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Docking protein 1 (Downstream of tyrosine kinase 1) (p62(dok)) (pp62)

 DOK1_HUMAN              Reviewed;         481 AA.
Q99704; O43204; Q53TY2; Q9UHG6;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
22-NOV-2017, entry version 166.
RecName: Full=Docking protein 1;
AltName: Full=Downstream of tyrosine kinase 1;
AltName: Full=p62(dok);
AltName: Full=pp62;
Name=DOK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PHOSPHORYLATION AT
TYROSINE RESIDUES.
PubMed=9008160; DOI=10.1016/S0092-8674(00)81840-1;
Carpino N., Wisniewski D., Strife A., Marshak D., Kobayashi R.,
Stillman B., Clarkson B.;
"p62(dok): a constitutively tyrosine-phosphorylated, GAP-associated
protein in chronic myelogenous leukemia progenitor cells.";
Cell 88:197-204(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10940083; DOI=10.1046/j.1365-2370.2000.00203.x;
Hubert P., Ferreira V., Debre P., Bismuth G.;
"Molecular cloning of a truncated p62Dok1 isoform, p22Dokdel.";
Eur. J. Immunogenet. 27:145-148(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Yu W., Sarginson J., Gibbs R.A.;
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[6]
PHOSPHORYLATION AT TYR-362 AND TYR-398, AND MUTAGENESIS OF TYR-362 AND
TYR-398.
PubMed=11551902; DOI=10.1074/jbc.M102116200;
Wick M.J., Dong L.Q., Hu D., Langlais P., Liu F.;
"Insulin receptor-mediated p62dok tyrosine phosphorylation at residues
362 and 398 plays distinct roles for binding GTPase-activating protein
and Nck and is essential for inhibiting insulin-stimulated activation
of Ras and Akt.";
J. Biol. Chem. 276:42843-42850(2001).
[7]
TISSUE SPECIFICITY.
PubMed=12595900; DOI=10.1038/sj.gene.6363891;
Favre C., Gerard A., Clauzier E., Pontarotti P., Olive D., Nunes J.A.;
"DOK4 and DOK5: new Dok-related genes expressed in human T cells.";
Genes Immun. 4:40-45(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-362; TYR-377; TYR-398
AND TYR-409, 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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
SUBCELLULAR LOCATION, ALTERNATIVE INITIATION (ISOFORM 3), AND
ACETYLATION AT MET-1 (ISOFORM 3).
PubMed=19481542; DOI=10.1016/j.febslet.2009.05.042;
Kobayashi R., Patenia R., Ashizawa S., Vykoukal J.;
"Targeted mass spectrometric analysis of N-terminally truncated
isoforms generated via alternative translation initiation.";
FEBS Lett. 583:2441-2445(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; TYR-341 AND
TYR-362, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[14]
PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH SRMS.
PubMed=23822091; DOI=10.1111/febs.12420;
Goel R.K., Miah S., Black K., Kalra N., Dai C., Lukong K.E.;
"The unique N-terminal region of SRMS regulates enzymatic activity and
phosphorylation of its novel substrate Dok1.";
FEBS J. 280:4539-4559(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-269 AND SER-460,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 152-256, FUNCTION, AND
INTERACTION WITH ITGB3.
PubMed=18156175; DOI=10.1074/jbc.M709435200;
Oxley C.L., Anthis N.J., Lowe E.D., Vakonakis I., Campbell I.D.,
Wegener K.L.;
"An integrin phosphorylation switch: the effect of beta3 integrin tail
phosphorylation on Dok1 and talin binding.";
J. Biol. Chem. 283:5420-5426(2008).
-!- 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. {ECO:0000269|PubMed:18156175}.
-!- SUBUNIT: Interacts with ABL1 (By similarity). Interacts with
RasGAP and INPP5D/SHIP1. Interacts directly with phosphorylated
ITGB3. Interacts with SRMS (via the SH2 and SH3 domains).
{ECO:0000250, ECO:0000269|PubMed:18156175,
ECO:0000269|PubMed:23822091}.
-!- INTERACTION:
Q9JIY2:Cbll1 (xeno); NbExp=2; IntAct=EBI-1384360, EBI-7644904;
P04626:ERBB2; NbExp=2; IntAct=EBI-1384360, EBI-641062;
Q9Q2G4:ORF (xeno); NbExp=2; IntAct=EBI-1384360, EBI-6248094;
Q9H3Y6:SRMS; NbExp=7; IntAct=EBI-1384360, EBI-8541270;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, perinuclear region.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=3;
Name=1; Synonyms=p62Dok1;
IsoId=Q99704-1; Sequence=Displayed;
Name=2; Synonyms=p22Dokdel;
IsoId=Q99704-2; Sequence=VSP_003852, VSP_003853;
Name=3; Synonyms=p44Dok;
IsoId=Q99704-3; Sequence=VSP_038224;
Note=Produced by alternative initiation at Met-140 of isoform 1.
