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Docking protein 2 (Dok-related protein) (Dok-R) (Downstream of tyrosine kinase 2) (IL-four receptor-interacting protein) (FRIP) (p56(dok-2))

 DOK2_MOUSE              Reviewed;         412 AA.
O70469; O70272; Q99KL1;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
22-NOV-2017, entry version 134.
RecName: Full=Docking protein 2;
AltName: Full=Dok-related protein;
Short=Dok-R;
AltName: Full=Downstream of tyrosine kinase 2;
AltName: Full=IL-four receptor-interacting protein;
Short=FRIP;
AltName: Full=p56(dok-2);
Name=Dok2; Synonyms=Frip;
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 PHOSPHORYLATION AT TYROSINE RESIDUES.
PubMed=9697832; DOI=10.1016/S1074-7613(00)80584-1;
Nelms K., Snow A.L., Hu-Li J., Paul W.E.;
"FRIP, a hematopoietic cell-specific rasGAP-interacting protein
phosphorylated in response to cytokine stimulation.";
Immunity 9:13-24(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=9478921; DOI=10.1074/jbc.273.9.4827;
Di Cristofano A., Carpino N., Dunant N., Friedland G., Kobayashi R.,
Strife A., Wisniewski D., Clarkson B., Pandolfi P.P., Resh M.D.;
"Molecular cloning and characterization of p56dok-2 defines a new
family of RasGAP-binding proteins.";
J. Biol. Chem. 273:4827-4830(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9764820; DOI=10.1038/sj.onc.1202115;
Jones N., Dumont D.J.;
"The Tek/Tie2 receptor signals through a novel Dok-related docking
protein, Dok-R.";
Oncogene 17:1097-1108(1998).
[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]
INTERACTION WITH EGFR; NCK AND RASGAP, PHOSPHORYLATION AT TYR-276;
TYR-304 AND TYR-351, AND MUTAGENESIS OF TYR-276; TYR-304 AND TYR-351.
PubMed=10508618; DOI=10.1016/S0960-9822(99)80458-8;
Jones N., Dumont D.J.;
"Recruitment of Dok-R to the EGF receptor through its PTB domain is
required for attenuation of Erk MAP kinase activation.";
Curr. Biol. 9:1057-1060(1999).
[6]
INTERACTION WITH RET, PHOSPHORYLATION, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=11470823; DOI=10.1083/jcb.200102032;
Grimm J., Sachs M., Britsch S., Di Cesare S., Schwarz-Romond T.,
Alitalo K., Birchmeier W.;
"Novel p62dok family members, dok-4 and dok-5, are substrates of the
c-Ret receptor tyrosine kinase and mediate neuronal differentiation.";
J. Cell Biol. 154:345-354(2001).
[7]
INTERACTION WITH TEK/TIE2, AND PHOSPHORYLATION.
PubMed=12665569; DOI=10.1128/MCB.23.8.2658-2668.2003;
Jones N., Chen S.H., Sturk C., Master Z., Tran J., Kerbel R.S.,
Dumont D.J.;
"A unique autophosphorylation site on Tie2/Tek mediates Dok-R
phosphotyrosine binding domain binding and function.";
Mol. Cell. Biol. 23:2658-2668(2003).
-!- FUNCTION: DOK proteins are enzymatically inert adaptor or
scaffolding proteins. They provide a docking platform for the
assembly of multimolecular signaling complexes. DOK2 may modulate
the cellular proliferation induced by IL-4, as well as IL-2 and
IL-3. May be involved in modulating Bcr-Abl signaling. Attenuates
EGF-stimulated MAP kinase activation.
-!- SUBUNIT: Interacts with phosphorylated RASGAP and EGFR. Interacts
with RET and NCK. Interacts (via PH domain) with TEK/TIE2
(tyrosine phosphorylated). {ECO:0000269|PubMed:10508618,
ECO:0000269|PubMed:11470823, ECO:0000269|PubMed:12665569}.
-!- TISSUE SPECIFICITY: Highly expressed in spleen and lung.
{ECO:0000269|PubMed:11470823, ECO:0000269|PubMed:9478921}.
-!- DEVELOPMENTAL STAGE: During embryonic liver development, expressed
in the islands of cells, consistent with an expression in
hematopoietic precursors. {ECO:0000269|PubMed:11470823}.
-!- DOMAIN: PTB domain mediates receptor interaction.
-!- PTM: On immunoreceptor stimulation, phosphorylated on C-terminal
tyrosine residues. Phosphorylation on Tyr-351 is required for
binding to the SH2 domain of NCK. Phosphorylation on both Tyr-276
and Tyr-304 is required for interaction with RASGAP.
Phosphorylated on tyrosine residues by TEK/TIE2.
{ECO:0000269|PubMed:10508618, ECO:0000269|PubMed:11470823,
ECO:0000269|PubMed:12665569, ECO:0000269|PubMed:9697832}.
-!- SIMILARITY: Belongs to the DOK family. Type A subfamily.
{ECO:0000305}.
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EMBL; AF030627; AAC31315.1; -; mRNA.
