Genular: Defining Cellular Identity and Function

Details for: Dok2

Gene ID: 13449

Symbol: Dok2

Ensembl ID: ENSMUSG00000022102

Description: docking protein 2

Associated with

Axon guidance
(R-MMU-422475)
Cell surface interactions at the vascular wall
(R-MMU-202733)
Developmental biology
(R-MMU-1266738)
Hemostasis
(R-MMU-109582)
Nervous system development
(R-MMU-9675108)
Ret signaling
(R-MMU-8853659)
Tie2 signaling
(R-MMU-210993)
Cytoplasm
(GO:0005737)
Negative regulation of mapk cascade
(GO:0043409)
Positive regulation of mapk cascade
(GO:0043410)
Protein binding
(GO:0005515)
Ras protein signal transduction
(GO:0007265)
Transmembrane receptor protein tyrosine kinase adaptor activity
(GO:0005068)
Transmembrane receptor protein tyrosine kinase signaling pathway
(GO:0007169)

Other Information

Proteins

Docking protein 2

Genular Protein ID: 216215086

Symbol: DOK2_MOUSE

Name: Docking protein 2

UniProtKB Accession Codes:

O70469 O70272 Q99KL1

Database IDs:

Citations:

PubMed ID: 9697832

Title: FRIP, a hematopoietic cell-specific rasGAP-interacting protein phosphorylated in response to cytokine stimulation.

PubMed ID: 9697832

DOI: 10.1016/s1074-7613(00)80584-1

PubMed ID: 9478921

Title: Molecular cloning and characterization of p56dok-2 defines a new family of RasGAP-binding proteins.

PubMed ID: 9478921

DOI: 10.1074/jbc.273.9.4827

PubMed ID: 9764820

Title: The Tek/Tie2 receptor signals through a novel Dok-related docking protein, Dok-R.

PubMed ID: 9764820

DOI: 10.1038/sj.onc.1202115

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 10508618

Title: Recruitment of Dok-R to the EGF receptor through its PTB domain is required for attenuation of Erk MAP kinase activation.

PubMed ID: 10508618

DOI: 10.1016/s0960-9822(99)80458-8

PubMed ID: 11470823

Title: Novel p62dok family members, dok-4 and dok-5, are substrates of the c-Ret receptor tyrosine kinase and mediate neuronal differentiation.

PubMed ID: 11470823

DOI: 10.1083/jcb.200102032

PubMed ID: 12665569

Title: A unique autophosphorylation site on Tie2/Tek mediates Dok-R phosphotyrosine binding domain binding and function.

PubMed ID: 12665569

DOI: 10.1128/mcb.23.8.2658-2668.2003

Sequence Information:

Length: 412
Mass: 45522
Checksum: 02AC02530DBED053
Sequence:

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

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: Dok2

Associated with

Other Information

FRIP, a hematopoietic cell-specific rasGAP-interacting protein phosphorylated in response to cytokine stimulation. PubMed ID: 9697832

Molecular cloning and characterization of p56dok-2 defines a new family of RasGAP-binding proteins. PubMed ID: 9478921

The Tek/Tie2 receptor signals through a novel Dok-related docking protein, Dok-R. PubMed ID: 9764820

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Recruitment of Dok-R to the EGF receptor through its PTB domain is required for attenuation of Erk MAP kinase activation. PubMed ID: 10508618

Novel p62dok family members, dok-4 and dok-5, are substrates of the c-Ret receptor tyrosine kinase and mediate neuronal differentiation. PubMed ID: 11470823

A unique autophosphorylation site on Tie2/Tek mediates Dok-R phosphotyrosine binding domain binding and function. PubMed ID: 12665569