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Docking protein 1 (Downstream of tyrosine kinase 1) (p62(dok))

 DOK1_MOUSE              Reviewed;         482 AA.
P97465; Q9R213;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
17-JAN-2003, sequence version 2.
23-MAY-2018, entry version 161.
RecName: Full=Docking protein 1;
AltName: Full=Downstream of tyrosine kinase 1;
AltName: Full=p62(dok);
Name=Dok1; Synonyms=Dok;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-46; 122-160;
257-276 AND 424-453.
STRAIN=C57BL/6J; TISSUE=B-cell, and Spleen;
PubMed=9008161; DOI=10.1016/S0092-8674(00)81841-3;
Yamanashi Y., Baltimore D.;
"Identification of the Abl- and rasGAP-associated 62 kDa protein as a
docking protein, Dok.";
Cell 88:205-211(1997).
[2]
SEQUENCE REVISION TO 381 AND 384.
Yamanashi Y., Baltimore D.;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
PubMed=9927484;
Jang W., Hua A., Spilson S.V., Miller W., Roe B.A., Meisler M.H.;
"Comparative sequence of human and mouse BAC clones from the mnd2
region of chromosome 2p13.";
Genome Res. 9:53-61(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION BY TEC.
PubMed=9872994; DOI=10.1074/jbc.274.2.607;
Yang W.C., Ghiotto M., Barbarat B., Olive D.;
"The role of Tec protein-tyrosine kinase in T cell signaling.";
J. Biol. Chem. 274:607-617(1999).
[6]
INTERACTION WITH INPP5D.
PubMed=10822173; DOI=10.1016/S0898-6568(00)00073-5;
Dunant N.M., Wisniewski D., Strife A., Clarkson B., Resh M.D.;
"The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates
with the dok1 phosphoprotein in bcr-Abl transformed cells.";
Cell. Signal. 12:317-326(2000).
[7]
DISRUPTION PHENOTYPE, AND PHOSPHORYLATION BY LYN.
PubMed=10640270;
Yamanashi Y., Tamura T., Kanamori T., Yamane H., Nariuchi H.,
Yamamoto T., Baltimore D.;
"Role of the rasGAP-associated docking protein p62(dok) in negative
regulation of B cell receptor-mediated signaling.";
Genes Dev. 14:11-16(2000).
[8]
INTERACTION WITH INPP5D.
PubMed=11031258; DOI=10.1074/jbc.M006250200;
Sattler M., Verma S., Pride Y.B., Salgia R., Rohrschneider L.R.,
Griffin J.D.;
"SHIP1, an SH2 domain containing polyinositol-5-phosphatase, regulates
migration through two critical tyrosine residues and forms a novel
signaling complex with DOK1 and CRKL.";
J. Biol. Chem. 276:2451-2458(2001).
[9]
CRYSTALLIZATION.
PubMed=14747716; DOI=10.1107/S0907444903026696;
Shi N., Liu Y., Ni M., Yang M., Wu J., Peng Y., Gao F., Sun F.,
Peng X., Qiang B., Rao Z., Yuan J.;
"Expression, crystallization and preliminary X-ray studies of the
recombinant PTB domain of mouse dok1 protein.";
Acta Crystallogr. D 60:334-336(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-295; TYR-336; TYR-340
AND TYR-361, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-361; TYR-408 AND
TYR-450, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-376, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 AND TYR-450, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[15]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 152-266.
PubMed=14607833; DOI=10.1074/jbc.M311030200;
Shi N., Ye S., Bartlam M., Yang M., Wu J., Liu Y., Sun F., Han X.,
Peng X., Qiang B., Yuan J., Rao Z.;
"Structural basis for the specific recognition of RET by the Dok1
phosphotyrosine binding domain.";
J. Biol. Chem. 279:4962-4969(2004).
-!- FUNCTION: DOK proteins are enzymatically inert adaptor or
scaffolding proteins. They provide a docking platform for the
assembly of multimolecular signaling complexes. DOK1 appears to be
a negative regulator of the insulin signaling pathway. Modulates
integrin activation by competing with talin for the same binding
site on ITGB3 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with RasGAP, INPP5D/SHIP1 and ABL1. Interacts
directly with phosphorylated ITGB3 (By similarity). Interacts with
SRMS (via the SH2 and SH3 domains) (By similarity). {ECO:0000250}.
-!- INTERACTION:
P00520:Abl1; NbExp=4; IntAct=EBI-914917, EBI-914519;
Q99M51:Nck1; NbExp=5; IntAct=EBI-914917, EBI-642202;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in lung, spleen, skeletal muscle and
kidney.
-!- DOMAIN: PTB domain mediates receptor interaction.
-!- PTM: Constitutively tyrosine-phosphorylated. Phosphorylated by
TEC. Phosphorylated on tyrosine residues by the insulin receptor
kinase. Results in the negative regulation of the insulin
signaling pathway (By similarity). Phosphorylated by LYN.
Phosphorylated on tyrosine residues by SRMS (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: No visible phenotype. Mice appear healthy
and are fertile. {ECO:0000269|PubMed:10640270}.
