Human Gene TDRKH (uc001eza.4)
  Description: Homo sapiens tudor and KH domain containing (TDRKH), transcript variant 2, mRNA.
Transcript (Including UTRs)
   Position: hg19 chr1:151,745,955-151,763,010 Size: 17,056 Total Exon Count: 13 Strand: -
Coding Region
   Position: hg19 chr1:151,746,928-151,755,498 Size: 8,571 Coding Exon Count: 12 

Page IndexSequence and LinksUniProtKB CommentsPrimersGenetic AssociationsMalaCards
CTDGene AllelesRNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein Structure
Other SpeciesGO AnnotationsmRNA DescriptionsPathwaysOther NamesModel Information
Methods
Data last updated at UCSC: 2013-06-14

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr1:151,745,955-151,763,010)mRNA (may differ from genome)Protein (561 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
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WikipediaBioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: TDRKH_HUMAN
DESCRIPTION: RecName: Full=Tudor and KH domain-containing protein; AltName: Full=Tudor domain-containing protein 2;
SUBUNIT: Interacts with PIWIL1 and PIWIL4 (By similarity).
SIMILARITY: Contains 2 KH domains.
SIMILARITY: Contains 1 Tudor domain.
SEQUENCE CAUTION: Sequence=AAD30971.1; Type=Erroneous termination; Positions=562; Note=Translated as stop; Sequence=BC022467; Type=Erroneous termination; Positions=175; Note=Translated as Lys;

-  Primer design for this transcript
 

Primer3Plus can design qPCR Primers that straddle exon-exon-junctions, which amplify only cDNA, not genomic DNA.
Click here to load the transcript sequence and exon structure into Primer3Plus

Exonprimer can design one pair of Sanger sequencing primers around every exon, located in non-genic sequence.
Click here to open Exonprimer with this transcript

To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  Genetic Association Studies of Complex Diseases and Disorders
  Genetic Association Database (archive): TDRKH
CDC HuGE Published Literature: TDRKH
Positive Disease Associations: Hemoglobins , Lipids , Triglycerides
Related Studies:
  1. Hemoglobins
    Qiong Yang et al. BMC medical genetics 2007, Genome-wide association and linkage analyses of hemostatic factors and hematological phenotypes in the Framingham Heart Study., BMC medical genetics. [PubMed 17903294]
    Using genome-wide association methodology, we have successfully identified a SNP in complete LD with a sequence variant previously shown to be strongly associated with factor VII, providing proof of principle for this approach. Further study of additional strongly associated SNPs and linked regions may identify novel variants that influence the inter-individual variability in hemostatic factors and hematological phenotypes.
  2. Lipids
    Sekar Kathiresan et al. BMC medical genetics 2007, A genome-wide association study for blood lipid phenotypes in the Framingham Heart Study., BMC medical genetics. [PubMed 17903299]
    Using a 100K genome-wide scan, we have generated a set of putative associations for common sequence variants and lipid phenotypes. Validation of selected hypotheses in additional samples did not identify any new loci underlying variability in blood lipids. Lack of replication may be due to inadequate statistical power to detect modest quantitative trait locus effects (i.e., <1% of trait variance explained) or reduced genomic coverage of the 100K array. GWAS in FHS using a denser genome-wide genotyping platform and a better-powered replication strategy may identify novel loci underlying blood lipids.
  3. Triglycerides
    Sekar Kathiresan et al. BMC medical genetics 2007, A genome-wide association study for blood lipid phenotypes in the Framingham Heart Study., BMC medical genetics. [PubMed 17903299]
    Using a 100K genome-wide scan, we have generated a set of putative associations for common sequence variants and lipid phenotypes. Validation of selected hypotheses in additional samples did not identify any new loci underlying variability in blood lipids. Lack of replication may be due to inadequate statistical power to detect modest quantitative trait locus effects (i.e., <1% of trait variance explained) or reduced genomic coverage of the 100K array. GWAS in FHS using a denser genome-wide genotyping platform and a better-powered replication strategy may identify novel loci underlying blood lipids.
           more ... click here to view the complete list

-  MalaCards Disease Associations
  MalaCards Gene Search: TDRKH
Diseases sorted by gene-association score: ewing sarcoma (2)

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene
  • D000082 Acetaminophen
  • D013749 Tetrachlorodibenzodioxin
  • C111118 2',3,3',4',5-pentachloro-4-hydroxybiphenyl
  • C548651 2-(1'H-indolo-3'-carbonyl)thiazole-4-carboxylic acid methyl ester
  • D001564 Benzo(a)pyrene
  • D002117 Calcitriol
  • D010795 Phthalic Acids

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 16.99 RPKM in Testis
Total median expression: 134.28 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -68.60157-0.437 Picture PostScript Text
3' UTR -287.58973-0.296 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR004087 - KH_dom
IPR004088 - KH_dom_type_1
IPR002999 - Tudor

Pfam Domains:
PF00013 - KH domain
PF00567 - Tudor domain

SCOP Domains:
63748 - Tudor/PWWP/MBT
54791 - Eukaryotic type KH-domain (KH-domain type I)
54814 - Prokaryotic type KH domain (KH-domain type II)

Protein Data Bank (PDB) 3-D Structure
MuPIT help
2DIQ - NMR MuPIT 3FDR - X-ray MuPIT