Contains a N-acetylmethionine at position 1.
{ECO:0000269|PubMed:19481542};
-!- TISSUE SPECIFICITY: Expressed in pancreas, heart, leukocyte and
spleen. Expressed in both resting and activated peripheral blood
T-cells. Expressed in breast cancer.
{ECO:0000269|PubMed:12595900}.
-!- DOMAIN: The PTB domain mediates receptor interaction.
-!- PTM: Constitutively tyrosine-phosphorylated. Phosphorylated by TEC
(By similarity). Phosphorylated by LYN (By similarity).
Phosphorylated on tyrosine residues by the insulin receptor
kinase. Results in the negative regulation of the insulin
signaling pathway. Phosphorylated on tyrosine residues by SRMS.
{ECO:0000250, ECO:0000269|PubMed:11551902,
ECO:0000269|PubMed:23822091, ECO:0000269|PubMed:9008160}.
-!- SIMILARITY: Belongs to the DOK family. Type A subfamily.
{ECO:0000305}.
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EMBL; U70987; AAC51127.1; -; mRNA.
EMBL; AF180527; AAF19167.1; -; mRNA.
EMBL; AF035299; AAB88182.1; -; mRNA.
EMBL; AC005033; AAX93224.1; -; Genomic_DNA.
EMBL; BC114440; AAI14441.1; -; mRNA.
CCDS; CCDS1954.1; -. [Q99704-1]
CCDS; CCDS56125.1; -. [Q99704-3]
CCDS; CCDS82474.1; -. [Q99704-2]
RefSeq; NP_001184189.1; NM_001197260.1. [Q99704-3]
RefSeq; NP_001305797.1; NM_001318868.1. [Q99704-2]
RefSeq; NP_001372.1; NM_001381.4. [Q99704-1]
UniGene; Hs.103854; -.
PDB; 2V76; X-ray; 1.60 A; A/B/C/D=152-256.
PDBsum; 2V76; -.
ProteinModelPortal; Q99704; -.
SMR; Q99704; -.
BioGrid; 108131; 37.
ELM; Q99704; -.
IntAct; Q99704; 13.
MINT; MINT-1494101; -.
STRING; 9606.ENSP00000233668; -.
iPTMnet; Q99704; -.
PhosphoSitePlus; Q99704; -.
BioMuta; DOK1; -.
DMDM; 17366642; -.
EPD; Q99704; -.
MaxQB; Q99704; -.
PaxDb; Q99704; -.
PeptideAtlas; Q99704; -.
PRIDE; Q99704; -.
Ensembl; ENST00000233668; ENSP00000233668; ENSG00000115325. [Q99704-1]
Ensembl; ENST00000340004; ENSP00000344330; ENSG00000115325. [Q99704-2]
Ensembl; ENST00000409429; ENSP00000387016; ENSG00000115325. [Q99704-3]
GeneID; 1796; -.
KEGG; hsa:1796; -.
UCSC; uc002smr.4; human. [Q99704-1]
CTD; 1796; -.
DisGeNET; 1796; -.
EuPathDB; HostDB:ENSG00000115325.13; -.
GeneCards; DOK1; -.
HGNC; HGNC:2990; DOK1.
HPA; CAB004224; -.
HPA; HPA048561; -.
MIM; 602919; gene.
neXtProt; NX_Q99704; -.
OpenTargets; ENSG00000115325; -.
PharmGKB; PA27456; -.
eggNOG; KOG4047; Eukaryota.
eggNOG; ENOG410XS2S; LUCA.
GeneTree; ENSGT00730000110348; -.
HOGENOM; HOG000112245; -.
HOVERGEN; HBG018962; -.
InParanoid; Q99704; -.
KO; K14752; -.
OMA; DPKEDPI; -.
OrthoDB; EOG091G075T; -.
PhylomeDB; Q99704; -.
TreeFam; TF324994; -.
Reactome; R-HSA-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
Reactome; R-HSA-8853659; RET signaling.
SignaLink; Q99704; -.
SIGNOR; Q99704; -.
EvolutionaryTrace; Q99704; -.
GeneWiki; DOK1; -.
GenomeRNAi; 1796; -.