-!- SIMILARITY: Belongs to the DOK family. Type A subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U78818; AAB48827.2; -; mRNA.
EMBL; AF084363; AAC95339.1; -; Genomic_DNA.
EMBL; BC013066; AAH13066.1; -; mRNA.
CCDS; CCDS20265.1; -.
RefSeq; NP_001278728.1; NM_001291799.1.
RefSeq; NP_034200.4; NM_010070.4.
UniGene; Mm.156; -.
PDB; 1P5T; X-ray; 2.35 A; A/B=152-266.
PDB; 1UEF; X-ray; 2.50 A; A/B=152-266.
PDBsum; 1P5T; -.
PDBsum; 1UEF; -.
ProteinModelPortal; P97465; -.
SMR; P97465; -.
BioGrid; 199267; 28.
CORUM; P97465; -.
IntAct; P97465; 13.
MINT; P97465; -.
STRING; 10090.ENSMUSP00000087079; -.
iPTMnet; P97465; -.
PhosphoSitePlus; P97465; -.
EPD; P97465; -.
MaxQB; P97465; -.
PaxDb; P97465; -.
PeptideAtlas; P97465; -.
PRIDE; P97465; -.
Ensembl; ENSMUST00000089651; ENSMUSP00000087079; ENSMUSG00000068335.
GeneID; 13448; -.
KEGG; mmu:13448; -.
UCSC; uc009clr.2; mouse.
CTD; 1796; -.
MGI; MGI:893587; Dok1.
eggNOG; KOG4047; Eukaryota.
eggNOG; ENOG410XS2S; LUCA.
GeneTree; ENSGT00730000110348; -.
HOGENOM; HOG000112245; -.
HOVERGEN; HBG018962; -.
InParanoid; P97465; -.
KO; K14752; -.
OMA; DPKEDPI; -.
OrthoDB; EOG091G075T; -.
PhylomeDB; P97465; -.
TreeFam; TF324994; -.
Reactome; R-MMU-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
Reactome; R-MMU-8853659; RET signaling.
ChiTaRS; Dok1; mouse.
EvolutionaryTrace; P97465; -.
PRO; PR:P97465; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000068335; -.
CleanEx; MM_DOK1; -.
ExpressionAtlas; P97465; baseline and differential.
Genevisible; P97465; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005057; F:signal transducer activity, downstream of receptor; IPI:MGI.
GO; GO:0035556; P:intracellular signal transduction; IPI:MGI.
GO; GO:0000165; P:MAPK cascade; TAS:MGI.
GO; GO:0007265; P:Ras protein signal transduction; IPI:MGI.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IPI:MGI.
CDD; cd01203; PTB_DOK1_DOK2_DOK3; 1.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR037751; Dok1/2/3_PTB.
InterPro; IPR002404; IRS_PTB.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
Pfam; PF02174; IRS; 1.
Pfam; PF00169; PH; 1.
SMART; SM00233; PH; 1.
SMART; SM00310; PTBI; 1.
PROSITE; PS51064; IRS_PTB; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Nucleus; Phosphoprotein;
Reference proteome.
CHAIN 1 482 Docking protein 1.
/FTId=PRO_0000187269.
DOMAIN 4 119 PH.
DOMAIN 151 259 IRS-type PTB. {ECO:0000255|PROSITE-
ProRule:PRU00389}.
COMPBIAS 280 322 Pro-rich.
COMPBIAS 359 430 Pro-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q99704}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000250|UniProtKB:Q99704}.
MOD_RES 269 269 Phosphoserine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000250|UniProtKB:Q99704}.
MOD_RES 295 295 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 336 336 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 340 340 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 361 361 Phosphotyrosine.
{ECO:0000244|PubMed:15592455,
ECO:0000244|PubMed:17947660}.
MOD_RES 376 376 Phosphotyrosine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 397 397 Phosphotyrosine; by INSR.
{ECO:0000250|UniProtKB:Q99704}.
MOD_RES 408 408 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 415 415 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 450 450 Phosphotyrosine.
{ECO:0000244|PubMed:17947660,
ECO:0000244|PubMed:19131326}.
CONFLICT 2 2 D -> N (in Ref. 4; AAH13066).
{ECO:0000305}.
CONFLICT 87 87 V -> A (in Ref. 3; AAC95339 and 4;
AAH13066). {ECO:0000305}.
STRAND 153 160 {ECO:0000244|PDB:1P5T}.
HELIX 163 167 {ECO:0000244|PDB:1P5T}.
STRAND 172 178 {ECO:0000244|PDB:1P5T}.
STRAND 180 188 {ECO:0000244|PDB:1P5T}.
TURN 190 192 {ECO:0000244|PDB:1P5T}.
STRAND 194 202 {ECO:0000244|PDB:1P5T}.
HELIX 203 205 {ECO:0000244|PDB:1P5T}.
STRAND 206 211 {ECO:0000244|PDB:1P5T}.
STRAND 213 220 {ECO:0000244|PDB:1P5T}.
STRAND 228 234 {ECO:0000244|PDB:1P5T}.
HELIX 238 253 {ECO:0000244|PDB:1P5T}.
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


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