EMBL; AF035117; AAC13266.1; -; mRNA.
EMBL; AF059583; AAC78606.1; -; mRNA.
EMBL; BC004590; AAH04590.1; -; mRNA.
CCDS; CCDS27262.1; -.
RefSeq; NP_034201.1; NM_010071.2.
UniGene; Mm.243323; -.
ProteinModelPortal; O70469; -.
SMR; O70469; -.
BioGrid; 199268; 6.
IntAct; O70469; 10.
MINT; MINT-100549; -.
STRING; 10090.ENSMUSP00000022698; -.
iPTMnet; O70469; -.
PhosphoSitePlus; O70469; -.
EPD; O70469; -.
PaxDb; O70469; -.
PeptideAtlas; O70469; -.
PRIDE; O70469; -.
Ensembl; ENSMUST00000022698; ENSMUSP00000022698; ENSMUSG00000022102.
GeneID; 13449; -.
KEGG; mmu:13449; -.
UCSC; uc007uoy.1; mouse.
CTD; 9046; -.
MGI; MGI:1332623; Dok2.
eggNOG; KOG4047; Eukaryota.
eggNOG; ENOG410XS2S; LUCA.
GeneTree; ENSGT00730000110348; -.
HOGENOM; HOG000112245; -.
HOVERGEN; HBG018962; -.
InParanoid; O70469; -.
KO; K20234; -.
OMA; EYAVPFD; -.
OrthoDB; EOG091G075T; -.
PhylomeDB; O70469; -.
TreeFam; TF324994; -.
Reactome; R-MMU-210993; Tie2 Signaling.
Reactome; R-MMU-8853659; RET signaling.
PRO; PR:O70469; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000022102; -.
CleanEx; MM_DOK2; -.
ExpressionAtlas; O70469; baseline and differential.
Genevisible; O70469; MM.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005158; F:insulin receptor binding; IEA:InterPro.
GO; GO:0005057; F:signal transducer activity, downstream of receptor; IPI:MGI.
GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; 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.
Gene3D; 2.30.29.30; -; 2.
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.
SUPFAM; SSF50729; SSF50729; 2.
PROSITE; PS51064; IRS_PTB; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Complete proteome; Phosphoprotein; Reference proteome.
CHAIN 1 412 Docking protein 2.
/FTId=PRO_0000187271.
DOMAIN 7 117 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 149 254 IRS-type PTB. {ECO:0000255|PROSITE-
ProRule:PRU00389}.
COMPBIAS 252 307 Pro-rich.
COMPBIAS 326 369 Pro-rich.
MOD_RES 276 276 Phosphotyrosine.
{ECO:0000269|PubMed:10508618}.
MOD_RES 304 304 Phosphotyrosine.
{ECO:0000269|PubMed:10508618}.
MOD_RES 351 351 Phosphotyrosine.
{ECO:0000269|PubMed:10508618}.
MUTAGEN 276 276 Y->F: No loss of binding to SH2 domain of
RASGAP or NCK. Complete loss of binding
to SH2 domain of RASGAP; when associated
with F-304.
{ECO:0000269|PubMed:10508618}.
MUTAGEN 304 304 Y->F: No loss of binding to SH2 domain of
RASGAP. Complete loss of binding to SH2
domain of RASGAP; when associated with F-
276. {ECO:0000269|PubMed:10508618}.
MUTAGEN 351 351 Y->F: No loss of binding to SH2 domain of
RASGAP. Complete loss of binding to SH2
domain of NCK.
{ECO:0000269|PubMed:10508618}.
CONFLICT 245 245 A -> T (in Ref. 4; AAH04590).
{ECO:0000305}.
CONFLICT 330 330 L -> F (in Ref. 2; AAC13266).
{ECO:0000305}.
CONFLICT 347 347 P -> T (in Ref. 2; AAC13266).
{ECO:0000305}.
CONFLICT 412 412 Missing (in Ref. 4; AAH04590).
{ECO:0000305}.
SEQUENCE 412 AA; 45522 MW; 02AC02530DBED053 CRC64;
MVRMEEPAVK QGFLHLQQQQ TFGKKWRRFA AVLYGESGCA LARLELQDVP EKTRRGEATR
KVVRLSDCLR VAEVGSEASS PRDTSAFILE TKERLYLLAA PSAERSDWIQ AICLLAFPGQ
RKGSPGLEEK SGSPCMEENE LYSSSTTGLC KEYMVTIRPT EASERCRLRG SYTLRTGVSA
LELWGGPEPG TQLYDWPYRF LRRFGRDKAT FSFEAGRRCL SGEGNFEFET RHGNEIFQAL
EKVIAVQKNA TPSGPPSLPA TGPMMPTVLP RPESPYSRPH DSLPSPSPGT LVPGMRPGAP
EGEYAVPFDT VAHSLRKSFR GLLTGPPPHL PDPLYDSIQE DPGAPLPDHI YDEPEGVAAL
SLYDRTQRPS GETWREQATA DGGPSSLQQD SSVPDWPQAT EYDNVILKKG PK


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