOCKING PROTEIN 1; 1.
DR   PANTHER; PTHR21258; DOCKING PROTEIN RELATED; 1.
DR   Pfam; PF02174; IRS; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM01244; IRS; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00310; PTBI; 1.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   PROSITE; PS51064; IRS_PTB; 1.
DR   Genevisible; P97465; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..482
FT                   /note="Docking protein 1"
FT                   /id="PRO_0000187269"
FT   DOMAIN          4..119
FT                   /note="PH"
FT   DOMAIN          151..259
FT                   /note="IRS-type PTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT   REGION          269..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..425
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99704"
FT   MOD_RES         48
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99704"
FT   MOD_RES         269
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326"
FT   MOD_RES         290
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99704"
FT   MOD_RES         295
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:15592455"
FT   MOD_RES         336
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:15592455"
FT   MOD_RES         340
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:15592455"
FT   MOD_RES         361
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:15592455,
FT                   ECO:0007744|PubMed:17947660"
FT   MOD_RES         376
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         397
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250|UniProtKB:Q99704"
FT   MOD_RES         408
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   MOD_RES         415
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         450
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660,
FT                   ECO:0007744|PubMed:19131326"
FT   CONFLICT        2
FT                   /note="D -> N (in Ref. 4; AAH13066)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="V -> A (in Ref. 3; AAC95339 and 4; AAH13066)"
FT                   /evidence="ECO:0000305"
FT   STRAND          153..160
FT                   /evidence="ECO:0007829|PDB:1P5T"
FT   HELIX           163..167
FT                   /evidence="ECO:0007829|PDB:1P5T"
FT   STRAND          172..178
FT                   /evidence="ECO:0007829|PDB:1P5T"
FT   STRAND          180..188
FT                   /evidence="ECO:0007829|PDB:1P5T"
FT   TURN            190..192
FT                   /evidence="ECO:0007829|PDB:1P5T"
FT   STRAND          194..202
FT                   /evidence="ECO:0007829|PDB:1P5T"
FT   HELIX           203..205
FT                   /evidence="ECO:0007829|PDB:1P5T"
FT   STRAND          206..211
FT                   /evidence="ECO:0007829|PDB:1P5T"
FT   STRAND          213..220
FT                   /evidence="ECO:0007829|PDB:1P5T"
FT   STRAND          228..234
FT                   /evidence="ECO:0007829|PDB:1P5T"
FT   HELIX           238..253
FT                   /evidence="ECO:0007829|PDB:1P5T"
SQ   SEQUENCE   482 AA;  52452 MW;  C999C9FE0DA58EA3 CRC64;
     MDGAVMEGPL FLQSQRFGTK RWRKTWAVLY PASPHGVARL EFFDHKGSSS RGGRGGSRRL
     DCKMIRLAEC VSVVPVTVES PPEPGAVAFR LDTAQRSHLL AADAVSSTAW VQTLCRTAFP
     KGGWALAQTE NQPKFSALEM LENSLYSPTW EGSQFWVTSQ KTEASERCGL QGSYILRVEA
     EKLTLLTLGA QSQILEPLLF WPYTLLRRYG RDKVMFSFEA GRRCPSGPGT FTFQTSQGND
     IFQAVEAAIQ QQKAQGKVGQ AQDILRTDSH DGETEGKTVP PPVPQDPLGS PPALYAEPLD
     SLRIPPGPSQ DSVYSDPLGS TPAGAGEGVH SKKPLYWDLY GHVQQQLLKT KLTDSKEDPI
     YDEPEGLAPA PPRGLYDLPQ EPRDAWWCQA RLKEEGYELP YNPATDDYAV PPPRSPKPAP
     APKPQGLILP ESGTTRGSGS KGFSSDTALY SQVQKSGTSG AWDCGLSKVG NDRAGVKSEG
     ST
//