Human Gene SHPK (uc002fvz.1)
  Description: Homo sapiens sedoheptulokinase (SHPK), mRNA.
RefSeq Summary (NM_013276): The protein encoded by this gene has weak homology to several carbohydrate kinases, a class of proteins involved in the phosphorylation of sugars as they enter a cell, inhibiting return across the cell membrane. Sequence variation between this novel gene and known carbohydrate kinases suggests the possibility of a different substrate, cofactor or changes in kinetic properties distinguishing it from other carbohydrate kinases. The gene resides in a region commonly deleted in cystinosis patients, suggesting a role as a modifier for the cystinosis phenotype. The genomic region is also rich in Alu repetitive sequences, frequently involved in chromosomal rearrangements. [provided by RefSeq, Jul 2008].
Transcript (Including UTRs)
   Position: hg19 chr17:3,511,556-3,539,616 Size: 28,061 Total Exon Count: 7 Strand: -
Coding Region
   Position: hg19 chr17:3,513,854-3,539,513 Size: 25,660 Coding Exon Count: 7 

Page IndexSequence and LinksUniProtKB CommentsPrimersGenetic AssociationsMalaCards
CTDGene AllelesMicroarray ExpressionRNA StructureProtein StructureOther Species
GO AnnotationsmRNA DescriptionsPathwaysOther NamesModel InformationMethods
Data last updated at UCSC: 2013-06-14

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr17:3,511,556-3,539,616)mRNA (may differ from genome)Protein (478 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
AlphaFoldBioGPSEnsemblEntrez GeneExonPrimerGeneCards
GeneNetworkH-INVHGNCHPRDLynxMalacards
MGIneXtProtOMIMPubMedReactomeTreefam
UniProtKBBioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: SHPK_HUMAN
DESCRIPTION: RecName: Full=Sedoheptulokinase; Short=SHK; EC=2.7.1.14; AltName: Full=Carbohydrate kinase-like protein;
FUNCTION: Acts as a modulator of macrophage activation through control of glucose metabolism (By similarity).
CATALYTIC ACTIVITY: ATP + sedoheptulose = ADP + sedoheptulose 7- phosphate.
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.06 mM for sedoheptulose; pH dependence: Optimum pH is 8.5;
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
TISSUE SPECIFICITY: Strongly expressed in liver, kidney and pancreas. Expressed at lower levels in placenta and heart. Very weakly expressed in lung and brain.
INDUCTION: Down-regulated by LPS.
SIMILARITY: Belongs to the FGGY kinase family.

-  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): SHPK
CDC HuGE Published Literature: SHPK

-  MalaCards Disease Associations
  MalaCards Gene Search: SHPK
Diseases sorted by gene-association score: sedoheptulokinase deficiency* (378), cystinosis (25)
* = Manually curated disease association

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

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

+  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 -43.80103-0.425 Picture PostScript Text
3' UTR -857.142298-0.373 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
IPR018484 - Carb_kinase_FGGY_N

Pfam Domains:
PF00370 - FGGY family of carbohydrate kinases, N-terminal domain

SCOP Domains:
53067 - Actin-like ATPase domain

ModBase Predicted Comparative 3D Structure on Q9UHJ6
FrontTopSide
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 orthologNo orthologGenome BrowserNo orthologGenome BrowserNo ortholog
Gene Details   Gene Details 
Gene Sorter   Gene Sorter 
  Ensembl WormBase 
  Protein Sequence Protein Sequence 
  Alignment Alignment 

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0000166 nucleotide binding
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016740 transferase activity
GO:0016773 phosphotransferase activity, alcohol group as acceptor
GO:0050277 sedoheptulokinase activity

Biological Process:
GO:0005975 carbohydrate metabolic process
GO:0006098 pentose-phosphate shunt
GO:0009052 pentose-phosphate shunt, non-oxidative branch
GO:0016310 phosphorylation
GO:0035963 cellular response to interleukin-13
GO:0043030 regulation of macrophage activation
GO:0050727 regulation of inflammatory response
GO:0071222 cellular response to lipopolysaccharide
GO:0071353 cellular response to interleukin-4

