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Protein

Docking protein 3

Gene

Dok3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK3 is a negative regulator of JNK signaling in B-cells through interaction with INPP5D/SHIP1. May modulate ABL1 function (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Docking protein 3
Alternative name(s):
Downstream of tyrosine kinase 3
Gene namesi
Name:Dok3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi1311840. Dok3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Docking protein 3PRO_0000356281Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei138 – 1381PhosphoserineBy similarity
Modified residuei274 – 2741PhosphoserineCombined sources
Modified residuei308 – 3081PhosphoserineBy similarity
Modified residuei314 – 3141PhosphoserineBy similarity
Modified residuei325 – 3251PhosphotyrosineBy similarity
Modified residuei371 – 3711PhosphoserineBy similarity

Post-translational modificationi

Constitutively tyrosine-phosphorylated.By similarity
On IL2 stimulation, phosphorylated on C-terminal tyrosine residues possibly by Src kinases. Can also be phosphorylated by ABL1 kinase (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiB2RYG7.
PeptideAtlasiB2RYG7.
PRIDEiB2RYG7.

PTM databases

iPTMnetiB2RYG7.
PhosphoSiteiB2RYG7.

Expressioni

Gene expression databases

GenevisibleiB2RYG7. RN.

Interactioni

Subunit structurei

On tyrosine phosphorylation, interacts with CSK and INPP5D/SHIP1 via their SH2 domains. Binds ABL1 through the PTB domain and in a kinase-dependent manner. Does not interact with RasGAP (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018232.

Structurei

3D structure databases

ProteinModelPortaliB2RYG7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 123117PHAdd
BLAST
Domaini157 – 261105IRS-type PTBPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi238 – 31578Pro-richAdd
BLAST

Domaini

PTB domain mediates receptor interaction.By similarity

Sequence similaritiesi

Belongs to the DOK family. Type A subfamily.Curated
Contains 1 IRS-type PTB domain.PROSITE-ProRule annotation
Contains 1 PH domain.Curated

Phylogenomic databases

eggNOGiKOG4047. Eukaryota.
ENOG410XS2S. LUCA.
GeneTreeiENSGT00730000110348.
HOGENOMiHOG000112245.
HOVERGENiHBG051391.
InParanoidiB2RYG7.
OMAiKGPAPCD.
OrthoDBiEOG77WWC5.
PhylomeDBiB2RYG7.
TreeFamiTF324994.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR002404. IRS_PTB.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF02174. IRS. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00310. PTBI. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 2 hits.
PROSITEiPS51064. IRS_PTB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2RYG7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESVETPVKD GLLYQQHMKF GKKCWRKVWA LLYAGGPSGV ARLESWDVRD
60 70 80 90 100
GGLGPGGDRP AGPGRRGERR IIRLADCVSV LPADGESCPR DTGAFLITTT
110 120 130 140 150
ERSHLLAAQH RQSWMDPICQ LAFPSTGECS SGSGQAESPK RGFVPMEENS
160 170 180 190 200
IYSSWQEVAE FPVVVQRTEA TTRCQLKGPY LLVLGQDDIQ LRETSKPQAC
210 220 230 240 250
YSWPYRFLRK FGSDKGVFSF EAGRRCDSGE GLFAFSSPRA PDICGAVAAA
260 270 280 290 300
IARQRERLPE LAMSPPCPLP RALSLPSLEP PGELREVAPE YELAPSRKLP
310 320 330 340 350
LTDPGPQSLP LLLSPTQDGT ASSLYASVCK QTSKHKATVE HLYENVFMLE
360 370 380 390 400
ASPGLSNGGP EAQEGPPGGR SPLGSPIYHN SEELSWPGSA HDSNLEAQYR
410 420 430 440
RLLELELDDA GGAGRPGAQT GIKAKLVTLL TRERKKGPAP CDRP
Length:444
Mass (Da):48,190
Last modified:July 1, 2008 - v1
Checksum:iDF79C5ADB1893046
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474032 Genomic DNA. Translation: EDL93971.1.
BC166772 mRNA. Translation: AAI66772.1.
RefSeqiNP_001100806.1. NM_001107336.1.
XP_006253681.1. XM_006253619.2.
UniGeneiRn.19911.

Genome annotation databases

EnsembliENSRNOT00000018232; ENSRNOP00000018232; ENSRNOG00000013564.
GeneIDi306760.
KEGGirno:306760.
UCSCiRGD:1311840. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474032 Genomic DNA. Translation: EDL93971.1.
BC166772 mRNA. Translation: AAI66772.1.
RefSeqiNP_001100806.1. NM_001107336.1.
XP_006253681.1. XM_006253619.2.
UniGeneiRn.19911.

3D structure databases

ProteinModelPortaliB2RYG7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018232.

PTM databases

iPTMnetiB2RYG7.
PhosphoSiteiB2RYG7.

Proteomic databases

PaxDbiB2RYG7.
PeptideAtlasiB2RYG7.
PRIDEiB2RYG7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000018232; ENSRNOP00000018232; ENSRNOG00000013564.
GeneIDi306760.
KEGGirno:306760.
UCSCiRGD:1311840. rat.

Organism-specific databases

CTDi79930.
RGDi1311840. Dok3.

Phylogenomic databases

eggNOGiKOG4047. Eukaryota.
ENOG410XS2S. LUCA.
GeneTreeiENSGT00730000110348.
HOGENOMiHOG000112245.
HOVERGENiHBG051391.
InParanoidiB2RYG7.
OMAiKGPAPCD.
OrthoDBiEOG77WWC5.
PhylomeDBiB2RYG7.
TreeFamiTF324994.

Miscellaneous databases

PROiB2RYG7.

Gene expression databases

GenevisibleiB2RYG7. RN.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR002404. IRS_PTB.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF02174. IRS. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00310. PTBI. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 2 hits.
PROSITEiPS51064. IRS_PTB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDOK3_RAT
AccessioniPrimary (citable) accession number: B2RYG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: July 1, 2008
Last modified: July 6, 2016
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.