ModBase Predicted Comparative 3D Structure on Q9Y2W6
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The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologGenome BrowserNo orthologNo orthologNo orthologNo ortholog
Gene DetailsGene Details    
Gene SorterGene Sorter    
 RGD    
 Protein Sequence    
 Alignment    

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0003676 nucleic acid binding
GO:0003723 RNA binding

Biological Process:
GO:0007140 male meiosis
GO:0007283 spermatogenesis
GO:0009566 fertilization
GO:0030154 cell differentiation
GO:0031047 gene silencing by RNA
GO:0034587 piRNA metabolic process
GO:0043046 DNA methylation involved in gamete generation

Cellular Component:
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0071546 pi-body
GO:0071547 piP-body


-  Descriptions from all associated GenBank mRNAs
  BC156177 - Synthetic construct Homo sapiens clone IMAGE:100062408, MGC:190507 tudor and KH domain containing (TDRKH) mRNA, encodes complete protein.
BC172470 - Synthetic construct Homo sapiens clone IMAGE:100069164, MGC:199175 tudor and KH domain containing (TDRKH) mRNA, encodes complete protein.
AK225160 - Homo sapiens mRNA for Splice isoform 2 of Q9Y2W6 variant, clone: CBR04030.
AF119121 - Homo sapiens putative RNA binding protein mRNA, alternatively spliced, complete cds.
BC032690 - Homo sapiens tudor and KH domain containing, mRNA (cDNA clone IMAGE:5241008).
BC022467 - Homo sapiens tudor and KH domain containing, mRNA (cDNA clone IMAGE:4796384), with apparent retained intron.
AF227192 - Homo sapiens tudor and KH domain-containing protein (TDRKH) (TDRKH) mRNA, complete cds.
AK056402 - Homo sapiens cDNA FLJ31840 fis, clone NT2RP7000109, highly similar to Tudor and KH domain-containing protein.
AK226092 - Homo sapiens mRNA for tudor and KH domain containing variant, clone: ef03729.
AK303063 - Homo sapiens cDNA FLJ61003 complete cds, highly similar to Tudor and KH domain-containing protein.
AK295948 - Homo sapiens cDNA FLJ54003 complete cds, highly similar to Tudor and KH domain-containing protein.
KJ898334 - Synthetic construct Homo sapiens clone ccsbBroadEn_07728 TDRKH gene, encodes complete protein.
DQ890822 - Synthetic construct clone IMAGE:100003452; FLH166228.01X; RZPDo839E0386D tudor and KH domain containing (TDRKH) gene, encodes complete protein.
DQ896752 - Synthetic construct Homo sapiens clone IMAGE:100011212; FLH166224.01L; RZPDo839E0385D tudor and KH domain containing (TDRKH) gene, encodes complete protein.
AB527643 - Synthetic construct DNA, clone: pF1KB5539, Homo sapiens TDRKH gene for tudor and KH domain containing, without stop codon, in Flexi system.
AK316279 - Homo sapiens cDNA, FLJ79178 complete cds, highly similar to Tudor and KH domain-containing protein.
DQ597075 - Homo sapiens piRNA piR-35141, complete sequence.
JD043947 - Sequence 24971 from Patent EP1572962.
JD151620 - Sequence 132644 from Patent EP1572962.
JD466834 - Sequence 447858 from Patent EP1572962.
JD462117 - Sequence 443141 from Patent EP1572962.
JD496213 - Sequence 477237 from Patent EP1572962.
JD281563 - Sequence 262587 from Patent EP1572962.
JD279239 - Sequence 260263 from Patent EP1572962.

-  Biochemical and Signaling Pathways
  Reactome (by CSHL, EBI, and GO)

Protein Q9Y2W6 (Reactome details) participates in the following event(s):

R-HSA-5615682 Complexed PIWIL1 binds pre-piRNA
R-HSA-5629203 HENMT1 methylates 2' hydroxyl at 3' end of piRNA in 4xMeR-PIWIL1:piRNA:TDRD6:TDRKH
R-HSA-5629237 HENMT1 methylates 2' hydroxyl at 3' end of piRNA in MeR-PIWIL4:piRNA:TDRD9:MAEL:TDRKH
R-HSA-5601884 PIWI-interacting RNA (piRNA) biogenesis
R-HSA-211000 Gene Silencing by RNA
R-HSA-74160 Gene expression (Transcription)

-  Other Names for This Gene
  Alternate Gene Symbols: D3DV24, NM_001083963, NP_006853, Q5SZR3, Q5SZR5, Q8N582, Q9NYV5, Q9Y2W6, TDRD2, TDRKH_HUMAN
UCSC ID: uc001eza.4
RefSeq Accession: NM_001083963
Protein: Q9Y2W6 (aka TDRKH_HUMAN or TDRH_HUMAN)
CCDS: CCDS41394.1

-  Gene Model Information
 
category: coding nonsense-mediated-decay: no RNA accession: NM_001083963.1
exon count: 13CDS single in 3' UTR: no RNA size: 2829
ORF size: 1686CDS single in intron: no Alignment % ID: 100.00
txCdsPredict score: 3404.00frame shift in genome: no % Coverage: 99.54
has start codon: yes stop codon in genome: no # of Alignments: 1
has end codon: yes retained intron: yes # AT/AC introns 0
selenocysteine: no end bleed into intron: 934# strange splices: 0
Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.