PRO; PR:Q99704; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115325; -.
CleanEx; HS_DOK1; -.
ExpressionAtlas; Q99704; baseline and differential.
Genevisible; Q99704; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005158; F:insulin receptor binding; IEA:InterPro.
GO; GO:0005057; F:signal transducer activity, downstream of receptor; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
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.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative initiation;
Alternative splicing; Complete proteome; Cytoplasm; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1 481 Docking protein 1.
/FTId=PRO_0000187268.
DOMAIN 4 119 PH.
DOMAIN 151 259 IRS-type PTB. {ECO:0000255|PROSITE-
ProRule:PRU00389}.
COMPBIAS 280 318 Pro-rich.
COMPBIAS 356 433 Pro-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 269 269 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 296 296 Phosphotyrosine.
{ECO:0000250|UniProtKB:P97465}.
MOD_RES 337 337 Phosphotyrosine.
{ECO:0000250|UniProtKB:P97465}.
MOD_RES 341 341 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 362 362 Phosphotyrosine; by INSR.
{ECO:0000244|PubMed:15592455,
ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:11551902}.
MOD_RES 377 377 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 398 398 Phosphotyrosine; by INSR.
{ECO:0000244|PubMed:15592455,
ECO:0000269|PubMed:11551902}.
MOD_RES 409 409 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 416 416 Phosphoserine.
{ECO:0000250|UniProtKB:P97465}.
MOD_RES 449 449 Phosphotyrosine.
{ECO:0000250|UniProtKB:P97465}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 139 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_038224.
VAR_SEQ 153 177 SQFWVTVQRTEAAERCGLHGSYVLR -> HVLFRGRPPLPL
RPWNLHLPDGTGK (in isoform 2).
{ECO:0000303|PubMed:10940083}.
/FTId=VSP_003852.
VAR_SEQ 178 481 Missing (in isoform 2).
{ECO:0000303|PubMed:10940083}.
/FTId=VSP_003853.
MUTAGEN 362 362 Y->F: No association with NCK. No
association with GAP; when associated
with F-398.
{ECO:0000269|PubMed:11551902}.
MUTAGEN 398 398 Y->F: No association with GAP; when
associated with F-362.
{ECO:0000269|PubMed:11551902}.
CONFLICT 1 20 MDGAVMEGPLFLQSQRFGTK -> RLPAQASATREREPRWS
PFQ (in Ref. 3; AAB88182). {ECO:0000305}.
STRAND 153 159 {ECO:0000244|PDB:2V76}.
HELIX 163 167 {ECO:0000244|PDB:2V76}.
STRAND 172 178 {ECO:0000244|PDB:2V76}.
STRAND 180 188 {ECO:0000244|PDB:2V76}.
TURN 190 192 {ECO:0000244|PDB:2V76}.
STRAND 195 202 {ECO:0000244|PDB:2V76}.
HELIX 203 205 {ECO:0000244|PDB:2V76}.
STRAND 206 211 {ECO:0000244|PDB:2V76}.
STRAND 213 220 {ECO:0000244|PDB:2V76}.
STRAND 228 234 {ECO:0000244|PDB:2V76}.
HELIX 238 251 {ECO:0000244|PDB:2V76}.
SEQUENCE 481 AA; 52392 MW; E9D947831244BA6C CRC64;
MDGAVMEGPL FLQSQRFGTK RWRKTWAVLY PASPHGVARL EFFDHKGSSS GGGRGSSRRL
DCKVIRLAEC VSVAPVTVET PPEPGATAFR LDTAQRSHLL AADAPSSAAW VQTLCRNAFP
KGSWTLAPTD NPPKLSALEM LENSLYSPTW EGSQFWVTVQ RTEAAERCGL HGSYVLRVEA
ERLTLLTVGA QSQILEPLLS WPYTLLRRYG RDKVMFSFEA GRRCPSGPGT FTFQTAQGND
IFQAVETAIH RQKAQGKAGQ GHDVLRADSH EGEVAEGKLP SPPGPQELLD SPPALYAEPL
DSLRIAPCPS QDSLYSDPLD STSAQAGEGV QRKKPLYWDL YEHAQQQLLK AKLTDPKEDP
IYDEPEGLAP VPPQGLYDLP REPKDAWWCQ ARVKEEGYEL PYNPATDDYA VPPPRSTKPL
LAPKPQGPAF PEPGTATGSG IKSHNSALYS QVQKSGASGS WDCGLSRVGT DKTGVKSEGS
T


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Genprice Inc, Invoices and accounting
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