Cellular Component:
GO:0005737 cytoplasm
GO:0005829 cytosol


-  Descriptions from all associated GenBank mRNAs
  AF163573 - Homo sapiens CARKL (CARKL) mRNA, complete cds.
AK055609 - Homo sapiens cDNA FLJ31047 fis, clone HSYRA2000424, highly similar to Carbohydrate kinase-like protein (EC 2.7.1.-).
BC020543 - Homo sapiens sedoheptulokinase, mRNA (cDNA clone MGC:21179 IMAGE:4413491), complete cds.
AL832420 - Homo sapiens mRNA; cDNA DKFZp762D092 (from clone DKFZp762D092).
AK298360 - Homo sapiens cDNA FLJ52918 complete cds, highly similar to Carbohydrate kinase-like protein (EC 2.7.1.-).
DQ891646 - Synthetic construct clone IMAGE:100004276; FLH178953.01X; RZPDo839B01130D carbohydrate kinase-like (CARKL) gene, encodes complete protein.
AK312428 - Homo sapiens cDNA, FLJ92772, highly similar to Homo sapiens carbohydrate kinase-like (CARKL), mRNA.
KJ893441 - Synthetic construct Homo sapiens clone ccsbBroadEn_02835 SHPK gene, encodes complete protein.
KJ905442 - Synthetic construct Homo sapiens clone ccsbBroadEn_15024 SHPK gene, encodes complete protein.
DQ894835 - Synthetic construct Homo sapiens clone IMAGE:100009295; FLH178949.01L; RZPDo839B01129D carbohydrate kinase-like (CARKL) gene, encodes complete protein.
AB529118 - Synthetic construct DNA, clone: pF1KB4835, Homo sapiens CARKL gene for sedoheptulokinase, without stop codon, in Flexi system.
CU676548 - Synthetic construct Homo sapiens gateway clone IMAGE:100019588 5' read CARKL mRNA.
AL136801 - Homo sapiens mRNA; cDNA DKFZp434K0220 (from clone DKFZp434K0220).
JD040294 - Sequence 21318 from Patent EP1572962.
JD163158 - Sequence 144182 from Patent EP1572962.
JD051878 - Sequence 32902 from Patent EP1572962.
AK057040 - Homo sapiens cDNA FLJ32478 fis, clone SKNMC2000877, moderately similar to Homo sapiens CARKL mRNA.
BC111366 - Homo sapiens cDNA clone IMAGE:7503396.
AK057020 - Homo sapiens cDNA FLJ32458 fis, clone SKNMC1000029.
JD549910 - Sequence 530934 from Patent EP1572962.
JD257419 - Sequence 238443 from Patent EP1572962.
JD368673 - Sequence 349697 from Patent EP1572962.
JD259584 - Sequence 240608 from Patent EP1572962.
JD313336 - Sequence 294360 from Patent EP1572962.
JD082399 - Sequence 63423 from Patent EP1572962.
JD430569 - Sequence 411593 from Patent EP1572962.
JD179043 - Sequence 160067 from Patent EP1572962.
JD533043 - Sequence 514067 from Patent EP1572962.
JD264163 - Sequence 245187 from Patent EP1572962.
JD420157 - Sequence 401181 from Patent EP1572962.
JD105314 - Sequence 86338 from Patent EP1572962.
JD420156 - Sequence 401180 from Patent EP1572962.
JD286619 - Sequence 267643 from Patent EP1572962.
JD121143 - Sequence 102167 from Patent EP1572962.
JD436861 - Sequence 417885 from Patent EP1572962.
JD478843 - Sequence 459867 from Patent EP1572962.
JD478844 - Sequence 459868 from Patent EP1572962.
JD543457 - Sequence 524481 from Patent EP1572962.
JD112963 - Sequence 93987 from Patent EP1572962.
JD543456 - Sequence 524480 from Patent EP1572962.
JD543458 - Sequence 524482 from Patent EP1572962.
JD395644 - Sequence 376668 from Patent EP1572962.
JD497865 - Sequence 478889 from Patent EP1572962.
JD543454 - Sequence 524478 from Patent EP1572962.
JD550537 - Sequence 531561 from Patent EP1572962.
JD090954 - Sequence 71978 from Patent EP1572962.
JD245002 - Sequence 226026 from Patent EP1572962.
JD454749 - Sequence 435773 from Patent EP1572962.
JD225635 - Sequence 206659 from Patent EP1572962.
JD242112 - Sequence 223136 from Patent EP1572962.
JD111579 - Sequence 92603 from Patent EP1572962.
JD174222 - Sequence 155246 from Patent EP1572962.
JD403086 - Sequence 384110 from Patent EP1572962.
JD371196 - Sequence 352220 from Patent EP1572962.
JD535605 - Sequence 516629 from Patent EP1572962.
JD056137 - Sequence 37161 from Patent EP1572962.
JD339655 - Sequence 320679 from Patent EP1572962.
JD089840 - Sequence 70864 from Patent EP1572962.
JD056927 - Sequence 37951 from Patent EP1572962.
JD353781 - Sequence 334805 from Patent EP1572962.
JD086421 - Sequence 67445 from Patent EP1572962.
JD403783 - Sequence 384807 from Patent EP1572962.
JD471928 - Sequence 452952 from Patent EP1572962.
JD437679 - Sequence 418703 from Patent EP1572962.
JD232025 - Sequence 213049 from Patent EP1572962.
JD086706 - Sequence 67730 from Patent EP1572962.
JD249313 - Sequence 230337 from Patent EP1572962.
JD383896 - Sequence 364920 from Patent EP1572962.
JD266288 - Sequence 247312 from Patent EP1572962.
JD099890 - Sequence 80914 from Patent EP1572962.
JD163823 - Sequence 144847 from Patent EP1572962.
JD372310 - Sequence 353334 from Patent EP1572962.
JD437764 - Sequence 418788 from Patent EP1572962.
JD458783 - Sequence 439807 from Patent EP1572962.
JD391079 - Sequence 372103 from Patent EP1572962.
JD124763 - Sequence 105787 from Patent EP1572962.

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

Protein Q9UHJ6 (Reactome details) participates in the following event(s):

R-HSA-8959719 SHPK phosphorylates Sedo to Sedo7P
R-HSA-71336 Pentose phosphate pathway (hexose monophosphate shunt)
R-HSA-71387 Metabolism of carbohydrates
R-HSA-1430728 Metabolism

-  Other Names for This Gene
  Alternate Gene Symbols: B2R640, CARKL, NM_013276, NP_037408, Q8WUH3, Q9UHJ6, SHPK_HUMAN
UCSC ID: uc002fvz.1
RefSeq Accession: NM_013276
Protein: Q9UHJ6 (aka SHPK_HUMAN)
CCDS: CCDS11030.1

-  Gene Model Information
 
category: coding nonsense-mediated-decay: no RNA accession: NM_013276.2
exon count: 7CDS single in 3' UTR: no RNA size: 3838
ORF size: 1437CDS single in intron: no Alignment % ID: 99.97
txCdsPredict score: 2873.00frame shift in genome: no % Coverage: 100.00
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: 0# 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.